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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR000935 | 935 | Thrombin receptor | Thrmbn_rcpt | Family | 909 | 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:0007596",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"G protein-coupled receptor signaling pathway",
"blood coagulation",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00908"
] | [
"THROMBINR"
] | [
909
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-140875",
"R-HSA-375276",
"R-HSA-416476",
"R-HSA-456926",
"R-MMU-140875",
"R-MMU-375276",
"R-MMU-416476",
"R-MMU-456926",
"R-RNO-140875",
"R-RNO-375276",
"R-RNO-416476",
"R-RNO-456926"
] | [
"REACTOME:R-HSA-140875",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-456926",
"REACTOME:R-MMU-140875",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-416476",
"REACTOME:R-MMU-456926",
"REACTOME:R-RNO-140875",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-416476",
"REACTOME:R-RNO-456... | 12 | [
"8xor",
"8xos",
"9d4z"
] | 3 | [
"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 | [
"IPR003912"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
909
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
20,
2,
2,
3
] | 4 | true | Family | Thrombin receptor | Thrombin receptor | Thrmbn_rcpt | 2 |
IPR000937 | 937 | Icosahedral viral capsid protein, S domain | Capsid_prot_S-dom_vir | Domain | 1,337 | false | false | The capsid proteins of plant icosahedral positive strand RNA viruses form 4 different domains, a positively charged, N-terminal 'R' domain, which interacts with RNA (66 residues); a connecting arm, 'a' (35 residues); a central, surface 'S' domain, which forms the virion shell; and a projecting, C-terminal 'P' domain [ ... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF00729",
"PR00233"
] | [
"Viral_coat",
"ICOSAHEDRAL"
] | [
1337,
570
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00480"
] | [
"PROSITEDOC:PDOC00480"
] | 1 | [
"1c8n",
"1f2n",
"1ng0",
"1opo",
"1smv",
"1vak",
"1vb2",
"1vb4",
"1x33",
"1x35",
"1x36",
"2izw",
"2tbv",
"2vq0",
"2wlp",
"2zah",
"3jb8",
"3zx8",
"3zx9",
"3zxa",
"4llf",
"4sbv",
"4v99",
"4y4y",
"4y5z",
"5yl1",
"6ab5",
"6ab6",
"6izl",
"6mrl",
"6mrm",
"9qvf"... | 36 | [
"PUB00003137",
"PUB00005242"
] | [
"1856686",
"7704529"
] | [
"Phylogeny of capsid proteins of small icosahedral RNA plant viruses.",
"The three-dimensional distribution of RNA and protein in the interior of tomato bushy stunt virus: a neutron low-resolution single-crystal diffraction study."
] | [
1991,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"aquatic metagenome"
] | [
12,
1324,
1
] | 3 | [] | [] | 0 | true | Domain | Icosahedral viral capsid protein, S domain | Icosahedral viral capsid protein, S domain | Capsid_prot_S-dom_vir | 4 |
IPR000938 | 938 | CAP Gly-rich domain | CAP-Gly_domain | Domain | 35,836 | false | false | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved glycine-rich domain, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the Caenorh... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART"
] | [
"PF01302",
"PS00845",
"PS50245",
"SM01052"
] | [
"CAP_GLY",
"CAP_GLY_1",
"CAP_GLY_2",
"CAP_GLY"
] | [
35457,
23206,
34601,
35256
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00660",
"R-BTA-168638",
"R-BTA-5357786",
"R-BTA-5357905",
"R-BTA-5357956",
"R-BTA-5689880",
"R-BTA-936440",
"R-DME-3371497",
"R-DME-6807878",
"R-DME-6811436",
"R-GGA-141444",
"R-GGA-2467813",
"R-GGA-2500257",
"R-GGA-5663220",
"R-GGA-9648025",
"R-HSA-141444",
"R-HSA-168638",
"R... | [
"PROSITEDOC:PDOC00660",
"REACTOME:R-BTA-168638",
"REACTOME:R-BTA-5357786",
"REACTOME:R-BTA-5357905",
"REACTOME:R-BTA-5357956",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-936440",
"REACTOME:R-DME-3371497",
"REACTOME:R-DME-6807878",
"REACTOME:R-DME-6811436",
"REACTOME:R-GGA-141444",
"REACTOME:R-G... | 103 | [
"1ixd",
"1lpl",
"1tov",
"1txq",
"1whg",
"1whh",
"1whj",
"1whk",
"1whl",
"1whm",
"2cow",
"2coy",
"2coz",
"2cp0",
"2cp2",
"2cp3",
"2cp5",
"2cp6",
"2cp7",
"2e3h",
"2e3i",
"2e4h",
"2hkn",
"2hkq",
"2hl3",
"2hl5",
"2hqh",
"2m02",
"2mpx",
"2qk0",
"2z0w",
"3e2u"... | 54 | [
"PUB00015605"
] | [
"12221106"
] | [
"Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"organismal metagenomes"
] | [
13,
35818,
5
] | 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... | [
6,
10,
129,
30,
87,
34,
4,
6,
67,
4,
3,
14
] | 12 | true | Domain | CAP Gly-rich domain | CAP Gly-rich domain | CAP-Gly_domain | 4 |
IPR000939 | 939 | Adenoviral fibre protein, repeat/shaft region | Adenobir_fibre_prot_rpt/shaft | Repeat | 1,365 | false | false | Adenoviruses are responsible for diseases such as pneumonia, cystitis, conjunctivitis and diarrhoea, all of which can be fatal to patients who are immunocompromised [ ]. Viral infection commences with recognition of host cell receptors by means of specialised proteins on viral surfaces. Specific attachment of adenoviru... | [
"GO:0019062"
] | [
"virion attachment to host cell"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00608"
] | [
"Adeno_shaft"
] | [
1365
] | 1 | [] | [] | [] | 0 | [
"1qiu",
"1v1h",
"1v1i",
"3izo",
"7tau",
"8qjx",
"8qjy",
"8qk3",
"9fae",
"9faf",
"9fag",
"9fah"
] | 12 | [
"PUB00005244"
] | [
"7704534"
] | [
"Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Adenoviridae",
"Bacteria",
"Eukaryota"
] | [
1353,
5,
7
] | 3 | [] | [] | 0 | true | Repeat | Adenoviral fibre protein, repeat/shaft region | Adenoviral fibre protein, repeat/shaft region | Adenobir_fibre_prot_rpt/shaft | 5 |
IPR000940 | 940 | Methyltransferase, NNMT/PNMT/TEMT | NNMT_TEMT_trans | Family | 3,765 | false | false | Methyl transfer from the ubiquitous S-adenosyl-L-methionine (AdoMet) to either nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalysed by methyltransferases (Mtases) and modifies DNA, RNA, proteins and small molecules, such as c... | [
"GO:0008168"
] | [
"methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PIRSF",
"PROFILE",
"PANTHER"
] | [
"PF01234",
"PIRSF000384",
"PS51681",
"PTHR10867"
] | [
"NNMT_PNMT_TEMT",
"PNMTase",
"SAM_MT_NNMT_PNMT_TEMT",
""
] | [
3579,
1262,
3723,
3518
] | 4 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1",
"PDOC00844",
"R-CEL-156581",
"R-CEL-196807",
"R-CEL-209905",
"R-HSA-156581",
"R-HSA-196807",
"R-HSA-209905",
"R-HSA-2408508",
"R-HSA-2408552",
"R-MMU-156581",
"R-MMU-196807",
"R-MMU-209905",
"R-RNO-209905",
"R-SSC-209905"
] | [
"EC:2.1.1",
"PROSITEDOC:PDOC00844",
"REACTOME:R-CEL-156581",
"REACTOME:R-CEL-196807",
"REACTOME:R-CEL-209905",
"REACTOME:R-HSA-156581",
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-209905",
"REACTOME:R-HSA-2408508",
"REACTOME:R-HSA-2408552",
"REACTOME:R-MMU-156581",
"REACTOME:R-MMU-196807",
"REA... | 15 | [
"1hnn",
"1n7i",
"1n7j",
"1yz3",
"2a14",
"2an3",
"2an4",
"2an5",
"2g70",
"2g71",
"2g72",
"2g8n",
"2i62",
"2iip",
"2obf",
"2ony",
"2onz",
"2opb",
"3hca",
"3hcb",
"3hcc",
"3hcd",
"3hce",
"3hcf",
"3kpj",
"3kpu",
"3kpv",
"3kpw",
"3kpy",
"3kqm",
"3kqo",
"3kqp"... | 78 | [
"PUB00000896",
"PUB00002846",
"PUB00004370",
"PUB00004446",
"PUB00004831",
"PUB00006319",
"PUB00009714",
"PUB00009715"
] | [
"8343957",
"8182091",
"2690010",
"8127644",
"7971991",
"7897657",
"2684970",
"7607476"
] | [
"Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine.",
"Human liver nicotinamide N-methyltransferase. cDNA cloning, expression, and biochemical characterization.",
"Sequence motifs characteristic of DNA[cytosine-N4]methyltransferases: similarity to adenine and cytosine-C5... | [
1993,
1994,
1989,
1994,
1994,
1995,
1989,
1995
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
545,
3220
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
11,
6,
10
] | 5 | true | Family | Methyltransferase, NNMT/PNMT/TEMT | Methyltransferase, NNMT/PNMT/TEMT | NNMT_TEMT_trans | 1 |
IPR000941 | 941 | Enolase | Enolase | Family | 49,905 | false | false | Enolase (2-phospho-D-glycerate hydrolase) is an essential, homodimeric enzyme that catalyses the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways [ , ]. The reaction is facilitated by the presence of metal ions [ ]. In vertebrates, there are 3... | [
"GO:0000287",
"GO:0004634",
"GO:0006096",
"GO:0000015"
] | [
"magnesium ion binding",
"phosphopyruvate hydratase activity",
"glycolytic process",
"phosphopyruvate hydratase complex"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"HAMAP",
"PIRSF",
"PRINTS",
"PANTHER",
"SFLD",
"NCBIFAM",
"CDD"
] | [
"MF_00318",
"PIRSF001400",
"PR00148",
"PTHR11902",
"SFLDF00002",
"TIGR01060",
"cd03313"
] | [
"Enolase",
"Enolase",
"ENOLASE",
"",
"enolase",
"eno",
"enolase"
] | [
38871,
36859,
43990,
49841,
36951,
39934,
39209
] | 7 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",... | [
"4.2.1.11",
"GenProp0691",
"GenProp1166",
"GenProp1306",
"GenProp1344",
"GenProp1407",
"GenProp1599",
"GenProp1612",
"PWY-1042",
"PWY-1622",
"PWY-2221",
"PWY-5484",
"PWY-5723",
"PWY-6142",
"PWY-6886",
"PWY-6901",
"PWY-7003",
"PWY-7124",
"PWY-7218",
"PWY-8004",
"PWY-8404",
"... | [
"EC:4.2.1.11",
"GP:GenProp0691",
"GP:GenProp1166",
"GP:GenProp1306",
"GP:GenProp1344",
"GP:GenProp1407",
"GP:GenProp1599",
"GP:GenProp1612",
"METACYC:PWY-1042",
"METACYC:PWY-1622",
"METACYC:PWY-2221",
"METACYC:PWY-5484",
"METACYC:PWY-5723",
"METACYC:PWY-6142",
"METACYC:PWY-6886",
"META... | 49 | [
"1e9i",
"1ebg",
"1ebh",
"1els",
"1iyx",
"1l8p",
"1nel",
"1oep",
"1one",
"1p43",
"1p48",
"1pdy",
"1pdz",
"1te6",
"1w6t",
"2akm",
"2akz",
"2al1",
"2al2",
"2fym",
"2one",
"2pa6",
"2psn",
"2ptw",
"2ptx",
"2pty",
"2ptz",
"2pu0",
"2pu1",
"2xgz",
"2xh0",
"2xh2"... | 112 | [
"PUB00000466",
"PUB00000496",
"PUB00004545",
"PUB00005102",
"PUB00029502"
] | [
"3390159",
"1840492",
"1859865",
"3589669",
"8605183"
] | [
"Enolase isoenzymes in adult and developing Xenopus laevis and characterization of a cloned enolase sequence.",
"Molecular structure of the human muscle-specific enolase gene (ENO3).",
"Characterization of a maize cDNA that complements an enolase-deficient mutant of Escherichia coli.",
"Recruitment of enzymes... | [
1988,
1991,
1991,
1987,
1996
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Streptococcus phage 20617",
"unclassified sequences"
] | [
1041,
27488,
20534,
1,
841
] | 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",... | [
12,
1,
13,
2,
1,
31,
26,
2,
20,
33,
5,
2,
54
] | 13 | true | Family | Enolase | Enolase | Enolase | 7 |
IPR000942 | 942 | Geminivirus AL2 coat protein, MSV type | Gemini_AL2 | Family | 4,564 | false | false | Geminiviruses are characterised by a genome of circular single-stranded DNA encapsidated in twinned (geminate) quasi-isometric particles, from which the group derives its name [ ]. Most geminiviruses can be divided into two subgroups on the basis of host range and/or insect vector: i.e. those that infect dicotyledenous... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF01440",
"PR00230"
] | [
"Gemini_AL2",
"GEMCOATAL2"
] | [
4564,
4136
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001133",
"PUB00001145",
"PUB00003142",
"PUB00003143",
"PUB00004348",
"PUB00004397",
"PUB00005574",
"PUB00005578"
] | [
"6526009",
"16453696",
"1919519",
"1588314",
"2829117",
"1840676",
"1984668",
"1926771"
] | [
"The nucleotide sequence of maize streak virus DNA.",
"The nucleotide sequence of an infectious clone of the geminivirus beet curly top virus.",
"The nucleotide sequence and genome structure of the geminivirus miscanthus streak virus.",
"The nucleotide sequence of an infectious insect-transmissible clone of t... | [
1984,
1986,
1991,
1992,
1988,
1991,
1991,
1991
