interpro_id string | interpro_numeric_id int64 | name string | short_name string | entry_type string | protein_count int64 | is_llm bool | is_llm_reviewed bool | abstract string | go_ids list | go_terms list | go_categories list | go_count int64 | member_databases list | member_accessions list | member_names list | member_protein_counts list | member_count int64 | external_databases list | external_accessions list | external_xrefs list | external_xref_count int64 | pdb_ids list | structure_count int64 | publication_ids list | pubmed_ids list | publication_titles list | publication_years list | publication_count int64 | parent_ids list | child_ids list | parent_count int64 | child_count int64 | tree_depth float64 | taxonomy_names list | taxonomy_protein_counts list | taxonomy_count int64 | key_species_names list | key_species_protein_counts list | key_species_count int64 | in_entry_list bool | entry_list_type string | entry_list_name string | names_dat_name string | short_names_dat_name string | split_bucket int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR001737 | 1,737 | Ribosomal RNA adenine methyltransferase KsgA/Erm | KsgA/Erm | Family | 43,130 | false | false | The bacterial enzyme KsgA catalyses the transfer of a total of four methyl groups from S-adenosyl-l-methionine (S-AdoMet) to two adjacent adenosine bases in 16S rRNA. This enzyme and the resulting modified adenosine bases appear to be conserved in all species of eubacteria, eukaryotes, and archaea, and in eukaryotic or... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"PANTHER"
] | [
"PF00398",
"PS51689",
"PTHR11727"
] | [
"RrnaAD",
"SAM_RNA_A_N6_MT",
""
] | [
42133,
40071,
41446
] | 3 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1",
"2.1.1.182",
"PDOC00871",
"R-BTA-163282",
"R-DME-163282",
"R-HSA-163282",
"R-HSA-2151201",
"R-HSA-6790901",
"R-HSA-6793080",
"R-MMU-163282",
"R-RNO-163282",
"R-SCE-163282",
"R-SPO-163282"
] | [
"EC:2.1.1",
"EC:2.1.1.182",
"PROSITEDOC:PDOC00871",
"REACTOME:R-BTA-163282",
"REACTOME:R-DME-163282",
"REACTOME:R-HSA-163282",
"REACTOME:R-HSA-2151201",
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6793080",
"REACTOME:R-MMU-163282",
"REACTOME:R-RNO-163282",
"REACTOME:R-SCE-163282",
"REACTOME:R-... | 13 | [
"1i4w",
"1qam",
"1qan",
"1qao",
"1qaq",
"1qyr",
"1yub",
"1zq9",
"2erc",
"2h1r",
"3ftc",
"3ftd",
"3fte",
"3ftf",
"3fut",
"3fuu",
"3fuv",
"3fuw",
"3fux",
"3fyc",
"3fyd",
"3grr",
"3gru",
"3grv",
"3gry",
"3r9x",
"3tpz",
"3tqs",
"3uzu",
"4adv",
"4gc5",
"4gc9"... | 116 | [
"PUB00003946",
"PUB00014820",
"PUB00030186",
"PUB00072555",
"PUB00101503",
"PUB00101504",
"PUB00101505"
] | [
"9187657",
"15136037",
"10366505",
"23804760",
"4336392",
"4329247",
"6575236"
] | [
"Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance.",
"Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli.",
"The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexe... | [
1997,
2004,
1999,
2013,
1972,
1971,
1983
] | 7 | [] | [
"IPR011530",
"IPR016586"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"plasmids",
"unclassified sequences"
] | [
972,
30449,
3,
10970,
3,
733
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
18,
2,
13,
3,
1,
16,
5,
2,
15,
9,
2,
2,
21
] | 13 | true | Family | Ribosomal RNA adenine methyltransferase KsgA/Erm | Ribosomal RNA adenine methyltransferase KsgA/Erm | KsgA/Erm | 8 |
IPR001738 | 1,738 | Rab protein geranylgeranyltransferase component A | Rab_escort | Family | 2,514 | false | false | Rab proteins constitute a family of small GTPases that serve a regulatory role in vesicular membrane traffic [ , ]; C-terminal geranylgeranylation is crucial for their membrane association and function. This post-translational modification is catalysed by Rab geranylgeranyl transferase (Rab-GGTase), a multi-subunit enz... | [
"GO:0006886",
"GO:0018344",
"GO:0005968"
] | [
"intracellular protein transport",
"protein geranylgeranylation",
"Rab-protein geranylgeranyltransferase complex"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF016550",
"PR00893"
] | [
"Rab_ger_ger_transf_A_euk",
"RABESCORT"
] | [
2249,
1614
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-6803205",
"R-CEL-8873719",
"R-CEL-8876198",
"R-DME-6803205",
"R-DME-8873719",
"R-DME-8876198",
"R-HSA-6803205",
"R-HSA-8873719",
"R-HSA-8876198",
"R-MMU-6803205",
"R-MMU-8873719",
"R-MMU-8876198",
"R-RNO-6803205",
"R-RNO-8873719",
"R-RNO-8876198"
] | [
"REACTOME:R-CEL-6803205",
"REACTOME:R-CEL-8873719",
"REACTOME:R-CEL-8876198",
"REACTOME:R-DME-6803205",
"REACTOME:R-DME-8873719",
"REACTOME:R-DME-8876198",
"REACTOME:R-HSA-6803205",
"REACTOME:R-HSA-8873719",
"REACTOME:R-HSA-8876198",
"REACTOME:R-MMU-6803205",
"REACTOME:R-MMU-8873719",
"REACTOM... | 15 | [
"1ltx",
"1vg0",
"1vg9"
] | 3 | [
"PUB00000888",
"PUB00001266",
"PUB00001997",
"PUB00004079",
"PUB00004775"
] | [
"8513495",
"7957092",
"7981670",
"2215697",
"1549574"
] | [
"cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein.",
"Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes.",
"Cloning and characterization of the human choroideremia gene.",
... | [
1993,
1994,
1994,
1990,
1992
] | 5 | [
"IPR018203"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2514
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
2,
1,
5,
8,
14,
4
] | 8 | true | Family | Rab protein geranylgeranyltransferase component A | Rab protein geranylgeranyltransferase component A | Rab_escort | 2 |
IPR001739 | 1,739 | Methyl-CpG DNA binding | Methyl_CpG_DNA-bd | Domain | 26,117 | false | false | This entry represents the MBD domain. The MBD folds into an α/β-sandwich structure comprising a layer of twisted β-sheet, backed by another layer formed by the α1 helix and a hairpin loop at the C-terminal. These layers are amphipathic, with the α1 helix and the β-sheet lying parallel and the hydrophobic faces tightly ... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01429",
"PS50982",
"SM00391"
] | [
"MBD",
"MBD",
"MBD"
] | [
23003,
24124,
19164
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50982",
"R-CEL-3214841",
"R-DME-3214841",
"R-DME-3214847",
"R-DME-5689603",
"R-DME-6804759",
"R-DME-9772755",
"R-DME-9843940",
"R-DRE-3214841",
"R-DRE-9843940",
"R-DRE-9843970",
"R-HSA-110328",
"R-HSA-110329",
"R-HSA-110357",
"R-HSA-3214815",
"R-HSA-3214841",
"R-HSA-3899300",
... | [
"PROSITEDOC:PDOC50982",
"REACTOME:R-CEL-3214841",
"REACTOME:R-DME-3214841",
"REACTOME:R-DME-3214847",
"REACTOME:R-DME-5689603",
"REACTOME:R-DME-6804759",
"REACTOME:R-DME-9772755",
"REACTOME:R-DME-9843940",
"REACTOME:R-DRE-3214841",
"REACTOME:R-DRE-9843940",
"REACTOME:R-DRE-9843970",
"REACTOME:... | 52 | [
"1d9n",
"1ig4",
"1qk9",
"1ub1",
"2kbu",
"2ky8",
"2mb7",
"2moe",
"2ysf",
"3c2i",
"3vxv",
"3vxx",
"3vyb",
"3vyq",
"4lg7",
"5agq",
"5bt2",
"5dzd",
"6acv",
"6c1a",
"6c1t",
"6c1u",
"6c1v",
"6c1y",
"6c2f",
"6cc8",
"6ccg",
"6ceu",
"6cev",
"6cnp",
"6cnq",
"6d1t"... | 52 | [
"PUB00015391",
"PUB00015392",
"PUB00015393"
] | [
"12787239",
"11371345",
"12529184"
] | [
"Characterization of Arabidopsis thaliana methyl-CpG-binding domain (MBD) proteins.",
"Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA.",
"Comparative study of methyl-CpG-binding domain proteins."
] | [
2003,
2001,
2003
] | 3 | [] | [
"IPR047232"
] | 0 | 1 | 0 | [
"Bacteria",
"Bathycoccus sp. RCC716 virus 2",
"Eukaryota",
"bird metagenome"
] | [
11,
1,
26104,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
51,
2,
126,
12,
58,
52,
52,
53,
81
] | 9 | true | Domain | Methyl-CpG DNA binding | Methyl-CpG DNA binding | Methyl_CpG_DNA-bd | 4 |
IPR001740 | 1,740 | GPCR family 2, EMR1-like receptor | GPCR_2_EMR1-like_rcpt | Family | 2,254 | false | false | Human epidermal growth factor (EGF)-like module containing mucin-like hormone receptor 1 (EMR1) is a surface receptor of unknown function that belongs to the EGF-seven-transmembrane (EGF-TM7) family of G-protein coupled receptors [ ]. Human EMR1 has been reported to be expressed exclusively on eosinophils [ ]. It is th... | [
"GO:0004930",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01128"
] | [
"EMR1HORMONER"
] | [
2254
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-373080",
"R-HSA-6798695",
"R-MMU-373080",
"R-RNO-373080"
] | [
"REACTOME:R-HSA-373080",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-373080",
"REACTOME:R-RNO-373080"
] | 4 | [] | 0 | [
"PUB00001208",
"PUB00001962",
"PUB00002980",
"PUB00004310",
"PUB00004961",
"PUB00005147",
"PUB00005148",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816",
"PUB00075328",
"PUB00075329",
"PUB00075330",
"PUB00075331",
"PUB00075332"
] | [
"1646711",
"7601460",
"8550607",
"1314625",
"8170923",
"1658940",
"1658941",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293",
"17823986",
"14647991",
"17108056",
"12023293",
"12731063"
] | [
"Molecular cloning and expression of a cDNA encoding the secretin receptor.",
"EMR1, an unusual member in the family of hormone receptors with seven transmembrane segments.",
"Molecular cloning of F4/80, a murine macrophage-restricted cell surface glycoprotein with homology to the G-protein-linked transmembrane... | [
1991,
1995,
1996,
1992,
1994,
1991,
1991,
2003,
1994,
2005,
2009,
2006,
2013,
2007,
2004,
2007,
2002,
2003
] | 18 | [
"IPR000832"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
2254
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
44,
16,
6,
12
] | 4 | true | Family | GPCR family 2, EMR1-like receptor | GPCR family 2, EMR1-like receptor | GPCR_2_EMR1-like_rcpt | 7 |
IPR001742 | 1,742 | Outer capsid protein VP2, Orbivirus | Capsid_VP2_Orbivir | Family | 1,569 | false | false | This family contains the outer capsid, VP2 proteins from the orbiviruses; these are dsRNA viruses belonging to the Reoviridae. VP2 acts as an anchor for VP1 and VP3 and contains a non-specific DNA and RNA binding domain in the N terminus [ , ]. | [
"GO:0005198"
] | [
"structural molecule activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00898"
] | [
"Orbi_VP2"
] | [
1569
] | 1 | [
"GP"
] | [
"GenProp1006"
] | [
"GP:GenProp1006"
] | 1 | [
"3iyk",
"3j9d",
"8w1o"
] | 3 | [
"PUB00003536",
"PUB00005622"
] | [
"9311813",
"9281498"
] | [
"Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: implications for the architecture of the VP2 capsid layer.",
"Structure of Broadhaven virus by cryoelectron microscopy: correlation of structural and antigenic properties of Broadhaven virus ... | [
1997,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Riboviria"
] | [
1569
] | 1 | [] | [] | 0 | true | Family | Outer capsid protein VP2, Orbivirus | Outer capsid protein VP2, Orbivirus | Capsid_VP2_Orbivir | 7 |
IPR001743 | 1,743 | Photosystem II PsbT | PSII_PsbT | Family | 15,721 | false | false | Oxygenic photosynthesis uses two multi-subunit photosystems (I and II) located in the cell membranes of cyanobacteria and in the thylakoid membranes of chloroplasts in plants and algae. Photosystem II (PSII) has a P680 reaction centre containing chlorophyll 'a' that uses light energy to carry out the oxidation (splitti... | [
"GO:0015979",
"GO:0009523",
"GO:0009539",
"GO:0016020"
] | [
"photosynthesis",
"photosystem II",
"photosystem II reaction center",
"membrane"
] | [
"biological_process",
"cellular_component",
"cellular_component",
"cellular_component"
] | 4 | [
"HAMAP",
"PFAM",
"PANTHER"
] | [
"MF_00808",
"PF01405",
"PTHR36411"
] | [
"PSII_PsbT",
"PsbT",
""
] | [
14336,
15720,
15531
] | 3 | [
"GP"
] | [
"GenProp0661"
] | [
"GP:GenProp0661"
] | 1 | [
"1s5l",
"2axt",
"3a0b",
"3a0h",
"3jcu",
"3kzi",
"3wu2",
"4fby",
"4il6",
"4ixq",
"4ixr",
"4pbu",
"4pj0",
"4rvy",
"4tnh",
"4tni",
"4tnj",
"4tnk",
"4ub6",
"4ub8",
"4v62",
"4v82",
"4yuu",
"5b5e",
"5b66",
"5e79",
"5e7c",
"5gth",
"5gti",
"5h2f",
"5kaf",
"5kai"... | 162 | [
"PUB00015357",
"PUB00015358",
"PUB00015359",
"PUB00015374",
"PUB00097583",
"PUB00152828"
] | [
"12518057",
"15100025",
"14871485",
"11451956",
"30076221",
"33846594"
] | [
"Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution.",
"The evolutionary development of the protein complement of photosystem 2.",
"The low molecular mass subunits of the photosynthetic supracomplex, photosystem II.",
"PsbT polypeptide is required for eff... | [
2003,
2004,
2004,
2001,
2018,
2021
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
315,
15406
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
3,
2
] | 3 | true | Family | Photosystem II PsbT | Photosystem II PsbT | PSII_PsbT | 5 |
IPR001747 | 1,747 | Vitellogenin, N-terminal | Vitellogenin_N | Domain | 12,148 | false | false | This entry represents a conserved region found in several lipid transport proteins, including vitellogenin, microsomal triglyceride transfer protein and apolipoprotein B-100 [ ]. Vitellinogen precursors provide the major egg yolk proteins that are a source of nutrients during early development of oviparous vertebrates ... | [
"GO:0005319",
"GO:0006869"
] | [
"lipid transporter activity",
"lipid transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01347",
"PS51211",
"SM00638"
] | [
"Vitellogenin_N",
"VITELLOGENIN",
"LPD_N"
] | [
12031,
10613,
9699
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51211",
"R-DME-8964041",
"R-DRE-8964041",
"R-HSA-202733",
"R-HSA-3000471",
"R-HSA-3000480",
"R-HSA-3000484",
"R-HSA-3000497",
"R-HSA-381426",
"R-HSA-432142",
"R-HSA-5686938",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-8866423",
"R-HSA-8957275",
"R-HSA-8963888",
"R-HSA-8963901",
... | [
"PROSITEDOC:PDOC51211",
"REACTOME:R-DME-8964041",
"REACTOME:R-DRE-8964041",
"REACTOME:R-HSA-202733",
"REACTOME:R-HSA-3000471",
"REACTOME:R-HSA-3000480",
"REACTOME:R-HSA-3000484",
"REACTOME:R-HSA-3000497",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-432142",
"REACTOME:R-HSA-5686938",
"REACTOME:R-H... | 64 | [
"1lsh",
"6i7s",
"8eoj",
"9bd1",
"9bd8",
"9bde",
"9bdt",
"9coo",
"9e9r",
"9ea7",
"9eag",
"9enr",
"9ens"
] | 13 | [
"PUB00005307",
"PUB00007158",
"PUB00035546",
"PUB00035550",
"PUB00035551"
] | [
"9687371",
"12135361",
"17314313",
"17403933",
"16238675"
] | [
"The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein.",
"Lipid-protein interactions in lipovitellin.",
"Vertebrate yolk complexes and the functional implications of phosvitins and other subdomains in vitellogenins.",
"A distal effect of microsomal triglyceride transfer protein de... | [
1998,
2002,
2007,
2007,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
79,
12069
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
28,
7,
14,
5,
5
] | 6 | true | Domain | Vitellogenin, N-terminal | Vitellogenin, N-terminal | Vitellogenin_N | 6 |
IPR001748 | 1,748 | Pre-mRNA-splicing factor BUD31 | BUD31 | Family | 4,828 | false | false | This family includes the pre-mRNA-splicing factor BUD31, also known as G10 protein, and its homologues. BUD31 is involved in the pre-mRNA splicing process [ , , ] and it is highly conserved in a wide range of eukaryotic species. Human BUD31 may play a role as regulator of androgen receptor (AR) transcriptional activity... | [
"GO:0005634"
] | [
"nucleus"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF01125",
"PR00322",
"PTHR19411"
] | [
"BUD31",
"G10",
""
] | [
4825,
4635,
4717
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00765",
"R-BTA-72163",
"R-CEL-72163",
"R-DRE-72163",
"R-HSA-72163",
"R-MMU-72163",
"R-RNO-72163",
"R-SPO-72163"
] | [
"PROSITEDOC:PDOC00765",
"REACTOME:R-BTA-72163",
"REACTOME:R-CEL-72163",
"REACTOME:R-DRE-72163",
"REACTOME:R-HSA-72163",
"REACTOME:R-MMU-72163",
"REACTOME:R-RNO-72163",
"REACTOME:R-SPO-72163"
] | 8 | [
"2my1",
"3jb9",
"5gm6",
"5gmk",
"5lj3",
"5lj5",
"5lqw",
"5mps",
"5mq0",
"5mqf",
"5wsg",
"5xjc",
"5y88",
"5ylz",
"5yzg",
"5z56",
"5z57",
"6bk8",
"6exn",
"6ff4",
"6ff7",
"6icz",
"6id0",
"6id1",
"6j6g",
"6j6h",
"6j6n",
"6j6q",
"6qdv",
"6zym",
"7aav",
"7abf"... | 62 | [
"PUB00001892",
"PUB00092514",
"PUB00097019",
"PUB00101588"
] | [
"2568313",
"28502770",
"28076346",
"25091737"
] | [
"Poly(A) elongation during Xenopus oocyte maturation is required for translational recruitment and is mediated by a short sequence element.",
"An Atomic Structure of the Human Spliceosome.",
"Cryo-EM structure of a human spliceosome activated for step 2 of splicing.",
"Identification of a new androgen recepto... | [
1989,
2017,
2017,
2014
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4828
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
2,
1,
2,
1,
3,
1,
1,
5,
2,
1,
1,
14
] | 12 | true | Family | Pre-mRNA-splicing factor BUD31 | Pre-mRNA-splicing factor BUD31 | BUD31 | 1 |
IPR001749 | 1,749 | GPCR, family 2, gastric inhibitory polypeptide receptor | GPCR_2_GIP_rcpt | Family | 930 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0016519",
"GO:0007186",
"GO:0016020"
] | [
"gastric inhibitory peptide receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01129"
] | [
"GIPRECEPTOR"
] | [
930
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"248",
"R-HSA-418555",
"R-HSA-420092",
"R-MMU-418555",
"R-MMU-420092",
"R-RNO-420092"
] | [
"IUPHAR:248",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-420092",
"REACTOME:R-MMU-418555",
"REACTOME:R-MMU-420092",
"REACTOME:R-RNO-420092"
] | 6 | [
"2qkh",
"4hj0",
"6dkj",
"6o9h",
"6o9i",
"7dty",
"7fin",
"7fiy",
"7ra3",
"7rbt",
"7vab",
"8itl",
"8itm",
"8wa3",
"8yw4"
] | 15 | [
"PUB00001208",
"PUB00001693",
"PUB00004310",
"PUB00004961",
"PUB00005147",
"PUB00005148",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"1646711",
"7589426",
"1314625",
"8170923",
"1658940",
"1658941",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"Molecular cloning and expression of a cDNA encoding the secretin receptor.",
"Molecular cloning, functional expression, and signal transduction of the GIP-receptor cloned from a human insulinoma.",
"Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.",
"Fi... | [
1991,
1995,
1992,
1994,
1991,
1991,
2003,
1994,
2005,
2009,
2006,
2013
] | 12 | [
"IPR000832"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
930
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
4,
1,
3
] | 4 | true | Family | GPCR, family 2, gastric inhibitory polypeptide receptor | GPCR, family 2, gastric inhibitory polypeptide receptor | GPCR_2_GIP_rcpt | 2 |
IPR001750 | 1,750 | NADH:quinone oxidoreductase/Mrp antiporter, transmembrane domain | ND/Mrp_TM | Domain | 380,562 | false | false | This entry represents the transmembrane segments of subunits NuoL/ND5, NuoM/ND4, and NuoN/ND2 of the NADH:quinone oxidoreductase (complex I), Mrp antiporters subunits A and D, and in membrane subunits of hydrogenase complexes, such as hydrogenase-4 and F420H2 dehydrogenase. Mrp-type antiporters comprise the cation/prot... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00361"
] | [
"Proton_antipo_M"
] | [
380562
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"7.1.1",
"R-BTA-5419276",
"R-BTA-611105",
"R-BTA-6799198",
"R-CEL-5419276",
"R-DME-5419276",
"R-DME-611105",
"R-DME-6799198",
"R-DRE-611105",
"R-GGA-5419276",
"R-GGA-611105",
"R-GGA-6799198",
"R-HSA-5419276",
"R-HSA-611105",
"R-HSA-6799198",
"R-HSA-9837999",
"R-MMU-5419276",
"R-MMU... | [
"EC:7.1.1",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-CEL-5419276",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-6799198",
"REACTOME:R-DRE-611105",
"REACTOME:R-GGA-5419276",
"REACTOME:R-GGA-611105",
"REACTOME:R-GGA-6799198",
... | 25 | [
"3rko",
"4he8",
"4hea",
"4wz7",
"5gpn",
"5gup",
"5lc5",
"5ldw",
"5ldx",
"5lnk",
"5o31",
"5xtc",
"5xtd",
"5xth",
"5xti",
"6cfw",
"6g2j",
"6g72",
"6gcs",
"6h8k",
"6hum",
"6i0d",
"6i1p",
"6khi",
"6khj",
"6l7o",
"6l7p",
"6nbq",
"6nbx",
"6nby",
"6q8o",
"6q8w"... | 324 | [
"PUB00009994",
"PUB00072925",
"PUB00072926",
"PUB00072927",
"PUB00072928",
"PUB00072929",
"PUB00072930",
"PUB00072931",
"PUB00072932"
] | [
"10751389",
"24142251",
"15980940",
"18408029",
"12914915",
"20826797",
"12460669",
"20595580",
"9387241"
] | [
"The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases.",
"Purification and functional reconstitution of a seven-subunit mrp-type na+/h+ antiporter.",
"The Mrp system: a giant among monovalent cation/proton antiporters?",
"Single gene deletions... | [
2000,
2014,
2005,
2008,
2003,
2010,
2002,
2010,
1997
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4577,
98861,
274472,
2652
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
52,
8,
4,
68,
7,
3387,
50,
5,
25,
30,
18
] | 11 | true | Domain | NADH:quinone oxidoreductase/Mrp antiporter, transmembrane domain | NADH:quinone oxidoreductase/Mrp antiporter, transmembrane domain | ND/Mrp_TM | 8 |
IPR001751 | 1,751 | S100/Calcium binding protein 7/8-like, conserved site | S100/CaBP7/8-like_CS | Conserved_site | 11,814 | false | false | The calcium-binding domain found in S100, CaBP7/8 and similar proteins mainly from animals. It is a subfamily of the EF-hand calcium-binding domain [ ]. S100s are small dimeric acidic calcium and zinc-binding proteins abundant in the brain, with S100B playing an important role in modulating the proliferation and differ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00303"
] | [
"S100_CABP"
] | [
11814
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00275",
"R-BTA-445989",
"R-BTA-5668599",
"R-BTA-5686938",
"R-BTA-6798695",
"R-BTA-6799990",
"R-BTA-75205",
"R-BTA-879415",
"R-BTA-933542",
"R-GGA-5668599",
"R-GGA-5686938",
"R-GGA-6798695",
"R-GGA-6799990",
"R-GGA-75205",
"R-HSA-1236974",
"R-HSA-1251985",
"R-HSA-166058",
"R-HS... | [
"PROSITEDOC:PDOC00275",
"REACTOME:R-BTA-445989",
"REACTOME:R-BTA-5668599",
"REACTOME:R-BTA-5686938",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6799990",
"REACTOME:R-BTA-75205",
"REACTOME:R-BTA-879415",
"REACTOME:R-BTA-933542",
"REACTOME:R-GGA-5668599",
"REACTOME:R-GGA-5686938",
"REACTOME:R-GGA... | 50 | [
"1a03",
"1a4p",
"1b1g",
"1b4c",
"1boc",
"1bod",
"1bt6",
"1cb1",
"1cdn",
"1cfp",
"1clb",
"1cnp",
"1d1o",
"1dt7",
"1e8a",
"1gqm",
"1ht9",
"1ig5",
"1igv",
"1irj",
"1j55",
"1jwd",
"1k2h",
"1k8u",
"1k96",
"1k9k",
"1k9p",
"1kcy",
"1kqv",
"1ksm",
"1kso",
"1m31"... | 179 | [
"PUB00027678",
"PUB00027679",
"PUB00027680",
"PUB00027681",
"PUB00099873"
] | [
"15284904",
"15006498",
"16288660",
"12520541",
"19458041"
] | [
"S100 proteins and their influence on pro-survival pathways in cancer.",
"S100B in schizophrenic psychosis.",
"Biology and physiology of Calbindin-D9k in female reproductive tissues: involvement of steroids and endocrine disruptors.",
"Mechanisms of intestinal calcium absorption.",
"Calneurons provide a cal... | [
2004,
2004,
2005,
2003,
2009
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nitrosocaldus cavascurensis",
"Eukaryota",
"bird metagenome"
] | [
25,
1,
11785,
3
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
3,
33,
44,
44,
47,
5
] | 6 | true | Conserved_site | S100/Calcium binding protein 7/8-like, conserved site | S100/Calcium binding protein 7/8-like, conserved site | S100/CaBP7/8-like_CS | 4 |
IPR001752 | 1,752 | Kinesin motor domain | Kinesin_motor_dom | Domain | 165,444 | false | false | null | [
"GO:0003777",
"GO:0005524",
"GO:0008017",
"GO:0007018"
] | [
"microtubule motor activity",
"ATP binding",
"microtubule binding",
"microtubule-based movement"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00225",
"PR00380",
"PS50067",
"SM00129"
] | [
"Kinesin",
"KINESINHEAVY",
"KINESIN_MOTOR_2",
"KISc"
] | [
161211,
146050,
163968,
156133
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00343",
"R-BTA-2132295",
"R-BTA-6811434",
"R-BTA-68884",
"R-BTA-983189",
"R-CEL-5620924",
"R-CEL-6811434",
"R-CEL-983189",
"R-DDI-5610787",
"R-DDI-983189",
"R-DME-209159",
"R-DME-209190",
"R-DME-209214",
"R-DME-209338",
"R-DME-209360",
"R-DME-216119",
"R-DME-216217",
"R-DME-56... | [
"PROSITEDOC:PDOC00343",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-6811434",
"REACTOME:R-BTA-68884",
"REACTOME:R-BTA-983189",
"REACTOME:R-CEL-5620924",
"REACTOME:R-CEL-6811434",
"REACTOME:R-CEL-983189",
"REACTOME:R-DDI-5610787",
"REACTOME:R-DDI-983189",
"REACTOME:R-DME-209159",
"REACTOME:R-DME-... | 87 | [
"1bg2",
"1cz7",
"1f9t",
"1f9u",
"1f9v",
"1f9w",
"1goj",
"1i5s",
"1i6i",
"1ia0",
"1ii6",
"1mkj",
"1n6m",
"1q0b",
"1ry6",
"1sdm",
"1t5c",
"1v8j",
"1v8k",
"1vfv",
"1vfw",
"1vfx",
"1vfz",
"1x88",
"1yrs",
"2fky",
"2fl2",
"2fl6",
"2fme",
"2g1q",
"2gm1",
"2gry"... | 284 | [
"PUB00000075",
"PUB00004968",
"PUB00005370",
"PUB00005510",
"PUB00031339",
"PUB00072953"
] | [
"2142876",
"8542443",
"1832505",
"14732151",
"15236970",
"20587735"
] | [
"Motor proteins of cytoplasmic microtubules.",
"Motor proteins 1: kinesins.",
"The emerging kinesin family of microtubule motor proteins.",
"A kinesin medley: biochemical and functional heterogeneity.",
"Crystal structure of the motor domain of the human kinetochore protein CENP-E.",
"A novel kinesin 13 p... | [
1990,
1995,
1991,
1995,
2004,
2010
] | 6 | [] | [
"IPR047241"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Halomarina salina",
"Viruses",
"metagenomes"
] | [
11,
165387,
1,
11,
34
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
344,
38,
340,
119,
254,
178,
13,
79,
205,
6,
9,
840
] | 12 | true | Domain | Kinesin motor domain | Kinesin motor domain | Kinesin_motor_dom | 6 |
IPR001753 | 1,753 | Enoyl-CoA hydratase/isomerase-like domain | Enoyl-CoA_hydra/iso | Domain | 251,922 | false | false | This entry contains a diverse set of enzymes from cellular organisms, including: fatty acid oxidation complex subunit alpha, enoyl-CoA hydratase, 1,4-dihydroxy-2-naphthoyl-CoA synthase (napthoate synthase), carnitinyl-CoA dehydratase (carnitine racemase), 3-hydroxybutyryl-CoA dehydratase and enoyl-CoA delta isomerase (... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00378"
] | [
"ECH_1"
] | [
251922
] | 1 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PRO... | [
"4.2.1",
"4.2.1.17",
"GenProp1308",
"GenProp1486",
"GenProp1488",
"GenProp1510",
"GenProp1533",
"GenProp1560",
"GenProp1562",
"GenProp1572",
"GenProp1673",
"GenProp1717",
"GenProp1723",
"PWY-1361",
"PWY-5136",
"PWY-5138",
"PWY-6443",
"PWY-6446",
"PWY-6458",
"PWY-7007",
"PWY-7... | [
"EC:4.2.1",
"EC:4.2.1.17",
"GP:GenProp1308",
"GP:GenProp1486",
"GP:GenProp1488",
"GP:GenProp1510",
"GP:GenProp1533",
"GP:GenProp1560",
"GP:GenProp1562",
"GP:GenProp1572",
"GP:GenProp1673",
"GP:GenProp1717",
"GP:GenProp1723",
"METACYC:PWY-1361",
"METACYC:PWY-5136",
"METACYC:PWY-5138",
... | 97 | [
"1dci",
"1dub",
"1ef8",
"1ef9",
"1ey3",
"1hno",
"1hnu",
"1hzd",
"1jxz",
"1k39",
"1mj3",
"1nzy",
"1o8u",
"1pjh",
"1q51",
"1q52",
"1rjm",
"1rjn",
"1sg4",
"1szo",
"1uiy",
"1wdk",
"1wdl",
"1wdm",
"1wz8",
"1xx4",
"2a7k",
"2a81",
"2d3t",
"2dub",
"2ej5",
"2f6q"... | 311 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
3415,
194984,
49253,
3,
4267
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
37,
16,
30,
19,
7,
63,
44,
6,
40,
67,
2,
78
] | 12 | true | Domain | Enoyl-CoA hydratase/isomerase-like domain | Enoyl-CoA hydratase/isomerase-like domain | Enoyl-CoA_hydra/iso | 6 |
IPR001754 | 1,754 | Orotidine 5'-phosphate decarboxylase domain | OMPdeCOase_dom | Domain | 38,654 | false | false | Orotidine 5'-phosphate decarboxylase (OMPdecase) [ , ] catalyses the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofu... | [
"GO:0004590",
"GO:0006207"
] | [
"orotidine-5'-phosphate decarboxylase activity",
"'de novo' pyrimidine nucleobase biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF00215",
"SM00934"
] | [
"OMPdecase",
"OMPdecase"
] | [
38637,
37790
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1.23",
"PWY-5686",
"PWY-7790",
"PWY-7791",
"PDOC00141",
"R-CEL-500753",
"R-DDI-500753",
"R-DME-500753",
"R-HSA-500753",
"R-MMU-500753"
] | [
"EC:4.1.1.23",
"METACYC:PWY-5686",
"METACYC:PWY-7790",
"METACYC:PWY-7791",
"PROSITEDOC:PDOC00141",
"REACTOME:R-CEL-500753",
"REACTOME:R-DDI-500753",
"REACTOME:R-DME-500753",
"REACTOME:R-HSA-500753",
"REACTOME:R-MMU-500753"
] | 10 | [
"1dbt",
"1dqw",
"1dqx",
"1dv7",
"1dvj",
"1eix",
"1jjk",
"1kly",
"1klz",
"1km0",
"1km1",
"1km2",
"1km3",
"1km4",
"1km5",
"1km6",
"1kv8",
"1kw1",
"1l2u",
"1lol",
"1loq",
"1lor",
"1los",
"1lp6",
"1q6l",
"1q6o",
"1q6q",
"1q6r",
"1so3",
"1so4",
"1so5",
"1so6"... | 271 | [
"PUB00002768",
"PUB00003724"
] | [
"1730672",
"2835631"
] | [
"The orotidine-5'-monophosphate decarboxylase gene of Myxococcus xanthus. Comparison to the OMP decarboxylase gene family.",
"Sequence analysis of the DdPYR5-6 gene coding for UMP synthase in Dictyostelium discoideum and comparison with orotate phosphoribosyl transferases and OMP decarboxylases."
] | [
1992,
1988
] | 2 | [] | [
"IPR017553",
"IPR041710"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
1520,
31098,
5238,
6,
792
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
4,
1,
1,
1,
3,
8,
3,
1,
5,
5,
1,
1,
15
] | 13 | true | Domain | Orotidine 5'-phosphate decarboxylase domain | Orotidine 5'-phosphate decarboxylase domain | OMPdeCOase_dom | 8 |
IPR001757 | 1,757 | P-type ATPase | P_typ_ATPase | Family | 298,549 | false | false | This entry represents the P-type ATPases. These P-ATPases are found in both prokaryotes and eukaryotes. P-ATPases (also known as E1-E2 ATPases) ( ) are found in bacteria and in a number of eukaryotic plasma membranes and organelles [ ]. P-ATPases function to transport a variety of different compounds, including ions an... | [
"GO:0005215",
"GO:0005524",
"GO:0016887",
"GO:0016020"
] | [
"transporter activity",
"ATP binding",
"ATP hydrolysis activity",
"membrane"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"cellular_component"
] | 4 | [
"PRINTS",
"NCBIFAM"
] | [
"PR00120",
"TIGR01494"
] | [
"HATPASE",
"ATPase_P-type"
] | [
81076,
297688
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"7.2.2",
"PDOC00139",
"R-BTA-418359",
"R-BTA-5578775",
"R-BTA-936837",
"R-CEL-418359",
"R-CEL-5578775",
"R-CEL-6798695",
"R-CEL-936837",
"R-CFA-418359",
"R-CFA-5578775",
"R-CFA-936837",
"R-DDI-418359",
"R-DDI-5578775",
"R-DDI-936837",
"R-DME-418359",
"R-DME-5578775",
"R-DME-936837"... | [
"EC:7.2.2",
"PROSITEDOC:PDOC00139",
"REACTOME:R-BTA-418359",
"REACTOME:R-BTA-5578775",
"REACTOME:R-BTA-936837",
"REACTOME:R-CEL-418359",
"REACTOME:R-CEL-5578775",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-936837",
"REACTOME:R-CFA-418359",
"REACTOME:R-CFA-5578775",
"REACTOME:R-CFA-936837",
"R... | 54 | [
"1iwo",
"1kju",
"1mhs",
"1su4",
"1t5s",
"1t5t",
"1vfp",
"1wpg",
"1xp5",
"2agv",
"2b8e",
"2by4",
"2c88",
"2c8k",
"2c8l",
"2c9m",
"2dqs",
"2ear",
"2eat",
"2eau",
"2hc8",
"2iye",
"2o9j",
"2oa0",
"2voy",
"2xzb",
"2yfy",
"2yj3",
"2yj4",
"2yj5",
"2yj6",
"2yn9"... | 421 | [
"PUB00009616",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789",
"PUB00160065",
"PUB00160066"
] | [
"9419228",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106",
"37264943",
"37838176"
] | [
"Evolution of substrate specificities in the P-type ATPase superfamily.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases... | [
1998,
2004,
2004,
2010,
2008,
1992,
1998,
2023,
2023
] | 9 | [] | [
"IPR005775",
"IPR005782",
"IPR006391",
"IPR006408",
"IPR006413",
"IPR006414",
"IPR006415",
"IPR006534",
"IPR006539",
"IPR006544",
"IPR027256"
] | 0 | 11 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4216,
133838,
158596,
12,
1887
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
237,
47,
196,
77,
4,
172,
145,
17,
145,
203,
16,
14,
559
] | 13 | true | Family | P-type ATPase | P-type ATPase | P_typ_ATPase | 7 |
IPR001758 | 1,758 | Prostanoid EP4 receptor | Prost_EP4_rcpt | Family | 2,108 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0004957",
"GO:0007186",
"GO:0016020"
] | [
"prostaglandin E receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00586"
] | [
"PRSTNOIDEP4R"
] | [
2108
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"343",
"R-HSA-391908",
"R-HSA-418555",
"R-MMU-391908",
"R-MMU-418555",
"R-RNO-391908"
] | [
"IUPHAR:343",
"REACTOME:R-HSA-391908",
"REACTOME:R-HSA-418555",
"REACTOME:R-MMU-391908",
"REACTOME:R-MMU-418555",
"REACTOME:R-RNO-391908"
] | 6 | [
"5yhl",
"5ywy",
"7d7m",
"8gcm",
"8gcp",
"8gd9",
"8gda",
"8gdb",
"9jqy",
"9jqz"
] | 10 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR001244"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
2108
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
2,
4,
6
] | 4 | true | Family | Prostanoid EP4 receptor | Prostanoid EP4 receptor | Prost_EP4_rcpt | 5 |
IPR001759 | 1,759 | Pentraxin domain | PTX_dom | Domain | 16,472 | false | false | This entry represents the pentraxin (PTX) domain, the C-terminal ~200 aa-long conserved domain of pentraxins (earlier also termed pentaxins). This domain contains an 8 aa-long conserved sequence (HxCxS/TWxS, in which x is any amino acid) [ , , ]. This domain covers the whole length of the protein in CRP (C-reactive pro... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00354",
"PR00895",
"PS51828",
"SM00159",
"cd00152"
] | [
"Pentaxin",
"PENTAXIN",
"PTX_2",
"PTX",
"PTX"
] | [
14587,
11481,
15603,
14799,
4312
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00261",
"R-DRE-9619665",
"R-HSA-173623",
"R-HSA-6798695",
"R-HSA-9619665",
"R-HSA-977225",
"R-MMU-173623",
"R-MMU-6798695",
"R-MMU-9619665",
"R-RNO-173623"
] | [
"PROSITEDOC:PDOC00261",
"REACTOME:R-DRE-9619665",
"REACTOME:R-HSA-173623",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9619665",
"REACTOME:R-HSA-977225",
"REACTOME:R-MMU-173623",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-9619665",
"REACTOME:R-RNO-173623"
] | 10 | [
"1b09",
"1gnh",
"1gyk",
"1lgn",
"1lj7",
"1sac",
"2a3w",
"2a3x",
"2a3y",
"2w08",
"3d5o",
"3flp",
"3flr",
"3flt",
"3kqr",
"3l2y",
"3pvn",
"3pvo",
"4avs",
"4avt",
"4avv",
"4ayu",
"4pbo",
"4pbp",
"6v55",
"6ype",
"7pk9",
"7pkb",
"7pkd",
"7pke",
"7pkf",
"7pkg"... | 49 | [
"PUB00000009",
"PUB00000262",
"PUB00000990",
"PUB00001068",
"PUB00001976",
"PUB00002885",
"PUB00003384",
"PUB00004168",
"PUB00005092",
"PUB00005239",
"PUB00081665",
"PUB00081666",
"PUB00093427",
"PUB00109114"
] | [
"6356809",
"9514915",
"9614930",
"7772283",
"8884281",
"7798266",
"9480764",
"8114934",
"9583999",
"7881902",
"8899296",
"10748068",
"31019517",
"20357257"
] | [
"Acute phase proteins with special reference to C-reactive protein and related proteins (pentaxins) and serum amyloid A protein.",
"Serum amyloid P component associates with high density lipoprotein as well as very low density lipoprotein but not with low density lipoprotein.",
"Inflammatory potential of C-reac... | [
1983,
1998,
1998,
1995,
1996,
1994,
1998,
1994,
1997,
1994,
1996,
2000,
2019,
2010
] | 14 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2,
221,
16233,
16
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
119,
3,
28,
37,
59
] | 5 | true | Domain | Pentraxin domain | Pentraxin domain | PTX_dom | 4 |
IPR001760 | 1,760 | Opsin | Opsin | Family | 23,804 | false | false | Visual pigments [ , ] are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to the chromophore cis-retinal. Vision is effected through the absorption of a photon by cis-retinal which is isomerised to trans-retinal. This isomerisation leads to a change of conforma... | [
"GO:0007186",
"GO:0007601",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"visual perception",
"membrane"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS",
"PRINTS"
] | [
"PR00238",
"PR00577"
] | [
"OPSIN",
"OPSINRH3RH4"
] | [
22287,
2013
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00211",
"R-BTA-2187335",
"R-BTA-2453902",
"R-BTA-2485179",
"R-BTA-2514859",
"R-BTA-418594",
"R-BTA-419771",
"R-BTA-5620916",
"R-CFA-2187335",
"R-CFA-418594",
"R-CFA-419771",
"R-DME-416476",
"R-DME-419771",
"R-DRE-2187335",
"R-DRE-2453902",
"R-DRE-2485179",
"R-DRE-2514859",
"R-... | [
"PROSITEDOC:PDOC00211",
"REACTOME:R-BTA-2187335",
"REACTOME:R-BTA-2453902",
"REACTOME:R-BTA-2485179",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-419771",
"REACTOME:R-BTA-5620916",
"REACTOME:R-CFA-2187335",
"REACTOME:R-CFA-418594",
"REACTOME:R-CFA-419771",
"REACTOME:R-DM... | 54 | [
"1f88",
"1gzm",
"1hzx",
"1jfp",
"1l9h",
"1ln6",
"1u19",
"2g87",
"2hpy",
"2i35",
"2i36",
"2i37",
"2j4y",
"2ped",
"2x72",
"2z73",
"2ziy",
"3aym",
"3ayn",
"3c9l",
"3c9m",
"3cap",
"3dqb",
"3oax",
"3pqr",
"3pxo",
"4a4m",
"4bey",
"4bez",
"4j4q",
"4pxf",
"4ww3"... | 78 | [
"PUB00000394",
"PUB00001159",
"PUB00003416",
"PUB00003460",
"PUB00003461",
"PUB00005641"
] | [
"7947717",
"2953598",
"1663559",
"2437266",
"2952772",
"3303660"
] | [
"A human opsin-related gene that encodes a retinaldehyde-binding protein.",
"An opsin gene that is expressed only in the R7 photoreceptor cell of Drosophila.",
"The evolution of rhodopsins and neurotransmitter receptors.",
"A rhodopsin gene expressed in photoreceptor cell R7 of the Drosophila eye: homologies ... | [
1994,
1987,
1991,
1987,
1987,
1986
] | 6 | [
"IPR000276"
] | [
"IPR000378",
"IPR000732",
"IPR001391",
"IPR001521",
"IPR001735",
"IPR002206"
] | 1 | 6 | 0 | [
"Opisthokonta"
] | [
23804
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
46,
13,
16,
9,
14
] | 5 | true | Family | Opsin | Opsin | Opsin | 8 |
IPR001761 | 1,761 | Periplasmic binding protein/LacI sugar binding domain | Peripla_BP/Lac1_sug-bd_dom | Domain | 38,488 | false | false | This entry represents periplasmic binding proteins, and the LacI family of transcriptional regulators sugar binding domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00532"
] | [
"Peripla_BP_1"
] | [
38488
] | 1 | [
"GP"
] | [
"GenProp0457"
] | [
"GP:GenProp0457"
] | 1 | [
"1abe",
"1abf",
"1apb",
"1bap",
"2iks",
"2o20",
"2wrz",
"3egc",
"3gv0",
"3hcw",
"3kjx",
"3o1h",
"3o1i",
"3o1j",
"3o74",
"3o75",
"3qk7",
"4kzk",
"4rk1",
"5abp",
"6abp",
"6ndi",
"7abp",
"7doa",
"7dob",
"7x7h",
"8abp",
"8jff",
"8jfv",
"9abp"
] | 30 | [
"PUB00003288",
"PUB00005216"
] | [
"1583688",
"8638105"
] | [
"1.7 A X-ray structure of the periplasmic ribose receptor from Escherichia coli.",
"Crystal structure of the lactose operon repressor and its complexes with DNA and inducer."
] | [
1992,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcina mazei",
"unclassified sequences"
] | [
38255,
36,
1,
196
] | 4 | [
"Escherichia coli (strain K12)"
] | [
7
] | 1 | true | Domain | Periplasmic binding protein/LacI sugar binding domain | Periplasmic binding protein/LacI sugar binding domain | Peripla_BP/Lac1_sug-bd_dom | 3 |
IPR001762 | 1,762 | Disintegrin domain | Disintegrin_dom | Domain | 33,533 | false | false | Disintegrins are a family of small proteins from viper venoms that function as potent inhibitors of both platelet aggregation and integrin-dependent cell adhesion [ , ]. Integrin receptors are involved in cell-cell and cell-extracellular matrix interactions, serving as the final common pathway leading to aggregation vi... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00200",
"PR00289",
"PS50214",
"SM00050"
] | [
"Disintegrin",
"DISINTEGRIN",
"DISINTEGRIN_2",
"DISIN"
] | [
31283,
14877,
33190,
33202
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00351",
"R-BTA-1474228",
"R-BTA-381426",
"R-BTA-6798695",
"R-BTA-8957275",
"R-CEL-1474228",
"R-CEL-381426",
"R-CEL-6798695",
"R-CEL-8957275",
"R-HSA-1251985",
"R-HSA-1442490",
"R-HSA-1474228",
"R-HSA-177929",
"R-HSA-193692",
"R-HSA-2122948",
"R-HSA-2534343",
"R-HSA-2644606",
"... | [
"PROSITEDOC:PDOC00351",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8957275",
"REACTOME:R-CEL-1474228",
"REACTOME:R-CEL-381426",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-8957275",
"REACTOME:R-HSA-1251985",
"REACTOME:R-HSA-1442490",
"REACTOME:R-... | 60 | [
"1fvl",
"1j2l",
"1l3x",
"1mpz",
"1n4y",
"1q7i",
"1q7j",
"1rmr",
"1ro3",
"1tej",
"1z1x",
"2ao7",
"2dw0",
"2dw1",
"2dw2",
"2e3x",
"2ech",
"2ero",
"2erp",
"2erq",
"2ljv",
"2m75",
"2m7f",
"2m7h",
"2mop",
"2mp5",
"2pjf",
"2pjg",
"2pji",
"3c05",
"3dsl",
"3g5c"... | 66 | [
"PUB00000515",
"PUB00004116",
"PUB00026241",
"PUB00026913",
"PUB00027415",
"PUB00030741",
"PUB00035680",
"PUB00035681",
"PUB00035682",
"PUB00035683",
"PUB00035684",
"PUB00035685"
] | [
"1417724",
"1552944",
"14499613",
"14661951",
"12742023",
"15535803",
"15578957",
"15974889",
"12050803",
"16918409",
"16101289",
"15962120"
] | [
"A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic peptides.",
"A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion.",
"Crystal structure of trimestatin, a disintegrin containing a cell adhesion recognition motif RGD.",
... | [
1992,
1992,
2003,
2003,
2003,
2005,
2004,
2005,
2001,
2006,
2005,
2005
] | 12 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Fermentimicrarchaeum limneticum",
"groundwater metagenome"
] | [
117,
33414,
1,
1
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
4,
87,
23,
84,
102,
1,
120,
1
] | 8 | true | Domain | Disintegrin domain | Disintegrin domain | Disintegrin_dom | 4 |
IPR001763 | 1,763 | Rhodanese-like domain | Rhodanese-like_dom | Domain | 248,463 | false | false | null | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00581",
"PS50206",
"SM00450"
] | [
"Rhodanese",
"RHODANESE_3",
"RHOD"
] | [
208926,
247433,
198218
] | 3 | [
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"GenProp1281",
"GenProp1313",
"GenProp1461",
"GenProp1681",
"GenProp1711",
"PDOC00322",
"R-BTA-112409",
"R-BTA-156711",
"R-BTA-202670",
"R-BTA-2565942",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-5620912",
"R-BTA-5625740",
"R-BTA-5675221",
"R-BTA-5689880... | [
"GP:GenProp1281",
"GP:GenProp1313",
"GP:GenProp1461",
"GP:GenProp1681",
"GP:GenProp1711",
"PROSITEDOC:PDOC00322",
"REACTOME:R-BTA-112409",
"REACTOME:R-BTA-156711",
"REACTOME:R-BTA-202670",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-380259",
"REACTOME:R-BTA-380270",
"REACTOME:R-BTA-380284",
... | 188 | [
"1boh",
"1boi",
"1c25",
"1cwr",
"1cws",
"1cwt",
"1dp2",
"1e0c",
"1gmx",
"1gn0",
"1h4k",
"1h4m",
"1hzm",
"1okg",
"1orb",
"1qb0",
"1qxn",
"1rhd",
"1rhs",
"1t3k",
"1tq1",
"1uar",
"1ub0",
"1uim",
"1uin",
"1urh",
"1v7c",
"1vrq",
"1whb",
"1wv9",
"1x31",
"1ym9"... | 170 | [
"PUB00002964",
"PUB00006580"
] | [
"8702871",
"9733650"
] | [
"Active site structural features for chemically modified forms of rhodanese.",
"A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain."
] | [
1996,
1998
] | 2 | [] | [
"IPR026340"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4200,
173907,
67097,
58,
3201
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
113,
24,
43,
18,
9,
88,
64,
14,
85,
99,
10,
8,
151
] | 13 | true | Domain | Rhodanese-like domain | Rhodanese-like domain | Rhodanese-like_dom | 4 |
IPR001764 | 1,764 | Glycoside hydrolase, family 3, N-terminal | Glyco_hydro_3_N | Domain | 106,754 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF00933",
"PR00133"
] | [
"Glyco_hydro_3",
"GLHYDRLASE3"
] | [
106533,
75856
] | 2 | [
"CAZY",
"EC",
"GP",
"PROSITEDOC"
] | [
"GH3",
"3.2.1",
"GenProp1623",
"PDOC00621"
] | [
"CAZY:GH3",
"EC:3.2.1",
"GP:GenProp1623",
"PROSITEDOC:PDOC00621"
] | 4 | [
"1ex1",
"1ieq",
"1iev",
"1iew",
"1iex",
"1j8v",
"1lq2",
"1tr9",
"1x38",
"1x39",
"1y65",
"2oxn",
"2x40",
"2x41",
"2x42",
"3abz",
"3ac0",
"3bmx",
"3gs6",
"3gsm",
"3lk6",
"3nvd",
"3rrx",
"3sql",
"3sqm",
"3tev",
"3u48",
"3u4a",
"3usz",
"3ut0",
"3wlh",
"3wli"... | 200 | [
"PUB00004870",
"PUB00005266",
"PUB00005846"
] | [
"7624375",
"8535779",
"10368285"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase."