] | 8 | [] | [] | 0 | 0 | null | [
"Pentapetalae",
"Viruses"
] | [
5,
4559
] | 2 | [] | [] | 0 | true | Family | Geminivirus AL2 coat protein, MSV type | Geminivirus AL2 coat protein, MSV type | Gemini_AL2 | 3 |
IPR000943 | 943 | RNA polymerase sigma-70 | RNA_pol_sigma70 | Domain | 104,924 | false | false | The bacterial core RNA polymerase complex, which consists of five subunits, is sufficient for transcription elongation and termination but is unable to initiate transcription. Transcription initiation from promoter elements requires a sixth, dissociable subunit called a sigma factor, which reversibly associates with th... | [
"GO:0003700",
"GO:0006352",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"DNA-templated transcription initiation",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PIRSF",
"PRINTS",
"PROSITE",
"PROSITE"
] | [
"PIRSF000770",
"PR00046",
"PS00715",
"PS00716"
] | [
"RNA_pol_sigma-SigE/K",
"SIGMA70FCT",
"SIGMA70_1",
"SIGMA70_2"
] | [
30607,
99266,
72796,
67911
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00592"
] | [
"PROSITEDOC:PDOC00592"
] | 1 | [
"1iw7",
"1ku2",
"1ku3",
"1ku7",
"1l0o",
"1l9u",
"1l9z",
"1rio",
"1rp3",
"1sc5",
"1sig",
"1smy",
"1tlh",
"1tty",
"1zyr",
"2a68",
"2a69",
"2a6e",
"2a6h",
"2be5",
"2cw0",
"2p7v",
"3dxj",
"3eql",
"3iyd",
"3les",
"3lev",
"3mzy",
"3n97",
"3t72",
"3ugo",
"3ugp"... | 371 | [
"PUB00000061",
"PUB00002181",
"PUB00004340",
"PUB00010647",
"PUB00088319"
] | [
"3052291",
"1597408",
"3092189",
"12540296",
"25596450"
] | [
"Structure and function of bacterial sigma factors.",
"The sigma 70 family: sequence conservation and evolutionary relationships.",
"Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.",
"The sigma70 family of sigma factors.",
"Plastid sigma factors: Their individual f... | [
1988,
1992,
1986,
2003,
2015
] | 5 | [
"IPR014284"
] | [
"IPR012760"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
6,
98315,
4835,
117,
1651
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
20,
4,
21,
39
] | 4 | true | Domain | RNA polymerase sigma-70 | RNA polymerase sigma-70 | RNA_pol_sigma70 | 2 |
IPR000944 | 944 | Transcription regulator Rrf2 | Tscrpt_reg_Rrf2 | Family | 53,238 | false | false | This entry represents transcriptional regulators such as Desulfovibrio vulgaris Protein Rrf2, Escherichia coli IscR and Bacillus subtilis NsrR. Protein Rrf2 is a repressor of the hmc operon encoding a cytochrome redox complex for electron transport from hydrogen to sulphate [ ]. E. coli IscR regulates the transcription... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"PANTHER",
"NCBIFAM"
] | [
"PF02082",
"PS51197",
"PTHR33221",
"TIGR00738"
] | [
"Rrf2",
"HTH_RRF2_2",
"",
"rrf2_super"
] | [
52264,
52371,
52251,
40475
] | 4 | [
"PROSITEDOC"
] | [
"PDOC01035"
] | [
"PROSITEDOC:PDOC01035"
] | 1 | [
"1xd7",
"1ylf",
"2y75",
"3k69",
"3lwf",
"3t8r",
"3t8t",
"4chu",
"4cic",
"4hf0",
"4hf1",
"4hf2",
"5n07",
"5n08",
"6hsd",
"6hse",
"6hsm",
"6y42",
"6y45",
"7b0c",
"7zpn"
] | 21 | [
"PUB00017575",
"PUB00033785",
"PUB00054980",
"PUB00057834"
] | [
"9148780",
"11742080",
"16824106",
"16885456"
] | [
"Deletion of two downstream genes alters expression of the hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough.",
"IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins.",
"IscR acts as an activator in respons... | [
1997,
2001,
2006,
2006
] | 4 | [] | [
"IPR010242",
"IPR014290",
"IPR023761"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
516,
51892,
52,
778
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
2
] | 2 | true | Family | Transcription regulator Rrf2 | Transcription regulator Rrf2 | Tscrpt_reg_Rrf2 | 2 |
IPR000945 | 945 | Dopamine beta-hydroxylase-like | DBH-like | Family | 7,584 | false | false | This family represents Dopamine beta-hydroxylase (DBH) and related enzymes, including tyramine beta-hydroxylase, MOXD1 homologue 1/2 and DBH-like monooxygenase protein 1/2 [ ]. DBH, also known as Dopamine beta-hydroxylase, is a class of ascorbate-dependent enzymes from the catecholamine biosynthetic pathway that requir... | [
"GO:0004500"
] | [
"dopamine beta-monooxygenase activity"
] | [
"molecular_function"
] | 1 | [
"PANTHER"
] | [
"PTHR10157"
] | [
""
] | [
7584
] | 1 | [
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.17.-",
"PWY-5404",
"PWY-7297",
"R-DME-209905",
"R-HSA-209905",
"R-MMU-209905",
"R-RNO-209905"
] | [
"EC:1.14.17.-",
"METACYC:PWY-5404",
"METACYC:PWY-7297",
"REACTOME:R-DME-209905",
"REACTOME:R-HSA-209905",
"REACTOME:R-MMU-209905",
"REACTOME:R-RNO-209905"
] | 7 | [
"4zel"
] | 1 | [
"PUB00002550",
"PUB00068461",
"PUB00068463"
] | [
"2295597",
"8656284",
"6998654"
] | [
"Primary amino acid sequence of bovine dopamine beta-hydroxylase.",
"Characterization of Drosophila tyramine beta-hydroxylase gene and isolation of mutant flies lacking octopamine.",
"Dopamine beta-hydroxylase in health and disease."
] | [
1990,
1996,
1980
] | 3 | [] | [
"IPR028460"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
582,
6953,
23,
26
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
16,
6,
5,
3,
9
] | 6 | true | Family | Dopamine beta-hydroxylase-like | Dopamine beta-hydroxylase-like | DBH-like | 4 |
IPR000949 | 949 | ELM2 domain | ELM2_dom | Domain | 25,248 | false | false | The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex [ ]. The domain is usually found to the N terminus of a myb-like DNA binding domain and a GATA binding domain. ELM2, in some instances, is also found associated with the A... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01448",
"PS51156",
"SM01189"
] | [
"ELM2",
"ELM2",
"ELM2"
] | [
20176,
24333,
20361
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51156",
"R-DME-3214815",
"R-DME-983231",
"R-HSA-3214815",
"R-HSA-3232118",
"R-HSA-427389",
"R-HSA-6804758",
"R-HSA-73762",
"R-HSA-8943724",
"R-HSA-9679191",
"R-HSA-983231",
"R-HSA-9843940",
"R-HSA-9844594",
"R-HSA-9845323",
"R-MMU-3214815",
"R-MMU-3232118",
"R-MMU-6804758",
"R... | [
"PROSITEDOC:PDOC51156",
"REACTOME:R-DME-3214815",
"REACTOME:R-DME-983231",
"REACTOME:R-HSA-3214815",
"REACTOME:R-HSA-3232118",
"REACTOME:R-HSA-427389",
"REACTOME:R-HSA-6804758",
"REACTOME:R-HSA-73762",
"REACTOME:R-HSA-8943724",
"REACTOME:R-HSA-9679191",
"REACTOME:R-HSA-983231",
"REACTOME:R-HSA... | 24 | [
"2xaf",
"2xag",
"2xah",
"2xaj",
"2xaq",
"2xas",
"3zms",
"3zmt",
"3zmu",
"3zmv",
"3zmz",
"3zn0",
"3zn1",
"4bkx",
"4czz",
"4uv8",
"4uv9",
"4uva",
"4uvb",
"4uvc",
"4uxn",
"5icn",
"5l3b",
"5l3c",
"5l3d",
"5lhg",
"5lhh",
"5lhi",
"6te1",
"6tuy",
"6z2j",
"6z2k"... | 41 | [
"PUB00009422"
] | [
"10226007"
] | [
"The Caenorhabditis elegans genes egl-27 and egr-1 are similar to MTA1, a member of a chromatin regulatory complex, and are redundantly required for embryonic patterning."
] | [
1999
] | 1 | [] | [
"IPR031724"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
33,
25208,
4,
3
] | 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",
"Zea mays"
] | [
25,
28,
75,
34,
40,
50,
1,
9,
62,
7
] | 10 | true | Domain | ELM2 domain | ELM2 domain | ELM2_dom | 7 |
IPR000952 | 952 | AB hydrolase 4, conserved site | AB_hydrolase_4_CS | Conserved_site | 7,199 | false | false | This entry represents a conserved site found in some of the AB hydrolase 4 family members, including mammalian ABHD1/2/3, budding yeast Eht1, Eeb1 and MGL2, and bacterial putative esterases. Human ABHD3 is a phospholipase that may play a role in phospholipids remodeling. It may selectively cleave myristate (C14)-contai... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01133"
] | [
"UPF0017"
] | [
7199
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.1",
"PDOC00872",
"R-BTA-1483191",
"R-CEL-1483191",
"R-HSA-1483191",
"R-MMU-1483191",
"R-SCE-1483191"
] | [
"EC:3.1.1",
"PROSITEDOC:PDOC00872",
"REACTOME:R-BTA-1483191",
"REACTOME:R-CEL-1483191",
"REACTOME:R-HSA-1483191",
"REACTOME:R-MMU-1483191",
"REACTOME:R-SCE-1483191"
] | 7 | [] | 0 | [
"PUB00074273",
"PUB00074274",
"PUB00074275",
"PUB00097271",
"PUB00097272"
] | [
"21926997",
"16361250",
"15721306",
"29225428",
"26991558"
] | [
"Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids.",
"The Saccharomyces cerevisiae EHT1 and EEB1 genes encode novel enzymes with medium-chain fatty acid ethyl ester synthesis and hydrolysis capacity.",
"Increase of smooth muscle cell migration and of intimal hyperplasia in m... | [
2011,
2006,
2005,
2017,
2016
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3999,
3174,
26
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
6,
2,
2,
6,
1,
9,
4,
2,
6,
3,
5
] | 11 | true | Conserved_site | AB hydrolase 4, conserved site | AB hydrolase 4, conserved site | AB_hydrolase_4_CS | 3 |
IPR000953 | 953 | Chromo/chromo shadow domain | Chromo/chromo_shadow_dom | Domain | 99,434 | false | false | The CHROMO (CHRromatin Organization MOdifier) domain [ , , , ] is a conserved region of around 60 amino acids, originally identified in Drosophila modifiers of variegation. These are proteins that alter the structure of chromatin to the condensed morphology of heterochromatin, a cytologically visible condition where ge... | [] | [] | [] | 0 | [
"PROFILE",
"SMART"
] | [
"PS50013",
"SM00298"
] | [
"CHROMO_2",
"CHROMO"
] | [
85333,
83971
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00517",
"R-CEL-4551638",
"R-CEL-5693607",
"R-CEL-6804758",
"R-CEL-73772",
"R-CEL-9031628",
"R-CEL-983231",
"R-DME-201722",
"R-DME-2559580",
"R-DME-2559586",
"R-DME-3108214",
"R-DME-3214815",
"R-DME-3899300",
"R-DME-427359",
"R-DME-4570464",
"R-DME-5693548",
"R-DME-5693565",
"R... | [
"PROSITEDOC:PDOC00517",
"REACTOME:R-CEL-4551638",
"REACTOME:R-CEL-5693607",
"REACTOME:R-CEL-6804758",
"REACTOME:R-CEL-73772",
"REACTOME:R-CEL-9031628",
"REACTOME:R-CEL-983231",
"REACTOME:R-DME-201722",
"REACTOME:R-DME-2559580",
"REACTOME:R-DME-2559586",
"REACTOME:R-DME-3108214",
"REACTOME:R-DM... | 164 | [
"1ap0",
"1dz1",
"1e0b",
"1g6z",
"1guw",
"1kna",
"1kne",
"1pdq",
"1pfb",
"1q3l",
"1s4z",
"1wgs",
"1x32",
"1x3p",
"1x3q",
"2b2t",
"2b2u",
"2b2v",
"2b2w",
"2b2y",
"2d9u",
"2dnt",
"2dnv",
"2dy7",
"2dy8",
"2ee1",
"2efi",
"2eko",
"2epb",
"2f5k",
"2fmm",
"2h1e"... | 215 | [
"PUB00004399",
"PUB00004460",
"PUB00004461",
"PUB00005519",
"PUB00017969"
] | [
"1708124",
"7667093",
"7501439",
"1982376",
"11574148"
] | [
"A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants.",
"The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1.",
"The chromo superfamily: new members, duplication of the chromo domain and possible role in delivering transcriptio... | [
1991,
1995,
1995,
1990,
2001
] | 5 | [] | [
"IPR008251",
"IPR023780"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
76,
99329,
14,
15
] | 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... | [
80,
24,
123,
77,
133,
100,
12,
104,
129,
4,
9,
202
] | 12 | true | Domain | Chromo/chromo shadow domain | Chromo/chromo shadow domain | Chromo/chromo_shadow_dom | 4 |
IPR000956 | 956 | Stathmin family | Stathmin_fam | Family | 6,721 | false | false | Stathmin [ ] (from the Greek 'stathmos' which means relay), is a ubiquitous intracellular protein, present in a variety of phosphorylated forms. It is involved in the regulation of the microtubule (MT) filament system by destabilising microtubules. It prevents assembly and promotes disassembly of microtubules [ ]. Howe... | [
"GO:0031110"
] | [
"regulation of microtubule polymerization or depolymerization"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PIRSF",
"PRINTS",
"PROFILE",
"PANTHER"
] | [
"PF00836",
"PIRSF002285",
"PR00345",
"PS51663",
"PTHR10104"
] | [
"Stathmin",
"Stathmin",
"STATHMIN",
"STATHMIN_3",
""