] | [
1995,
1995,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
543,
70541,
34932,
2,
736
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
84,
2,
10,
55,
1,
98
] | 6 | true | Domain | Glycoside hydrolase, family 3, N-terminal | Glycoside hydrolase, family 3, N-terminal | Glyco_hydro_3_N | 8 |
IPR001765 | 1,765 | Carbonic anhydrase | Carbonic_anhydrase | Family | 46,630 | false | false | Carbonic anhydrases ( ) (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of ce... | [
"GO:0004089",
"GO:0008270"
] | [
"carbonate dehydratase activity",
"zinc ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PANTHER",
"PANTHER",
"SMART"
] | [
"PF00484",
"PTHR11002",
"PTHR43175",
"SM00947"
] | [
"Pro_CA",
"",
"",
"Pro_CA"
] | [
45735,
34031,
9594,
45725
] | 4 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.2.1.1",
"GenProp1072",
"GenProp1669",
"PWY-241",
"PWY-5743",
"PWY-5744",
"PWY-5789",
"PWY-6142",
"PWY-7115",
"PWY-7117"
] | [
"EC:4.2.1.1",
"GP:GenProp1072",
"GP:GenProp1669",
"METACYC:PWY-241",
"METACYC:PWY-5743",
"METACYC:PWY-5744",
"METACYC:PWY-5789",
"METACYC:PWY-6142",
"METACYC:PWY-7115",
"METACYC:PWY-7117"
] | 10 | [
"1ddz",
"1ekj",
"1g5c",
"1i6o",
"1i6p",
"1t75",
"1ylk",
"1ym3",
"2a5v",
"2a8c",
"2a8d",
"2esf",
"2w3n",
"2w3q",
"3e1v",
"3e1w",
"3e24",
"3e28",
"3e2a",
"3e2w",
"3e2x",
"3e31",
"3e3f",
"3e3g",
"3e3i",
"3eyx",
"3las",
"3mf3",
"3qy1",
"3ten",
"3teo",
"3ucj"... | 75 | [
"PUB00002753",
"PUB00004782",
"PUB00065060",
"PUB00086422"
] | [
"1740425",
"1584776",
"23406161",
"22012399"
] | [
"Carbonic anhydrase in Escherichia coli. A product of the cyn operon.",
"A gene homologous to chloroplast carbonic anhydrase (icfA) is essential to photosynthetic carbon dioxide fixation by Synechococcus PCC7942.",
"Carbonyl Sulfide Hydrolase from Thiobacillus thioparus Strain THI115 Is One of the β-Carbonic An... | [
1992,
1992,
2013,
2011
] | 4 | [] | [
"IPR045066"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
595,
34743,
10891,
8,
393
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosacchar... | [
35,
5,
3,
2,
3,
9,
1,
2,
45
] | 9 | true | Family | Carbonic anhydrase | Carbonic anhydrase | Carbonic_anhydrase | 9 |
IPR001766 | 1,766 | Fork head domain | Fork_head_dom | Domain | 62,057 | false | false | The fork head domain is a conserved DNA-binding domain (also known as a "winged helix") of about 100 amino-acid residues. Drosophila melanogaster fork head protein is a transcription factor that promotes terminal rather than segmental development, contains neither homeodomains nor zinc-fingers characteristic of other t... | [
"GO:0003700",
"GO:0043565",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"sequence-specific DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00250",
"PR00053",
"PS50039",
"SM00339"
] | [
"Forkhead",
"FORKHEAD",
"FORK_HEAD_3",
"FH"
] | [
61347,
57085,
61883,
60964
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00564",
"R-BTA-3232118",
"R-CEL-1181150",
"R-CEL-198693",
"R-CEL-211163",
"R-CEL-3232118",
"R-CEL-5687128",
"R-CEL-5689880",
"R-CEL-9607240",
"R-CEL-9614399",
"R-CEL-9615017",
"R-CEL-9617629",
"R-CEL-9617828",
"R-CEL-9634638",
"R-CEL-9841251",
"R-DME-110478",
"R-DME-1181150",
... | [
"PROSITEDOC:PDOC00564",
"REACTOME:R-BTA-3232118",
"REACTOME:R-CEL-1181150",
"REACTOME:R-CEL-198693",
"REACTOME:R-CEL-211163",
"REACTOME:R-CEL-3232118",
"REACTOME:R-CEL-5687128",
"REACTOME:R-CEL-5689880",
"REACTOME:R-CEL-9607240",
"REACTOME:R-CEL-9614399",
"REACTOME:R-CEL-9615017",
"REACTOME:R-... | 112 | [
"1d5v",
"1e17",
"1jxs",
"1kq8",
"1vtn",
"2a07",
"2a3s",
"2as5",
"2c6y",
"2d2w",
"2hdc",
"2hfh",
"2k86",
"2kiu",
"2mbf",
"2uzk",
"3co6",
"3co7",
"3coa",
"3g73",
"3l2c",
"3qrf",
"4lg0",
"4wk8",
"5a5u",
"5dui",
"5ocn",
"5x07",
"6ako",
"6akp",
"6el8",
"6fec"... | 66 | [
"PUB00000827",
"PUB00004151",
"PUB00004800"
] | [
"2566386",
"8332212",
"1356269"
] | [
"The homeotic gene fork head encodes a nuclear protein and is expressed in the terminal regions of the Drosophila embryo.",
"Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5.",
"Developmentally regulated Drosophila gene family encoding the fork head domain."
] | [
1989,
1993,
1992
] | 3 | [] | [
"IPR047364",
"IPR047366",
"IPR047388",
"IPR047389",
"IPR047391",
"IPR047392",
"IPR047393",
"IPR047394",
"IPR047397",
"IPR047401",
"IPR047403",
"IPR047408",
"IPR047409",
"IPR047410",
"IPR047412",
"IPR047413",
"IPR047414",
"IPR047511",
"IPR047512",
"IPR047514",
"IPR047515",
"... | 0 | 24 | 0 | [
"Avian sarcoma virus (strain 31)",
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
2,
113,
61941,
1
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
33,
193,
76,
176,
110,
4,
133,
4,
4
] | 9 | true | Domain | Fork head domain | Fork head domain | Fork_head_dom | 5 |
IPR001767 | 1,767 | Hedgehog protein, Hint domain | Hedgehog_Hint | Domain | 6,622 | false | false | Hedgehog proteins are a family of secreted signal molecules required for embryonic cell differentiation. They are synthesised as inactive precursors with an N-terminal signalling domain linked to a C-terminal autoprocessing domain. The three-dimensional structure of the autolytic domain of the hedgehog protein of shows... | [
"GO:0016540"
] | [
"protein autoprocessing"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01079"
] | [
"Hint"
] | [
6622
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-DME-209338",
"R-DME-209471",
"R-DME-5358346",
"R-DME-5362798",
"R-DME-5632681",
"R-DRE-5358346",
"R-DRE-5362798",
"R-DRE-5632681",
"R-GGA-5358346",
"R-GGA-5362798",
"R-GGA-5632681",
"R-HSA-373080",
"R-HSA-5358346",
"R-HSA-5362768",
"R-HSA-5362798",
"R-HSA-5632681",
"R-HSA-5632684"... | [
"REACTOME:R-DME-209338",
"REACTOME:R-DME-209471",
"REACTOME:R-DME-5358346",
"REACTOME:R-DME-5362798",
"REACTOME:R-DME-5632681",
"REACTOME:R-DRE-5358346",
"REACTOME:R-DRE-5362798",
"REACTOME:R-DRE-5632681",
"REACTOME:R-GGA-5358346",
"REACTOME:R-GGA-5362798",
"REACTOME:R-GGA-5632681",
"REACTOME:... | 31 | [
"1at0",
"6td6",
"6tyy",
"7e2i"
] | 4 | [
"PUB00011705"
] | [
"9489693"
] | [
"Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
5,
83,
6523,
4,
7
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
23,
1,
7,
7,
10
] | 6 | true | Domain | Hedgehog protein, Hint domain | Hedgehog protein, Hint domain | Hedgehog_Hint | 1 |
IPR001769 | 1,769 | Gingipain | Gingipain | Domain | 4,169 | false | false | This domain is found in cysteine peptidases belonging to MEROPS peptidase family C25 (gingipain). Gingipains are cysteine proteinases acting as key virulence factors of the bacterium Porphyromonas gingivalis (Bacteroides gingivalis), a Gram-negative anaerobic bacterial species strongly associated with adult periodontit... | [
"GO:0008234",
"GO:0006508"
] | [
"cysteine-type peptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01364"
] | [
"Peptidase_C25"
] | [
4169
] | 1 | [
"EC"
] | [
"3.4.22"
] | [
"EC:3.4.22"
] | 1 | [
"1cvr",
"4ief",
"4rbm",
"4tkx",
"6i9a",
"6za2"
] | 6 | [
"PUB00011704",
"PUB00020025",
"PUB00021351",
"PUB00030423",
"PUB00076953"
] | [
"11517925",
"9891971",
"10523290",
"14725770",
"7044372"
] | [
"Evolutionary lines of cysteine peptidases.",
"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.",
"Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold.",
"The structure ... | [
2001,
1998,
1999,
2004,
1982
] | 5 | [] | [
"IPR039392"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
86,
3755,
35,
293
] | 4 | [] | [] | 0 | true | Domain | Gingipain | Gingipain | Gingipain | 3 |
IPR001770 | 1,770 | G-protein, gamma subunit | G-protein_gamma | Family | 9,909 | false | false | This entry represents the G protein gamma subunit. Guanine nucleotide binding proteins (G-proteins) are membrane-associated, heterotrimeric proteins composed of three subunits: alpha ( ), beta ( ) and gamma ( ) [ ]. G proteins and their receptors (GPCRs) form one of the most prevalent signalling systems in mammalian ce... | [
"GO:0031681",
"GO:0007186",
"GO:0005834"
] | [
"G-protein beta-subunit binding",
"G protein-coupled receptor signaling pathway",
"heterotrimeric G-protein complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS",
"PANTHER"
] | [
"PR00321",
"PTHR13809"
] | [
"GPROTEING",
""
] | [
8406,
9359
] | 2 | [
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"GenProp2089",
"GenProp2092",
"GenProp2093",
"GenProp2094",
"PDOC01002",
"R-BTA-1296041",
"R-BTA-202040",
"R-BTA-2485179",
"R-BTA-2514859",
"R-BTA-381676",
"R-BTA-392170",
"R-BTA-392451",
"R-BTA-392851",
"R-BTA-400042",
"R-BTA-4086398",
"R-BTA-416476",
"R-BTA-416482",
"R-BTA-418217... | [
"GP:GenProp2089",
"GP:GenProp2092",
"GP:GenProp2093",
"GP:GenProp2094",
"PROSITEDOC:PDOC01002",
"REACTOME:R-BTA-1296041",
"REACTOME:R-BTA-202040",
"REACTOME:R-BTA-2485179",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-381676",
"REACTOME:R-BTA-392170",
"REACTOME:R-BTA-392451",
"REACTOME:R-BTA-39... | 177 | [
"1a0r",
"1b9x",
"1b9y",
"1gg2",
"1got",
"1gp2",
"1omw",
"1tbg",
"1xhm",
"2bcj",
"2trc",
"3ah8",
"3cik",
"3krw",
"3krx",
"3psc",
"3pvu",
"3pvw",
"3sn6",
"3uzs",
"3v5w",
"4kfm",
"4mk0",
"4pnk",
"5he0",
"5he1",
"5he2",
"5he3",
"5kdo",
"5tdh",
"5ukk",
"5ukl"... | 1,278 | [
"PUB00005142",
"PUB00015166",
"PUB00015168",
"PUB00015169",
"PUB00015170",
"PUB00015171",
"PUB00015172"
] | [
"1902986",
"15294442",
"15119945",
"14762218",
"11313912",
"9278091",
"11882385"
] | [
"Diversity of G proteins in signal transduction.",
"G protein activation by G protein coupled receptors: ternary complex formation or catalyzed reaction?",
"Biochemistry of transmembrane signaling mediated by trimeric G proteins.",
"G protein signaling: insights from new structures.",
"Regulation of G prote... | [
1991,
2004,
2004,
2004,
2001,
1997,
2002
] | 7 | [] | [] | 0 | 0 | null | [
"Azospirillum isscasi",
"Metazoa"
] | [
2,
9907
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
23,
6,
21,
25,
35
] | 6 | true | Family | G-protein, gamma subunit | G-protein, gamma subunit | G-protein_gamma | 6 |
IPR001771 | 1,771 | GPCR, family 2, vasoactive intestinal peptide receptor 1 | GPCR_2_VIP_rcpt_1 | Family | 2,697 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0004999",
"GO:0007186",
"GO:0016020"
] | [
"vasoactive intestinal polypeptide receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01154"
] | [
"VIP1RECEPTOR"
] | [
2697
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"371",
"R-HSA-418555",
"R-HSA-420092",
"R-MMU-418555",
"R-MMU-420092",
"R-RNO-420092"
] | [
"IUPHAR:371",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-420092",
"REACTOME:R-MMU-418555",
"REACTOME:R-MMU-420092",
"REACTOME:R-RNO-420092"
] | 6 | [
"6vn7",
"8e3y",
"8e3z"
] | 3 | [
"PUB00001208",
"PUB00003458",
"PUB00003459",
"PUB00004310",
"PUB00004822",
"PUB00004961",
"PUB00005147",
"PUB00005148",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"1646711",
"8933357",
"8784257",
"1314625",
"8392197",
"8170923",
"1658940",
"1658941",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"Molecular cloning and expression of a cDNA encoding the secretin receptor.",
"Tissue specific expression of different human receptor types for pituitary adenylate cyclase activating polypeptide and vasoactive intestinal polypeptide: implications for their role in human physiology.",
"Differential expression of... | [
1991,
1996,
1996,
1992,
1993,
1994,
1991,
1991,
2003,
1994,
2005,
2009,
2006,
2013
] | 14 | [
"IPR001571"
] | [] | 1 | 0 | 1 | [
"Chordata"
] | [
2697
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
4,
1,
4
] | 4 | true | Family | GPCR, family 2, vasoactive intestinal peptide receptor 1 | GPCR, family 2, vasoactive intestinal peptide receptor 1 | GPCR_2_VIP_rcpt_1 | 6 |
IPR001772 | 1,772 | Kinase associated domain 1 (KA1) | KA1_dom | Domain | 17,141 | false | false | Members of the KIN2/PAR-1/MARK kinase subfamily are conserved from yeast to human and share the same domain organisation: an N-terminal kinase domain ( ) and a C-terminal kinase associated domain 1 (KA1). Some members of the KIN1/PAR-1/MARK family also contain an UBA domain ( ). Members of this kinase subfamily are inv... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF02149",
"PS50032"
] | [
"KA1",
"KA1"
] | [
16447,
17034
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11.1",
"PDOC50032",
"R-CEL-5673000",
"R-CEL-5674135",
"R-CEL-5675221",
"R-CEL-9856649",
"R-DDI-1632852",
"R-DDI-163680",
"R-DDI-200425",
"R-DDI-380972",
"R-DDI-5628897",
"R-DDI-5673000",
"R-DDI-5675221",
"R-HSA-5620912",
"R-HSA-5673000",
"R-HSA-5674135",
"R-HSA-5675221",
"R-HS... | [
"EC:2.7.11.1",
"PROSITEDOC:PDOC50032",
"REACTOME:R-CEL-5673000",
"REACTOME:R-CEL-5674135",
"REACTOME:R-CEL-5675221",
"REACTOME:R-CEL-9856649",
"REACTOME:R-DDI-1632852",
"REACTOME:R-DDI-163680",
"REACTOME:R-DDI-200425",
"REACTOME:R-DDI-380972",
"REACTOME:R-DDI-5628897",
"REACTOME:R-DDI-5673000"... | 38 | [
"1ul7",
"1v5s",
"3ose",
"6c9d"
] | 4 | [
"PUB00035303",
"PUB00035304",
"PUB00035305",
"PUB00035306",
"PUB00037875"
] | [
"15182702",
"12429843",
"7758115",
"15563607",
"17075132"
] | [
"An overview of the KIN1/PAR-1/MARK kinase family.",
"Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity.",
"par-1, a gene required for establishing polarity in C. elegans embryos, encodes a putative Ser/Thr kinase that is asymmetrically distributed.",
"The yeas... | [
2004,
2002,
1995,
2005,
2006
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nitrosocosmicus oleophilus",
"Eukaryota"
] | [
20,
1,
17120
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
13,
4,
99,
10,
50,
23,
1,
9,
31,
2,
1,
23
] | 12 | true | Domain | Kinase associated domain 1 (KA1) | Kinase associated domain 1 (KA1) | KA1_dom | 5 |
IPR001774 | 1,774 | Delta/Serrate/lag-2 (DSL) protein | DSL | Domain | 9,824 | false | false | Ligands of the Delta/Serrate/lag-2 (DSL) family and their receptors, members of the lin-12/Notch family, mediate cell-cell interactions that specify cell fate in invertebrates and vertebrates. In Caenorhabditis elegans, two DSL genes, lag-2 and apx-1, influence different cell fate decisions during development [ ]. Mole... | [
"GO:0007154",
"GO:0016020"
] | [
"cell communication",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01414",
"PS51051",
"SM00051"
] | [
"DSL",
"DSL",
"DSL"
] | [
9424,
8917,
9225
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51051",
"R-DME-1912420",
"R-DME-2979096",
"R-DME-9013700",
"R-DME-9604323",
"R-DRE-2979096",
"R-HSA-2122948",
"R-HSA-2644606",
"R-HSA-2660826",
"R-HSA-2691232",
"R-HSA-2894862",
"R-HSA-2979096",
"R-HSA-8941856",
"R-HSA-9013149",
"R-HSA-9013423",
"R-HSA-9013507",
"R-HSA-9013700",... | [
"PROSITEDOC:PDOC51051",
"REACTOME:R-DME-1912420",
"REACTOME:R-DME-2979096",
"REACTOME:R-DME-9013700",
"REACTOME:R-DME-9604323",
"REACTOME:R-DRE-2979096",
"REACTOME:R-HSA-2122948",
"REACTOME:R-HSA-2644606",
"REACTOME:R-HSA-2660826",
"REACTOME:R-HSA-2691232",
"REACTOME:R-HSA-2894862",
"REACTOME:... | 30 | [
"2vj2",
"4cbz",
"4cc0",
"4cc1",
"4xbm",
"4xl1",
"4xlw",
"5bo1",
"5mvx",
"5mw5",
"5mw7",
"5mwf",
"5uk5",
"7alk",
"7alt"
] | 15 | [
"PUB00000862",
"PUB00001103",
"PUB00005202"
] | [
"1657403",
"8575327",
"7716513"
] | [
"Specific EGF repeats of Notch mediate interactions with Delta and Serrate: implications for Notch as a multifunctional receptor.",
"Interchangeability of Caenorhabditis elegans DSL proteins and intrinsic signalling activity of their extracellular domains in vivo.",
"Notch signaling."
] | [
1991,
1995,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9824
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
20,
5,
9,
5,
18
] | 6 | true | Domain | Delta/Serrate/lag-2 (DSL) protein | Delta/Serrate/lag-2 (DSL) protein | DSL | 5 |
IPR001775 | 1,775 | GspD/PilQ family | GspD/PilQ | Family | 27,886 | false | false | The general (type II) secretion pathway (Gsp) within Gram-negative bacteria is a signal sequence-dependent process responsible for protein export [ , , ]. The process has two stages: exoproteins are first translocated across the inner membrane by the general signal-dependent export pathway (GEP), and then across the ou... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00811"
] | [
"BCTERIALGSPD"
] | [
27886
] | 1 | [
"REACTOME"
] | [
"R-HSA-9760173"
] | [
"REACTOME:R-HSA-9760173"
] | 1 | [
"3jc8",
"3jc9",
"4av2",
"5w68",
"5wln",
"5wq7",
"5wq8",
"5wq9",
"5zdh",
"6hcg",
"6i1x",
"6i1y",
"6ve2",
"6ve3",
"6ve4",
"6w6m",
"7ofh",
"8jvb",
"8odn",
"9k8v"
] | 20 | [
"PUB00002179",
"PUB00002516",
"PUB00005409",
"PUB00005523"
] | [
"1592799",
"2677007",
"8438237",
"1365398"
] | [
"Determinants of extracellular protein secretion in gram-negative bacteria.",
"Protein secretion by gram-negative bacteria. Characterization of two membrane proteins required for pullulanase secretion by Escherichia coli K-12.",
"Membrane traffic wardens and protein secretion in gram-negative bacteria.",
"Sec... | [
1992,
1989,
1993,
1992
] | 4 | [] | [
"IPR013355",
"IPR013356",
"IPR013358"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Inoviridae",
"environmental samples",
"unclassified sequences"
] | [
27313,
51,
17,
2,
503
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | GspD/PilQ family | GspD/PilQ family | GspD/PilQ | 1 |
IPR001779 | 1,779 | Two pore domain potassium channel, TWIK-1 | 2pore_dom_K_chnl_TWIK1 | Family | 1,424 | false | false | Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr... | [
"GO:0005267",
"GO:0071805",
"GO:0016020"
] | [
"potassium channel activity",
"potassium ion transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01096"
] | [
"TWIK1CHANNEL"
] | [
1424
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-1299308",
"R-BTA-5576886",
"R-HSA-1299308",
"R-HSA-5576886",
"R-MMU-1299308",
"R-MMU-5576886",
"R-RNO-1299308",
"R-RNO-5576886"
] | [
"REACTOME:R-BTA-1299308",
"REACTOME:R-BTA-5576886",
"REACTOME:R-HSA-1299308",
"REACTOME:R-HSA-5576886",
"REACTOME:R-MMU-1299308",
"REACTOME:R-MMU-5576886",
"REACTOME:R-RNO-1299308",
"REACTOME:R-RNO-5576886"
] | 8 | [
"3ukm",
"7sk0",
"7sk1"
] | 3 | [
"PUB00001055",
"PUB00001278",
"PUB00001298",
"PUB00001308",
"PUB00001622",
"PUB00002771",
"PUB00004011",
"PUB00004020",
"PUB00004219",
"PUB00004878",
"PUB00006577",
"PUB00007784",
"PUB00009378"
] | [
"1772658",
"8605869",
"9003761",
"9312005",
"1879548",
"1373731",
"2448635",
"2451788",
"7651518",
"8917578",
"2555158",
"10075682",
"11178249"
] | [
"The molecular biology of K+ channels.",
"TWIK-1, a ubiquitous human weakly inward rectifying K+ channel with a novel structure.",
"Cloning, functional expression and brain localization of a novel unconventional outward rectifier K+ channel.",
"TASK, a human background K+ channel to sense external pH variatio... | [
1991,
1996,
1996,
1997,
1991,
1992,
1988,
1988,
1995,
1996,
1989,
1999,
2000
] | 13 | [
"IPR005408"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
1424
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
3,
2,
2
] | 4 | true | Family | Two pore domain potassium channel, TWIK-1 | Two pore domain potassium channel, TWIK-1 | 2pore_dom_K_chnl_TWIK1 | 4 |
IPR001780 | 1,780 | Large ribosomal subunit protein eL33 | Ribosomal_eL33 | Family | 6,291 | false | false | The ribosomal eL33 eukaryotic and archaebacterial ribosomal proteins, previously known as L35A, can be grouped on the basis of sequence similarities. One of these families consists of: Vertebrate eL33 (old name L35A). Caenorhabditis elegans eL33 (old name L35A (F10E7.7)). Saccharomyces cerevisiae eL33A/eL33B (old name ... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PANTHER"
] | [
"MF_00573",
"PF01247",
"PTHR10902"
] | [
"Ribosomal_eL33",
"Ribosomal_L35Ae",
""
] | [
5484,
6276,
5958
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00849",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",... | [
"PROSITEDOC:PDOC00849",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-7270... | 52 | [
"1sqr",
"2lp6",
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j79",
"3j7o",
"3j7p",
"3j7q",
"3j7r",
"3j92",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jan",
"3jbn",
"3jbo",
"3jbp",
"3jcs",
"3jct",
"4d5y",
"4d67",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q",
"4u4r",
"4u4u"... | 591 | [
"PUB00004463",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"7899076",
"11297922",
"11290319",
"11114498"
] | [
"Novel protein families in archaean genomes.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1995,
2001,
2001,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
99,
2,
6171,
19
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
9,
1,
1,
1,
4,
4,
1,
7,
19,
2,
2,
23
] | 12 | true | Family | Large ribosomal subunit protein eL33 | Large ribosomal subunit protein eL33 | Ribosomal_eL33 | 1 |
IPR001781 | 1,781 | Zinc finger, LIM-type | Znf_LIM | Domain | 139,033 | false | false | This entry represents LIM-type zinc finger (Znf) domains. LIM domains coordinate one or more zinc atoms, and are named after the three proteins (LIN-11, Isl1 and MEC-3) in which they were first found. They consist of two zinc-binding motifs that resemble GATA-like Znf's, however the residues holding the zinc atom(s) ar... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART"
] | [
"PF00412",
"PS00478",
"PS50023",
"SM00132"
] | [
"LIM",
"LIM_DOMAIN_1",
"LIM_DOMAIN_2",
"LIM"
] | [
134556,
127559,
137701,
136158
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00382",
"R-BTA-1234176",
"R-BTA-2565942",
"R-BTA-446353",
"R-BTA-5683826",
"R-BTA-8853659",
"R-BTA-8939236",
"R-BTA-9841922",
"R-CEL-446353",
"R-CEL-446388",
"R-DDI-446353",
"R-DDI-446388",
"R-DDI-8849471",
"R-DDI-983231",
"R-DME-1234176",
"R-DME-2029482",
"R-DME-350368",
"R-D... | [
"PROSITEDOC:PDOC00382",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-446353",
"REACTOME:R-BTA-5683826",
"REACTOME:R-BTA-8853659",
"REACTOME:R-BTA-8939236",
"REACTOME:R-BTA-9841922",
"REACTOME:R-CEL-446353",
"REACTOME:R-CEL-446388",
"REACTOME:R-DDI-446353",
"REACTOME:R-DD... | 108 | [
"1a7i",
"1b8t",
"1ctl",
"1cxx",
"1g47",
"1ibi",
"1iml",
"1j2o",
"1m3v",
"1nyp",
"1qli",
"1rut",
"1u5s",
"1v6g",
"1wig",
"1wyh",
"1x3h",
"1x4k",
"1x4l",
"1x61",
"1x62",
"1x63",
"1x64",
"1x68",
"1x6a",
"1zfo",
"2co8",
"2cor",
"2cu8",
"2cup",
"2cuq",
"2cur"... | 90 | [
"PUB00004063",
"PUB00004454",
"PUB00004517",
"PUB00004815"
] | [
"1970421",
"8065929",
"1467648",
"8506279"
] | [
"Novel cysteine-rich motif and homeodomain in the product of the Caenorhabditis elegans cell lineage gene lin-11.",
"LRG1 is expressed during sporulation in Saccharomyces cerevisiae and contains motifs similar to LIM and rho/racGAP domains.",
"A LIM motif is present in a pollen-specific protein.",
"The LIM mo... | [
1990,
1994,
1992,
1993
] | 4 | [] | [
"IPR001904",
"IPR028537",
"IPR028740",
"IPR033725",
"IPR033726",
"IPR033727",
"IPR034958",
"IPR034959",
"IPR034960",
"IPR044115",
"IPR047072",
"IPR047075",
"IPR047244",
"IPR047245",
"IPR047247",
"IPR047248",
"IPR047944",
"IPR047956",
"IPR049593",
"IPR049618",
"IPR049619"
] | 0 | 21 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
10,
70,
138926,
7,
20
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
56,
58,
708,
144,
335,
268,
5,
29,
372,
4,
5,
72
] | 12 | true | Domain | Zinc finger, LIM-type | Zinc finger, LIM-type | Znf_LIM | 9 |
IPR001782 | 1,782 | Flagellar P-ring protein | Flag_FlgI | Family | 10,699 | false | false | The flgH, flgI and fliF genes of Salmonella typhimurium encode the major proteins for the L, P and M rings of the flagellar basal body [ ]. In fact, the basal body consists of four rings (L,P,S and M) surrounding the flagellar rod, which is believed to transmit motor rotation to the filament [ ]. The M ring is integral... | [
"GO:0005198",
"GO:0071973",
"GO:0009428",
"GO:0030288"
] | [
"structural molecule activity",
"bacterial-type flagellum-dependent cell motility",
"bacterial-type flagellum basal body, distal rod, P ring",
"outer membrane-bounded periplasmic space"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"HAMAP",
"PFAM",
"PRINTS",
"PANTHER"
] | [
"MF_00416",
"PF02119",
"PR01010",
"PTHR30381"
] | [
"FlgI",
"FlgI",
"FLGPRINGFLGI",
""
] | [
10087,
10680,
10494,
10647
] | 4 | [
"GP"
] | [
"GenProp0880"
] | [
"GP:GenProp0880"
] | 1 | [
"7bgl",
"7bj2",
"7cbl",
"7cgo",
"7clr",
"7nvg",
"8wht",
"8wl2",
"8wle",
"8wlt",
"8wo5",
"8woe",
"8z5n",
"8z60"
] | 14 | [
"PUB00002059",
"PUB00002086",
"PUB00003254"
] | [
"3549691",
"2544561",
"2129540"
] | [
"The flaFIX gene product of Salmonella typhimurium is a flagellar basal body component with a signal peptide for export.",
"L-, P-, and M-ring proteins of the flagellar basal body of Salmonella typhimurium: gene sequences and deduced protein sequences.",
"FlgB, FlgC, FlgF and FlgG. A family of structurally rela... | [
1987,
1989,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
10523,
33,
143
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flagellar P-ring protein | Flagellar P-ring protein | Flag_FlgI | 4 |
IPR001783 | 1,783 | Lumazine-binding protein | Lumazine-bd | Family | 26,935 | false | false | null | [] | [] | [] | 0 | [
"PIRSF",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"PIRSF000498",
"PTHR21098",
"TIGR00187",
"cd00402"
] | [
"Riboflavin_syn_A",
"",
"ribE",
"Riboflavin_synthase_like"
] | [
25227,
26801,
25934,
26608
] | 4 | [
"EC",
"GP",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"2.5.1.9",
"GenProp1734",
"PWY-6167",
"PWY-6168",
"PDOC00581"
] | [
"EC:2.5.1.9",
"GP:GenProp1734",
"METACYC:PWY-6167",
"METACYC:PWY-6168",
"PROSITEDOC:PDOC00581"
] | 5 | [
"1hze",
"1i18",
"1i8d",
"1kzl",
"1pkv",
"3a35",
"3a3b",
"3a3g",
"3ddy",
"4e0f",
"4fxu",
"4g6i",
"4gqn",
"7wuo"
] | 14 | [
"PUB00004728",
"PUB00028001"
] | [
"1996310",
"1560772"
] | [
"Borrowed proteins in bacterial bioluminescence.",
"Evolutionary origins of bacterial bioluminescence."