] | [
6382,
3631,
5947,
6392,
6408
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00487",
"R-GGA-9696273",
"R-HSA-1251985",
"R-HSA-9696273",
"R-MMU-9696273",
"R-RNO-9696273"
] | [
"PROSITEDOC:PDOC00487",
"REACTOME:R-GGA-9696273",
"REACTOME:R-HSA-1251985",
"REACTOME:R-HSA-9696273",
"REACTOME:R-MMU-9696273",
"REACTOME:R-RNO-9696273"
] | 6 | [
"1sa0",
"1sa1",
"1z2b",
"3du7",
"3e22",
"3hkb",
"3hkc",
"3hkd",
"3hke",
"3n2g",
"3n2k",
"3ryc",
"3ryf",
"3ryh",
"3ryi",
"3ut5",
"4eb6",
"4f61",
"4f6r",
"4i4t",
"4i50",
"4i55",
"4ihj",
"4iij",
"4o2a",
"4o2b",
"4o4h",
"4o4i",
"4o4j",
"4o4l",
"4tuy",
"4tv8"... | 329 | [
"PUB00005376",
"PUB00017960",
"PUB00017961",
"PUB00030967",
"PUB00062130",
"PUB00062131",
"PUB00069417"
] | [
"1957351",
"9603203",
"9342231",
"15014504",
"11160824",
"14598370",
"11278715"
] | [
"Stathmin: a relay phosphoprotein for multiple signal transduction?",
"SCLIP: a novel SCG10-like protein of the stathmin family expressed in the nervous system.",
"The stathmin family -- molecular and biological characterization of novel mammalian proteins expressed in the nervous system.",
"Insight into tubu... | [
1991,
1998,
1997,
2004,
2001,
2004,
2001
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"viral metagenome"
] | [
6,
6714,
1
] | 3 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
9,
21,
22,
28
] | 5 | true | Family | Stathmin family | Stathmin family | Stathmin_fam | 4 |
IPR000957 | 957 | Sulphate/thiosulphate-binding, conserved site | Sulphate/thiosulphate-bd_CS | Conserved_site | 2,973 | false | false | Sulphate-binding protein (gene sbp or sbpA) and thiosulphate-binding protein (gene cysP) are two structurally related periplasmic bacterial proteins which specifically bind sulphate and thiosulphate and are involved in the transport systems for these nutrients [ , ]. There are two conserved regions in the protein, one ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00401"
] | [
"PROK_SULFATE_BIND_1"
] | [
2973
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00337"
] | [
"PROSITEDOC:PDOC00337"
] | 1 | [
"1sbp"
] | 1 | [
"PUB00002107",
"PUB00003227",
"PUB00028072"
] | [
"2188959",
"3288756",
"1708375"
] | [
"Sulfate and thiosulfate transport in Escherichia coli K-12: identification of a gene encoding a novel protein involved in thiosulfate binding.",
"The 2 A resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium.",
"Characterization and mutagenesis of sulfur-reg... | [
1990,
1988,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2968,
3,
2
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Conserved_site | Sulphate/thiosulphate-binding, conserved site | Sulphate/thiosulphate-binding, conserved site | Sulphate/thiosulphate-bd_CS | 1 |
IPR000959 | 959 | POLO box domain | POLO_box_dom | Domain | 8,084 | false | false | A subgroup of serine/threonine protein kinases, Polo or Polo-like kinases play multiple roles during the cell cycle. Polo kinases are required at several key points through mitosis, starting from control of the G2/M transition through phosphorylation of Cdc25C and mitotic cyclins. They are also involved in meiosis I as... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF00659",
"PS50078"
] | [
"POLO_box",
"POLO_BOX"
] | [
6388,
7859
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11.21",
"PDOC50078",
"R-BTA-141444",
"R-BTA-156711",
"R-BTA-162658",
"R-BTA-174178",
"R-BTA-176412",
"R-BTA-176417",
"R-BTA-2299718",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-2565942",
"R-BTA-2980767",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-5620... | [
"EC:2.7.11.21",
"PROSITEDOC:PDOC50078",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-156711",
"REACTOME:R-BTA-162658",
"REACTOME:R-BTA-174178",
"REACTOME:R-BTA-176412",
"REACTOME:R-BTA-176417",
"REACTOME:R-BTA-2299718",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-2565942",
... | 168 | [
"1mby",
"1q4k",
"1q4o",
"1umw",
"2n19",
"2ogq",
"2ojx",
"3bzi",
"3c5l",
"3fvh",
"3hih",
"3hik",
"3p2w",
"3p2z",
"3p34",
"3p35",
"3p36",
"3p37",
"3q1i",
"3rq7",
"4dfw",
"4e67",
"4e9c",
"4e9d",
"4h5x",
"4h71",
"4hab",
"4hco",
"4hy2",
"4j7b",
"4lkl",
"4lkm"... | 81 | [
"PUB00006187",
"PUB00006188",
"PUB00006189",
"PUB00010649",
"PUB00010650",
"PUB00083696",
"PUB00094294"
] | [
"9914175",
"1660828",
"10594031",
"12352953",
"12615979",
"25533956",
"22018922"
] | [
"Polo-like kinases: positive regulators of cell division from start to finish.",
"polo encodes a protein kinase homolog required for mitosis in Drosophila.",
"Essential function of the polo box of Cdc5 in subcellular localization and induction of cytokinetic structures.",
"The Sak polo-box comprises a structu... | [
1998,
1991,
2000,
2002,
2003,
2015,
2011
] | 7 | [] | [
"IPR033695",
"IPR033696",
"IPR033701"
] | 0 | 3 | 0 | [
"Eukaryota",
"marine sediment metagenome"
] | [
8083,
1
] | 2 | [
"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... | [
3,
10,
2,
15,
17,
1,
23,
1,
1,
1
] | 10 | true | Domain | POLO box domain | POLO box domain | POLO_box_dom | 9 |
IPR000960 | 960 | Flavin monooxygenase FMO | Flavin_mOase | Family | 31,704 | false | false | Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic-metabolising enzymes [ ]. Using an NADPH cofactor and FAD prosthetic group, these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen, sulphur, phosphorus and selenium atoms in a range of structurally diverse compounds. FMOs hav... | [
"GO:0050660",
"GO:0050661"
] | [
"flavin adenine dinucleotide binding",
"NADP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF000332",
"PR00370"
] | [
"FMO",
"FMOXYGENASE"
] | [
25138,
23224
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.13",
"R-BTA-217271",
"R-CFA-1614558",
"R-CFA-217271",
"R-HSA-1614558",
"R-HSA-217271",
"R-HSA-5579019",
"R-MMU-1614558",
"R-MMU-217271",
"R-RNO-1614558",
"R-RNO-217271",
"R-SSC-1614558",
"R-SSC-217271"
] | [
"EC:1.14.13",
"REACTOME:R-BTA-217271",
"REACTOME:R-CFA-1614558",
"REACTOME:R-CFA-217271",
"REACTOME:R-HSA-1614558",
"REACTOME:R-HSA-217271",
"REACTOME:R-HSA-5579019",
"REACTOME:R-MMU-1614558",
"REACTOME:R-MMU-217271",
"REACTOME:R-RNO-1614558",
"REACTOME:R-RNO-217271",
"REACTOME:R-SSC-1614558",... | 13 | [
"1vqw",
"2gv8",
"2gvc",
"2vq7",
"2vqb",
"2xlp",
"2xlr",
"2xls",
"2xlt",
"2xlu",
"2xve",
"2xvf",
"2xvh",
"2xvi",
"2xvj",
"5gsn",
"5ipy",
"5iq1",
"5iq4",
"5nmw",
"5nmx",
"6hns",
"6kbw",
"6se3",
"6sek",
"6sem",
"6sf0",
"6wpu",
"7al4",
"7d4k",
"7d4m",
"7d4n"... | 40 | [
"PUB00000158",
"PUB00000516",
"PUB00002611",
"PUB00002642",
"PUB00002834",
"PUB00004772",
"PUB00005185",
"PUB00082329",
"PUB00101886"
] | [
"8311461",
"1417778",
"2318837",
"1712018",
"8486656",
"1542660",
"8091229",
"27166860",
"32156684"
] | [
"A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities.",
"Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family.",
"The flavin-containing monooxygenase enzymes expressed in... | [
1994,
1992,
1990,
1991,
1993,
1992,
1994,
2016,
2020
] | 9 | [
"IPR020946"
] | [
"IPR002253",
"IPR002254",
"IPR002255",
"IPR002256",
"IPR002257"
] | 1 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5,
6966,
24642,
91
] | 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... | [
78,
8,
8,
4,
23,
25,
4,
59,
31,
1,
1,
64
] | 12 | true | Family | Flavin monooxygenase FMO | Flavin monooxygenase FMO | Flavin_mOase | 5 |
IPR000961 | 961 | AGC-kinase, C-terminal | AGC-kinase_C | Domain | 135,260 | false | false | The AGC (cAMP-dependent, cGMP-dependent and protein kinase C) protein kinase family embraces a collection of protein kinases that display a high degree of sequence similarity within their respective kinase domains. AGC kinase proteins are characterised by three conserved phosphorylation sites that critically regulate t... | [
"GO:0004674",
"GO:0005524",
"GO:0006468"
] | [
"protein serine/threonine kinase activity",
"ATP binding",
"protein phosphorylation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROFILE",
"SMART"
] | [
"PS51285",
"SM00133"
] | [
"AGC_KINASE_CTER",
"S_TK_X"
] | [
134133,
107626
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11",
"R-BTA-111933",
"R-BTA-114516",
"R-BTA-1169091",
"R-BTA-163615",
"R-BTA-164378",
"R-BTA-180024",
"R-BTA-2514859",
"R-BTA-2565942",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-381676",
"R-BTA-392517",
"R-BTA-416476",
"R-BTA-416993",
"R-BTA-418457... | [
"EC:2.7.11",
"REACTOME:R-BTA-111933",
"REACTOME:R-BTA-114516",
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-163615",
"REACTOME:R-BTA-164378",
"REACTOME:R-BTA-180024",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-380259",
"REACTOME:R-BTA-380270",
"REACTOME:R-BTA-380284",
"... | 865 | [
"1apm",
"1atp",
"1bkx",
"1bx6",
"1cdk",
"1cmk",
"1ctp",
"1fmo",
"1fot",
"1gzk",
"1gzn",
"1gzo",
"1j3h",
"1jbp",
"1jlu",
"1l3r",
"1mrv",
"1mry",
"1o6k",
"1o6l",
"1omw",
"1q24",
"1q61",
"1q62",
"1q8t",
"1q8u",
"1q8w",
"1rdq",
"1re8",
"1rej",
"1rek",
"1smh"... | 652 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00022308",
"PUB00034898",
"PUB00034899",
"PUB00043770",
"PUB00043771",
"PUB00043772"
] | [
"3291115",
"12368087",
"12471243",
"12434148",
"15078142",
"15320712",
"12495431",
"11709088",
"15209375"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-P... | [
1988,
2002,
2002,
2002,
2004,
2004,
2003,
2001,
2004
] | 9 | [] | [
"IPR017892"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Gammaretrovirus",
"Natranaeroarchaeum",
"ecological metagenomes"
] | [
56,
135194,
5,
2,
3
] | 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... | [
72,
44,
352,
94,
207,
183,
12,
34,
291,
13,
13,
118
] | 12 | true | Domain | AGC-kinase, C-terminal | AGC-kinase, C-terminal | AGC-kinase_C | 3 |
IPR000962 | 962 | Zinc finger, DksA/TraR C4-type | Znf_DskA_TraR | Domain | 35,006 | false | false | This entry represents domains identified in zinc finger-containing members of the DksA/TraR family. DksA is a critical component of the rRNA transcription initiation machinery that potentiates the regulation of rRNA promoters by ppGpp and the initiating NTP. In delta-dksA mutants, rRNA promoters are unresponsive to cha... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01258"
] | [
"zf-dskA_traR"
] | [
35006
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00846"
] | [
"PROSITEDOC:PDOC00846"
] | 1 | [
"1tjl",
"2kgo",
"2kq9",
"4ijj",
"5vsw",
"5w1s",
"5w1t",
"6n57",
"6n58",
"6psq",
"6psr",
"6pss",
"6pst",
"6psu",
"6psv",
"6psw",
"6ptg",
"7khe",
"7khi"
] | 19 | [
"PUB00001850",
"PUB00002103",
"PUB00002247",
"PUB00014077",
"PUB00015435",
"PUB00015436",
"PUB00015437",
"PUB00015438",
"PUB00015439",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"8063112",
"2180916",
"8021201",
"12665246",
"15294156",
"15294157",
"12775693",
"12932736",
"10049694",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"Sequence of the rec-2 locus of Haemophilus influenzae: homologies to comE-ORF3 of Bacillus subtilis and msbA of Escherichia coli.",
"Identification and characterization of a new Escherichia coli gene that is a dosage-dependent suppressor of a dnaK deletion mutation.",
"Molecular analysis of the F plasmid traVR... | [
1994,
1990,
1994,
2002,
2004,
2004,
2003,
2003,
1999,
2007,
2005,
2005,
1999,
2001
] | 14 | [] | [
"IPR020460"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
253,
33738,
54,
360,
601
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
3
] | 2 | true | Domain | Zinc finger, DksA/TraR C4-type | Zinc finger, DksA/TraR C4-type | Znf_DskA_TraR | 1 |
IPR000965 | 965 | GPR domain | GPR_dom | Domain | 29,277 | false | false | Gamma-glutamyl phosphate reductase ( ) (GPR) is the enzyme that catalyses the second step in the biosynthesis of proline from glutamate, the NADP-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. In bacteria (gene proA) and yeast [ ] (gene PRO2), GPR is a monofunctional prote... | [
"GO:0004350",
"GO:0055129"
] | [
"glutamate-5-semialdehyde dehydrogenase activity",
"L-proline biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_00412",
"TIGR00407",
"cd07079"
] | [
"ProA",
"proA",
"ALDH_F18-19_ProA-GPR"
] | [
28916,
28595,
29086
] | 3 | [
"EC",
"GP",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.2.1.41",
"GenProp0111",
"PWY-6922",
"PDOC00940",
"R-CEL-8964539",
"R-CEL-9837999",
"R-HSA-8964539",
"R-HSA-9837999",
"R-MMU-8964539",
"R-MMU-9837999",
"R-SCE-8964539",
"R-SCE-9837999",
"R-SPO-8964539",
"R-SPO-9837999"
] | [
"EC:1.2.1.41",
"GP:GenProp0111",
"METACYC:PWY-6922",
"PROSITEDOC:PDOC00940",
"REACTOME:R-CEL-8964539",
"REACTOME:R-CEL-9837999",
"REACTOME:R-HSA-8964539",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-8964539",
"REACTOME:R-MMU-9837999",
"REACTOME:R-SCE-8964539",
"REACTOME:R-SCE-9837999",
"REACTO... | 14 | [
"1o20",
"1vlu",
"2h5g",
"4ghk",
"7f5t",
"7f5u",
"7f5v",
"7f5x",
"7wx3",
"7wx4",
"7wxf",
"7wxg",
"7wxh",
"7wxi",
"8j0e",
"8j0f",
"8j0g",
"8j27",
"8j28",
"8y2h",
"8zok",
"8zon",
"8zoo"
] | 23 | [
"PUB00004804",
"PUB00005656",
"PUB00081169",
"PUB00081170"
] | [
"1384052",
"8896266",
"9765552",
"10037775"
] | [
"A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants.",
"Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII.",
"Comparative analysis of the regulation ... | [
1992,
1996,
1998,
1999
] | 4 | [
"IPR015590"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Hyperionvirus sp.",
"unclassified sequences"
] | [
267,
22705,
5894,
1,
410
] | 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",... | [
11,
1,
4,
1,
1,
1,
3,
1,
3,
2,
1,
1,
30
] | 13 | true | Domain | GPR domain | GPR domain | GPR_dom | 4 |
IPR000966 | 966 | Metallothionein, family 5, Diptera | Metalthion_5 | Family | 168 | false | false | Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, and nickel. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , , ] species, including sea urchins, fungi, insects and cyanobacteria. Class III MTs are atypical polyp... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF02067",
"PR00872"
] | [
"Metallothio_5",
"MTDIPTERA"
] | [
156,
123
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000300",
"PUB00001490",
"PUB00002412",
"PUB00003570"
] | [
"3064814",
"2959513",
"2578462",
"1779825"
] | [
"Biochemistry of metallothionein.",
"Chemistry and biochemistry of metallothionein.",
"Nucleotide sequence and expression of a Drosophila metallothionein.",
"Overview of metallothionein."
] | [
1988,
1987,
1985,
1991
] | 4 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
168
] | 1 | [
"Drosophila melanogaster"
] | [
12
] | 1 | true | Family | Metallothionein, family 5, Diptera | Metallothionein, family 5, Diptera | Metalthion_5 | 5 |
IPR000967 | 967 | Zinc finger, NF-X1-type | Znf_NFX1 | Domain | 9,326 | false | false | Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b... | [
"GO:0008270",
"GO:0005634"
] | [
"zinc ion binding",
"nucleus"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF01422",
"SM00438"
] | [
"zf-NF-X1",
"ZnF_NFX"
] | [
5884,
9318
] | 2 | [] | [] | [] | 0 | [
"7zw0"
] | 1 | [
"PUB00003109",
"PUB00014077",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00082545",
"PUB00082546",
"PUB00095666",
"PUB00095667"
] | [
"7964459",
"12665246",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"8524296",
"10998178",
"17267499",
"12047746"
] | [
"A novel cysteine-rich sequence-specific DNA-binding protein interacts with the conserved X-box motif of the human major histocompatibility complex class II genes via a repeated Cys-His domain and functions as a transcriptional repressor.",
"Zinc fingers--folds for many occasions.",
"Sticky fingers: zinc-finger... | [
1994,
2002,
2007,
2005,
2005,
1999,
2001,
1996,
2000,
2007,
2002
] | 11 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9326
] | 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... | [
9,
2,
6,
19,
7,
7,
1,
10,
17,
1,
1,
18
] | 12 | true | Domain | Zinc finger, NF-X1-type | Zinc finger, NF-X1-type | Znf_NFX1 | 5 |
IPR000968 | 968 | Influenza nuclear export protein NS2 | Flu_NS2 | Family | 61,539 | false | false | The Influenza A virus belongs to the class of ssRNA negative-strand viruses. Influenza virus NS2 protein (also known as NEP) has an important role in the nucleocytoplasmic transport of the viral ribonucleoprotein. The NS2 proteins perform this function in virus-infected cells by interacting with nuclear pore complex co... | [
"GO:0039675"
] | [
"exit of virus from host cell nucleus through nuclear pore"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"PFAM"
] | [
"MF_04067",
"PF00601"
] | [
"INFV_NEP",
"Flu_NS2"
] | [
56883,
61409
] | 2 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1012",
"R-HSA-168255",
"R-HSA-168275",
"R-HSA-168288",
"R-HSA-168298",
"R-HSA-168302",
"R-HSA-168303",
"R-HSA-168330",
"R-HSA-168333",
"R-HSA-168336",
"R-HSA-192823"
] | [
"GP:GenProp1012",
"REACTOME:R-HSA-168255",
"REACTOME:R-HSA-168275",
"REACTOME:R-HSA-168288",
"REACTOME:R-HSA-168298",
"REACTOME:R-HSA-168302",
"REACTOME:R-HSA-168303",
"REACTOME:R-HSA-168330",
"REACTOME:R-HSA-168333",
"REACTOME:R-HSA-168336",
"REACTOME:R-HSA-192823"
] | 11 | [
"1pd3",
"8y7m",
"8y7o",
"9t1m"
] | 4 | [
"PUB00094709",
"PUB00094710"
] | [
"32256144",
"23236273"
] | [
"Interaction of influenza A virus NS2/NEP protein with the amino-terminal part of Nup214.",
"Emerging roles for the influenza A virus nuclear export protein (NEP)."
] | [
2020,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Orthomyxoviridae"
] | [
9,
61530
] | 2 | [] | [] | 0 | true | Family | Influenza nuclear export protein NS2 | Influenza nuclear export protein NS2 | Flu_NS2 | 6 |
IPR000969 | 969 | FACT complex subunit SSRP1/POB3 | SSRP1/POB3 | Family | 5,473 | false | false | FACT (facilitates chromatin transactions) is a general chromatin factor that acts to reorganise nucleosomes. It is a complex that consists of several subunits [ , , , ]. This entry represents the FACT complex subunits POB3, which is present in yeast, and the related SSRP1, found in higher eukaryotes. SSRP1 binds specif... | [
"GO:0003677",
"GO:0005634"
] | [
"DNA binding",
"nucleus"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00887"
] | [
"SSRCOGNITION"
] | [
5473
] | 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-CEL-112382",
"R-CEL-674695",
"R-CEL-6796648",
"R-CEL-6804756",
"R-CEL-75955",
"R-DDI-674695",
"R-DDI-6796648",
"R-DDI-6804756",
"R-DME-112382",
"R-DME-674695",
"R-DME-6796648",
"R-DME-6804756",
"R-DME-75955",
"R-HSA-112382",
"R-HSA-167152",
"R-HSA-167200",
"R-HSA-167238",
"R-HSA... | [
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-6804756",
"REACTOME:R-CEL-75955",
"REACTOME:R-DDI-674695",
"REACTOME:R-DDI-6796648",
"REACTOME:R-DDI-6804756",
"REACTOME:R-DME-112382",
"REACTOME:R-DME-674695",
"REACTOME:R-DME-6796648",
"REACTOME:R-DME... | 41 | [
"2gcj",
"2gcl",
"4ifs",
"4pq0",
"5ums",
"6l1e",
"6upk",
"6upl",
"7nky",
"7xsx",
"7xt7",
"7xtd",
"7xti",
"8xgc",
"9eh2",
"9s3g"
] | 16 | [
"PUB00003673",
"PUB00004417",
"PUB00004776",
"PUB00004823",
"PUB00033331",
"PUB00033373",
"PUB00033374",
"PUB00070237",
"PUB00070238",
"PUB00101031",
"PUB00101032",
"PUB00101034"
] | [
"1678855",
"8479916",
"1372440",
"7688122",
"15987999",
"12524332",
"12934006",
"12815073",
"10413469",
"21454601",
"31775157",
"33846633"
] | [
"HMG1-related DNA-binding protein isolated with V-(D)-J recombination signal probes.",
"Isolation and characterization of cDNA clones encoding the Drosophila homolog of the HMG-box SSRP family that recognizes specific DNA structures.",
"Isolation and characterization of human cDNA clones encoding a high mobilit... | [
1991,
1993,
1992,
1993,
2005,
2002,
2003,
2003,
1999,
2011,
2020,
2021
] | 12 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Sagittula salina"
] | [
5472,
1
] | 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... | [
2,
2,
2,
22,
2,
3,
1,
2,
4,
1,
1,
11
] | 12 | true | Family | FACT complex subunit SSRP1/POB3 | FACT complex subunit SSRP1/POB3 | SSRP1/POB3 | 9 |
IPR000972 | 972 | Octamer-binding transcription factor | TF_octamer | Family | 4,044 | false | false | The octamer-binding protein is a transcription factor that binds specifically to the octamer motif (ATTTGCAT) [ ] of immunoglobulin promoters and activates these genes. There are two Ig octamer-binding proteins, designated NF-A1 and NF-A2. NF-A1 is found in all cell types, while NF-A2 is found only in lymphoid cells. T... | [
"GO:0003700",
"GO:0006355",
"GO:0005634"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription",
"nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00029"
] | [
"OCTAMER"
] | [
4044
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6785807",
"R-HSA-6807505",
"R-HSA-749476",
"R-HSA-76071",
"R-HSA-9018519",
"R-MMU-6807505",
"R-MMU-76071",
"R-RNO-6807505",
"R-RNO-76071",
"R-RNO-9018519",
"R-XTR-6807505"
] | [
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6807505",
"REACTOME:R-HSA-749476",
"REACTOME:R-HSA-76071",
"REACTOME:R-HSA-9018519",
"REACTOME:R-MMU-6807505",
"REACTOME:R-MMU-76071",
"REACTOME:R-RNO-6807505",
"REACTOME:R-RNO-76071",
"REACTOME:R-RNO-9018519",
"REACTOME:R-XTR-6807505"
] | 11 | [] | 0 | [
"PUB00053855"
] | [
"8474450"
] | [
"An octamer motif contributes to the expression of the retinoic acid-regulated zinc finger gene Rex-1 (Zfp-42) in F9 teratocarcinoma cells."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Deuterostomia"
] | [
4044
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
80,
18,
13,
23
] | 4 | true | Family | Octamer-binding transcription factor | Octamer-binding transcription factor | TF_octamer | 5 |
IPR000973 | 973 | T-cell surface antigen CD4 | CD4 | Family | 372 | false | false | CD4 is a glycoprotein found on the surface of T cells. It is a co-receptor that assists the T cell receptor (TCR) in communicating with an antigen-presenting cell (APC). The structure of a soluble fragment of CD4 has been determined to 2.3 A and reveals that the molecule has two intimately-associated immunoglobulin-lik... | [
"GO:0015026",
"GO:0006955",
"GO:0016020"
] | [
"coreceptor activity",
"immune response",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00692"
] | [
"CD4TCANTIGEN"
] | [
372
] | 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-CFA-202424",
"R-CFA-202427",
"R-CFA-202430",
"R-CFA-202433",
"R-CFA-389948",
"R-CFA-449836",
"R-CFA-8856825",
"R-CFA-8856828",
"R-HSA-1462054",
"R-HSA-167590",
"R-HSA-173107",
"R-HSA-180534",
"R-HSA-202424",
"R-HSA-202427",
"R-HSA-202430",
"R-HSA-202433",
"R-HSA-389948",
"R-HSA-... | [
"REACTOME:R-CFA-202424",
"REACTOME:R-CFA-202427",
"REACTOME:R-CFA-202430",
"REACTOME:R-CFA-202433",
"REACTOME:R-CFA-389948",
"REACTOME:R-CFA-449836",
"REACTOME:R-CFA-8856825",
"REACTOME:R-CFA-8856828",
"REACTOME:R-HSA-1462054",
"REACTOME:R-HSA-167590",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-... | 38 | [
"1cid",
"1wio",
"1wip",
"1wiq",
"3t0e",
"5u1f",
"6met",
"7t0o",
"7t0r",
"8fyi",
"8fyj",
"8z7n"
] | 12 | [
"PUB00004083",
"PUB00004084",
"PUB00095338"
] | [
"1701030",
"2247146",
"24942581"
] | [
"Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains.",
"Crystal structure of an HIV-binding recombinant fragment of human CD4.",
"CD4 ligation on human blood monocytes triggers macrophage differentiation and enhances HIV infection."