] | [
1991,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
476,
23313,
2662,
3,
481
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
1,
1,
4,
1,
1,
8
] | 7 | true | Family | Lumazine-binding protein | Lumazine-binding protein | Lumazine-bd | 8 |
IPR001784 | 1,784 | Bunyavirus nucleocapsid (N) protein | Bunya_nucleocap | Family | 972 | false | false | Orthobunyavirus are enveloped viruses with a genome consisting of 3 ssRNA segments (called L, M and S). The nucleocapsid protein (also known as nucleoprotein) is encoded on the small (S) genomic RNA. The N protein is the major component of the nucleocapsids. This protein is thought to interact with the L protein, virus... | [
"GO:0019013"
] | [
"viral nucleocapsid"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PIRSF"
] | [
"PF00952",
"PIRSF003947"
] | [
"Bunya_nucleocap",
"N_OrthobunV"
] | [
972,
468
] | 2 | [
"GP"
] | [
"GenProp1007"
] | [
"GP:GenProp1007"
] | 1 | [
"3zl9",
"3zla",
"4bgp",
"4bhh",
"4idu",
"4idx",
"4ijs",
"4j1g",
"4j1j",
"4jng",
"7aoy"
] | 11 | [
"PUB00003164"
] | [
"7897347"
] | [
"Determination and comparative analysis of the small RNA genomic sequences of California encephalitis, Jamestown Canyon, Jerry Slough, Melao, Keystone and Trivittatus viruses (Bunyaviridae, genus Bunyavirus, California serogroup)."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Ecdysozoa",
"Polyploviricotina"
] | [
40,
932
] | 2 | [] | [] | 0 | true | Family | Bunyavirus nucleocapsid (N) protein | Bunyavirus nucleocapsid (N) protein | Bunya_nucleocap | 2 |
IPR001786 | 1,786 | GPCR, family 3, metabotropic glutamate receptor 4 | GPCR_3_mGluR4 | Family | 4,038 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR01054"
] | [
"MTABOTROPC4R"
] | [
4038
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"292",
"R-HSA-418594",
"R-HSA-420499",
"R-HSA-9717207",
"R-MMU-418594",
"R-MMU-420499",
"R-RNO-418594",
"R-RNO-420499"
] | [
"IUPHAR:292",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-420499",
"REACTOME:R-HSA-9717207",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-420499",
"REACTOME:R-RNO-418594",
"REACTOME:R-RNO-420499"
] | 8 | [
"8jd4",
"8jd5",
"8wg9",
"8wgb",
"8wgc",
"8wgd"
] | 6 | [
"PUB00000773",
"PUB00002720",
"PUB00004090",
"PUB00004161",
"PUB00004309",
"PUB00004961",
"PUB00005138",
"PUB00007343",
"PUB00036049",
"PUB00036050",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"8738157",
"1320017",
"1847995",
"8255296",
"1309649",
"8170923",
"1656524",
"9292726",
"17266540",
"10773016",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"Molecular characterization and localization of human metabotropic glutamate receptor type 4.",
"Molecular characterization of a novel metabotropic glutamate receptor mGluR5 coupled to inositol phosphate/Ca2+ signal transduction.",
"Sequence and expression of a metabotropic glutamate receptor.",
"Cloning and ... | [
1996,
1992,
1991,
1993,
1992,
1994,
1991,
1997,
2007,
2000,
2003,
1994,
2005,
2009,
2006,
2013
] | 16 | [
"IPR000162"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
4038
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
10,
7,
7
] | 4 | true | Family | GPCR, family 3, metabotropic glutamate receptor 4 | GPCR, family 3, metabotropic glutamate receptor 4 | GPCR_3_mGluR4 | 8 |
IPR001787 | 1,787 | Large ribosomal subunit protein bL21 | Ribosomal_bL21 | Family | 27,048 | false | false | This entry represents the Large ribosomal subunit protein bL21 found in bacteria and eukaryotic organelles such as chloroplast and mitochondria. In Escherichia coli, bL21 is known to bind to the 23S rRNA in the presence of bL20. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities, ... | [
"GO:0003723",
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"RNA binding",
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01363",
"TIGR00061"
] | [
"Ribosomal_bL21",
"L21"
] | [
26300,
26903
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00899",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383"
] | [
"PROSITEDOC:PDOC00899",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9937383",
"REACTOME:R-MMU-5389840",
"REACTOME:R-MMU-5419276",
"REACTOME:R-MMU-9937383"
] | 8 | [
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"2j28",
"2rdo",
"2zjp",
"2zjq",
"2zjr",
"3bbx",
"3cf5",
"3dll",
"3iy9",
"3j3v",
"3j3w",
"3j5l",
"3j7y",
"3j7z",
"3j8g",
"3j9m",
"3j9w",
"3j9y",
"3j9z",
"3ja1",
"3jbu",
"3jbv"... | 1,253 | [] | [] | [] | [] | 0 | [
"IPR028909"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
23452,
3098,
498
] | 3 | [
"Arabidopsis thaliana",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
9,
1,
1,
1,
1,
6,
17
] | 7 | true | Family | Large ribosomal subunit protein bL21 | Large ribosomal subunit protein bL21 | Ribosomal_bL21 | 4 |
IPR001788 | 1,788 | RNA-dependent RNA polymerase, alsuviricetes | RNA-dep_RNA_pol_alsuvir | Domain | 10,460 | false | false | This entry represents the C-terminal domain of RNA dependent RNA polymerases found in Alsuviricetes class of positive-strand RNA viruses that infect eukaryotes [ ], including those with a tripartite genome (RNA1, RNA2 and RNA3) and an encapsidated subgenomic RNA (RNA4) from which the coat protein is expressed, such as ... | [
"GO:0003723",
"GO:0003968",
"GO:0006351"
] | [
"RNA binding",
"RNA-directed RNA polymerase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF00978"
] | [
"RdRP_2"
] | [
10460
] | 1 | [
"EC",
"EC",
"EC"
] | [
"2.7.7",
"2.7.7.48",
"3.6.4.13"
] | [
"EC:2.7.7",
"EC:2.7.7.48",
"EC:3.6.4.13"
] | 3 | [
"7f0s",
"7vb4",
"7vw5",
"7y38"
] | 4 | [
"PUB00001007",
"PUB00003501",
"PUB00003525",
"PUB00035782",
"PUB00102540"
] | [
"8269709",
"8445717",
"8709249",
"15746101",
"35037043"
] | [
"Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences.",
"Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription.",
"Complete replication in vitro of tobacco mosaic virus RNA by a temp... | [
1993,
1993,
1996,
2005,
2022
] | 5 | [] | [
"IPR047306",
"IPR047307",
"IPR047308",
"IPR047309",
"IPR047310",
"IPR047311"
] | 0 | 6 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"viral metagenome"
] | [
6,
66,
10384,
4
] | 4 | [] | [] | 0 | true | Domain | RNA-dependent RNA polymerase, alsuviricetes | RNA-dependent RNA polymerase, alsuviricetes | RNA-dep_RNA_pol_alsuvir | 7 |
IPR001789 | 1,789 | Signal transduction response regulator, receiver domain | Sig_transdc_resp-reg_receiver | Domain | 1,261,208 | false | false | The response regulators act as phosphorylation-activated switches to affect a cellular response, usually by transcriptional regulation. Most of these proteins consist of two domains, an N-terminal response regulator receiver domain, and a variable C-terminal effector domain with DNA-binding activity. This entry represe... | [
"GO:0000160"
] | [
"phosphorelay signal transduction system"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00072",
"PS50110",
"SM00448"
] | [
"Response_reg",
"RESPONSE_REGULATORY",
"REC"
] | [
1211350,
1259866,
1203701
] | 3 | [
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp0292",
"GenProp1139",
"GenProp1147",
"GenProp1194",
"PDOC50110",
"R-DDI-111957",
"R-DDI-165160",
"R-DDI-180024",
"R-DDI-418457",
"R-DDI-418555",
"R-SCE-2465910",
"R-SPO-2465910"
] | [
"GP:GenProp0292",
"GP:GenProp1139",
"GP:GenProp1147",
"GP:GenProp1194",
"PROSITEDOC:PDOC50110",
"REACTOME:R-DDI-111957",
"REACTOME:R-DDI-165160",
"REACTOME:R-DDI-180024",
"REACTOME:R-DDI-418457",
"REACTOME:R-DDI-418555",
"REACTOME:R-SCE-2465910",
"REACTOME:R-SPO-2465910"
] | 12 | [
"1a04",
"1a0o",
"1a2o",
"1ab5",
"1ab6",
"1b00",
"1bdj",
"1c4w",
"1cey",
"1chn",
"1cye",
"1d4z",
"1d5w",
"1dbw",
"1dc7",
"1dc8",
"1dcf",
"1dck",
"1dcm",
"1djm",
"1dz3",
"1e6k",
"1e6l",
"1e6m",
"1eay",
"1ehc",
"1f4v",
"1f51",
"1ffg",
"1ffs",
"1ffw",
"1fqw"... | 489 | [
"PUB00003437",
"PUB00010651",
"PUB00011096",
"PUB00013308",
"PUB00042804",
"PUB00042805",
"PUB00042806",
"PUB00042807"
] | [
"7699720",
"12372152",
"10966457",
"12015152",
"16176121",
"18076326",
"11934609",
"11489844"
] | [
"Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution.",
"Histidine protein kinases: key signal transducers outside the animal kingdom.",
"Two-component signal transduction.",
"Tandem DNA recognition by PhoB, a two-component signal transduction transcriptio... | [
1995,
2002,
2000,
2002,
2005,
2007,
2002,
2001
] | 8 | [] | [
"IPR047673",
"IPR048029",
"IPR049510",
"IPR055158",
"IPR056839",
"IPR058071",
"IPR058124",
"IPR058245"
] | 0 | 8 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid Ti",
"Viruses",
"unclassified sequences"
] | [
10521,
1175532,
62161,
1,
75,
12918
] | 6 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"... | [
224,
39,
1,
16,
108,
4,
6,
294
] | 8 | true | Domain | Signal transduction response regulator, receiver domain | Signal transduction response regulator, receiver domain | Sig_transdc_resp-reg_receiver | 9 |
IPR001790 | 1,790 | Large ribosomal subunit protein uL10, N-terminal | Ribosomal_uL10_N | Domain | 38,286 | false | false | This entry represents the conserved domain found at the N-terminal of large ribosomal subunit protein uL10 family, with includes ribosomal proteins found in bacteria, archaea and eukaryotes as well as in eukaryotic organelles such as chloroplast and mitochondria. On the basis of sequence similarities the following prok... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00466"
] | [
"Ribosomal_L10"
] | [
38286
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",
"R-DDI-975956",
"R-DDI-975957",
"R-DME-156827",
"R-DME-1799339",
"R-DME-5... | [
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-975956",
"REACTOME:R-CEL-975957",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-1799339",
"REACTOME:R-DDI-... | 85 | [
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b",
"1yhq"... | 782 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
933,
23886,
12969,
498
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
19,
3,
4,
4,
1,
20,
10,
2,
18,
11,
3,
2,
25
] | 13 | true | Domain | Large ribosomal subunit protein uL10, N-terminal | Large ribosomal subunit protein uL10, N-terminal | Ribosomal_uL10_N | 4 |
IPR001791 | 1,791 | Laminin G domain | Laminin_G | Domain | 88,998 | false | false | null | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00054",
"PF02210",
"PS50025",
"SM00282",
"cd00110"
] | [
"Laminin_G_1",
"Laminin_G_2",
"LAM_G_DOMAIN",
"LamG",
"LamG"
] | [
18968,
72985,
77682,
80162,
83804
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50025",
"R-BTA-114608",
"R-BTA-140837",
"R-BTA-140875",
"R-BTA-159740",
"R-BTA-159763",
"R-BTA-159782",
"R-BTA-202733",
"R-CEL-351906",
"R-CEL-376176",
"R-CEL-6798695",
"R-CEL-6809371",
"R-CEL-9010553",
"R-CEL-9013404",
"R-CEL-9013408",
"R-CEL-9013423",
"R-DME-1474228",
"R-DME... | [
"PROSITEDOC:PDOC50025",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-140837",
"REACTOME:R-BTA-140875",
"REACTOME:R-BTA-159740",
"REACTOME:R-BTA-159763",
"REACTOME:R-BTA-159782",
"REACTOME:R-BTA-202733",
"REACTOME:R-CEL-351906",
"REACTOME:R-CEL-376176",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-680... | 173 | [
"1c4r",
"1d2s",
"1dyk",
"1f5f",
"1h30",
"1kdk",
"1kdm",
"1lhn",
"1lho",
"1lhu",
"1lhv",
"1lhw",
"1okq",
"1pz7",
"1pz8",
"1pz9",
"1q56",
"1qu0",
"1z78",
"1za4",
"2c5d",
"2erf",
"2es3",
"2h0b",
"2jd4",
"2ouh",
"2ouj",
"2r16",
"2r1b",
"2r1d",
"2wjs",
"2wqz"... | 79 | [
"PUB00002576",
"PUB00003384",
"PUB00010694",
"PUB00016682",
"PUB00016683"
] | [
"1975589",
"9480764",
"10747011",
"15823034",
"15037599"
] | [
"Structure of the human laminin B1 chain gene.",
"Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins.",
"Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for a... | [
1990,
1998,
2000,
2005,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
35,
3825,
85055,
18,
65
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
30,
557,
80,
254,
167,
258
] | 6 | true | Domain | Laminin G domain | Laminin G domain | Laminin_G | 6 |
IPR001792 | 1,792 | Acylphosphatase-like domain | Acylphosphatase-like_dom | Domain | 29,107 | false | false | Acylphosphatase ( ) is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [ ], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [ ]. The enzyme has a mainly β-sheet structure with 2 short α-helical segments.... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00708",
"PS51160"
] | [
"Acylphosphatase",
"ACYLPHOSPHATASE_3"
] | [
28763,
29023
] | 2 | [
"EC",
"GP",
"PROSITEDOC"
] | [
"3.6.1.7",
"GenProp0754",
"PDOC00136"
] | [
"EC:3.6.1.7",
"GP:GenProp0754",
"PROSITEDOC:PDOC00136"
] | 3 | [
"1aps",
"1gxt",
"1gxu",
"1ulr",
"1urr",
"1v3z",
"1w2i",
"1y9o",
"2acy",
"2bjd",
"2bje",
"2fhm",
"2gv1",
"2hlt",
"2hlu",
"2k7j",
"2k7k",
"2lxf",
"2vh7",
"2w4c",
"2w4d",
"2w4p",
"3br8",
"3tnv",
"3toq",
"3trg",
"3vth",
"3vti",
"4g9i",
"4hi1",
"4hi2",
"4oix"... | 45 | [
"PUB00002331",
"PUB00002351",
"PUB00003238",
"PUB00011085",
"PUB00033805"
] | [
"2830253",
"1664426",
"2538623",
"12206761",
"9799289"
] | [
"The primary structure of chicken muscle acylphosphatase isozyme Ch1.",
"The primary structure of two molecular species of porcine organ-common type acylphosphatase.",
"Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy.",
"Cry... | [
1987,
1991,
1989,
2002,
1998
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ssRNA phage SRR6254351_1",
"unclassified sequences"
] | [
1493,
21790,
5424,
1,
399
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
4,
12,
2,
13,
4,
1,
5,
10,
9
] | 10 | true | Domain | Acylphosphatase-like domain | Acylphosphatase-like domain | Acylphosphatase-like_dom | 6 |
IPR001793 | 1,793 | Retinal pigment epithelium GPCR | RPE_GPCR | Family | 1,165 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0004930",
"GO:0007186",
"GO:0007601",
"GO:0007602",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"G protein-coupled receptor signaling pathway",
"visual perception",
"phototransduction",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00667"
] | [
"RPERETINALR"
] | [
1165
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-418594",
"R-BTA-419771",
"R-HSA-418594",
"R-HSA-419771",
"R-MMU-418594",
"R-MMU-419771"
] | [
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-419771",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-419771",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-419771"
] | 6 | [] | 0 | [
"PUB00000131",
"PUB00000394",
"PUB00002049",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"7947717",
"8258527",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"A human opsin-related gene that encodes a retinaldehyde-binding protein.",
"An opsin homologue in the retina and pigment epithelium.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"... | [
1990,
1994,
1993,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 12 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1165
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
8,
5,
2
] | 4 | true | Family | Retinal pigment epithelium GPCR | Retinal pigment epithelium GPCR | RPE_GPCR | 8 |
IPR001795 | 1,795 | RNA-directed RNA polymerase, luteovirus | RNA-dir_pol_luteovirus | Family | 6,952 | false | false | RNA-directed RNA polymerase (RdRp) ( ) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage [ , ]. It catalyses synthesis of the RNA strand complementary to a given RNA template, but the precise molecular mechanism remains unclear. The postulated RNA replication process is a tw... | [
"GO:0003723",
"GO:0003968",
"GO:0006351"
] | [
"RNA binding",
"RNA-directed RNA polymerase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PRINTS"
] | [
"PF02123",
"PR00914"
] | [
"RdRP_4",
"LVIRUSRNAPOL"
] | [
6700,
1642
] | 2 | [
"EC"
] | [
"2.7.7.48"
] | [
"EC:2.7.7.48"
] | 1 | [
"2r7o",
"2r7q",
"2r7r",
"2r7s",
"2r7t",
"2r7u",
"2r7v",
"2r7w",
"2r7x",
"4au6",
"4f5x",
"6ogy",
"6ogz",
"6oj3",
"6oj4",
"6oj5",
"6oj6",
"9c1l"
] | 18 | [
"PUB00001567",
"PUB00003126",
"PUB00003140",
"PUB00004354",
"PUB00005564",
"PUB00009392",
"PUB00030617",
"PUB00033622",
"PUB00033623",
"PUB00033624",
"PUB00033625"
] | [
"2466700",
"2732710",
"1875194",
"3194229",
"2823471",
"9878607",
"9309225",
"2759231",
"8709232",
"11531403",
"10827187"
] | [
"Nucleotide sequence and organization of potato leafroll virus genomic RNA.",
"Nucleotide sequence of potato leafroll luteovirus RNA.",
"The nucleotide sequence and luteovirus-like nature of RNA 1 of an aphid non-transmissible strain of pea enation mosaic virus.",
"Nucleotide sequence of beet western yellows ... | [
1989,
1989,
1991,
1988,
1987,
1998,
1997,
1989,
1996,
2001,
2000
] | 11 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"viral metagenome"
] | [
43,
6868,
41
] | 3 | [] | [] | 0 | true | Family | RNA-directed RNA polymerase, luteovirus | RNA-directed RNA polymerase, luteovirus | RNA-dir_pol_luteovirus | 8 |
IPR001796 | 1,796 | Dihydrofolate reductase domain | DHFR_dom | Domain | 30,567 | false | false | Dihydrofolate reductase (DHFR) ( ) catalyses the NADPH-dependent reduction of dihydrofolate to tetrahydrofolate, which can be used in de novo synthesis both certain amino acids, purines and deoxythymidine phosphate (the precursors of DNA synthesis) [ ], and important also in the conversion of deoxyuridine monophosphate... | [
"GO:0004146",
"GO:0046654"
] | [
"dihydrofolate reductase activity",
"tetrahydrofolate biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE",
"CDD"
] | [
"PF00186",
"PS51330",
"cd00209"
] | [
"DHFR_1",
"DHFR_2",
"DHFR"
] | [
30375,
30141,
29726
] | 3 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.5.1.3",
"GenProp0038",
"GenProp1356",
"PWY-3841",
"PWY-6614",
"PDOC00072",
"R-CEL-196757",
"R-DME-196757",
"R-HSA-1474151",
"R-HSA-196757",
"R-HSA-69205",
"R-MMU-196757",
"R-RNO-196757",
"R-SCE-196757",
"R-SPO-196757"
] | [
"EC:1.5.1.3",
"GP:GenProp0038",
"GP:GenProp1356",
"METACYC:PWY-3841",
"METACYC:PWY-6614",
"PROSITEDOC:PDOC00072",
"REACTOME:R-CEL-196757",
"REACTOME:R-DME-196757",
"REACTOME:R-HSA-1474151",
"REACTOME:R-HSA-196757",
"REACTOME:R-HSA-69205",
"REACTOME:R-MMU-196757",
"REACTOME:R-RNO-196757",
"... | 15 | [
"1ai9",
"1ao8",
"1aoe",
"1boz",
"1bzf",
"1cd2",
"1cz3",
"1d1g",
"1daj",
"1ddr",
"1dds",
"1df7",
"1dg5",
"1dg7",
"1dg8",
"1dhf",
"1dhi",
"1dhj",
"1dis",
"1diu",
"1dlr",
"1dls",
"1dr1",
"1dr2",
"1dr3",
"1dr4",
"1dr5",
"1dr6",
"1dr7",
"1dra",
"1drb",
"1dre"... | 671 | [
"PUB00001361",
"PUB00002379",
"PUB00002387",
"PUB00003657",
"PUB00005107"
] | [
"3383852",
"500653",
"6815178",
"2601715",
"2830673"
] | [
"Crystal structure of human dihydrofolate reductase complexed with folate.",
"Porcine liver dihydrofolate reductase. Purification, properties, and amino acid sequence.",
"Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and b... | [
1988,
1979,
1982,
1989,
1988
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid R483",
"Viruses",
"unclassified sequences"
] | [
479,
22121,
6722,
1,
857,
387
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
18,
1,
3,
2,
1,
6,
2,
1,
6,
4,
1,
1,
19
] | 13 | true | Domain | Dihydrofolate reductase domain | Dihydrofolate reductase domain | DHFR_dom | 1 |
IPR001799 | 1,799 | Ephrin receptor-binding domain | Ephrin_RBD | Domain | 8,863 | false | false | Ephrins are a family of proteins [ ] that are ligands of class V (EPH-related) receptor protein-tyrosine kinases. Initially identified as regulators of axon pathfinding and neuronal cell migration, the Eph receptors and their ephrin ligands are now known to have roles in many other cell-cell interactions, including tho... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF00812",
"PR01347",
"PS51551"
] | [
"Ephrin",
"EPHRIN",
"EPHRIN_RBD_2"
] | [
8704,
8057,
8790
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC01003",
"R-BTA-2682334",
"R-BTA-3928663",
"R-BTA-3928665",
"R-CEL-2682334",
"R-CEL-3928662",
"R-CEL-3928663",
"R-CEL-3928664",
"R-CEL-3928665",
"R-DRE-2682334",
"R-DRE-3928663",
"R-DRE-3928665",
"R-HSA-2682334",
"R-HSA-3928662",
"R-HSA-3928663",
"R-HSA-3928664",
"R-HSA-3928665",... | [
"PROSITEDOC:PDOC01003",
"REACTOME:R-BTA-2682334",
"REACTOME:R-BTA-3928663",
"REACTOME:R-BTA-3928665",
"REACTOME:R-CEL-2682334",
"REACTOME:R-CEL-3928662",
"REACTOME:R-CEL-3928663",
"REACTOME:R-CEL-3928664",
"REACTOME:R-CEL-3928665",
"REACTOME:R-DRE-2682334",
"REACTOME:R-DRE-3928663",
"REACTOME:... | 27 | [
"1iko",
"1kgy",
"1shw",
"1shx",
"2hle",
"2i85",
"2vsk",
"2vsm",
"2wo2",
"2wo3",
"2x11",
"3czu",
"3d12",
"3gxu",
"3hei",
"3mbw",
"3mx0",
"4bk5",
"4bka",
"4bkf",
"4l0p",
"4m4r",
"4uf7",
"6p7s",
"6p7y",
"6pdl",
"6thg",
"9dvd"
] | 28 | [
"PUB00004495",
"PUB00010665",
"PUB00021838"
] | [
"7838529",
"11780069",
"11703926"
] | [
"Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins.",
"Crystal structure of an Eph receptor-ephrin complex.",
"Crystal structure of an ephrin ectodomain."
] | [
1995,
2001,
2001
] | 3 | [] | [
"IPR034252",
"IPR034255"
] | 0 | 2 | 0 | [
"Eukaryota",
"Pseudomonadati"
] | [
8855,
8
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
20,
1,
15,
20,
39
] | 6 | true | Domain | Ephrin receptor-binding domain | Ephrin receptor-binding domain | Ephrin_RBD | 1 |
IPR001800 | 1,800 | Lipoprotein, OspC-type | Lipoprotein_OspC | Family | 1,223 | false | false | Members of this family are lipoproteins that are probably involved in evasion of the host immune system by Spirochaeta pathogens [ ]. Borrelia burgdorferi, the causative agent of Lyme disease, has the potential of producing more than 100 different lipoproteins that could become anchored to the outer membrane [ ]. One o... | [
"GO:0009279"
] | [
"cell outer membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF01441"
] | [
"Lipoprotein_6"
] | [
1223
] | 1 | [] | [] | [] | 0 | [
"1f1m",
"1g5z",
"1ggq",
"1yjg",
"2ga0",
"7bml",
"7nen",
"7uij",
"7uj2",
"7uj6",
"9bif",
"9c1s",
"9c24"
] | 13 | [
"PUB00004268",
"PUB00019466",
"PUB00086562"
] | [
"9403685",
"10672174",
"26438793"
] | [
"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.",
"A bacterial genome in flux: the twelve linear and nine circular extrachromosomal DNAs in an infectious isolate of the Lyme disease spirochete Borrelia burgdorferi.",
"Outer surface protein OspC is an antiphagocytic factor that protects Bo... | [
1997,
2000,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Borreliaceae"
] | [
1223
] | 1 | [] | [] | 0 | true | Family | Lipoprotein, OspC-type | Lipoprotein, OspC-type | Lipoprotein_OspC | 8 |
IPR001801 | 1,801 | DNA-binding protein H-NS-like | Histone_HNS | Family | 3,915 | false | false | The histone-like nucleoid-structuring (H-NS) protein is a DNA-binding protein implicated in transcriptional repression (silencing) as well as in bacterial chromosome organisation [ ]. H-NS binds tightly to AT-rich dsDNA, increases its thermal stability and inhibits transcription. It also binds to ssDNA and RNA but with... | [
"GO:0003677",
"GO:0030527",
"GO:0006355"
] | [
"DNA binding",
"structural constituent of chromatin",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF002096"
] | [
"HnS"
] | [
3915
] | 1 | [
"GP",
"GP",
"GP"
] | [
"GenProp0052",
"GenProp1182",
"GenProp1206"
] | [
"GP:GenProp0052",
"GP:GenProp1182",
"GP:GenProp1206"
] | 3 | [
"3nr7"
] | 1 | [
"PUB00001682",
"PUB00064539"
] | [
"7875316",
"18387844"
] | [
"Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli.",
"New insights into transcriptional regulation by H-NS."