] | [
1990,
1990,
2014
] | 3 | [] | [] | 0 | 0 | null | [
"Theria"
] | [
372
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
4,
4
] | 3 | true | Family | T-cell surface antigen CD4 | T-cell surface antigen CD4 | CD4 | 3 |
IPR000974 | 974 | Glycoside hydrolase, family 22, lysozyme | Glyco_hydro_22_lys | Family | 3,716 | 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:0003796"
] | [
"lysozyme activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00137"
] | [
"LYSOZYME"
] | [
3716
] | 1 | [
"CAZY",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH22",
"3.2.1.17",
"R-BTA-6798695",
"R-BTA-6803157",
"R-CFA-6798695",
"R-CFA-6803157",
"R-DME-5653890",
"R-GGA-5653890",
"R-GGA-6798695",
"R-GGA-6803157",
"R-HSA-6798695",
"R-HSA-6803157",
"R-HSA-977225",
"R-MMU-6798695",
"R-MMU-6803157",
"R-RNO-6798695",
"R-RNO-6803157",
"R-SSC-6... | [
"CAZY:GH22",
"EC:3.2.1.17",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6803157",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-6803157",
"REACTOME:R-DME-5653890",
"REACTOME:R-GGA-5653890",
"REACTOME:R-GGA-6798695",
"REACTOME:R-GGA-6803157",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6803157",
"REA... | 19 | [
"132l",
"133l",
"134l",
"135l",
"193l",
"194l",
"1a2y",
"1aki",
"1at5",
"1at6",
"1azf",
"1b0d",
"1b2k",
"1b5u",
"1b5v",
"1b5w",
"1b5x",
"1b5y",
"1b5z",
"1b7l",
"1b7m",
"1b7n",
"1b7o",
"1b7p",
"1b7q",
"1b7r",
"1b7s",
"1bb3",
"1bb4",
"1bb5",
"1bb6",
"1bb7"... | 1,582 | [
"PUB00001550",
"PUB00002403",
"PUB00002496",
"PUB00004009",
"PUB00004663",
"PUB00004870",
"PUB00005266",
"PUB00071535",
"PUB00071536",
"PUB00071537",
"PUB00071539",
"PUB00095074"
] | [
"3666156",
"6715332",
"2738070",
"3120013",
"3413092",
"7624375",
"8535779",
"21676251",
"12606493",
"16014814",
"24013621",
"28182716"
] | [
"The calcium-binding property of equine lysozyme.",
"Evolution of alpha-lactalbumins. The complete amino acid sequence of the alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat alpha-lactalbumins.",
"Multiple cDNA sequences and the evolution of bo... | [
1987,
1984,
1989,
1987,
1988,
1995,
1995,
2011,
2003,
2005,
2013,
2017
] | 12 | [
"IPR001916"
] | [] | 1 | 0 | 1 | [
"Hymenobacter edaphi",
"Opisthokonta"
] | [
1,
3715
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
12,
20,
19,
26
] | 5 | true | Family | Glycoside hydrolase, family 22, lysozyme | Glycoside hydrolase, family 22, lysozyme | Glyco_hydro_22_lys | 7 |
IPR000975 | 975 | Interleukin-1 family | IL-1_fam | Family | 5,069 | false | false | Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis [ ]. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and dif... | [
"GO:0005125",
"GO:0006954",
"GO:0006955",
"GO:0005615"
] | [
"cytokine activity",
"inflammatory response",
"immune response",
"extracellular space"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00340",
"PR00264",
"PTHR10078"
] | [
"IL1",
"INTERLEUKIN1",
""
] | [
4715,
3280,
4896
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00226",
"R-BTA-448706",
"R-BTA-5620971",
"R-BTA-9012546",
"R-BTA-9020702",
"R-CFA-9020702",
"R-HSA-2559582",
"R-HSA-448706",
"R-HSA-5620971",
"R-HSA-5660668",
"R-HSA-6783783",
"R-HSA-6785807",
"R-HSA-9007892",
"R-HSA-9008059",
"R-HSA-9012546",
"R-HSA-9014826",
"R-HSA-9020702",
... | [
"PROSITEDOC:PDOC00226",
"REACTOME:R-BTA-448706",
"REACTOME:R-BTA-5620971",
"REACTOME:R-BTA-9012546",
"REACTOME:R-BTA-9020702",
"REACTOME:R-CFA-9020702",
"REACTOME:R-HSA-2559582",
"REACTOME:R-HSA-448706",
"REACTOME:R-HSA-5620971",
"REACTOME:R-HSA-5660668",
"REACTOME:R-HSA-6783783",
"REACTOME:R-... | 35 | [
"1hib",
"1i1b",
"1ilr",
"1ilt",
"1iob",
"1ira",
"1irp",
"1itb",
"1j0s",
"1l2h",
"1md6",
"1s0l",
"1t4q",
"1too",
"1tp0",
"1twe",
"1twm",
"21bi",
"2i1b",
"2ila",
"2irt",
"2kh2",
"2kki",
"2l5x",
"2mib",
"2nvh",
"2vxt",
"2wry",
"31bi",
"3f62",
"3ltq",
"3nj5"... | 112 | [
"PUB00007346",
"PUB00007347",
"PUB00007348",
"PUB00070147"
] | [
"2969618",
"8702856",
"1833184",
"24332029"
] | [
"cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.",
"Cloning and characterization of an alternatively processed human type II interleukin-1 receptor mRNA.",
"A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types.",
"The int... | [
1988,
1996,
1991,
2013
] | 4 | [] | [
"IPR003297",
"IPR015529"
] | 0 | 2 | 0 | [
"Cervidpoxvirus",
"Vertebrata"
] | [
5,
5064
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
18,
18,
29,
34
] | 4 | true | Family | Interleukin-1 family | Interleukin-1 family | IL-1_fam | 3 |
IPR000977 | 977 | DNA ligase, ATP-dependent | DNA_ligase_ATP-dep | Family | 17,476 | false | false | This entry represents DNA ligases from the three domains of life. DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalysing the formation of an internucleotide ester bond between phosphate and deoxyribose. It is active during DNA replication, DNA repair and DNA recombination... | [
"GO:0003910",
"GO:0005524",
"GO:0071897"
] | [
"DNA ligase (ATP) activity",
"ATP binding",
"DNA biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00574"
] | [
"dnl1"
] | [
17476
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"6.5.1",
"6.5.1.1",
"R-CEL-5358565",
"R-CEL-5358606",
"R-CEL-5651801",
"R-CEL-6782210",
"R-CEL-69183",
"R-DDI-110362",
"R-DDI-110381",
"R-DDI-5358565",
"R-DDI-5358606",
"R-DDI-5649702",
"R-DDI-5651801",
"R-DDI-5693571",
"R-DDI-6782210",
"R-DDI-69183",
"R-DME-5358565",
"R-DME-535860... | [
"EC:6.5.1",
"EC:6.5.1.1",
"REACTOME:R-CEL-5358565",
"REACTOME:R-CEL-5358606",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-69183",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-110381",
"REACTOME:R-DDI-5358565",
"REACTOME:R-DDI-5358606",
"REACTOME:R-DDI-5649702",
"REACTOME:... | 65 | [
"1x9n",
"2cfm",
"2hiv",
"2hix",
"3gde",
"3l2p",
"3rr5",
"3w1b",
"3w1g",
"3w5o",
"4eq5",
"6bkf",
"6bkg",
"6p09",
"6p0a",
"6p0b",
"6p0c",
"6p0d",
"6p0e",
"6q1v",
"6wbo",
"7kr3",
"7kr4",
"7l34",
"7l35",
"7lsy",
"7lt3",
"7nfc",
"7nfe",
"7qnz",
"7qo1",
"7rpo"... | 60 | [
"PUB00000083",
"PUB00004409",
"PUB00004738",
"PUB00010654"
] | [
"1497311",
"1437556",
"1988940",
"11983065"
] | [
"Mammalian DNA ligases.",
"Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases.",
"Location of the active site for enzyme-adenylate formation in DNA ligases.",
"ATP-dependent DNA ligases."
... | [
1992,
1992,
1991,
2002
] | 4 | [] | [
"IPR022865",
"IPR029710"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
978,
3305,
12978,
181,
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... | [
17,
1,
6,
5,
18,
12,
3,
7,
15,
2,
3,
17
] | 12 | true | Family | DNA ligase, ATP-dependent | DNA ligase, ATP-dependent | DNA_ligase_ATP-dep | 3 |
IPR000978 | 978 | Adenoviral fibre protein, knob | Adeno_fibre_knob | Domain | 1,237 | false | false | Adenoviruses are responsible for diseases such as pneumonia, cystitis, conjunctivitis and diarrhoea, all of which can be fatal to patients who are immunocompromised [ ]. Viral infection commences with recognition of host cell receptors by means of specialised proteins on viral surfaces. Specific attachment of adenoviru... | [
"GO:0019062",
"GO:0019028"
] | [
"virion attachment to host cell",
"viral capsid"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00541"
] | [
"Adeno_knob"
] | [
1237
] | 1 | [] | [] | [] | 0 | [
"1h7z",
"1kac",
"1knb",
"1nob",
"1p69",
"1p6a",
"1qhv",
"1qiu",
"1uxa",
"1uxb",
"1uxe",
"2bzu",
"2bzv",
"2j12",
"2j1k",
"2j2j",
"2o39",
"2qlk",
"2w9l",
"2wbv",
"2wbw",
"2wgt",
"2wgu",
"2wst",
"3bq4",
"3cnc",
"3exv",
"3exw",
"3f0y",
"3izo",
"3l88",
"3l89"... | 85 | [
"PUB00005244",
"PUB00066852",
"PUB00066853"
] | [
"7704534",
"11152512",
"22754652"
] | [
"Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution.",
"Adenovirus serotype 7 retention in a late endosomal compartment prior to cytosol escape is modulated by fiber protein.",
"Latest insights on adenovirus structure and assembly."