] | [
1995,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"biofilter metagenome"
] | [
3908,
6,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | DNA-binding protein H-NS-like | DNA-binding protein H-NS-like | Histone_HNS | 7 |
IPR001802 | 1,802 | Mercuric transport protein periplasmic component/copper chaperone CopZ | MerP/CopZ | Family | 3,845 | false | false | This entry includes a group of metal binding proteins, including copper chaperone CopZ [ ] and mercuric transport protein periplasmic component MerP. They both contain a heavy-metal-associated (HMA) domain. | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00946"
] | [
"HGSCAVENGER"
] | [
3845
] | 1 | [] | [] | [] | 0 | [
"1afi",
"1afj",
"1jww",
"1kqk",
"1osd",
"1p6t",
"1s6o",
"1s6u",
"2gcf",
"2hqi",
"2rml",
"2voy",
"2xmw",
"4a48",
"4a4j",
"6ff2"
] | 16 | [
"PUB00000447",
"PUB00043383"
] | [
"9188683",
"18048940"
] | [
"Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system.",
"Molecular characterization of the copper transport system in Staphylococcus aureus."
] | [
1997,
2007
] | 2 | [] | [
"IPR011795"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"plasmids",
"unclassified sequences",
"uncultured virus"
] | [
110,
3585,
56,
2,
91,
1
] | 6 | [] | [] | 0 | true | Family | Mercuric transport protein periplasmic component/copper chaperone CopZ | Mercuric transport protein periplasmic component/copper chaperone CopZ | MerP/CopZ | 5 |
IPR001803 | 1,803 | Orbivirus inner capsid protein VP7 | Orbi_VP7_capsid | Family | 641 | false | false | Bluetongue virus is a representative of the Orbivirus genus of the Reoviridae [ ]. Orbiviruses infect mammalian hosts through insect vectors, causing economically-important diseases of domesticated animals [ ]. They possess a segmented, double-stranded RNA genome within a capsid that comprises four major polypeptides, ... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF00897",
"PR00903"
] | [
"Orbi_VP7",
"VP7CAPSID"
] | [
641,
619
] | 2 | [
"GP"
] | [
"GenProp1006"
] | [
"GP:GenProp1006"
] | 1 | [
"1ahs",
"1bvp",
"2btv"
] | 3 | [
"PUB00003521",
"PUB00004198"
] | [
"8648715",
"7816101"
] | [
"Crystal structure of the top domain of African horse sickness virus VP7: comparisons with bluetongue virus VP7.",
"The crystal structure of bluetongue virus VP7."
] | [
1996,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Riboviria"
] | [
641
] | 1 | [] | [] | 0 | true | Family | Orbivirus inner capsid protein VP7 | Orbivirus inner capsid protein VP7 | Orbi_VP7_capsid | 6 |
IPR001805 | 1,805 | Adenosine kinase | Adenokinase | Family | 7,630 | false | false | Adenosine kinase (ADK) phosphorylates adenosine and other related nucleosides [ , ]. It is exclusive to eukaryotes [ ] and is a key enzyme in the purine salvage pathway. ADK catalyses the reaction: Adenosine + ATP = ADP + AMP This reaction prevents toxic levels of adenosine building up within the cell. Experiments have... | [
"GO:0004001",
"GO:0006166"
] | [
"adenosine kinase activity",
"purine ribonucleoside salvage"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS",
"PANTHER"
] | [
"PR00989",
"PTHR45769"
] | [
"ADENOKINASE",
""
] | [
6569,
7557
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.20",
"PWY-6619",
"R-DDI-74217",
"R-DDI-9755088",
"R-HSA-74217",
"R-HSA-9755088",
"R-MMU-74217",
"R-MMU-9755088",
"R-RNO-74217",
"R-RNO-9755088",
"R-SCE-74217",
"R-SCE-9755088",
"R-SPO-74217",
"R-SPO-9755088"
] | [
"EC:2.7.1.20",
"METACYC:PWY-6619",
"REACTOME:R-DDI-74217",
"REACTOME:R-DDI-9755088",
"REACTOME:R-HSA-74217",
"REACTOME:R-HSA-9755088",
"REACTOME:R-MMU-74217",
"REACTOME:R-MMU-9755088",
"REACTOME:R-RNO-74217",
"REACTOME:R-RNO-9755088",
"REACTOME:R-SCE-74217",
"REACTOME:R-SCE-9755088",
"REACTO... | 14 | [
"1bx4",
"1dgm",
"1lii",
"1lij",
"1lik",
"1lio",
"2a9y",
"2a9z",
"2aa0",
"2ab8",
"2abs",
"2i6a",
"2i6b",
"2xtb",
"3loo",
"3otx",
"3uq6",
"3uq9",
"3vaq",
"3vas",
"4dc3",
"4n08",
"4n09",
"4o1l",
"5kb5",
"5kb6",
"8rf7",
"8rgj",
"8rpa",
"9fw6"
] | 30 | [
"PUB00000259",
"PUB00001470",
"PUB00001483",
"PUB00004319",
"PUB00004876"
] | [
"9070863",
"8917457",
"9650842",
"9654340",
"8577746"
] | [
"Cloning and expression of the adenosine kinase gene from rat and human tissues.",
"Cloning and characterization of cDNA for adenosine kinase from mammalian (Chinese hamster, mouse, human and rat) species. High frequency mutants of Chinese hamster ovary cells involve structural alterations in the gene.",
"Adeno... | [
1997,
1996,
1998,
1998,
1996
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
67,
7563
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
8,
1,
4,
6,
11,
6,
1,
10,
6,
1,
1,
18
] | 12 | true | Family | Adenosine kinase | Adenosine kinase | Adenokinase | 1 |
IPR001806 | 1,806 | Small GTPase | Small_GTPase | Family | 317,648 | false | false | Small GTPases form an independent superfamily within the larger class of regulatory GTP hydrolases. This superfamily contains proteins that control a vast number of important processes and possess a common, structurally preserved GTP-binding domain [ , ]. Sequence comparisons of small G proteins from various species ha... | [
"GO:0003924",
"GO:0005525"
] | [
"GTPase activity",
"GTP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00071",
"PS51421",
"SM00174"
] | [
"Ras",
"RAS",
"RHO"
] | [
316339,
269884,
270421
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114604",
"R-BTA-114608",
"R-BTA-1222556",
"R-BTA-1257604",
"R-BTA-1655829",
"R-BTA-1660499",
"R-BTA-170968",
"R-BTA-170984",
"R-BTA-181429",
"R-BTA-181430",
"R-BTA-182971",
"R-BTA-193634",
"R-BTA-198203",
"R-BTA-2029482",
"R-BTA-209563",
"R-BTA-210500",
"R-BTA-212676",
"R-BT... | [
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1655829",
"REACTOME:R-BTA-1660499",
"REACTOME:R-BTA-170968",
"REACTOME:R-BTA-170984",
"REACTOME:R-BTA-181429",
"REACTOME:R-BTA-181430",
"REACTOME:R-BTA-182971",
"REACTOME:R-BTA... | 1,249 | [
"121p",
"1a2b",
"1a4r",
"1aa9",
"1agp",
"1aje",
"1am4",
"1an0",
"1bkd",
"1byu",
"1c1y",
"1cc0",
"1cee",
"1cf4",
"1clu",
"1crp",
"1crq",
"1crr",
"1ctq",
"1cxz",
"1d5c",
"1doa",
"1dpf",
"1ds6",
"1e0a",
"1e96",
"1ees",
"1ek0",
"1foe",
"1ftn",
"1g16",
"1g17"... | 1,543 | [
"PUB00000348",
"PUB00004087",
"PUB00015117",
"PUB00023196",
"PUB00052600"
] | [
"2029511",
"1898771",
"11995995",
"2196171",
"2122258"
] | [
"The ras protein family: evolutionary tree and role of conserved amino acids.",
"The GTPase superfamily: conserved structure and molecular mechanism.",
"Structure of small G proteins and their regulators.",
"Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implicat... | [
1991,
1991,
2001,
1990,
1990
] | 5 | [] | [
"IPR002041",
"IPR003578",
"IPR017231",
"IPR017358",
"IPR020849",
"IPR021181",
"IPR030697",
"IPR037872",
"IPR039677",
"IPR041822",
"IPR041824",
"IPR041826",
"IPR041828",
"IPR041830",
"IPR041833",
"IPR041835",
"IPR041836",
"IPR041837",
"IPR042227",
"IPR050209",
"IPR050227"
] | 0 | 21 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
210,
1085,
315456,
180,
717
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
289,
108,
412,
180,
563,
451,
31,
164,
532,
26,
19,
446
] | 12 | true | Family | Small GTPase | Small GTPase | Small_GTPase | 3 |
IPR001807 | 1,807 | Chloride channel | ClC | Family | 63,971 | false | false | Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t... | [
"GO:0015108",
"GO:0006821",
"GO:0055085",
"GO:0016020"
] | [
"chloride transmembrane transporter activity",
"chloride transport",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"PRINTS"
] | [
"PF00654",
"PR00762"
] | [
"Voltage_CLC",
"CLCHANNEL"
] | [
63721,
58965
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-2672351",
"R-CEL-2672351",
"R-CFA-2672351",
"R-DDI-2672351",
"R-DME-2672351",
"R-HSA-2672351",
"R-HSA-6802952",
"R-MMU-2672351",
"R-RNO-2672351",
"R-SCE-2672351",
"R-SPO-2672351",
"R-SSC-2672351"
] | [
"REACTOME:R-BTA-2672351",
"REACTOME:R-CEL-2672351",
"REACTOME:R-CFA-2672351",
"REACTOME:R-DDI-2672351",
"REACTOME:R-DME-2672351",
"REACTOME:R-HSA-2672351",
"REACTOME:R-HSA-6802952",
"REACTOME:R-MMU-2672351",
"REACTOME:R-RNO-2672351",
"REACTOME:R-SCE-2672351",
"REACTOME:R-SPO-2672351",
"REACTOM... | 12 | [
"1kpk",
"1kpl",
"1ots",
"1ott",
"1otu",
"2exw",
"2exy",
"2ez0",
"2fec",
"2fed",
"2fee",
"2h2p",
"2h2s",
"2hlf",
"2ht2",
"2ht3",
"2ht4",
"2htk",
"2htl",
"2r9h",
"3det",
"3ejy",
"3ejz",
"3nd0",
"3nmo",
"3org",
"3q17",
"4ene",
"4fg6",
"4kjp",
"4kjq",
"4kjw"... | 118 | [
"PUB00000734",
"PUB00001999",
"PUB00004085",
"PUB00004230",
"PUB00004913",
"PUB00155406"
] | [
"9046241",
"7581380",
"2174129",
"8559248",
"9207144",
"29845874"
] | [
"Chloride channels: an emerging molecular picture.",
"Myotonia levior is a chloride channel disorder.",
"Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes.",
"A common molecular basis for three inherited kidney stone diseases.",
"Transmembrane topology... | [
1997,
1995,
1990,
1996,
1997,
2018
] | 6 | [] | [
"IPR002242",
"IPR002243",
"IPR002244",
"IPR002245",
"IPR002246",
"IPR002247",
"IPR002248",
"IPR002249",
"IPR002250",
"IPR002251",
"IPR022969",
"IPR023790",
"IPR023861"
] | 0 | 13 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sylvanvirus sp.",
"unclassified sequences"
] | [
463,
30983,
32105,
1,
419
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
35,
27,
71,
7,
3,
57,
54,
4,
34,
53,
1,
2,
102
] | 13 | true | Family | Chloride channel | Chloride channel | ClC | 9 |
IPR001809 | 1,809 | Outer surface lipoprotein, Borrelia | OM_lipoprot_Borrelia | Family | 869 | false | false | The ospA and ospB genes encode the major outer membrane proteins of the Lyme disease spirochaete Borrelia burgdorferi [ ]. The deduced gene products OspA and OspB, contain 273 and 296 residues respectively [ ]. The two Osp proteins show a high degree of sequence similarity, indicating a recent evolutionary event. Molec... | [
"GO:0009279"
] | [
"cell outer membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF00820",
"PR00968"
] | [
"Lipoprotein_1",
"OUTRSURFACE"
] | [
869,
835
] | 2 | [] | [] | [] | 0 | [
"1fj1",
"1osp",
"1p4p",
"1rjl",
"2af5",
"2fkg",
"2fkj",
"2g8c",
"2hkd",
"2i5v",
"2i5z",
"2ol6",
"2ol7",
"2ol8",
"2oy1",
"2oy5",
"2oy7",
"2oy8",
"2oyb",
"2pi3",
"3aum",
"3cka",
"3ckf",
"3ckg",
"3ec5",
"3eex",
"5b2a",
"5ys7",
"5z1o",
"6ais",
"6ics",
"6idc"... | 65 | [
"PUB00003793",
"PUB00003832"
] | [
"2761388",
"1560779"
] | [
"Molecular analysis of linear plasmid-encoded major surface proteins, OspA and OspB, of the Lyme disease spirochaete Borrelia burgdorferi.",
"Molecular analysis and expression of a Borrelia burgdorferi gene encoding a 22 kDa protein (pC) in Escherichia coli."
] | [
1989,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Borreliaceae"
] | [
869
] | 1 | [] | [] | 0 | true | Family | Outer surface lipoprotein, Borrelia | Outer surface lipoprotein, Borrelia | OM_lipoprot_Borrelia | 3 |
IPR001810 | 1,810 | F-box domain | F-box_dom | Domain | 415,530 | false | false | First identified in cyclin-F as a protein-protein interaction motif, the F-box is a conserved domain that is present in numerous proteins with a bipartite structure [ ]. Through the F-box, these proteins are linked to the Skp1 protein and the core of SCFs (Skp1-cullin-F-box protein ligase) complexes. SCFs complexes con... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00646",
"PF12937",
"PF13013",
"PF15966",
"PS50181",
"SM00256"
] | [
"F-box",
"F-box-like",
"F-box-like_2",
"F-box_4",
"FBOX",
"FBOX"
] | [
173074,
197940,
316,
2738,
265366,
187432
] | 6 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1754",
"PDOC50181",
"R-BTA-8951664",
"R-BTA-917937",
"R-BTA-983168",
"R-CEL-8951664",
"R-CEL-983168",
"R-CFA-8951664",
"R-CFA-983168",
"R-DDI-193648",
"R-DDI-9013148",
"R-DDI-9013149",
"R-DDI-9013423",
"R-DDI-9013424",
"R-DRE-174113",
"R-DRE-176408",
"R-DRE-176417",
"R-DRE-... | [
"GP:GenProp1754",
"PROSITEDOC:PDOC50181",
"REACTOME:R-BTA-8951664",
"REACTOME:R-BTA-917937",
"REACTOME:R-BTA-983168",
"REACTOME:R-CEL-8951664",
"REACTOME:R-CEL-983168",
"REACTOME:R-CFA-8951664",
"REACTOME:R-CFA-983168",
"REACTOME:R-DDI-193648",
"REACTOME:R-DDI-9013148",
"REACTOME:R-DDI-9013149... | 120 | [
"1fqv",
"1fs1",
"1fs2",
"1ldk",
"1nex",
"1p22",
"2ass",
"2ast",
"2e31",
"2e32",
"2ovp",
"2ovq",
"2ovr",
"2p1m",
"2p1n",
"2p1o",
"2p1p",
"2p1q",
"3c6n",
"3c6o",
"3c6p",
"3hjl",
"3l2o",
"3mks",
"3v7d",
"3wso",
"4i6j",
"4ui9",
"5hyw",
"5hzg",
"5ibk",
"5jh5"... | 96 | [
"PUB00000938",
"PUB00000952",
"PUB00018180",
"PUB00018181"
] | [
"8706131",
"9346238",
"9529603",
"10581972"
] | [
"SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box.",
"F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex.",
"Proteolysis and the G1-S transition: the SCF connection.",
"The F-box: a new motif for ub... | [
1996,
1997,
1998,
1999
] | 4 | [] | [
"IPR047505",
"IPR047922",
"IPR047932",
"IPR047948",
"IPR048003",
"IPR053781"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
3,
1033,
412403,
1982,
109
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
2756,
405,
234,
67,
210,
207,
37,
1685,
267,
11,
15,
828
] | 12 | true | Domain | F-box domain | F-box domain | F-box_dom | 5 |
IPR001811 | 1,811 | Chemokine interleukin-8-like domain | Chemokine_IL8-like_dom | Domain | 26,157 | false | false | Many low-molecular weight factors secreted by cells including fibroblasts, macrophages and endothelial cells, in response to a variety of stimuli such as growth factors, interferons, viral transformation and bacterial products, are structurally related [ , , ]. Most members of this family of proteins seem to have mitog... | [
"GO:0008009",
"GO:0006955",
"GO:0005576"
] | [
"chemokine activity",
"immune response",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF00048",
"SM00199"
] | [
"IL8",
"SCY"
] | [
26143,
22367
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-375276",
"R-BTA-380108",
"R-BTA-418594",
"R-BTA-6798695",
"R-CFA-375276",
"R-CFA-380108",
"R-CFA-418594",
"R-DRE-380108",
"R-DRE-418594",
"R-GGA-380108",
"R-GGA-416476",
"R-GGA-418594",
"R-GGA-6798695",
"R-HSA-114608",
"R-HSA-1251985",
"R-HSA-140875",
"R-HSA-202733",
"R-HSA-... | [
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-380108",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CFA-375276",
"REACTOME:R-CFA-380108",
"REACTOME:R-CFA-418594",
"REACTOME:R-DRE-380108",
"REACTOME:R-DRE-418594",
"REACTOME:R-GGA-380108",
"REACTOME:R-GGA-416476",
"REACTOME:R-GGA-41... | 54 | [
"1a15",
"1b2t",
"1b3a",
"1b50",
"1b53",
"1bo0",
"1cm9",
"1dok",
"1dol",
"1dom",
"1don",
"1eig",
"1eih",
"1el0",
"1eot",
"1eqt",
"1esr",
"1f2l",
"1f9p",
"1f9q",
"1f9r",
"1f9s",
"1g2s",
"1g2t",
"1g91",
"1ha6",
"1hfg",
"1hfn",
"1hhv",
"1hrj",
"1hum",
"1hun"... | 253 | [
"PUB00000108",
"PUB00001499",
"PUB00004320"
] | [
"1910690",
"2687068",
"2149646"
] | [
"Properties of the novel proinflammatory supergene \"intercrine\" cytokine family.",
"Macrophage inflammatory proteins 1 and 2: members of a novel superfamily of cytokines.",
"Two burgeoning families of platelet factor 4-related proteins: mediators of the inflammatory response."
] | [
1991,
1989,
1990
] | 3 | [] | [
"IPR033899",
"IPR034127",
"IPR034133"
] | 0 | 3 | 0 | [
"Bilateria",
"Viruses"
] | [
25904,
253
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
100,
93,
99,
110
] | 4 | true | Domain | Chemokine interleukin-8-like domain | Chemokine interleukin-8-like domain | Chemokine_IL8-like_dom | 9 |
IPR001815 | 1,815 | Trichovirus movement protein | Trichovirus_mp | Family | 741 | false | false | ORF2 of the capilloviruses (trichoviruses) contain a serine peptidase signature which belongs to the MEROPS peptidase family S35 (clan PA(S)). In a number of capilloviruses that have been sequenced to date ORF2 has been identified as the putative movement protein, though it also contains the consensus sequence Gly-Asp-... | [
"GO:0004252",
"GO:0006508"
] | [
"serine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00995"
] | [
"CAPILLOPTASE"
] | [
741
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005590"
] | [
"1413530"
] | [
"The nucleotide sequence of apple stem grooving capillovirus genome."
] | [
1992
] | 1 | [
"IPR028919"
] | [] | 1 | 0 | 1 | [
"Ananas comosus var. bracteatus",
"Viruses"
] | [
1,
740
] | 2 | [] | [] | 0 | true | Family | Trichovirus movement protein | Trichovirus movement protein | Trichovirus_mp | 6 |
IPR001817 | 1,817 | Vasopressin receptor | Vasoprsn_rcpt | Family | 6,854 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0005000",
"GO:0007186",
"GO:0016020"
] | [
"vasopressin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00896"
] | [
"VASOPRESSINR"
] | [
6854
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-388479",
"R-BTA-416476",
"R-BTA-418555",
"R-BTA-432040",
"R-BTA-8856825",
"R-BTA-8856828",
"R-HSA-375276",
"R-HSA-388479",
"R-HSA-416476",
"R-HSA-418555",
"R-HSA-432040",
"R-HSA-5619099",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-9036092",
"R-MMU-375276",
"R-MMU-388479",
"R-M... | [
"REACTOME:R-BTA-388479",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-432040",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-388479",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-432040",
"REACTOME:R-HSA-5... | 28 | [
"6tpk",
"7bb6",
"7bb7",
"7kh0",
"7qvm",
"7r0c",
"7ryc",
"9hap",
"9hb3"
] | 9 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR000276"
] | [
"IPR000161",
"IPR000628",
"IPR001224",
"IPR002062"
] | 1 | 4 | 0 | [
"Bilateria"
] | [
6854
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
11,
4,
16,
15,
18
] | 6 | true | Family | Vasopressin receptor | Vasopressin receptor | Vasoprsn_rcpt | 3 |
IPR001819 | 1,819 | Chromogranin A/B | Chromogranin_AB | Family | 1,960 | false | false | Chromogranins and secretogranins are acidic proteins present in the secretory granules of endocrine and neuro-endocrine cells [ , ]. Granins may be precursors of biologically-active peptides, or they may be helper proteins in the packaging of peptide hormones and neuropeptides - their precise role is unclear. Chromogra... | [
"GO:0030141"
] | [
"secretory granule"
] | [
"cellular_component"
] | 1 | [
"PRINTS",
"PANTHER"
] | [
"PR00659",
"PTHR10583"
] | [
"CHROMOGRANIN",
""
] | [
1677,
1943
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00365",
"R-HSA-381426",
"R-HSA-6803157",
"R-HSA-8957275",
"R-MMU-381426",
"R-MMU-6803157",
"R-MMU-8957275",
"R-RNO-381426",
"R-RNO-6803157",
"R-RNO-8957275",
"R-SSC-381426",
"R-SSC-8957275"
] | [
"PROSITEDOC:PDOC00365",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-6803157",
"REACTOME:R-HSA-8957275",
"REACTOME:R-MMU-381426",
"REACTOME:R-MMU-6803157",
"REACTOME:R-MMU-8957275",
"REACTOME:R-RNO-381426",
"REACTOME:R-RNO-6803157",
"REACTOME:R-RNO-8957275",
"REACTOME:R-SSC-381426",
"REACTOME:R-SS... | 12 | [] | 0 | [
"PUB00000478",
"PUB00005374"
] | [
"2684154",
"2053134"
] | [
"Biochemistry of the chromogranin A protein family.",
"The granin (chromogranin/secretogranin) family."
] | [
1989,
1991
] | 2 | [
"IPR001990"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
1960
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
7,
8,
16
] | 4 | true | Family | Chromogranin A/B | Chromogranin A/B | Chromogranin_AB | 7 |
IPR001820 | 1,820 | Protease inhibitor I35 (TIMP) | TIMP | Family | 5,356 | false | false | Tissue inhibitors of metalloproteinases (TIMPs, [ , , , , ]) and their target matrix metalloproteinases (MMPs, MEROPS peptidase family M10A) are important in connective tissue re-modelling in diseases of the cardiovascular system and in the physiological degradation of connective tissue, as well as in pathological stat... | [
"GO:0008191"
] | [
"metalloendopeptidase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PANTHER",
"SMART"
] | [
"PF00965",
"PTHR11844",
"SM00206"
] | [
"TIMP",
"",
"NTR"
] | [
5256,
4998,
4263
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00260",
"R-CEL-114608",
"R-CEL-1592389",
"R-CEL-381426",
"R-CEL-6798695",
"R-CEL-8957275",
"R-CFA-1592389",
"R-CFA-6798695",
"R-CFA-9839383",
"R-DME-114608",
"R-DME-1592389",
"R-DME-381426",
"R-DME-6798695",
"R-DME-8957275",
"R-GGA-114608",
"R-HSA-114608",
"R-HSA-1592389",
"R-... | [
"PROSITEDOC:PDOC00260",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-1592389",
"REACTOME:R-CEL-381426",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-8957275",
"REACTOME:R-CFA-1592389",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-9839383",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-1592389",
"REACTOME:R-D... | 35 | [
"1bqq",
"1br9",
"1buv",
"1d2b",
"1gxd",
"1oo9",
"1uea",
"2e2d",
"2j0t",
"2tmp",
"3cki",
"3ma2",
"3v96",
"4ilw",
"6mav",
"6n9d",
"7s7l",
"7s7m",
"9sop",
"9soq",
"9sos"
] | 21 | [
"PUB00000392",
"PUB00000485",
"PUB00001508",
"PUB00002515",
"PUB00002738",
"PUB00015035",
"PUB00062660",
"PUB00095218"
] | [
"7918391",
"2163605",
"1850705",
"2793861",
"1512267",
"12032297",
"22427646",
"23522389"
] | [
"Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family.",
"Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP).",
"Matrix metalloproteinases and their inhibitors in connective tissue remodeling.",
"Tissue i... | [
1994,
1990,
1991,
1989,
1992,
2002,
2012,
2013
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nitrosopumilus sediminis",
"Eukaryota",
"metagenome"
] | [
231,
1,
5123,
1
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
8,
1,
17,
17,
13
] | 6 | true | Family | Protease inhibitor I35 (TIMP) | Protease inhibitor I35 (TIMP) | TIMP | 7 |
IPR001821 | 1,821 | [NiFe]-hydrogenase, small subunit | NiFe_hydrogenase_ssu | Family | 7,554 | false | false | Hydrogenases catalyse the reversible oxidation of molecular hydrogen and play a vital role in anaerobic metabolism. Metal-containing hydrogenases are subdivided into three classes: Fe ('iron only') hydrogenases; Ni-Fe hydrogenases; and Ni-Fe-Se hydrogenases [ ]. Hydrogen oxidation is coupled to the reduction of electro... | [
"GO:0008901",
"GO:0051536",
"GO:0009375"
] | [
"ferredoxin hydrogenase activity",
"iron-sulfur cluster binding",
"ferredoxin hydrogenase complex"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"PIRSF000310",
"PTHR30013",
"TIGR00391"
] | [
"NiFe_hyd_ssu",
"",
"hydA"
] | [
6929,
7553,
4961
] | 3 | [
"EC",
"GP",
"GP",
"GP"
] | [
"1.12.99.6",
"GenProp1209",
"GenProp1582",
"GenProp1672"
] | [
"EC:1.12.99.6",
"GP:GenProp1209",
"GP:GenProp1582",
"GP:GenProp1672"
] | 4 | [
"1cc1",
"1e3d",
"1frf",
"1frv",
"1h2a",
"1h2r",
"1ubh",
"1ubj",
"1ubk",
"1ubl",
"1ubm",
"1ubo",
"1ubr",
"1ubt",
"1ubu",
"1wuh",
"1wui",
"1wuj",
"1wuk",
"1wul",
"1yq9",
"1yqw",
"1yrq",
"2frv",
"2wpn",
"3ayx",
"3ayz",
"3cur",
"3cus",
"3h3x",
"3myr",
"3rgw"... | 149 | [
"PUB00001739",
"PUB00001742",
"PUB00020978"
] | [
"3078655",
"1558764",
"7854413"
] | [
"The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio.",
"Structure-function relationships among the nickel-containing hydrogenases.",
"Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas."
] | [
1988,
1992,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
241,
7194,
3,
116
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | [NiFe]-hydrogenase, small subunit | [NiFe]-hydrogenase, small subunit | NiFe_hydrogenase_ssu | 9 |
IPR001826 | 1,826 | RHS protein, conserved region | RHS | Domain | 5,350 | false | false | This entry represents a conserved region found in RHS (Rearrangement hotspot) proteins. RHS (Rearrangement hotspot) proteins are distantly related to the wall-associated protein A (WapA) and mediate intercellular competition. The protein sequences comprise highly conserved 141kDa domain containing multiple tandem 22-re... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03527"
] | [
"RHS"
] | [
5350
] | 1 | [] | [] | [] | 0 | [
"8cp6",
"8uxt",
"8uy4"
] | 3 | [
"PUB00002114",
"PUB00003864",
"PUB00088067",
"PUB00097193"
] | [
"2403547",
"7934896",
"23572593",
"32641830"
] | [
"Structure of the rhsA locus from Escherichia coli K-12 and comparison of rhsA with other members of the rhs multigene family.",
"Rhs elements of Escherichia coli: a family of genetic composites each encoding a large mosaic protein.",
"Rhs proteins from diverse bacteria mediate intercellular competition.",
"A... | [
1990,
1994,
2013,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes",
"uncultured Caudovirales phage"
] | [
5321,
5,
22,
2
] | 4 | [
"Escherichia coli (strain K12)"
] | [
8
] | 1 | true | Domain | RHS protein, conserved region | RHS protein, conserved region | RHS | 6 |
IPR001827 | 1,827 | Homeobox protein, antennapedia type, conserved site | Homeobox_Antennapedia_CS | Conserved_site | 17,985 | false | false | The homeobox is a 60-residue motif first identified in a number of Drosophila homeotic and segmentation proteins, but now known to be well-conserved in many other animals, including vertebrates [ , ]. Proteins containing homeobox domains are likely to play an important role in development - most are known to be sequenc... | [
"GO:0003677",
"GO:0003700",
"GO:0006355"
] | [
"DNA binding",
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00032"
] | [
"ANTENNAPEDIA"
] | [
17985
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00032",
"R-DRE-9762293",
"R-GGA-9762293",
"R-HSA-5617472",
"R-HSA-9010553",
"R-HSA-9762293",
"R-HSA-9830364",
"R-MMU-9762293"
] | [
"PROSITEDOC:PDOC00032",
"REACTOME:R-DRE-9762293",
"REACTOME:R-GGA-9762293",
"REACTOME:R-HSA-5617472",
"REACTOME:R-HSA-9010553",
"REACTOME:R-HSA-9762293",
"REACTOME:R-HSA-9830364",
"REACTOME:R-MMU-9762293"
] | 8 | [
"1b8i",
"2r5y",
"2r5z",
"4cyc",
"4uut"
] | 5 | [
"PUB00000591",
"PUB00000881",
"PUB00005390"
] | [
"2568852",
"1358459",
"1357790"
] | [
"The structure and function of the homeodomain.",
"Vertebrate homeobox gene nomenclature.",
"The homeobox in perspective."
] | [
1989,
1992,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"marine metagenome"
] | [
3,
122,
17859,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
4,
2,
46,
15,
36,
44,
42,
1
] | 8 | true | Conserved_site | Homeobox protein, antennapedia type, conserved site | Homeobox protein, antennapedia type, conserved site | Homeobox_Antennapedia_CS | 2 |
IPR001828 | 1,828 | Receptor, ligand binding region | ANF_lig-bd_rcpt | Domain | 113,531 | false | false | This describes a ligand binding domain and includes extracellular ligand binding domains of a wide range of receptors, as well as the bacterial amino acid binding proteins of known structure [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01094"
] | [
"ANF_receptor"
] | [
113531
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-416476",
"R-BTA-418594",
"R-BTA-420499",
"R-BTA-5578768",
"R-CEL-1296041",
"R-CEL-204005",
"R-CEL-2514859",
"R-CEL-399710",
"R-CEL-418594",
"R-CEL-420499",
"R-CEL-438066",
"R-CEL-5694530",
"R-CEL-8849932",
"R-CEL-977444",
"R-CEL-997272",
"R-CFA-3928662",
"R-CFA-438066",
"R-C... | [
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-420499",
"REACTOME:R-BTA-5578768",
"REACTOME:R-CEL-1296041",
"REACTOME:R-CEL-204005",
"REACTOME:R-CEL-2514859",
"REACTOME:R-CEL-399710",
"REACTOME:R-CEL-418594",
"REACTOME:R-CEL-420499",
"REACTOME:R-CEL-438066",
"REACTOME:R-CEL-... | 116 | [
"1dp4",
"1ewk",
"1ewt",
"1ewv",
"1isr",
"1iss",
"1jdn",
"1jdp",
"1t34",
"1yk0",
"1yk1",
"2e4u",
"2e4v",
"2e4w",
"2e4x",
"2e4y",
"2e4z",
"2wjw",
"2wjx",
"3a3k",
"3h5v",
"3h5w",
"3h6g",
"3h6h",
"3hsy",
"3jpw",
"3jpy",
"3kg2",
"3ks9",
"3lmk",
"3mq4",
"3n6v"... | 615 | [
"PUB00004312"
] | [
"8011339"
] | [
"Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins."
] | [
1994
] | 1 | [] | [
"IPR044440",
"IPR049873"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
140,
907,
112423,
61
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
130,
53,
415,
76,
220,
449,
53,
350,
80
] | 9 | true | Domain | Receptor, ligand binding region | Receptor, ligand binding region | ANF_lig-bd_rcpt | 3 |
IPR001829 | 1,829 | Pili assembly chaperone, bacterial | Pili_assmbl_chaperone_bac | Family | 21,335 | false | false | Most Gram-negative bacteria possess a supramolecular structure - the pili - on their surface, which mediates attachment to specific receptors. Many interactive subunits are required to assemble pili, but their assembly only takes place after translocation across the cytoplasmic membrane. Periplasmic chaperones assist p... | [
"GO:0043711",
"GO:0030288"
] | [
"pilus organization",
"outer membrane-bounded periplasmic space"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00969"
] | [
"CHAPERONPILI"
] | [
21335
] | 1 | [] | [] | [] | 0 | [
"1bf8",
"1kiu",
"1klf",
"1l4i",
"1n0l",
"1p5u",
"1p5v",
"1pdk",
"1qpp",
"1qpx",
"1qun",
"1z9s",
"1ze3",
"2co6",
"2co7",
"2j2z",
"2j7l",
"2os7",
"2uy6",
"2uy7",
"2w07",
"2wmp",
"2xg4",
"2xg5",
"3bwu",
"3dos",
"3dpa",
"3dpb",
"3dsn",
"3f65",
"3f6i",
"3f6l"... | 66 | [
"PUB00000121",
"PUB00001218",
"PUB00001290",
"PUB00041859"
] | [
"1683764",
"1348692",
"8670884",
"17082819"
] | [
"Chaperone-assisted assembly and molecular architecture of adhesive pili.",
"Conserved immunoglobulin-like features in a family of periplasmic pilus chaperones in bacteria.",
"Molecular basis of two subfamilies of immunoglobulin-like chaperones.",
"Molecular mechanism of P pilus termination in uropathogenic E... | [
1991,
1992,
1996,
2006
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
21287,
35,
13
] | 3 | [
"Escherichia coli (strain K12)"
] | [
10
] | 1 | true | Family | Pili assembly chaperone, bacterial | Pili assembly chaperone, bacterial | Pili_assmbl_chaperone_bac | 3 |
IPR001830 | 1,830 | Glycosyl transferase, family 20 | Glyco_trans_20 | Family | 29,595 | false | false | The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferas... | [
"GO:0003824",
"GO:0005992"
] | [
"catalytic activity",
"trehalose biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PANTHER",
"CDD"
] | [
"PF00982",
"PTHR10788",
"cd03788"
] | [
"Glyco_transf_20",
"",
"GT20_TPS"
] | [
28730,
29484,
26157
] | 3 | [
"CAZY",
"EC",
"EC",
"REACTOME"
] | [
"GT20",
"2.4.1",
"2.4.1.15",
"R-MTU-868688"
] | [
"CAZY:GT20",
"EC:2.4.1",
"EC:2.4.1.15",
"REACTOME:R-MTU-868688"
] | 4 | [
"1gz5",
"1uqt",
"1uqu",
"2wtx",
"3t5t",
"3t7d",
"3vdm",
"3vdn",
"4f96",
"4f97",
"4f9f",
"5dx9",
"5dxf",
"5dxi",
"5dxl",
"5dxn",
"5dxo",
"5hus",
"5hut",
"5huu",
"5huv",
"5hvl",
"5hvm",
"5hvo",
"5hxa",
"5jij",
"5jio",
"5k41",
"5k42",
"5k44",
"5k5c",
"5l3k"... | 46 | [
"PUB00001848",
"PUB00006377",
"PUB00009409"
] | [
"8045430",
"9194697",
"9334165"
] | [
"Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex.",
"Structural analysis of the subunits of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cer... | [
1994,
1997,
1997
] | 3 | [] | [
"IPR012764",
"IPR012766"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
310,
12873,
16274,
138
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosacchar... | [
52,
2,
1,
1,
3,
48,
4,
5,
142
] | 9 | true | Family | Glycosyl transferase, family 20 | Glycosyl transferase, family 20 | Glyco_trans_20 | 6 |
IPR001831 | 1,831 | Immunodeficiency virus transactivating regulatory protein (Tat) | IV_Tat | Family | 16,887 | false | false | Like other lentiviruses, Human immunodeficiency virus 1 (HIV-1) encodes a trans-activating regulatory protein (Tat), which is essential for efficient transcription of the viral genome [ , ]. Tat acts by binding to an RNA stem-loop structure, the trans-activating response element (TAR), found at the 5' ends of nascent H... | [
"GO:0001070",
"GO:0050434",
"GO:0042025"
] | [
"RNA-binding transcription regulator activity",
"positive regulation of viral transcription",
"host cell nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PRINTS"
] | [
"MF_04079",
"PF00539",
"PR00055"
] | [
"HIV_TAT",
"Tat",
"HIVTATDOMAIN"
] | [
8955,
16881,
16222
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-167200",
"R-HSA-167238",
"R-HSA-167243",
"R-HSA-167246",
"R-HSA-176034",
"R-HSA-9833482"
] | [
"REACTOME:R-HSA-167200",
"REACTOME:R-HSA-167238",
"REACTOME:R-HSA-167243",
"REACTOME:R-HSA-167246",
"REACTOME:R-HSA-176034",
"REACTOME:R-HSA-9833482"
] | 6 | [
"1jfw",
"1k5k",
"1tac",
"1tbc",
"1tiv",
"1tvs",
"1tvt",
"3mi9",
"3mia",
"3o6l",
"4ogr",
"4or5",
"5l1z",
"6cyt",
"6mce",
"6mcf",
"7t1o",
"7t1p",
"8ccz",
"9de5"
] | 20 | [
"PUB00000079",
"PUB00000839",
"PUB00004167",
"PUB00004851",
"PUB00014504"
] | [
"1883204",
"2117500",
"8121496",
"8058789",
"12126615"
] | [
"The biochemistry of AIDS.",
"Trans-activation by HIV-1 Tat via a heterologous RNA binding protein.",
"Direct interaction of human TFIID with the HIV-1 transactivator tat.",
"NMR structure of a biologically active peptide containing the RNA-binding domain of human immunodeficiency virus type 1 Tat.",
"A bim... | [
1991,
1990,
1994,
1994,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Methylobacterium oryzihabitans",
"Orthoretrovirinae"
] | [
1,
16886
] | 2 | [] | [] | 0 | true | Family | Immunodeficiency virus transactivating regulatory protein (Tat) | Immunodeficiency virus transactivating regulatory protein (Tat) | IV_Tat | 8 |
IPR001834 | 1,834 | NADH:cytochrome b5 reductase-like | CBR-like | Family | 17,113 | false | false | null | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PANTHER"
] | [
"PTHR19370"
] | [
""
] | [
17113
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.6.2.2",
"R-BTA-114608",
"R-BTA-1237044",
"R-BTA-196836",
"R-BTA-211945",
"R-BTA-6798695",
"R-CFA-196836",
"R-CFA-211945",
"R-CFA-6798695",
"R-DDI-114608",
"R-DDI-196836",
"R-DDI-211945",
"R-DDI-6798695",
"R-DRE-1237044",
"R-HSA-114608",
"R-HSA-1237044",
"R-HSA-196836",
"R-HSA-21... | [
"EC:1.6.2.2",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1237044",
"REACTOME:R-BTA-196836",
"REACTOME:R-BTA-211945",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CFA-196836",
"REACTOME:R-CFA-211945",
"REACTOME:R-CFA-6798695",
"REACTOME:R-DDI-114608",
"REACTOME:R-DDI-196836",
"REACTOME:R-DDI-211945",
... | 36 | [
"1cne",
"1cnf",
"1i7p",
"1ib0",
"1ndh",
"1qx4",
"1umk",
"2cnd",
"2eix",
"3w2e",
"3w2f",
"3w2g",
"3w2h",
"3w2i",
"3w5h",
"5gv7",
"5gv8",
"5yly",
"6mv1",
"6mv2",
"7rom",
"7thg",
"7tnv",
"7tsw",
"7w3o"
] | 25 | [
"PUB00000415",
"PUB00002329",
"PUB00002370",
"PUB00002397",
"PUB00002674",
"PUB00004935",
"PUB00005247",
"PUB00005356"
] | [
"7893687",
"3654589",
"8027025",
"6436247",
"1748631",
"2695933",
"7812715",
"2204158"
] | [
"Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution.",
"Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b5 reductase by HPLC mapping.",
"Structure-function relations for ferredoxin reductase.",
"Identification of the NH2-terminal blocking group o... | [
1995,
1987,
1994,
1984,
1991,
1989,
1994,
1990
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
22,
17088,
3
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
2,
5,
8,
31,
12,
5,
11,
24,
5,
2,
31
] | 12 | true | Family | NADH:cytochrome b5 reductase-like | NADH:cytochrome b5 reductase-like | CBR-like | 3 |
IPR001835 | 1,835 | Heat-labile enterotoxin, B chain | Enterotoxin_B | Family | 136 | false | false | Escherichia coli heat-labile enterotoxin is a bacterial protein toxin with an AB5 multimer structure, in which the B pentamer has a membrane-binding function and the A chain ( ) is needed for enzymatic activity [ ]. The B subunits are arranged as a donut-shaped pentamer, each subunit participating in ~30 hydrogen bonds... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF01376",
"PR00772"
] | [
"Enterotoxin_b",
"ENTEROTOXINB"
] | [
136,
136
] | 2 | [
"REACTOME"
] | [
"R-HSA-9760173"
] | [
"REACTOME:R-HSA-9760173"
] | 1 | [
"1b44",
"1chp",
"1chq",
"1ct1",
"1djr",
"1eef",
"1eei",
"1efi",
"1fd7",
"1fgb",
"1g8z",
"1htl",
"1jqy",
"1jr0",
"1llr",
"1lt3",
"1lt4",
"1lt5",
"1lt6",
"1lta",
"1ltb",
"1ltg",
"1lti",
"1ltr",
"1lts",
"1ltt",
"1md2",
"1pzi",
"1pzj",
"1pzk",
"1rcv",
"1rd9"... | 68 | [
"PUB00003304"
] | [
"8478941"
] | [
"Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Affertcholeramvirus",
"Gammaproteobacteria",
"Musa acuminata"
] | [
11,
124,
1
] | 3 | [] | [] | 0 | true | Family | Heat-labile enterotoxin, B chain | Heat-labile enterotoxin, B chain | Enterotoxin_B | 7 |
IPR001839 | 1,839 | Transforming growth factor-beta, C-terminal | TGF-b_C | Domain | 39,415 | false | false | The transforming growth factor-beta (TGF-beta) superfamily comprises a number of structurally related, secreted polypeptides that regulate a multitude of cellular processes including proliferation, differentiation, cell invasion, immune regulation, and neoplastic transformation [ , ]. Family members include the activin... | [
"GO:0008083"
] | [
"growth factor activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00019",
"PS51362",
"SM00204"
] | [
"TGF_beta",
"TGF_BETA_2",
"TGFB"
] | [
39045,
39345,
37103
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00223",
"R-BTA-114608",
"R-BTA-1502540",
"R-BTA-201451",
"R-BTA-209822",
"R-BTA-2129379",
"R-BTA-2173789",
"R-BTA-2473224",
"R-BTA-381426",
"R-BTA-8957275",
"R-BTA-9839389",
"R-BTA-9839406",
"R-CEL-114608",
"R-CEL-201451",
"R-CEL-2129379",
"R-CEL-2173788",
"R-CEL-2173789",
"R-... | [
"PROSITEDOC:PDOC00223",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1502540",
"REACTOME:R-BTA-201451",
"REACTOME:R-BTA-209822",
"REACTOME:R-BTA-2129379",
"REACTOME:R-BTA-2173789",
"REACTOME:R-BTA-2473224",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-9839389",
"REACTOME:R-BT... | 143 | [
"1agq",
"1bmp",
"1es7",
"1kla",
"1klc",
"1kld",
"1ktz",
"1lx5",
"1lxi",
"1m4u",
"1nys",
"1nyu",
"1reu",
"1rew",
"1s4y",
"1tfg",
"1tgj",
"1tgk",
"1waq",
"1zkz",
"2arp",
"2arv",
"2ask",
"2b0u",
"2bhk",
"2gh0",
"2goo",
"2gyr",
"2gyz",
"2h62",
"2h64",
"2p6a"... | 174 | [
"PUB00000211",
"PUB00004939",
"PUB00005153",
"PUB00007614",
"PUB00035159",
"PUB00035160",
"PUB00043835",
"PUB00096668",
"PUB00096669",
"PUB00097278"
] | [
"1575734",
"8199356",
"1631557",
"8679613",
"15032667",
"15180456",
"18662538",
"29109152",
"30696809",
"24086041"
] | [
"Evolutionary grouping of the transforming growth factor-beta superfamily.",
"Evolution of the transforming growth factor-beta superfamily.",
"Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.",
"Transforming growth factor beta 1: three-dimensional structure in solut... | [
1992,
1994,
1992,
1996,
2004,
2004,
2008,
2018,
2019,
2013
] | 10 | [] | [
"IPR000381",
"IPR015616",
"IPR015617",
"IPR047020",
"IPR047833",
"IPR047953"
] | 0 | 6 | 0 | [
"Bacteria",
"Chordopoxvirinae",
"Eukaryota",
"bird metagenome"
] | [
3,
27,
39384,
1
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
113,
11,
120,
85,
114
] | 6 | true | Domain | Transforming growth factor-beta, C-terminal | Transforming growth factor-beta, C-terminal | TGF-b_C | 3 |
IPR001840 | 1,840 | Anaphylatoxin, complement system domain | Anaphylatoxn_comp_syst_dom | Domain | 1,244 | false | false | Complement components C3, C4 and C5 are large glycoproteins that have important functions in the immune response and host defence [ ]. They have a wide variety of biological activities and are proteolytically activated by cleavage at a specific site, forming a-and b-fragments [ ]. A-fragments form distinct structural d... | [
"GO:0006954",
"GO:0006956",
"GO:0005576"
] | [
"inflammatory response",
"complement activation",
"extracellular region"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00004"
] | [
"ANAPHYLATOXN"
] | [
1244
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-173736",
"R-BTA-174577",
"R-BTA-198933",
"R-BTA-375276",
"R-BTA-381426",
"R-BTA-418594",
"R-BTA-6798695",
"R-BTA-8957275",
"R-BTA-977606",
"R-HSA-166663",
"R-HSA-166665",
"R-HSA-173736",
"R-HSA-174577",
"R-HSA-198933",
"R-HSA-375276",
"R-HSA-381426",
"R-HSA-418594",
"R-HSA-6... | [
"REACTOME:R-BTA-173736",
"REACTOME:R-BTA-174577",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-977606",
"REACTOME:R-HSA-166663",
"REACTOME:R-HSA-166665",
"REACTOME:R-HSA-1... | 41 | [
"1c5a",
"1cfa",
"1kjs",
"2a73",
"3cu7",
"3hqa",
"3hqb",
"3kls",
"3km9",
"3prx",
"3pvm",
"4e0s",
"4hw5",
"4hwj",
"4i6o",
"4p39",
"4p3a",
"4p3b",
"4uu9",
"4wb2",
"4wb3",
"5b4p",
"5hcc",
"5hcd",
"5hce",
"5i5k",
"5jpm",
"5jpn",
"6jv7",
"6jv8",
"6rqj",
"6ru5"... | 57 | [
"PUB00001343",
"PUB00002512",
"PUB00003181"
] | [
"3081348",
"2777798",
"1431125"
] | [
"C5a fragment of bovine complement. Purification, bioassays, amino-acid sequence and other structural studies.",
"Sequence of the gene for murine complement component C4.",
"Primary structure of cobra complement component C3."