] | [
1994,
2001,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Adenoviridae"
] | [
1237
] | 1 | [] | [] | 0 | true | Domain | Adenoviral fibre protein, knob | Adenoviral fibre protein, knob | Adeno_fibre_knob | 2 |
IPR000979 | 979 | Phosphodiesterase MJ0936/Vps29 | Phosphodiesterase_MJ0936/Vps29 | Family | 23,074 | false | false | Members of this largely uncharacterised family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterised archaeal putative phosphoesterases. In this family, the His residue in GNHD portion of the motif is not conserve... | [] | [] | [] | 0 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR11124",
"TIGR00040"
] | [
"",
"yfcE"
] | [
17576,
22581
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00976",
"R-BTA-3238698",
"R-DDI-3238698",
"R-HSA-3238698",
"R-MMU-3238698",
"R-RNO-3238698",
"R-SCE-3238698",
"R-SPO-3238698",
"R-XTR-3238698"
] | [
"PROSITEDOC:PDOC00976",
"REACTOME:R-BTA-3238698",
"REACTOME:R-DDI-3238698",
"REACTOME:R-HSA-3238698",
"REACTOME:R-MMU-3238698",
"REACTOME:R-RNO-3238698",
"REACTOME:R-SCE-3238698",
"REACTOME:R-SPO-3238698",
"REACTOME:R-XTR-3238698"
] | 9 | [
"1s3l",
"1s3m",
"1s3n",
"1su1",
"1w24",
"1z2w",
"1z2x",
"2a22",
"2ahd",
"2kkn",
"2r17",
"3ck2",
"3psn",
"3pso",
"5gtu",
"5osh",
"5osi",
"5w8m",
"5wyh",
"5xce",
"5xch",
"5xcj",
"5xck",
"6h7w",
"6tl0",
"6vab",
"6vac",
"6xs5",
"6xs7",
"6xs8",
"6xs9",
"6xsa"... | 51 | [
"PUB00015606",
"PUB00016030",
"PUB00027771"
] | [
"15128743",
"9700157",
"9105038"
] | [
"Structural and functional characterization of a novel phosphodiesterase from Methanococcus jannaschii.",
"A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast.",
"Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, V... | [
2004,
1998,
1997
] | 3 | [] | [
"IPR028661"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1753,
15645,
5400,
276
] | 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",... | [
3,
2,
1,
2,
1,
6,
4,
1,
2,
4,
1,
1,
9
] | 13 | true | Family | Phosphodiesterase MJ0936/Vps29 | Phosphodiesterase MJ0936/Vps29 | Phosphodiesterase_MJ0936/Vps29 | 6 |
IPR000980 | 980 | SH2 domain | SH2 | Domain | 160,090 | false | false | The Src homology 2 (SH2) domain is a protein domain of about 100 amino-acid residues first identified as a conserved sequence region between the oncoproteins Src and Fps [ ]. Similar sequences were later found in many other intracellular signal-transducing proteins [ ]. SH2 domains function as regulatory modules of int... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00017",
"PF21990",
"PS50001",
"SM00252"
] | [
"SH2",
"SH2_1",
"SH2",
"SH2"
] | [
144701,
6144,
154390,
144424
] | 4 | [
"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... | [
"GenProp1229",
"GenProp1509",
"GenProp1511",
"GenProp1548",
"PDOC50001",
"R-BTA-1059683",
"R-BTA-109704",
"R-BTA-112399",
"R-BTA-114604",
"R-BTA-1227986",
"R-BTA-1250196",
"R-BTA-1250342",
"R-BTA-1250347",
"R-BTA-1251985",
"R-BTA-1257604",
"R-BTA-1266695",
"R-BTA-1306955",
"R-BTA-1... | [
"GP:GenProp1229",
"GP:GenProp1509",
"GP:GenProp1511",
"GP:GenProp1548",
"PROSITEDOC:PDOC50001",
"REACTOME:R-BTA-1059683",
"REACTOME:R-BTA-109704",
"REACTOME:R-BTA-112399",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1227986",
"REACTOME:R-BTA-1250196",
"REACTOME:R-BTA-1250342",
"REACTOME:R-BTA-1... | 1,420 | [
"1a07",
"1a08",
"1a09",
"1a1a",
"1a1b",
"1a1c",
"1a1e",
"1a81",
"1ab2",
"1ad5",
"1aot",
"1aou",
"1aya",
"1ayb",
"1ayc",
"1ayd",
"1bf5",
"1bfi",
"1bfj",
"1bg1",
"1bhf",
"1bhh",
"1bkl",
"1bkm",
"1blj",
"1blk",
"1bm2",
"1bmb",
"1cj1",
"1csy",
"1csz",
"1cwd"... | 665 | [
"PUB00001025",
"PUB00001638",
"PUB00003096",
"PUB00003647",
"PUB00004203",
"PUB00005506",
"PUB00007102",
"PUB00022267",
"PUB00022290",
"PUB00023226",
"PUB00026131",
"PUB00027224"
] | [
"15335710",
"1377638",
"7883800",
"3025655",
"7531822",
"14731533",
"11911873",
"12551896",
"12706723",
"9174343",
"11782172",
"12450381"
] | [
"SH2 and SH3 domains.",
"Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains.",
"Structure and function of SH2 domains.",
"A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujina... | [
1993,
1992,
1994,
1986,
1995,
1993,
2002,
2003,
2003,
1997,
2002,
2002
] | 12 | [] | [
"IPR035012",
"IPR035020",
"IPR035022",
"IPR035023",
"IPR035024",
"IPR035027",
"IPR035031",
"IPR035032",
"IPR035034",
"IPR035037",
"IPR035042",
"IPR035044",
"IPR035045",
"IPR035046",
"IPR035047",
"IPR035049",
"IPR035052",
"IPR035057",
"IPR035058",
"IPR035059",
"IPR035061",
"... | 0 | 71 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"bird metagenome"
] | [
42,
159978,
67,
3
] | 4 | [
"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"
] | [
8,
75,
551,
91,
568,
337,
5,
459,
1,
13
] | 10 | true | Domain | SH2 domain | SH2 domain | SH2 | 1 |
IPR000981 | 981 | Neurohypophysial hormone | Neurhyp_horm | Family | 2,130 | false | false | Oxytocin and vasopressin are nine-residue, structurally and functionally related neurohypophysial peptide hormones. Oxytocin mediates contraction of the smooth muscle of the uterus and mammary gland, while vasopressin has antidiuretic action on the kidney, and mediates vasoconstriction of the peripheral vessels [ ]. In... | [
"GO:0005185",
"GO:0005576"
] | [
"neurohypophyseal hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PIRSF",
"PRINTS",
"PANTHER",
"SMART"
] | [
"PF00184",
"PIRSF001815",
"PR00831",
"PTHR11681",
"SM00003"
] | [
"Hormone_5",
"Nonapeptide_hormone_precursor",
"NEUROPHYSIN",
"",
"NH"
] | [
2107,
1601,
2042,
2069,
2091
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00237",
"R-BTA-388479",
"R-BTA-416476",
"R-HSA-1368108",
"R-HSA-388479",
"R-HSA-416476",
"R-HSA-418555",
"R-HSA-432040",
"R-HSA-5619099",
"R-HSA-879518",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-9036092",
"R-MMU-388479",
"R-MMU-416476",
"R-MMU-418555",
"R-MMU-432040",
"R-MMU-8... | [
"PROSITEDOC:PDOC00237",
"REACTOME:R-BTA-388479",
"REACTOME:R-BTA-416476",
"REACTOME:R-HSA-1368108",
"REACTOME:R-HSA-388479",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-432040",
"REACTOME:R-HSA-5619099",
"REACTOME:R-HSA-879518",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8... | 33 | [
"1jk4",
"1jk6",
"1l5c",
"1l5d",
"1npo",
"2bn2",
"2hnu",
"2hnv",
"2hnw",
"2lbh",
"2lbn"
] | 11 | [
"PUB00000683",
"PUB00002048",
"PUB00094341"
] | [
"3147712",
"7591488",
"23112335"
] | [
"Structure, processing and evolution of the neurohypophysial hormone-neurophysin precursors.",
"A new neurohypophysial peptide, seritocin ([Ser5,Ile8]-oxytocin), identified in a dryness-resistant African toad, Bufo regularis.",
"Oxytocin/vasopressin-related peptides have an ancient role in reproductive behavior... | [
1988,
1995,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
2130
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
5,
6,
3
] | 5 | true | Family | Neurohypophysial hormone | Neurohypophysial hormone | Neurhyp_horm | 6 |
IPR000982 | 982 | Matrix protein, N-terminal domain | Matrix_Paramyxo_N | Domain | 2,089 | false | false | This entry represents the N-terminal domain found in a variety of paramyxoviruses such as Morbillivirus, paramyxovirus, pneumovirus M proteins. The N-terminal domain of the NDV matrix protein adopts a β-sandwich fold in which the β-strands in the opposing β-sheets are approximately orthogonal to each other. Several α-h... | [
"GO:0005198",
"GO:0019068"
] | [
"structural molecule activity",
"virion assembly"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00661"
] | [
"Matrix_Paramyxo_N"
] | [
2089
] | 1 | [] | [] | [] | 0 | [
"4g1g",
"4g1l",
"4g1o",
"6bk6",
"7sks",
"7skt",
"7sku"
] | 7 | [
"PUB00062701"
] | [
"22891297"
] | [
"Structure and assembly of a paramyxovirus matrix protein."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Paramyxoviridae"
] | [
2089
] | 1 | [] | [] | 0 | true | Domain | Matrix protein, N-terminal domain | Matrix protein, N-terminal domain | Matrix_Paramyxo_N | 6 |
IPR000983 | 983 | General secretion pathway protein G-type pilin | GSPG_pilin | Family | 21,303 | false | false | The general (type II) secretion pathway (GSP) within Gram-negative bacteria is a signal sequence-dependent process responsible for protein export [ , , ], including virulence factors. The process has two stages, exoproteins are first translocated across the inner membrane by the general signal-dependent export pathway ... | [
"GO:0015628",
"GO:0015627"
] | [
"protein secretion by the type II secretion system",
"type II protein secretion system complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00813"
] | [
"BCTERIALGSPG"
] | [
21303
] | 1 | [] | [] | [] | 0 | [
"7tgg"
] | 1 | [
"PUB00002179",
"PUB00002231",
"PUB00002265",
"PUB00005409",
"PUB00005523",
"PUB00053545",
"PUB00094517"
] | [
"1592799",
"8407845",
"7896718",
"8438237",
"1365398",
"12700254",
"21255118"
] | [
"Determinants of extracellular protein secretion in gram-negative bacteria.",
"Isolation and analysis of eight exe genes and their involvement in extracellular protein secretion and outer membrane assembly in Aeromonas hydrophila.",
"Identification of the hopG gene, a component of Escherichia coli K-12 type II ... | [
1992,
1993,
1995,
1993,
1992,
2003,
2011
] | 7 | [] | [
"IPR010054",
"IPR016940",
"IPR025922"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"candidate division MSBL1 archaeon SCGC-AAA382A20",
"unclassified sequences"
] | [
20790,
23,
1,
489
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | General secretion pathway protein G-type pilin | General secretion pathway protein G-type pilin | GSPG_pilin | 3 |
IPR000984 | 984 | G protein-coupled receptor 3 | GPR3 | Family | 171 | false | false | G protein-coupled receptor 12 (GPR12) was initially isolated from a rat pituitary library, and is found in discrete regions of the brain, pituitary and testis, but is absent in other tissues [ , ]. Three human homologues (GPR12, GPR6 and GPR3) have also been isolated [ ]. The 3 genes have been localised to human chromo... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PRINTS"
] | [
"PR00648"
] | [
"GPR3ORPHANR"
] | [
171
] | 1 | [] | [] | [] | 0 | [
"8u8f",
"8ww2",
"8x2k",
"9lyb",
"9lyc",
"9lyd",
"9m88",
"9m8p",
"9m8v"
] | 9 | [
"PUB00001626",
"PUB00001967"
] | [
"1840531",
"8530049"
] | [
"Cloning, sequencing and tissue distribution of a candidate G protein-coupled receptor from rat pituitary gland.",
"Molecular cloning and chromosomal localization of human genes encoding three closely related G protein-coupled receptors."
] | [
1991,
1995
] | 2 | [
"IPR000723"
] | [] | 1 | 0 | 1 | [
"Theria"
] | [
171
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
3
] | 3 | true | Family | G protein-coupled receptor 3 | G protein-coupled receptor 3 | GPR3 | 6 |
IPR000985 | 985 | Legume lectin, alpha chain, conserved site | Lectin_LegA_CS | Conserved_site | 3,237 | false | false | null | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00308"
] | [
"LECTIN_LEGUME_ALPHA"
] | [
3237
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00278"
] | [
"PROSITEDOC:PDOC00278"
] | 1 | [
"1apn",
"1avb",
"1ax0",
"1ax1",
"1ax2",
"1axy",
"1axz",
"1azd",
"1bjq",
"1bqp",
"1bxh",
"1bzw",
"1c57",
"1ces",
"1ciw",
"1cjp",
"1cn1",
"1con",
"1cq9",
"1cr7",
"1cvn",
"1dbn",
"1dgl",
"1dhk",
"1dq0",
"1dq1",
"1dq2",
"1dq4",
"1dq5",
"1dq6",
"1dzq",
"1enq"... | 319 | [
"PUB00000041",
"PUB00001507"
] | [
"3527046",
"2227211"
] | [
"Lectins as molecules and as tools.",
"Legume lectins--a large family of homologous proteins."