] | [
1986,
1989,
1992
] | 3 | [
"IPR000020"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1244
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
16,
14
] | 3 | true | Domain | Anaphylatoxin, complement system domain | Anaphylatoxin, complement system domain | Anaphylatoxn_comp_syst_dom | 2 |
IPR001841 | 1,841 | Zinc finger, RING-type | Znf_RING | Domain | 766,300 | false | false | This entry represents RING-type zinc finger domains. The RING-finger is a specialised type of Zn-finger of 40 to 60 residues that binds two atoms of zinc, and is probably involved in mediating protein-protein interactions [ , , ]. There are two different variants, the C3HC4-type and a C3H2C3-type, which are clearly rel... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF13639",
"PF13923",
"PF14634",
"PF17121",
"PF17122",
"PF17123",
"PS50089",
"SM00184"
] | [
"zf-RING_2",
"zf-C3HC4_2",
"zf-RING_5",
"zf-C3HC4_5",
"zf-C3H2C3",
"zf-RING_11",
"ZF_RING_2",
"RING"
] | [
228717,
54050,
10915,
3002,
1415,
7680,
750928,
561677
] | 8 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REAC... | [
"2.3.2",
"2.3.2.27",
"PWY-7511",
"PDOC00449",
"R-BTA-1169408",
"R-BTA-1257604",
"R-BTA-141430",
"R-BTA-166058",
"R-BTA-174048",
"R-BTA-174084",
"R-BTA-174154",
"R-BTA-174178",
"R-BTA-174184",
"R-BTA-176407",
"R-BTA-176408",
"R-BTA-176409",
"R-BTA-176412",
"R-BTA-179409",
"R-BTA-1... | [
"EC:2.3.2",
"EC:2.3.2.27",
"METACYC:PWY-7511",
"PROSITEDOC:PDOC00449",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-141430",
"REACTOME:R-BTA-166058",
"REACTOME:R-BTA-174048",
"REACTOME:R-BTA-174084",
"REACTOME:R-BTA-174154",
"REACTOME:R-BTA-174178",
"REACTOME:R-BTA-174... | 941 | [
"1bor",
"1chc",
"1e4u",
"1f62",
"1fbv",
"1g25",
"1iym",
"1jm7",
"1ldj",
"1ldk",
"1rmd",
"1u6g",
"1ur6",
"1v87",
"1weo",
"1wim",
"1x4j",
"1z6u",
"2ckl",
"2csy",
"2ct0",
"2ct2",
"2d8s",
"2d8t",
"2djb",
"2ea5",
"2ea6",
"2ecg",
"2eci",
"2ecj",
"2ecl",
"2ecm"... | 578 | [
"PUB00001094",
"PUB00005712",
"PUB00006216",
"PUB00006474",
"PUB00006516",
"PUB00006565",
"PUB00014077",
"PUB00014857",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"8804826",
"8317827",
"8744354",
"10662664",
"10577187",
"10514377",
"12665246",
"12944364",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"The RING finger domain: a recent example of a sequence-structure family.",
"The RING finger. A novel protein sequence motif related to the zinc finger.",
"Does this have a familiar RING?",
"RING for destruction?",
"A new finger on the protein destruction button.",
"The tyrosine kinase negative regulator ... | [
1996,
1993,
1996,
2000,
1999,
1999,
2002,
2003,
2007,
2005,
2005,
1999,
2001
] | 13 | [] | [
"IPR018957",
"IPR024766",
"IPR024991",
"IPR027133",
"IPR027139",
"IPR027370",
"IPR027934",
"IPR028511",
"IPR032043",
"IPR033609",
"IPR035691",
"IPR039503",
"IPR039520",
"IPR039571",
"IPR039804",
"IPR040089",
"IPR040100",
"IPR040178",
"IPR040380",
"IPR041888",
"IPR042656",
"... | 0 | 53 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
47,
638,
761722,
2404,
1489
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
2159,
203,
1253,
288,
1005,
706,
57,
1270,
936,
33,
47,
2333
] | 12 | true | Domain | Zinc finger, RING-type | Zinc finger, RING-type | Znf_RING | 4 |
IPR001843 | 1,843 | Fragilysin | Fragilysin | Family | 32 | false | false | Fragilysin is a metalloprotease toxin which is cytopathic to intestinal epithelial cells and induces fluid secretion and tissue damage in ligated intestinal loops [ ]. | [
"GO:0008237"
] | [
"metallopeptidase activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS",
"NCBIFAM"
] | [
"PR00997",
"TIGR03935"
] | [
"FRAGILYSIN",
"fragilysin"
] | [
29,
27
] | 2 | [] | [] | [] | 0 | [
"3p24",
"4on1",
"7pnd",
"7pol",
"7poo",
"7poq",
"7pou",
"8h3x",
"8h3y",
"8wem",
"8wen",
"8weo"
] | 12 | [
"PUB00070774"
] | [
"9529104"
] | [
"Molecular characterization of the fragilysin pathogenicity islet of enterotoxigenic Bacteroides fragilis."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
32
] | 1 | [] | [] | 0 | true | Family | Fragilysin | Fragilysin | Fragilysin | 9 |
IPR001844 | 1,844 | Chaperonin Cpn60/GroEL | Cpn60/GroEL | Family | 65,772 | false | false | The assembly of proteins has been thought to be the sole result of properties inherent in the primary sequence of polypeptides themselves. In some cases, however, structural information from other protein molecules is required for correct folding and subsequent assembly into oligomers [ ]. These `helper' molecules are ... | [
"GO:0140662",
"GO:0042026"
] | [
"ATP-dependent protein folding chaperone",
"protein refolding"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PRINTS",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00600",
"PR00298",
"PTHR45633",
"TIGR02348",
"cd03344"
] | [
"CH60",
"CHAPERONIN60",
"",
"GroEL",
"GroEL"
] | [
39397,
49041,
65654,
42861,
44890
] | 5 | [
"EC",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.6.1.7",
"GenProp0245",
"GenProp1181",
"PDOC00268",
"R-CEL-9837999",
"R-DDI-9837999",
"R-DME-9837999",
"R-GGA-1268020",
"R-GGA-9837999",
"R-HSA-1268020",
"R-HSA-8869496",
"R-HSA-9837999",
"R-HSA-9841251",
"R-MMU-1268020",
"R-MMU-9837999",
"R-RNO-1268020",
"R-RNO-9837999",
"R-SCE-... | [
"EC:5.6.1.7",
"GP:GenProp0245",
"GP:GenProp1181",
"PROSITEDOC:PDOC00268",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-9837999",
"REACTOME:R-GGA-1268020",
"REACTOME:R-GGA-9837999",
"REACTOME:R-HSA-1268020",
"REACTOME:R-HSA-8869496",
"REACTOME:R-HSA-9837999",
"REACTOME:... | 21 | [
"1aon",
"1dk7",
"1dkd",
"1fy9",
"1fya",
"1gr5",
"1grl",
"1gru",
"1iok",
"1jon",
"1kid",
"1kp8",
"1la1",
"1mnf",
"1oel",
"1pcq",
"1pf9",
"1sjp",
"1srv",
"1ss8",
"1svt",
"1sx3",
"1sx4",
"1xck",
"2c7c",
"2c7d",
"2c7e",
"2cgt",
"2eu1",
"2nwc",
"2yey",
"2ynj"... | 153 | [
"PUB00000632",
"PUB00001725",
"PUB00004022",
"PUB00004190",
"PUB00004550",
"PUB00099589"
] | [
"1347461",
"1672279",
"2897629",
"7935790",
"1349837",
"15289485"
] | [
"Cloning and nucleotide sequence of the Brucella abortus groE operon.",
"Sequence analysis of the Legionella micdadei groELS operon.",
"Homologous plant and bacterial proteins chaperone oligomeric protein assembly.",
"The crystal structure of the bacterial chaperonin GroEL at 2.8 A.",
"cDNA clones encoding ... | [
1992,
1991,
1988,
1994,
1992,
2004
] | 6 | [
"IPR002423"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
85,
49773,
14742,
183,
989
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
39,
4,
1,
5,
1,
25,
3,
1,
36,
4,
2,
1,
65
] | 13 | true | Family | Chaperonin Cpn60/GroEL | Chaperonin Cpn60/GroEL | Cpn60/GroEL | 4 |
IPR001845 | 1,845 | HTH ArsR-type DNA-binding domain | HTH_ArsR_DNA-bd_dom | Domain | 181,307 | false | false | The ArsR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain present in transcription regulators of the ArsR/SmtB family, involved in stress-response to heavy metal ions. This family of prokaryotic metal-sensing transcription repressors is named after Escherichia coli ArsR, an arsenic-responsive rep... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF01022",
"PR00778",
"PS50987",
"SM00418"
] | [
"HTH_5",
"HTHARSR",
"HTH_ARSR_2",
"HTH_ARSR"
] | [
99117,
126683,
150490,
175120
] | 4 | [
"GP",
"PROSITEDOC"
] | [
"GenProp0474",
"PDOC00661"
] | [
"GP:GenProp0474",
"PROSITEDOC:PDOC00661"
] | 2 | [
"1ku9",
"1r1t",
"1r1u",
"1r1v",
"1r22",
"1r23",
"1smt",
"1u2w",
"1ub9",
"1uly",
"2cwe",
"2jsc",
"2kjb",
"2kjc",
"2kko",
"2lkp",
"2m30",
"2oqg",
"2p4w",
"2qlz",
"2quf",
"2zkz",
"3cuo",
"3f6o",
"3f6v",
"3f72",
"3gw2",
"3jth",
"3pqj",
"3pqk",
"3tgn",
"4ggg"... | 62 | [
"PUB00003383",
"PUB00004420",
"PUB00015397",
"PUB00015398",
"PUB00015399",
"PUB00057829",
"PUB00057830"
] | [
"9466913",
"8506147",
"14568530",
"12829264",
"14960585",
"7543476",
"15966722"
] | [
"Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins.",
"A possible mechanism for metal-ion induced DNA-protein dissociation in a family of prokaryotic transcriptional regulators.",
"A metal-ligand-mediated intersubunit allosteric switch in related SmtB... | [
1998,
1993,
2003,
2003,
2004,
1995,
2005
] | 7 | [
"IPR011991"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
8515,
171024,
198,
18,
2,
1550
] | 6 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | HTH ArsR-type DNA-binding domain | HTH ArsR-type DNA-binding domain | HTH_ArsR_DNA-bd_dom | 8 |
IPR001846 | 1,846 | von Willebrand factor, type D domain | VWF_type-D | Domain | 35,935 | false | false | Von Willebrand factor (VWF) is a large, multimeric blood glycoprotein synthesized in endothelial cells and megakaryocytes, that is required for normal hemostasis. Mutant forms are involved in the most common inherited bleeding disorder (von Willebrand disease: VWD). VWF mediates the adhesion of platelets to sites of va... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00094",
"PS51233",
"SM00216"
] | [
"VWD",
"VWFD",
"VWD"
] | [
32988,
35621,
28952
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51233",
"R-CFA-114608",
"R-CFA-216083",
"R-CFA-354192",
"R-CFA-354194",
"R-CFA-372708",
"R-CFA-430116",
"R-CFA-5674135",
"R-CFA-75892",
"R-HSA-114608",
"R-HSA-140837",
"R-HSA-163125",
"R-HSA-216083",
"R-HSA-354192",
"R-HSA-354194",
"R-HSA-372708",
"R-HSA-430116",
"R-HSA-508362... | [
"PROSITEDOC:PDOC51233",
"REACTOME:R-CFA-114608",
"REACTOME:R-CFA-216083",
"REACTOME:R-CFA-354192",
"REACTOME:R-CFA-354194",
"REACTOME:R-CFA-372708",
"REACTOME:R-CFA-430116",
"REACTOME:R-CFA-5674135",
"REACTOME:R-CFA-75892",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-140837",
"REACTOME:R-HSA-1631... | 59 | [
"1lsh",
"6n29",
"6rbf",
"6tm2",
"7a5o",
"7kwo",
"7pmv",
"7pnf",
"7pov",
"7pp6",
"7prl",
"7qcl",
"7qcn",
"7qcu",
"7wn3",
"7wn4",
"7wn6",
"7wpp",
"7wpq",
"7wpr",
"7wps",
"7wqt",
"7zwh",
"8d3c",
"8d3d",
"8oer",
"8oes",
"8qci",
"8qsp",
"8qtb",
"8qtv",
"8r0t"... | 40 | [
"PUB00005690",
"PUB00005829",
"PUB00006533",
"PUB00087264",
"PUB00093468"
] | [
"2311582",
"9759493",
"10807780",
"22490677",
"30642920"
] | [
"Domains involved in multimer assembly of von willebrand factor (vWF): multimerization is independent of dimerization.",
"Biochemistry and genetics of von Willebrand factor.",
"Conformational changes in the D' domain of von Willebrand factor induced by CYS 25 and CYS 95 mutations lead to factor VIII binding def... | [
1990,
1998,
2000,
2012,
2019
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
451,
35468,
4,
12
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
70,
12,
84,
73,
60
] | 6 | true | Domain | von Willebrand factor, type D domain | von Willebrand factor, type D domain | VWF_type-D | 1 |
IPR001847 | 1,847 | Peptidase S21 | Peptidase_S21 | Family | 814 | false | false | This group of serine peptidases belong to MEROPS peptidase family S21 (assemblin family, clan 21). Assemblin is a serine protease with a unique fold and an active site that comprises the unusual triad Ser-His-His. It is found in herpesviruses, one of the groups of DNA viruses. Assemblin is involved in the late stages o... | [
"GO:0004252",
"GO:0006508"
] | [
"serine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"PRINTS"
] | [
"MF_04008",
"PF00716",
"PR00236"
] | [
"HSV_SCAF",
"Peptidase_S21",
"HSVCAPSIDP40"
] | [
632,
814,
637
] | 3 | [
"EC",
"REACTOME"
] | [
"3.4.21.97",
"R-HSA-9610379"
] | [
"EC:3.4.21.97",
"REACTOME:R-HSA-9610379"
] | 2 | [
"1at3",
"1cmv",
"1fl1",
"1id4",
"1iec",
"1ied",
"1ief",
"1ieg",
"1jq6",
"1jq7",
"1lay",
"1njt",
"1nju",
"1nkk",
"1nkm",
"1o6e",
"1vzv",
"1wpo",
"2pbk",
"2wpo",
"3njq",
"4cx8",
"4p2t",
"4p3h",
"4v07",
"4v08",
"4v0t",
"5ur3",
"5ute",
"5utn",
"5uv3",
"5uvp"... | 40 | [
"PUB00000522",
"PUB00003576",
"PUB00075717",
"PUB00075718",
"PUB00075719"
] | [
"8439290",
"7845208",
"26161660",
"24977643",
"19158247"
] | [
"Evolutionary families of peptidases.",
"Families of serine peptidases.",
"Dimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine Protease.",
"Broad-spectrum allosteric inhibition of herpesvirus proteases.",
"Self-assembly of ... | [
1993,
1994,
2015,
2014,
2009
] | 5 | [] | [] | 0 | 0 | null | [
"Bilateria",
"Herpesvirales"
] | [
6,
808
] | 2 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | Peptidase S21 | Peptidase S21 | Peptidase_S21 | 7 |
IPR001848 | 1,848 | Small ribosomal subunit protein uS10 | Ribosomal_uS10 | Family | 35,005 | false | false | This entry represents the small ribosomal subunit protein uS10 found in archaea, bacteria and eukaryotes including the eukaryotic organelles such as mitochondria and chloroplast. Evidence suggests that, in prokaryotes, the peptidyl transferase reaction is performed by the large subunit 23S rRNA, whereas proteins probab... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"MF_00508",
"PR00971",
"PTHR11700",
"TIGR01049"
] | [
"Ribosomal_uS10",
"RIBOSOMALS10",
"",
"rpsJ_bact"
] | [
33256,
31817,
33542,
24827
] | 4 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp0132",
"PDOC00312",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72695",
"R-DDI-72702",
"R-DDI-72706",
"R... | [
"GP:GenProp0132",
"PROSITEDOC:PDOC00312",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"RE... | 91 | [
"1fjg",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xmo",
"1xmq",
"1xnq",
"1xnr",
"2e5l",
"2f4v"... | 1,753 | [
"PUB00003326",
"PUB00003381",
"PUB00004907",
"PUB00005065",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"8021936",
"9281425",
"9371771",
"2179947",
"11297922",
"11290319",
"11114498"
] | [
"Suppression of yeast RNA polymerase III mutations by the URP2 gene encoding a protein homologous to the mammalian ribosomal protein S20.",
"A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. II. The RNA-protein interaction data.",
"Proteins on ribosome surface: measurements o... | [
1994,
1997,
1997,
1990,
2001,
2001,
2000
] | 7 | [] | [
"IPR005729"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1198,
22957,
10431,
419
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
13,
1,
3,
2,
1,
4,
7,
2,
11,
10,
2,
2,
31
] | 13 | true | Family | Small ribosomal subunit protein uS10 | Small ribosomal subunit protein uS10 | Ribosomal_uS10 | 1 |
IPR001850 | 1,850 | Non-structural protein NS3, peptidase S7, flavivirus | Flavi_NS3_S7 | Domain | 11,717 | false | false | The viral genome of Flavivirus is a positive strand RNA that encodes a single polyprotein precursor. Processing of the polyprotein precursor into mature proteins is carried out by the host signal peptidase and by NS3 serine protease, which requires NS2B ( ) as a cofactor. This entry also includes a few bacterial sequen... | [
"GO:0003723",
"GO:0003724",
"GO:0005524"
] | [
"RNA binding",
"RNA helicase activity",
"ATP binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PFAM",
"PROFILE"
] | [
"PF00949",
"PS51528"
] | [
"Peptidase_S7",
"FLAVIVIRUS_NS3PRO"
] | [
11674,
11607
] | 2 | [
"EC",
"EC",
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.1.1.56",
"2.1.1.57",
"2.7.7.48",
"3.4.21.91",
"3.6.1.15",
"3.6.4.13",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210",
"PWY-7375",
"PWY-7379"
] | [
"EC:2.1.1.56",
"EC:2.1.1.57",
"EC:2.7.7.48",
"EC:3.4.21.91",
"EC:3.6.1.15",
"EC:3.6.4.13",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210",
"METACYC:PWY-7375",
"METACYC:PWY-7379"
] | 13 | [
"2fom",
"2fp7",
"2ggv",
"2ijo",
"2m9p",
"2m9q",
"2vbc",
"2whx",
"2wv9",
"2wzq",
"2yol",
"3e90",
"3l6p",
"3lkw",
"3u1i",
"3u1j",
"4m9f",
"4m9i",
"4m9k",
"4m9m",
"4m9t",
"4r8t",
"5gj4",
"5gpi",
"5gxj",
"5h4i",
"5h6v",
"5idk",
"5lc0",
"5t1v",
"5tfn",
"5tfo"... | 269 | [
"PUB00041729",
"PUB00057952",
"PUB00057953"
] | [
"17400917",
"19693793",
"20042502"
] | [
"Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold.",
"Homology modeling and molecular dynamics simulations of Dengue virus NS2B/NS3 protease: insight into molecular interaction.",
"Serotype-specific structural differences in the protease-cofactor ... | [
2007,
2010,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
56,
17,
11644
] | 3 | [] | [] | 0 | true | Domain | Non-structural protein NS3, peptidase S7, flavivirus | Non-structural protein NS3, peptidase S7, flavivirus | Flavi_NS3_S7 | 1 |
IPR001852 | 1,852 | Pyridoxal 5'-phosphate synthase subunit PdxS/SNZ | PdxS/SNZ | Family | 13,548 | false | false | The family of pyridoxal 5'-phosphate synthase subunits, known as the PdxS/SNZ family, occur in organisms in four kingdoms and form one of the most highly conserved families [ ]. A PdxS/SNZ protein has a classic (β/α)8-barrel fold, consisting of eight parallel β-strands alternating with eight α helices. PdxS subunits fo... | [
"GO:0042819",
"GO:0042823"
] | [
"vitamin B6 biosynthetic process",
"pyridoxal phosphate biosynthetic process"
] | [
"biological_process",
"biological_process"
] | 2 | [
"HAMAP",
"PIRSF",
"PROSITE",
"PROFILE",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_01824",
"PIRSF029271",
"PS01235",
"PS51129",
"PTHR31829",
"TIGR00343",
"cd04727"
] | [
"PdxS",
"Pdx1",
"PDXS_SNZ_1",
"PDXS_SNZ_2",
"",
"",
"pdxS"
] | [
11670,
12253,
11305,
13516,
13397,
11460,
11750
] | 7 | [
"EC",
"METACYC",
"PROSITEDOC"
] | [
"4.3.3.6",
"PWY-6466",
"PDOC00949"
] | [
"EC:4.3.3.6",
"METACYC:PWY-6466",
"PROSITEDOC:PDOC00949"
] | 3 | [
"1znn",
"2iss",
"2nv1",
"2nv2",
"2yzr",
"2zbt",
"3fem",
"3o05",
"3o06",
"3o07",
"4ads",
"4adt",
"4adu",
"4fiq",
"4fir",
"4jdy",
"4wxy",
"4wxz",
"4wy0",
"5k2z",
"5k3v",
"5lnr",
"5lns",
"5lnt",
"5lnu",
"5lnv",
"5lnw",
"6hx3",
"6hxg",
"6hye",
"7lb5",
"7lb6"... | 40 | [
"PUB00007160",
"PUB00018041",
"PUB00018042",
"PUB00018043",
"PUB00027968",
"PUB00041771",
"PUB00042048"
] | [
"10430950",
"14764090",
"14762015",
"15911615",
"16030023",
"17144654",
"17159152"
] | [
"A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis.",
"Characterization of the products of the genes SNO1 and SNZ1 involved in pyridoxine synthesis in Saccharomyces cerevisiae.",
"Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyri... | [
1999,
2004,
2004,
2005,
2005,
2006,
2006
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctg0K17",
"unclassified sequences"
] | [
856,
8412,
3900,
1,
379
] | 5 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
14,
1,
16,
3,
1,
9
] | 6 | true | Family | Pyridoxal 5'-phosphate synthase subunit PdxS/SNZ | Pyridoxal 5'-phosphate synthase subunit PdxS/SNZ | PdxS/SNZ | 3 |
IPR001853 | 1,853 | DSBA-like thioredoxin domain | DSBA-like_thioredoxin_dom | Domain | 51,399 | false | false | null | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01323"
] | [
"DSBA"
] | [
51399
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-156590",
"R-CEL-9033241",
"R-HSA-156590",
"R-HSA-9033241",
"R-HSA-9760173",
"R-MMU-156590",
"R-MMU-9033241",
"R-RNO-156590",
"R-RNO-9033241"
] | [
"REACTOME:R-CEL-156590",
"REACTOME:R-CEL-9033241",
"REACTOME:R-HSA-156590",
"REACTOME:R-HSA-9033241",
"REACTOME:R-HSA-9760173",
"REACTOME:R-MMU-156590",
"REACTOME:R-MMU-9033241",
"REACTOME:R-RNO-156590",
"REACTOME:R-RNO-9033241"
] | 9 | [
"1a23",
"1a24",
"1a2j",
"1a2l",
"1a2m",
"1ac1",
"1acv",
"1bed",
"1bq7",
"1dsb",
"1fvj",
"1fvk",
"1r4w",
"1ti1",
"1u3a",
"1un2",
"1yzx",
"2b3s",
"2b6m",
"2hi7",
"2ijy",
"2imd",
"2ime",
"2imf",
"2in3",
"2leg",
"2mbs",
"2mbt",
"2ndo",
"2rem",
"2zup",
"3a3t"... | 286 | [
"PUB00003378",
"PUB00006416"
] | [
"9149147",
"9655827"
] | [
"Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae.",
"Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization."
] | [
1997,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"plasmids",
"unclassified sequences"
] | [
352,
42070,
8398,
2,
577
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
5,
2,
20,
1,
6,
2,
3,
4,
3,
19
] | 10 | true | Domain | DSBA-like thioredoxin domain | DSBA-like thioredoxin domain | DSBA-like_thioredoxin_dom | 5 |
IPR001854 | 1,854 | Large ribosomal subunit protein uL29 | Ribosomal_uL29 | Family | 31,763 | false | false | This family includes ribosomal proteins, which constitute the uL29 family [ ]. These were previously known as L29 from eubacteria and archaea and L35 from eukaryotes. Ribosomal protein uL29 is one of the proteins from the large ribosomal subunit. uL29 belongs to a family of ribosomal proteins of 63 to 138 amino-acid re... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"NCBIFAM",
"CDD"
] | [
"MF_00374",
"PF00831",
"TIGR00012",
"cd00427"
] | [
"Ribosomal_uL29",
"Ribosomal_L29",
"L29",
"Ribosomal_L29_HIP"
] | [
30476,
31093,
31320,
28160
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00501",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",... | [
"PROSITEDOC:PDOC00501",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-7270... | 83 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1r73",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk"... | 1,848 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00079483",
"PUB00080279",
"PUB00080476"
] | [
"11297922",
"11290319",
"11114498",
"10937990",
"24524803",
"12756233"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The structural basis of ribosome activity in peptide bond synthesis.",
"A new system for naming ribosomal proteins.",
"Interplay of signal recognition parti... | [
2001,
2001,
2000,
2000,
2014,
2003
] | 6 | [] | [
"IPR045059"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
901,
22998,
7425,
439
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
22,
1,
1,
3,
1,
3,
3,
1,
10,
9,
2,
1,
32
] | 13 | true | Family | Large ribosomal subunit protein uL29 | Large ribosomal subunit protein uL29 | Ribosomal_uL29 | 5 |
IPR001855 | 1,855 | Beta-defensin-like domain | Defensin_beta-like | Domain | 4,430 | false | false | This entry represents a range of Beta defensins. Defensins are 2-6kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses [ . ], containing three pairs of intramolecular disulphide bonds. On the basis of their size and pattern of disulphide bonding... | [
"GO:0006952",
"GO:0005576"
] | [
"defense response",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00711"
] | [
"Defensin_beta"
] | [
4430
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-1461957",
"R-BTA-1461973",
"R-GGA-1461957",
"R-GGA-1461973",
"R-HSA-1461957",
"R-HSA-1461973",
"R-MMU-1461957",
"R-MMU-1461973",
"R-MMU-1462054",
"R-MMU-6798695",
"R-RNO-1461957",
"R-RNO-1461973",
"R-SSC-1461957"
] | [
"REACTOME:R-BTA-1461957",
"REACTOME:R-BTA-1461973",
"REACTOME:R-GGA-1461957",
"REACTOME:R-GGA-1461973",
"REACTOME:R-HSA-1461957",
"REACTOME:R-HSA-1461973",
"REACTOME:R-MMU-1461957",
"REACTOME:R-MMU-1461973",
"REACTOME:R-MMU-1462054",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-1461957",
"REACTOM... | 13 | [
"1bnb",
"1e4q",
"1e4r",
"1e4s",
"1e4t",
"1fd3",
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"1fqq",
"1iju",
"1ijv",
"1kj5",
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"1ut3",
"2lg5",
"2lg6",
"2lxo",
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"2nlc",
"2nld",
"2nle",
"2nlf",
"2nlg",
"2nlh",
"2nlp",
"2nlq",
"2nls",
"2plz",
"5lcs",
"6cs9",
"6m56",
"7lzl",
"7t9q"... | 34 | [
"PUB00001093",
"PUB00100818"
] | [
"8528769",
"33224970"
] | [
"Structure, function, and membrane integration of defensins.",
"Expression and Functional Characterization of a Novel Antimicrobial Peptide: Human Beta-Defensin 118."
] | [
1995,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bilateria"
] | [
4,
4426
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
33,
33
] | 3 | true | Domain | Beta-defensin-like domain | Beta-defensin-like domain | Defensin_beta-like | 7 |
IPR001856 | 1,856 | Somatostatin receptor 3 | Somatstn_rcpt_3 | Family | 981 | false | false | Somatostatin (SST), also known as somatotropin release-inhibiting factor (SRIF), is a hypothalamic hormone, a pancreatic hormone, and a central and peripheral neurotransmitter. Somatostatin has a wide distribution throughout the central nervous system (CNS) as well as in peripheral tissues, for example in the pituitary... | [
"GO:0004994",
"GO:0007186",
"GO:0016020"
] | [
"somatostatin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00589"
] | [
"SOMATOSTTN3R"
] | [
981
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"357",
"R-HSA-375276",
"R-HSA-418594",
"R-HSA-5620922",
"R-MMU-375276",
"R-MMU-418594",
"R-MMU-5620922",
"R-RNO-375276",
"R-RNO-418594",
"R-RNO-5620922"
] | [
"IUPHAR:357",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-5620922",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-5620922",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-418594",
"REACTOME:R-RNO-5620922"
] | 10 | [
"8xiq",
"8xir",
"8zbi"
] | 3 | [
"PUB00013316",
"PUB00063572",
"PUB00063590",
"PUB00063595",
"PUB00063596",
"PUB00063597",
"PUB00063598",
"PUB00063599",
"PUB00063600",
"PUB00063601",
"PUB00063602",
"PUB00063603",
"PUB00063604",
"PUB00063605",
"PUB00063619",
"PUB00063624"
] | [
"14507421",
"10433861",
"7792934",
"8243278",
"8078491",
"7907795",
"1346068",
"8483934",
"15361490",
"10598790",
"1328199",
"7538774",
"9426226",
"8684611",
"8034040",
"12639942"
] | [
"Somatostatin receptors.",
"Somatostatin and its receptor family.",
"Classification and nomenclature of somatostatin receptors.",
"Tissue distribution of somatostatin receptor subtype messenger ribonucleic acid in the rat.",
"Characterization of cloned human somatostatin receptor SSTR5.",
"Stimulation of ... | [
2003,
1999,
1995,
1993,
1994,
1994,
1992,
1993,
2004,
1999,
1992,
1995,
1997,
1996,
1994,
2003
] | 16 | [
"IPR000586"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
981
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
2,
2,
2
] | 4 | true | Family | Somatostatin receptor 3 | Somatostatin receptor 3 | Somatstn_rcpt_3 | 1 |
IPR001857 | 1,857 | Large ribosomal subunit protein bL19 | Ribosomal_bL19 | Family | 29,675 | false | false | This family represents the large ribosomal subunit protein bL19 found in bacteria and eukaryotes (which includes bL19c from plants (chloroplast), mitochondrial bL19m from animals, also referred to as MRLP19) [ , , , ]. In Escherichia coli, bL19 is known to be located at the 30S-50S ribosomal subunit interface [ ] and m... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PIRSF",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"MF_00402",
"PF01245",
"PIRSF002191",
"PR00061",
"PTHR15680",
"TIGR01024"
] | [
"Ribosomal_bL19",
"Ribosomal_L19",
"Ribosomal_L19",
"RIBOSOMALL19",
"",
"rplS_bact"
] | [
23242,
29623,
22563,
27116,
29263,
25110
] | 6 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00778",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-9937383",
"R-DME-5389840",
"R-DME-5419276",
"R-DME-9937383",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383"
] | [
"PROSITEDOC:PDOC00778",
"REACTOME:R-CEL-5389840",
"REACTOME:R-CEL-5419276",
"REACTOME:R-CEL-9937383",
"REACTOME:R-DME-5389840",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-9937383",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9937383",
"REACTOME:... | 14 | [
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"2ftc",
"2j28",
"2rdo",
"2zjp",
"2zjq",
"2zjr",
"3bbx",
"3cf5",
"3dll",
"3j3v",
"3j3w",
"3j5l",
"3j6b",
"3j7y",
"3j7z",
"3j8g",
"3j9m",
"3j9w",
"3j9y",
"3j9z",
"3ja1",
"3jbu"... | 1,249 | [
"PUB00000273",
"PUB00001241",
"PUB00002697",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00080279",
"PUB00089007"
] | [
"339951",
"8262035",
"1985969",
"11297922",
"11290319",
"11114498",
"24524803",
"25278503"
] | [
"Primary structure of protein L19 from the large subunit of Escherichia coli ribosomes.",
"Ribosomal protein L6: structural evidence of gene duplication from a primitive RNA binding protein.",
"Cloning, sequencing, and overexpression of genes for ribosomal proteins from Bacillus stearothermophilus.",
"Atomic ... | [
1978,
1993,
1991,
2001,
2001,
2000,
2014,
2014
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
23377,
2,
5755,
541
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
22,
1,
1,
1,
1,
5,
3,
1,
7,
2,
1,
1,
13
] | 13 | true | Family | Large ribosomal subunit protein bL19 | Large ribosomal subunit protein bL19 | Ribosomal_bL19 | 3 |
IPR001858 | 1,858 | Phosphatidylethanolamine-binding, conserved site | Phosphatidylethanolamine-bd_CS | Conserved_site | 7,435 | false | false | This entry groups metazoan phosphatidylethanolamine-binding proteins, carboxypeptidase Y inhibitor from Saccharomyces cerevisiae (Baker's yeast) ( ), and homologues from plants which function in flower development. The members of this family belong to MEROPS proteinase inhibitor family I51, clan I-. | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01220"
] | [
"PBP"
] | [
7435
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00938",
"R-BTA-5674135",
"R-BTA-5675221",
"R-CEL-5674135",
"R-CEL-5675221",
"R-CFA-5674135",
"R-CFA-5675221",
"R-HSA-5674135",
"R-HSA-5675221",
"R-HSA-6802946",
"R-HSA-6802948",
"R-HSA-6802952",
"R-HSA-6802955",
"R-HSA-9649948",
"R-MMU-5674135",
"R-MMU-5675221",
"R-RNO-5674135",... | [
"PROSITEDOC:PDOC00938",
"REACTOME:R-BTA-5674135",
"REACTOME:R-BTA-5675221",
"REACTOME:R-CEL-5674135",
"REACTOME:R-CEL-5675221",
"REACTOME:R-CFA-5674135",
"REACTOME:R-CFA-5675221",
"REACTOME:R-HSA-5674135",
"REACTOME:R-HSA-5675221",
"REACTOME:R-HSA-6802946",
"REACTOME:R-HSA-6802948",
"REACTOME:... | 18 | [
"1a44",
"1b7a",
"1bd9",
"1beh",
"1kn3",
"1qou",
"1wko",
"1wkp",
"1wpx",
"2gzq",
"2iqx",
"2iqy",
"2l7w",
"2qyq",
"2r77",
"3axy",
"5tvd",
"6ens",
"6ent",
"6igg",
"6igh",
"6igi",
"6igj"
] | 23 | [
"PUB00001689",
"PUB00003436",
"PUB00015036",
"PUB00015037",
"PUB00015038",
"PUB00015039"
] | [
"7641877",
"7807553",
"11457954",
"14682620",
"15055534",
"10583960"
] | [
"From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site.",
"Amino acid sequence of the Homo sapiens brain 21-23-kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos ... | [
1995,
1994,
2001,
2003,
2004,
1999
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
7435
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
26,
2,
2,
5,
6,
8,
46,
9,
2,
64
] | 10 | true | Conserved_site | Phosphatidylethanolamine-binding, conserved site | Phosphatidylethanolamine-binding, conserved site | Phosphatidylethanolamine-bd_CS | 3 |
IPR001859 | 1,859 | Large ribosomal subunit protein P1/P2, eukaryota | Ribosomal_P1/P2_euk | Family | 2,488 | false | false | This entry represents a family of eukaryotic ribosomal proteins P1/P2. Eukaryotic ribosomal P proteins have been classified according to their similarity to the mammalian P0, P1 and P2 proteins [ ], all of which share a similar primary structure: an apparently globular N-terminal domain (which includes the protein core... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00456"
] | [
"RIBOSOMALP2"
] | [
2488
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-SPO-156827",
"R-SPO-1799339",
"R-SPO-72689",
"R-SPO-72706",
"R-SPO-975956",
"R-SPO-975957"
] | [
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-975956",
"REACTOME:R-CEL-975957",
"REACTOME:R-SPO-156827",
"REACTOME:R-SPO-1799339",
"REACTOME:R-SPO-72689",
"REACTOME:R-SPO-72706",
"REACTOME:R-SPO-975956",
"REACTOME:R-SPO-97595... | 12 | [] | 0 | [
"PUB00004501"
] | [
"15463674"
] | [
"The Trypanosoma cruzi ribosomal P protein family: classification and antigenicity."