] | [
1986,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
13,
3224
] | 2 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
16,
10
] | 2 | true | Conserved_site | Legume lectin, alpha chain, conserved site | Legume lectin, alpha chain, conserved site | Lectin_LegA_CS | 2 |
IPR000986 | 986 | Neuropeptide Y6 receptor | NeuroY6_rcpt | Family | 507 | false | false | Neuropeptide Y (NPY) acts as a neurotransmitter in the brain and in the autonomic nervous system. In the brain it is thought to have several functions, including increasing food intake and storage of energy as fat [ , , , ], facilitation of learning and memory via the modulation of hippocampal activity [ , , ], inhibit... | [
"GO:0004983",
"GO:0007186",
"GO:0016020"
] | [
"neuropeptide Y receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01017"
] | [
"NRPEPTIDEY6R"
] | [
507
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00002957",
"PUB00063739",
"PUB00063740",
"PUB00063741",
"PUB00063742",
"PUB00063743",
"PUB00063744",
"PUB00063745",
"PUB00063746",
"PUB00063747",
"PUB00063748",
"PUB00063749",
"PUB00063750",
"PUB00063751",
"PUB00063752",
"PUB00063753",
"PUB00063754",
"PUB00063755",
"PUB000637... | [
"8663568",
"6549409",
"16874931",
"6547387",
"6549039",
"2821236",
"8395947",
"16190896",
"7529442",
"7644568",
"15337373",
"8685245",
"8369959",
"11287113",
"7629398",
"6133408",
"3855566",
"12678499",
"17222466",
"8013354",
"9833945",
"9389418",
"9446690",
"2453065",
... | [
"Cloning and expression of a novel neuropeptide Y receptor.",
"Neuropeptide Y: a potent inducer of consummatory behavior in rats.",
"Neuropeptide Y in normal eating and in genetic and dietary-induced obesity.",
"Neuropeptide Y and human pancreatic polypeptide stimulate feeding behavior in rats.",
"Neuropept... | [
1996,
1984,
2006,
1984,
1984,
1987,
1993,
2005,
1994,
1995,
2004,
1996,
1993,
2001,
1995,
1982,
1985,
2003,
2007,
1994,
1998,
1997,
1998,
1988,
1991,
1995,
2003,
2007,
1998,
2004,
2007,
2007,
2007,
2006,
2007,
2006,
2007,
2008,
1996,
1996... | 44 | [
"IPR000611"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
507
] | 1 | [
"Homo sapiens",
"Mus musculus"
] | [
3,
1
] | 2 | true | Family | Neuropeptide Y6 receptor | Neuropeptide Y6 receptor | NeuroY6_rcpt | 3 |
IPR000987 | 987 | Sphingosine 1-phosphate receptor 1 | EDG1 | Family | 779 | 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:0038036",
"GO:0007186",
"GO:0016020"
] | [
"sphingosine-1-phosphate receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"CDD"
] | [
"cd15346"
] | [
"7tmA_S1PR1_Edg1"
] | [
779
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"275",
"R-BTA-419408",
"R-DRE-419408",
"R-HSA-419408",
"R-HSA-6785807",
"R-HSA-9679191",
"R-MMU-419408",
"R-RNO-419408"
] | [
"IUPHAR:275",
"REACTOME:R-BTA-419408",
"REACTOME:R-DRE-419408",
"REACTOME:R-HSA-419408",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-9679191",
"REACTOME:R-MMU-419408",
"REACTOME:R-RNO-419408"
] | 8 | [
"7eo2",
"7eo4",
"7evy",
"7evz",
"7ew0",
"7ew7",
"7td3",
"7td4",
"7vie",
"7vif",
"7vig",
"7vih",
"7wf7",
"8g94",
"8yic"
] | 15 | [
"PUB00000131",
"PUB00002477",
"PUB00002628",
"PUB00004960",
"PUB00004961",
"PUB00007103",
"PUB00007104",
"PUB00007105",
"PUB00007106",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"2160972",
"8386361",
"8170923",
"11264467",
"10603487",
"11150592",
"9931453",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"An abundant transcript induced in differentiating human endothelial cells encodes a polypeptide with structural similarities to G-protein-coupled receptors.",
"Design of a discriminating fingerprint for G-protein-co... | [
1990,
1988,
1990,
1993,
1994,
2001,
1999,
2000,
1999,
2003,
1994,
2005,
2009,
2006,
2013
] | 15 | [
"IPR004061"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
779
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
4,
2
] | 4 | true | Family | Sphingosine 1-phosphate receptor 1 | Sphingosine 1-phosphate receptor 1 | EDG1 | 7 |
IPR000988 | 988 | Large ribosomal subunit protein eL24-related, N-terminal | Ribosomal_eL24-rel_N | Domain | 11,308 | false | false | This entry represents a domain found N-terminal in large ribosomal subunit protein eL24 and related proteins. A number of eukaryotic and archaeabacterial ribosomal proteins can be grouped on the basis of sequence similarities. One of these families [ ] consists of mammalian ribosomal protein eL24; yeast ribosomal prote... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF01246",
"cd00472"
] | [
"Ribosomal_L24e",
"Ribosomal_L24e_L24"
] | [
11304,
9944
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00824",
"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:PDOC00824",
"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... | 70 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp"... | 684 | [
"PUB00000236",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00028498",
"PUB00054250",
"PUB00080482",
"PUB00080483",
"PUB00080484"
] | [
"8048931",
"11297922",
"11290319",
"11114498",
"10937989",
"2591382",
"15289434",
"17462931",
"15270688"
] | [
"The primary structure of rat ribosomal protein L24.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.",
"Primary structur... | [
1994,
2001,
2001,
2000,
2000,
1989,
2004,
2007,
2004
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Gammaproteobacteria",
"ecological metagenomes"
] | [
888,
10396,
2,
22
] | 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... | [
10,
2,
3,
4,
11,
10,
2,
13,
8,
3,
3,
18
] | 12 | true | Domain | Large ribosomal subunit protein eL24-related, N-terminal | Large ribosomal subunit protein eL24-related, N-terminal | Ribosomal_eL24-rel_N | 4 |
IPR000989 | 989 | Replication protein | Rep | Family | 2,175 | false | false | Replication proteins (rep) are involved in plasmid replication. The Rep protein binds to the plasmid DNA and nicks it at the double strand origin (dso) of replication. The 3'-hydroxyl end created is extended by the host DNA replicase, and the 5' end is displaced during synthesis. At the end of one replication round, Re... | [
"GO:0003677",
"GO:0006260"
] | [
"DNA binding",
"DNA replication"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01446"
] | [
"Rep_1"
] | [
2175
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00003879"
] | [
"9570403"
] | [
"A rolling circle replication initiator protein with a nucleotidyl-transferase activity encoded by the plasmid pGT5 from the hyperthermophilic archaeon Pyrococcus abyssi."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"Propionibacterium phage Philemon",
"plasmids",
"unclassified sequences"
] | [
1814,
24,
4,
1,
5,
327
] | 6 | [] | [] | 0 | true | Family | Replication protein | Replication protein | Rep | 6 |
IPR000990 | 990 | Innexin | Innexin | Family | 14,851 | false | false | This entry includes pannexins from vertebrates and innexins from invertebrate [ ]. Gap junctions are composed of membrane proteins, which form a channel permeable for ions and small molecules connecting cytoplasm of adjacent cells. Although gap junctions provide similar functions in all multicellular organisms, until r... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROFILE",
"PANTHER"
] | [
"PF00876",
"PR01262",
"PS51013",
"PTHR11893"
] | [
"Innexin",
"INNEXIN",
"PANNEXIN",
""
] | [
14001,
9782,
14138,
11034
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC51013",
"R-HSA-112303",
"R-HSA-844456",
"R-HSA-9856530",
"R-HSA-9856532",
"R-MMU-112303",
"R-MMU-844456",
"R-RNO-112303",
"R-RNO-844456"
] | [
"PROSITEDOC:PDOC51013",
"REACTOME:R-HSA-112303",
"REACTOME:R-HSA-844456",
"REACTOME:R-HSA-9856530",
"REACTOME:R-HSA-9856532",
"REACTOME:R-MMU-112303",
"REACTOME:R-MMU-844456",
"REACTOME:R-RNO-112303",
"REACTOME:R-RNO-844456"
] | 9 | [
"5h1q",
"5h1r",
"6kff",
"6kfg",
"6kfh",
"6ltn",
"6lto",
"6m02",
"6m66",
"6m67",
"6m68",
"6uzy",
"6v6d",
"6vd7",
"6wbf",
"6wbg",
"6wbi",
"6wbk",
"6wbl",
"6wbm",
"6wbn",
"7dwb",
"7f8j",
"7f8n",
"7f8o",
"7wsv",
"7xl6",
"7xlb",
"8a3b",
"8f7c",
"8gtr",
"8gts"... | 50 | [
"PUB00004270",
"PUB00005532",
"PUB00015426",
"PUB00015427",
"PUB00015428",
"PUB00015429",
"PUB00015430"
] | [
"9428764",
"9769729",
"14651471",
"12205780",
"5028292",
"12492443",
"10898987"
] | [
"Drosophila Shaking-B protein forms gap junctions in paired Xenopus oocytes.",
"Innexins: a family of invertebrate gap-junction proteins.",
"Polydnavirus genes and genomes: emerging gene families and new insights into polydnavirus replication.",
"Perspectives on polydnavirus origins and evolution.",
"Interr... | [
1998,
1998,
2004,
2002,
1972,
2002,
2000
] | 7 | [] | [
"IPR039099"
] | 0 | 1 | 0 | [
"Eukaryota",
"Viruses incertae sedis"
] | [
14823,
28
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
50,
6,
18,
6,
5,
10
] | 6 | true | Family | Innexin | Innexin | Innexin | 9 |
IPR000992 | 992 | Stress-induced protein SRP1/TIP1 | SRP1_TIP1 | Family | 732 | false | false | It has recently been shown [ ] that three yeast proteins, two of which are known to be induced by various stress conditions, are structurally related and are probably part of a larger family. These proteins include cold-shock inducible protein TIR1 (also known as serine-rich protein 1, SRP1), which is induced by glucos... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE"
] | [
"PF00660",
"PS00724"
] | [
"SRP1_TIP1",
"SRP1_TIP1"
] | [
712,
467
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00596"
] | [
"PROSITEDOC:PDOC00596"
] | 1 | [] | 0 | [
"PUB00001851",
"PUB00003229",
"PUB00003868",
"PUB00005001"
] | [
"7926827",
"3139887",
"7746155",
"1304897"
] | [
"Seripauperins of Saccharomyces cerevisiae: a new multigene family encoding serine-poor relatives of serine-rich proteins.",
"Yeast gene SRP1 (serine-rich protein). Intragenic repeat structure and identification of a family of SRP1-related DNA sequences.",
"Cold-shock induction of a family of TIP1-related prote... | [
1994,
1988,
1995,
1992
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcina mazei"
] | [
12,
717,
3
] | 3 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
32
] | 1 | true | Family | Stress-induced protein SRP1/TIP1 | Stress-induced protein SRP1/TIP1 | SRP1_TIP1 | 4 |
IPR000994 | 994 | Peptidase M24 | Pept_M24 | Domain | 162,092 | false | false | This entry contains proteins that belong to MEROPS peptidase family M24 (clan MG), which share a common structural-fold, the "pita-bread" fold. The fold contains both α helices and an anti-parallel β sheet within two structurally similar domains that are thought to be derived from an ancient gene duplication. The activ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00557"
] | [
"Peptidase_M24"
] | [
162092
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.11",
"R-BTA-2514859",
"R-CEL-112382",
"R-CEL-674695",
"R-CEL-6796648",
"R-CEL-6804756",
"R-CEL-75955",
"R-DDI-163125",
"R-DDI-2514859",
"R-DDI-674695",
"R-DDI-6796648",
"R-DDI-6798695",
"R-DDI-6804756",
"R-DME-112382",
"R-DME-674695",
"R-DME-6796648",
"R-DME-6804756",
"R-DME-7... | [
"EC:3.4.11",
"REACTOME:R-BTA-2514859",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-6804756",
"REACTOME:R-CEL-75955",
"REACTOME:R-DDI-163125",
"REACTOME:R-DDI-2514859",
"REACTOME:R-DDI-674695",
"REACTOME:R-DDI-6796648",
"REACTOME:R-DDI-6798695",
... | 57 | [
"1a16",
"1b59",
"1b6a",
"1bn5",
"1boa",
"1c21",
"1c22",
"1c23",
"1c24",
"1c27",
"1chm",
"1jaw",
"1kp0",
"1kq0",
"1kq9",
"1m35",
"1mat",
"1n51",
"1o0x",
"1pv9",
"1qxw",
"1qxy",
"1qxz",
"1qzy",
"1r58",
"1r5g",
"1r5h",
"1w2m",
"1w7v",
"1wbq",
"1wkm",
"1wl6"... | 334 | [
"PUB00000379",
"PUB00026792",
"PUB00033331",
"PUB00033373",
"PUB00033374",
"PUB00044073",
"PUB00044074"
] | [
"8471602",
"12136144",
"15987999",
"12524332",
"12934006",
"8146141",
"18579787"
] | [
"Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme.",
"Structure of creatine amidinohydrolase from Actinobacillus.",