] | [
1993
] | 1 | [
"IPR027534"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
24,
190,
2270,
4
] | 4 | [
"Caenorhabditis elegans",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
1,
1,
1,
3,
9
] | 5 | true | Family | Large ribosomal subunit protein P1/P2, eukaryota | Large ribosomal subunit protein P1/P2, eukaryota | Ribosomal_P1/P2_euk | 2 |
IPR001860 | 1,860 | Glycoside hydrolase, family 34 | Glyco_hydro_34 | Family | 101,515 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004308",
"GO:0005975",
"GO:0016020",
"GO:0033644",
"GO:0055036"
] | [
"exo-alpha-sialidase activity",
"carbohydrate metabolic process",
"membrane",
"host cell membrane",
"virion membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component",
"cellular_component"
] | 5 | [
"HAMAP",
"PFAM"
] | [
"MF_04071",
"PF00064"
] | [
"INFV_NRAM",
"Neur"
] | [
83978,
101515
] | 2 | [
"CAZY",
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH34",
"3.2.1.18",
"GenProp1012",
"R-HSA-168255",
"R-HSA-168275",
"R-HSA-168277",
"R-HSA-168288",
"R-HSA-168298",
"R-HSA-168302",
"R-HSA-168303",
"R-HSA-168316",
"R-HSA-168336",
"R-HSA-168874",
"R-HSA-192823"
] | [
"CAZY:GH34",
"EC:3.2.1.18",
"GP:GenProp1012",
"REACTOME:R-HSA-168255",
"REACTOME:R-HSA-168275",
"REACTOME:R-HSA-168277",
"REACTOME:R-HSA-168288",
"REACTOME:R-HSA-168298",
"REACTOME:R-HSA-168302",
"REACTOME:R-HSA-168303",
"REACTOME:R-HSA-168316",
"REACTOME:R-HSA-168336",
"REACTOME:R-HSA-16887... | 14 | [
"1a14",
"1a4g",
"1a4q",
"1b9s",
"1b9t",
"1b9v",
"1bji",
"1f8b",
"1f8c",
"1f8d",
"1f8e",
"1inf",
"1ing",
"1inh",
"1inv",
"1inw",
"1inx",
"1iny",
"1ivb",
"1ivc",
"1ivd",
"1ive",
"1ivf",
"1ivg",
"1l7f",
"1l7g",
"1l7h",
"1mwe",
"1nca",
"1ncb",
"1ncc",
"1ncd"... | 303 | [
"PUB00004870",
"PUB00005266",
"PUB00006572"
] | [
"7624375",
"8535779",
"10623375"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Measures for control of influenza."
] | [
1995,
1995,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Orthomyxoviridae"
] | [
11,
101504
] | 2 | [] | [] | 0 | true | Family | Glycoside hydrolase, family 34 | Glycoside hydrolase, family 34 | Glyco_hydro_34 | 7 |
IPR001862 | 1,862 | Membrane attack complex component/perforin/complement C9 | MAC_perforin | Family | 6,345 | false | false | Complement component C9 is a multi-domain protein that contains an N-terminal type-1 TSP domain, an LDL-receptor class A repeat, a number of potential transmembrane (TM) regions and a C-terminal EGF-like domain [ , , ]. Hydropathy analysis of the sequence indicates the N-terminal half of C9 to be predominantly hydrophi... | [
"GO:0006955",
"GO:0005579"
] | [
"immune response",
"membrane attack complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00764"
] | [
"COMPLEMENTC9"
] | [
6345
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00251",
"R-BTA-166665",
"R-BTA-977606",
"R-HSA-166665",
"R-HSA-977606",
"R-MMU-166665",
"R-MMU-977606",
"R-RNO-166665",
"R-RNO-977606"
] | [
"PROSITEDOC:PDOC00251",
"REACTOME:R-BTA-166665",
"REACTOME:R-BTA-977606",
"REACTOME:R-HSA-166665",
"REACTOME:R-HSA-977606",
"REACTOME:R-MMU-166665",
"REACTOME:R-MMU-977606",
"REACTOME:R-RNO-166665",
"REACTOME:R-RNO-977606"
] | 9 | [
"2rd7",
"3ojy",
"3t5o",
"4a5w",
"4e0s",
"5fmw",
"6cxo",
"6dlw",
"6h03",
"6h04",
"7nyc",
"7nyd",
"8b0f",
"8b0g",
"8b0h",
"8de6"
] | 16 | [
"PUB00000295",
"PUB00001056",
"PUB00001141",
"PUB00004608"
] | [
"3219351",
"1722985",
"4018030",
"6095282"
] | [
"Relationships between the gene and protein structure in human complement component C9.",
"Assembly of macromolecular pores by immune defense systems.",
"The sequence and topology of human complement component C9.",
"Nucleotide sequence of cDNA and derived amino acid sequence of human complement component C9.... | [
1988,
1991,
1985,
1984
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Kangiella spongicola"
] | [
6344,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
29,
29,
9,
16
] | 4 | true | Family | Membrane attack complex component/perforin/complement C9 | Membrane attack complex component/perforin/complement C9 | MAC_perforin | 8 |
IPR001863 | 1,863 | Glypican | Glypican | Family | 9,312 | false | false | Glypicans [ , ] are a family of heparan sulphate proteoglycans which are anchored to cell membranes by a glycosylphosphatidylinositol (GPI) linkage. Six members (GPC1-6) are known in vertebrates [ ]. The main function of glypicans is to regulate several signaling pathways, including those of Wnts, Hedgehogs, fibroblast... | [
"GO:0009966",
"GO:0005886",
"GO:0031012"
] | [
"regulation of signal transduction",
"plasma membrane",
"extracellular matrix"
] | [
"biological_process",
"cellular_component",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF01153",
"PTHR10822"
] | [
"Glypican",
""
] | [
9287,
9066
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00927",
"R-DME-1971475",
"R-DME-2022928",
"R-DME-2024096",
"R-DME-209471",
"R-DME-381426",
"R-DME-5362798",
"R-DME-8957275",
"R-DRE-1971475",
"R-DRE-2022928",
"R-DRE-2024096",
"R-HSA-1971475",
"R-HSA-2022928",
"R-HSA-2024096",
"R-HSA-202733",
"R-HSA-3560783",
"R-HSA-3560801",
... | [
"PROSITEDOC:PDOC00927",
"REACTOME:R-DME-1971475",
"REACTOME:R-DME-2022928",
"REACTOME:R-DME-2024096",
"REACTOME:R-DME-209471",
"REACTOME:R-DME-381426",
"REACTOME:R-DME-5362798",
"REACTOME:R-DME-8957275",
"REACTOME:R-DRE-1971475",
"REACTOME:R-DRE-2022928",
"REACTOME:R-DRE-2024096",
"REACTOME:R-... | 48 | [
"3odn",
"4acr",
"4ad7",
"4bwe",
"4ywt",
"6wjl",
"6xtz",
"7t62",
"7za1",
"7za2",
"7za3",
"7zav",
"7zaw",
"9ntq"
] | 14 | [
"PUB00003081",
"PUB00003899",
"PUB00034826",
"PUB00075035",
"PUB00088080"
] | [
"7657705",
"8589707",
"11474185",
"24412155",
"18505598"
] | [
"K-glypican: a novel GPI-anchored heparan sulfate proteoglycan that is highly expressed in developing brain and kidney.",
"Glypicans: a growing trend.",
"Mapping of the rat glypican genes.",
"The role of glypicans in Hedgehog signaling.",
"Glypicans."
] | [
1995,
1996,
2001,
2014,
2008
] | 5 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
9312
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
19,
6,
25,
26,
27
] | 6 | true | Family | Glypican | Glypican | Glypican | 4 |
IPR001864 | 1,864 | Trypanothione reductase | Trypnth_redctse | Family | 123 | false | false | Trypanothione reductase from Leishmania, and African and South American trypanosomes, has been purified and characterised [ ]. The enzymes have similar physical, mechanistic and kinetic properties, and are members of the flavoprotein disulphide oxidoreductase family. Trypanothione is the parasite analogue of glutathion... | [
"GO:0015036"
] | [
"disulfide oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS",
"NCBIFAM"
] | [
"PR00470",
"TIGR01423"
] | [
"TRYPANRDTASE",
"trypano_reduc"
] | [
123,
93
] | 2 | [
"EC"
] | [
"1.8.1.12"
] | [
"EC:1.8.1.12"
] | 1 | [
"1aog",
"1bzl",
"1fea",
"1feb",
"1fec",
"1gxf",
"1nda",
"1typ",
"1tyt",
"2jk6",
"2tpr",
"2w0h",
"2wba",
"2woi",
"2wov",
"2wow",
"2wp5",
"2wp6",
"2wpc",
"2wpe",
"2wpf",
"2x50",
"2yau",
"4adw",
"4apn",
"4nev",
"4new",
"5ebk",
"5s9s",
"5s9t",
"5s9u",
"5s9v"... | 64 | [
"PUB00003614",
"PUB00004988"
] | [
"2011150",
"8159665"
] | [
"Cloning, sequencing, overproduction and purification of trypanothione reductase from Trypanosoma cruzi.",
"The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state."
] | [
1991,
1994
] | 2 | [
"IPR046952"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Pseudomonadota"
] | [
115,
8
] | 2 | [] | [] | 0 | true | Family | Trypanothione reductase | Trypanothione reductase | Trypnth_redctse | 3 |
IPR001865 | 1,865 | Small ribosomal subunit protein uS2 | Ribosomal_uS2 | Family | 52,535 | false | false | This entry represents the family of ribosomal uS2 proteins. They are required for the assembly of different ribosomal subunits and are widely distributed among all living organisms [ ]. Ribosomal uS2 family in humans includes three members: Small ribosomal subunits uS2 (also known as RPSA). Small ribosomal subunits uS2... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"CDD"
] | [
"PF00318",
"PR00395",
"cd01425"
] | [
"Ribosomal_S2",
"RIBOSOMALS2",
"RPS2"
] | [
52344,
51268,
51134
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00744",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-BTA-9837999",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-7264... | [
"PROSITEDOC:PDOC00744",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-97595... | 150 | [
"1fjg",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1vi5",
"1vi6",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1x18",
"1xmo",
"1xmq",
"1xnq"... | 1,793 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00151136",
"PUB00151137",
"PUB00151138"
] | [
"11297922",
"11290319",
"11114498",
"31694957",
"23579497",
"25706898"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Foot-and-Mouth Disease Virus Capsid Protein VP1 Interacts with Host Ribosomal Protein SA To Maintain Activation of the MAPK Signal Pathway and Promote Virus Rep... | [
2001,
2001,
2000,
2020,
2013,
2015
] | 6 | [] | [
"IPR005706",
"IPR005707"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Myoviridae sp. ct2th6",
"unclassified sequences"
] | [
899,
24462,
26534,
1,
639
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
17,
2,
3,
3,
1,
10,
6,
2,
16,
13,
3,
3,
43
] | 13 | true | Family | Small ribosomal subunit protein uS2 | Small ribosomal subunit protein uS2 | Ribosomal_uS2 | 5 |
IPR001866 | 1,866 | Papillomavirus E2, N-terminal | PPV_E2_N | Domain | 2,714 | false | false | E2 is an early regulatory protein found in the dsDNA papillomaviruses. E2 regulates viral transcription and DNA replication. It binds to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory region. It can either activate or repress transcription, depending on E2RE's position with ... | [
"GO:0006275",
"GO:0006355",
"GO:0016032"
] | [
"regulation of DNA replication",
"regulation of DNA-templated transcription",
"viral process"
] | [
"biological_process",
"biological_process",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF00508"
] | [
"PPV_E2_N"
] | [
2714
] | 1 | [] | [] | [] | 0 | [
"1dto",
"1qqh",
"1r6k",
"1r6n",
"1tue",
"2jeu",
"2jex",
"2nnu"
] | 8 | [
"PUB00006164",
"PUB00097439"
] | [
"1328886",
"25340539"
] | [
"Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target.",
"Phosphorylation of HPV-16 E2 at serine 243 enables binding to Brd4 and mitotic chromosomes."
] | [
1992,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Lasius niger",
"Papillomaviridae"
] | [
1,
2713
] | 2 | [] | [] | 0 | true | Domain | Papillomavirus E2, N-terminal | Papillomavirus E2, N-terminal | PPV_E2_N | 5 |
IPR001867 | 1,867 | OmpR/PhoB-type DNA-binding domain | OmpR/PhoB-type_DNA-bd | Domain | 377,972 | false | false | Bacteria and plants frequently use two-components signal transduction systems (TCSs) to adapt to environmental changes and to survive under stress conditions. Typical TCSs couple a transmembrane histidine protein kinase (HK), which detects changes in the environmnent, to a cytosolic response regulator (RR), which often... | [
"GO:0003677",
"GO:0000160",
"GO:0006355"
] | [
"DNA binding",
"phosphorelay signal transduction system",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00486",
"PS51755",
"SM00862",
"cd00383"
] | [
"Trans_reg_C",
"OMPR_PHOB",
"Trans_reg_C",
"trans_reg_C"
] | [
365579,
368395,
372842,
333732
] | 4 | [] | [] | [] | 0 | [
"1gxp",
"1gxq",
"1kgs",
"1odd",
"1opc",
"1p2f",
"1qqi",
"1ys6",
"1ys7",
"2d1v",
"2fez",
"2ff4",
"2gwr",
"2hqn",
"2hqr",
"2hwv",
"2jpb",
"2jzy",
"2k4j",
"2m1b",
"2m87",
"2mlk",
"2naz",
"2oqr",
"2pmu",
"2rv8",
"2z33",
"2zxj",
"3q9s",
"3q9v",
"3r0j",
"3rjp"... | 93 | [
"PUB00005284",
"PUB00047220",
"PUB00048723",
"PUB00077752",
"PUB00077753",
"PUB00079826",
"PUB00079827"
] | [
"9016718",
"18789936",
"18052041",
"21634789",
"24990372",
"11934608",
"9199401"
] | [
"The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor.",
"Response regulator YycF essential for bacterial growth: X-ray crystal structure of the DNA-binding domain and its PhoB-like DNA recognition motif.",
"Structure of the DNA-binding domain of the response regulator PhoP ... | [
1997,
2008,
2007,
2011,
2014,
2002,
1997
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
7,
373767,
634,
9,
3555
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
2,
20
] | 2 | true | Domain | OmpR/PhoB-type DNA-binding domain | OmpR/PhoB-type DNA-binding domain | OmpR/PhoB-type_DNA-bd | 2 |
IPR001869 | 1,869 | Thiol-activated cytolysin | Thiol_cytolysin | Family | 1,811 | false | false | Thiol-activated cytolysins [ ] are toxins produced by a variety of Gram-positive bacteria and are characterised by their ability to lyse cholesterol-containing membranes, their reversible inactivation by oxidation and their capacity to bind to cholesterol. All these proteins contain a single cysteine residue, located i... | [
"GO:0015485"
] | [
"cholesterol binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PROSITE"
] | [
"PF01289",
"PR01400",
"PS00481"
] | [
"Thiol_cytolysin",
"TACYTOLYSIN",
"THIOL_CYTOLYSINS"
] | [
1761,
1329,
555
] | 3 | [
"PROSITEDOC"
] | [
"PDOC00436"
] | [
"PROSITEDOC:PDOC00436"
] | 1 | [
"1m3i",
"1m3j",
"1pfo",
"1s3r",
"2bk1",
"2bk2",
"3cqf",
"3hvn",
"4bik",
"4cdb",
"4hsc",
"4qqa",
"4qqq",
"4zgh",
"5aod",
"5aoe",
"5aof",
"5cr6",
"5cr8",
"5dhl",
"5dim",
"5imt",
"5imw",
"5imy",
"5ly6",
"6jmp",
"6nal",
"6xd4",
"6zd0",
"7wvh",
"8g32",
"8g33"... | 34 | [
"PUB00001356",
"PUB00002128"
] | [
"2888650",
"2254290"
] | [
"Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens.",
"Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and contains a single cysteine."
] | [
1987,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"ecological metagenomes"
] | [
1797,
8,
2,
4
] | 4 | [] | [] | 0 | true | Family | Thiol-activated cytolysin | Thiol-activated cytolysin | Thiol_cytolysin | 5 |
IPR001870 | 1,870 | B30.2/SPRY domain | B30.2/SPRY | Domain | 128,493 | false | false | The B30.2 domain was first identified as a protein domain encoded by an exon (named B30-2) in the Homo sapiens class I major histocompatibility complex region [ ], whereas the SPRY domain was first identified in a Dictyostelium discoideum kinase splA and mammalian calcium-release channels ryanodine receptors [ ]. B30.2... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50188"
] | [
"B302_SPRY"
] | [
128493
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50188",
"R-BTA-3134975",
"R-BTA-8951664",
"R-BTA-9755511",
"R-BTA-983168",
"R-CEL-3214841",
"R-CEL-72163",
"R-CEL-72203",
"R-CEL-8936459",
"R-CEL-9772755",
"R-DDI-5675482",
"R-DME-201722",
"R-DME-8936459",
"R-DME-8951664",
"R-DME-9772755",
"R-DME-983168",
"R-DME-9861718",
"R-D... | [
"PROSITEDOC:PDOC50188",
"REACTOME:R-BTA-3134975",
"REACTOME:R-BTA-8951664",
"REACTOME:R-BTA-9755511",
"REACTOME:R-BTA-983168",
"REACTOME:R-CEL-3214841",
"REACTOME:R-CEL-72163",
"REACTOME:R-CEL-72203",
"REACTOME:R-CEL-8936459",
"REACTOME:R-CEL-9772755",
"REACTOME:R-DDI-5675482",
"REACTOME:R-DME... | 109 | [
"2afj",
"2fbe",
"2fnj",
"2ihs",
"2iwg",
"2jk9",
"2lm3",
"2v24",
"2vok",
"2wl1",
"2yyo",
"3ek9",
"3emw",
"3f2o",
"3j8h",
"3kb5",
"3toj",
"3uv9",
"3zo0",
"4b3n",
"4b8e",
"4cfg",
"4cg4",
"4n7i",
"4n7u",
"4p9i",
"4p9j",
"4p9l",
"4qt6",
"4uwa",
"4uwe",
"4v1p"... | 480 | [
"PUB00005467",
"PUB00033710",
"PUB00033711",
"PUB00033712",
"PUB00033713"
] | [
"9204703",
"8114113",
"16498413",
"9196055",
"10223295"
] | [
"SPRY domains in ryanodine receptors (Ca(2+)-release channels).",
"Evolutionary study of multigenic families mapping close to the human MHC class I region.",
"Structural and functional insights into the B30.2/SPRY domain.",
"B30.2-like domain proteins: a growing family.",
"Protein fold analysis of the B30.2... | [
1997,
1993,
2006,
1997,
1999
] | 5 | [] | [
"IPR003879",
"IPR035731",
"IPR035778",
"IPR035780",
"IPR035784",
"IPR035785",
"IPR035786",
"IPR035787",
"IPR035790",
"IPR035791",
"IPR042723",
"IPR042780",
"IPR042828",
"IPR044116",
"IPR044736"
] | 0 | 15 | 0 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"Viruses",
"unclassified sequences"
] | [
201,
128233,
2,
37,
20
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
31,
43,
1109,
29,
300,
207,
3,
13,
228,
3,
3,
40
] | 12 | true | Domain | B30.2/SPRY domain | B30.2/SPRY domain | B30.2/SPRY | 7 |
IPR001872 | 1,872 | Peptidase A8, signal peptidase II | Peptidase_A8 | Family | 29,210 | false | false | This group of aspartic endopeptidases belong to the MEROPS peptidase family A8 (signal peptidase II family). The type example is the Escherichia coli lipoprotein signal peptidase or SPase II ( , MEROPS identifier A08.001), which removes the signal peptide from the N terminus of the murein prolipoprotein, an essential s... | [
"GO:0004190",
"GO:0006508",
"GO:0016020"
] | [
"aspartic-type endopeptidase activity",
"proteolysis",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PRINTS",
"PROSITE",
"PANTHER",
"NCBIFAM"
] | [
"MF_00161",
"PF01252",
"PR00781",
"PS00855",
"PTHR33695",
"TIGR00077"
] | [
"LspA",
"Peptidase_A8",
"LIPOSIGPTASE",
"SPASE_II",
"",
"lspA"
] | [
27809,
29182,
28199,
19525,
28735,
23616
] | 6 | [
"EC",
"GP",
"GP",
"METACYC",
"PROSITEDOC"
] | [
"3.4.23.36",
"GenProp0061",
"GenProp1327",
"PWY-7884",
"PDOC00669"
] | [
"EC:3.4.23.36",
"GP:GenProp0061",
"GP:GenProp1327",
"METACYC:PWY-7884",
"PROSITEDOC:PDOC00669"
] | 5 | [
"5dir",
"6fms",
"6ryo",
"6ryp",
"9emz"
] | 5 | [
"PUB00000093",
"PUB00000349",
"PUB00000522",
"PUB00001330",
"PUB00011023",
"PUB00011707",
"PUB00021296",
"PUB00042504",
"PUB00065205",
"PUB00066803",
"PUB00076784",
"PUB00076785",
"PUB00076786",
"PUB00076820",
"PUB00076821"
] | [
"2194475",
"1851433",
"8439290",
"6795036",
"10331925",
"11566868",
"10864493",
"2682266",
"23254940",
"21765428",
"4912600",
"10497172",
"21751400",
"3888977",
"6381496"
] | [
"The structure and function of the aspartic proteinases.",
"Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.",
"Evolutionary families of peptidases.",
"Gastric proteinases--structure, function, evolution and mechanism of action.",
"Crystal structure of the hy... | [
1990,
1991,
1993,
1981,
1999,
2001,
2000,
1989,
2013,
2011,
1970,
1999,
2011,
1985,
1984
] | 15 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"candidate division MSBL1",
"unclassified Klosneuvirinae",
"unclassified sequences"
] | [
28489,
60,
2,
2,
657
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Peptidase A8, signal peptidase II | Peptidase A8, signal peptidase II | Peptidase_A8 | 8 |
IPR001873 | 1,873 | Epithelial sodium channel | ENaC | Family | 28,419 | false | false | The apical membrane of many tight epithelia contains sodium channels that are primarily characterised by their high affinity to the diuretic blocker amiloride [ , , ]. These channels mediate the first step of active sodium reabsorption essential for the maintenance of body salt and water homeostasis [ ]. In vertebrates... | [
"GO:0005272",
"GO:0006814",
"GO:0016020"
] | [
"sodium channel activity",
"sodium ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00858",
"PR01078",
"PTHR11690"
] | [
"ASC",
"AMINACHANNEL",
""
] | [
28358,
19959,
25190
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00926",
"R-BTA-2672351",
"R-BTA-9730628",
"R-CEL-2672351",
"R-CEL-9730628",
"R-DME-2672351",
"R-DRE-2672351",
"R-GGA-2672351",
"R-HSA-2672351",
"R-HSA-9730628",
"R-MMU-2672351",
"R-MMU-9730628",
"R-RNO-2672351",
"R-RNO-9730628"
] | [
"PROSITEDOC:PDOC00926",
"REACTOME:R-BTA-2672351",
"REACTOME:R-BTA-9730628",
"REACTOME:R-CEL-2672351",
"REACTOME:R-CEL-9730628",
"REACTOME:R-DME-2672351",
"REACTOME:R-DRE-2672351",
"REACTOME:R-GGA-2672351",
"REACTOME:R-HSA-2672351",
"REACTOME:R-HSA-9730628",
"REACTOME:R-MMU-2672351",
"REACTOME:... | 14 | [
"2qts",
"3ij4",
"3s3w",
"3s3x",
"4fz0",
"4fz1",
"4ntw",
"4ntx",
"4nty",
"4nyk",
"5wku",
"5wkv",
"5wkx",
"5wky",
"6ave",
"6bqn",
"6cmc",
"6l6i",
"6l6n",
"6l6p",
"6vtk",
"6vtl",
"6wth",
"6x9h",
"7cfs",
"7cft",
"7lie",
"7rnn",
"7yvb",
"7yvc",
"8on7",
"8on8"... | 47 | [
"PUB00001528",
"PUB00002871",
"PUB00002932",
"PUB00003784"
] | [
"8181670",
"7929098",
"7499195",
"8905643"
] | [
"Molecular properties of epithelial, amiloride-blockable Na+ channels.",
"Membrane topology of the amiloride-sensitive epithelial sodium channel.",
"Molecular cloning and functional expression of a novel amiloride-sensitive Na+ channel.",
"Phylogenetic characterization of the epithelial Na+ channel (ENaC) fam... | [
1994,
1994,
1995,
1996
] | 4 | [] | [
"IPR004724",
"IPR004726"
] | 0 | 2 | 0 | [
"Eukaryota"
] | [
28419
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
45,
33,
60,
44,
27,
38
] | 6 | true | Family | Epithelial sodium channel | Epithelial sodium channel | ENaC | 5 |
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