"The yeast FACT complex has a role in transcriptional initiation.",
"Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisi... | [
1993,
2002,
2005,
2002,
2003,
1994,
2008
] | 7 | [] | [
"IPR033740",
"IPR033825",
"IPR039394"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3490,
107621,
48427,
19,
2535
] | 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",... | [
62,
11,
37,
17,
4,
44,
37,
9,
53,
48,
6,
8,
127
] | 13 | true | Domain | Peptidase M24 | Peptidase M24 | Pept_M24 | 7 |
IPR000995 | 995 | Muscarinic acetylcholine receptor family | Musac_Ach_rcpt | Family | 6,044 | false | false | Muscarinic acetylcholine receptors are members of rhodopsin-like G-protein coupled receptor family. They play several important roles; they mediate many of the effects of acetylcholine in the central and peripheral nervous system and modulate a variety of physiological functions, such as airway, eye and intestinal smoo... | [
"GO:0016907",
"GO:0007186",
"GO:0005886"
] | [
"G protein-coupled acetylcholine receptor activity",
"G protein-coupled receptor signaling pathway",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00243"
] | [
"MUSCARINICR"
] | [
6044
] | 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-390648",
"R-BTA-418594",
"R-BTA-8856825",
"R-BTA-8856828",
"R-CEL-390648",
"R-CEL-390650",
"R-CEL-416476",
"R-CEL-418594",
"R-CEL-8856825",
"R-CEL-8856828",
"R-DME-390648",
"R-DME-390650",
"R-DME-416476",
"R-DME-418594",
"R-DME-8856825",
"R-DME-8856828",
"R-GGA-390648",
"R-G... | [
"REACTOME:R-BTA-390648",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-CEL-390648",
"REACTOME:R-CEL-390650",
"REACTOME:R-CEL-416476",
"REACTOME:R-CEL-418594",
"REACTOME:R-CEL-8856825",
"REACTOME:R-CEL-8856828",
"REACTOME:R-DME-390648",
"REACTOME:R-DME... | 39 | [
"4mqs",
"4mqt",
"4u15",
"4u16",
"5dsg",
"5yc8",
"5zhp",
"5zk3",
"5zk8",
"5zkb",
"5zkc",
"6kp6",
"6oij",
"6oik",
"6u1n",
"7t8x",
"7t90",
"7t94",
"7t96",
"7trk",
"7trp",
"7trq",
"7trs",
"7v68",
"7v69",
"7v6a",
"8e9w",
"8e9x",
"8e9y",
"8e9z",
"8ea0",
"8fx5"... | 39 | [
"PUB00064316",
"PUB00064317",
"PUB00064318",
"PUB00064319",
"PUB00064320",
"PUB00064321",
"PUB00064322",
"PUB00064323",
"PUB00064324",
"PUB00064325",
"PUB00064326",
"PUB00064336",
"PUB00064337",
"PUB00064343"
] | [
"3443095",
"3272174",
"3037705",
"9647869",
"2470172",
"8853955",
"10841527",
"14641022",
"12725869",
"17762886",
"15850824",
"14744253",
"15474550",
"11714883"
] | [
"Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors.",
"Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes.",
"Identification of a family of muscarinic acetylcholine receptor genes.",
"Inter... | [
1987,
1988,
1987,
1998,
1989,
1996,
2000,
2003,
2003,
2007,
2005,
2004,
2004,
2001
] | 14 | [
"IPR000276"
] | [
"IPR000502",
"IPR001065",
"IPR001183",
"IPR001432",
"IPR002228"
] | 1 | 5 | 0 | [
"Eumetazoa"
] | [
6044
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
17,
1,
18,
9,
12
] | 6 | true | Family | Muscarinic acetylcholine receptor family | Muscarinic acetylcholine receptor family | Musac_Ach_rcpt | 2 |
IPR000996 | 996 | Clathrin light chain | Clathrin_L-chain | Family | 8,218 | false | false | Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are ... | [
"GO:0005198",
"GO:0006886",
"GO:0016192",
"GO:0030130",
"GO:0030132"
] | [
"structural molecule activity",
"intracellular protein transport",
"vesicle-mediated transport",
"clathrin coat of trans-Golgi network vesicle",
"clathrin coat of coated pit"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component",
"cellular_component"
] | 5 | [
"PFAM",
"PROSITE",
"PROSITE",
"PANTHER"
] | [
"PF01086",
"PS00224",
"PS00581",
"PTHR10639"
] | [
"Clathrin_lg_ch",
"CLATHRIN_LIGHT_CHN_1",
"CLATHRIN_LIGHT_CHN_2",
""
] | [
7801,
1890,
3177,
7530
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00196",
"R-BTA-177504",
"R-BTA-190873",
"R-BTA-196025",
"R-BTA-2132295",
"R-BTA-432720",
"R-BTA-432722",
"R-BTA-437239",
"R-BTA-5099900",
"R-BTA-5140745",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-8866427",
"R-BTA-8964038",
"R-DDI-432720",
"R-DDI-437239",
"R-DDI-8856828",
"R-DD... | [
"PROSITEDOC:PDOC00196",
"REACTOME:R-BTA-177504",
"REACTOME:R-BTA-190873",
"REACTOME:R-BTA-196025",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-432722",
"REACTOME:R-BTA-437239",
"REACTOME:R-BTA-5099900",
"REACTOME:R-BTA-5140745",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-... | 83 | [
"1xi4",
"3iyv",
"3lvg",
"3lvh",
"6sct",
"6wcj",
"6yai"
] | 7 | [
"PUB00016275",
"PUB00035753",
"PUB00035765",
"PUB00035769",
"PUB00035906",
"PUB00035907",
"PUB00035908",
"PUB00035909"
] | [
"14617352",
"17449236",
"11598180",
"15261670",
"15752139",
"16806884",
"16734666",
"16699812"
] | [
"Compromise of clathrin function and membrane association by clathrin light chain deletion.",
"Do different endocytic pathways make different synaptic vesicles?",
"Adaptins: the final recount.",
"COP and clathrin-coated vesicle budding: different pathways, common approaches.",
"New faces of the familiar cla... | [
2003,
2007,
2001,
2004,
2005,
2006,
2006,
2006
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
12,
8206
] | 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... | [
10,
1,
5,
2,
7,
12,
1,
4,
13,
1,
1,
11
] | 12 | true | Family | Clathrin light chain | Clathrin light chain | Clathrin_L-chain | 6 |
IPR000997 | 997 | Cholinesterase | Cholinesterase | Family | 10,082 | false | false | Cholinesterase enzymes are members of the broader alpha/beta hydrolase family and can be dividied into two distinct groups: those that catalyse the hydrolysis of acetylcholine to choline and acetate (acetylcholinesterases ) acetylcholine + H 2 O ->choline + acetate and those that catalyse the conversion of other acylch... | [
"GO:0004104"
] | [
"cholinesterase activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00878"
] | [
"CHOLNESTRASE"
] | [
10082
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.1.7",
"R-BTA-422085",
"R-BTA-9749641",
"R-CEL-112311",
"R-CEL-1483191",
"R-CEL-9749641",
"R-DME-112311",
"R-DME-1483191",
"R-DME-9749641",
"R-HSA-112311",
"R-HSA-1483191",
"R-HSA-422085",
"R-HSA-9749641",
"R-MMU-422085",
"R-MMU-9749641"
] | [
"EC:3.1.1.7",
"REACTOME:R-BTA-422085",
"REACTOME:R-BTA-9749641",
"REACTOME:R-CEL-112311",
"REACTOME:R-CEL-1483191",
"REACTOME:R-CEL-9749641",
"REACTOME:R-DME-112311",
"REACTOME:R-DME-1483191",
"REACTOME:R-DME-9749641",
"REACTOME:R-HSA-112311",
"REACTOME:R-HSA-1483191",
"REACTOME:R-HSA-422085",... | 15 | [
"1acj",
"1acl",
"1amn",
"1ax9",
"1b41",
"1c2b",
"1c2o",
"1c7i",
"1c7j",
"1cfj",
"1dx6",
"1e3q",
"1e66",
"1ea5",
"1eea",
"1eve",
"1f8u",
"1fss",
"1gpk",
"1gpn",
"1gqr",
"1gqs",
"1h22",
"1h23",
"1hbj",
"1j06",
"1j07",
"1jjb",
"1ku6",
"1maa",
"1mah",
"1n5m"... | 417 | [
"PUB00010129",
"PUB00029676",
"PUB00036069",
"PUB00036070",
"PUB00036071",
"PUB00036072",
"PUB00036073"
] | [
"1678899",
"12869558",
"15907917",
"8161450",
"8890157",
"8608006",
"11169626"
] | [
"Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.",
"Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.",
"Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology.",
"Acetylch... | [
1991,
2003,
2005,
1994,
1996,
1996,
2001
] | 7 | [] | [
"IPR000908",
"IPR001445"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Methanomicrobiales",
"unclassified sequences"
] | [
2515,
7532,
4,
31
] | 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"
] | [
5,
13,
7,
14,
8,
1,
6
] | 7 | true | Family | Cholinesterase | Cholinesterase | Cholinesterase | 6 |
IPR000998 | 998 | MAM domain | MAM_dom | Domain | 40,042 | false | false | MAM is an acronym derived from meprin, A-5 protein, and receptor protein-tyrosine phosphatase mu. The MAM domain consists of approximately 170 amino acids. It occurs in several cell surface proteins and is likely to have an adhesive function [ ]. The domain has been shown to play a role in homodimerization of protein-t... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PRINTS",
"PROSITE",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00629",
"PR00020",
"PS00740",
"PS50060",
"SM00137",
"cd06263"
] | [
"MAM",
"MAMDOMAIN",
"MAM_1",
"MAM_2",
"MAM",
"MAM"
] | [
37564,
17549,
12362,
39459,
34509,
33731
] | 6 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00604",
"R-DRE-1433557",
"R-DRE-194306",
"R-DRE-201556",
"R-DRE-399954",
"R-DRE-399956",
"R-DRE-9842663",
"R-DRE-9851151",
"R-HSA-1433557",
"R-HSA-163125",
"R-HSA-182971",
"R-HSA-194306",
"R-HSA-201556",
"R-HSA-376176",
"R-HSA-399954",
"R-HSA-399955",
"R-HSA-399956",
"R-HSA-44... | [
"PROSITEDOC:PDOC00604",
"REACTOME:R-DRE-1433557",
"REACTOME:R-DRE-194306",
"REACTOME:R-DRE-201556",
"REACTOME:R-DRE-399954",
"REACTOME:R-DRE-399956",
"REACTOME:R-DRE-9842663",
"REACTOME:R-DRE-9851151",
"REACTOME:R-HSA-1433557",
"REACTOME:R-HSA-163125",
"REACTOME:R-HSA-182971",
"REACTOME:R-HSA-... | 49 | [
"2c9a",
"2v5y",
"4gwm",
"4gwn",
"5l73",
"5oj2",
"5oj6",
"7aq1",
"7auw",
"7t4s",
"7uab",
"7uac",
"7uae",
"7uaf",
"7uai",
"8a1f",
"8a28",
"8h3s",
"8h3u",
"8yt7",
"8zi4",
"8ziv",
"8ziy",
"8zj4"
] | 24 | [
"PUB00005405",
"PUB00006426",
"PUB00054016",
"PUB00054017"
] | [
"8387703",
"9857066",
"7782276",
"8798668"
] | [
"An adhesive domain detected in functionally diverse receptors.",
"Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase.",
"Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM do... | [
1993,
1998,
1995,
1996
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1918,
38101,
4,
19
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
291,
93,
75,
57,
94
] | 6 | true | Domain | MAM domain | MAM domain | MAM_dom | 2 |
IPR000999 | 999 | Ribonuclease III domain | RNase_III_dom | Domain | 57,287 | false | false | This domain is found in eukaryotic, bacterial and archeal ribonuclease III (RNAse III) proteins. RNAse III is a double stranded RNA-specific endonuclease [ , ]. Prokaryotic RNAse III is important in post-transcriptional control of mRNA stability and translational efficiency. It is involved in the processing of ribosoma... | [
"GO:0004525",
"GO:0006396"
] | [
"ribonuclease III activity",
"RNA processing"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PFAM",
"PROSITE",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00636",
"PF14622",
"PS00517",
"PS50142",
"SM00535",
"cd00593"
] | [
"Ribonuclease_3",
"Ribonucleas_3_3",
"RNASE_3_1",
"RNASE_3_2",
"RIBOc",
"RIBOc"
] | [
24690,
31172,
37422,
49398,
49967,
49453
] | 6 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.26.3",
"PDOC00448",
"R-CEL-203927",
"R-CEL-426486",
"R-DME-203927",
"R-DME-426486",
"R-HSA-203927",
"R-HSA-426486",
"R-HSA-9708296",
"R-HSA-9820841",
"R-HSA-9824594",
"R-MMU-203927",
"R-MMU-426486",
"R-XTR-203927",
"R-XTR-426486"
] | [
"EC:3.1.26.3",
"PROSITEDOC:PDOC00448",
"REACTOME:R-CEL-203927",
"REACTOME:R-CEL-426486",
"REACTOME:R-DME-203927",
"REACTOME:R-DME-426486",
"REACTOME:R-HSA-203927",
"REACTOME:R-HSA-426486",
"REACTOME:R-HSA-9708296",
"REACTOME:R-HSA-9820841",
"REACTOME:R-HSA-9824594",
"REACTOME:R-MMU-203927",
... | 15 | [
"1i4s",
"1jfz",
"1o0w",
"1rc5",
"1rc7",
"1u61",
"1yyk",
"1yyo",
"1yyw",
"1yz9",
"2a11",
"2eb1",
"2ez6",
"2ffl",
"2gsl",
"2nue",
"2nuf",
"2nug",
"2qvw",
"3c4b",
"3c4t",
"3j6b",
"3n3w",
"3o2r",
"3rv0",
"3rv1",
"4m2z",
"4m30",
"4oog",
"4oun",
"5b16",
"5mrc"... | 89 | [
"PUB00010737",
"PUB00028101",
"PUB00030596",
"PUB00080037",
"PUB00080038"
] | [
"11738048",
"11809414",
"15016361",
"14983173",
"15066275"
] | [
"Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage.",
"Ribonuclease III: new sense from nuisance.",
"Noncatalytic assembly of ribonuclease III with double-stranded RNA.",
"RNase III enzymes and the initiation of gene silencing.",
"Dicers at RISC; the mec... | [
2001,
2002,
2004,
2004,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
193,
30318,
25648,
214,
914
] | 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",... | [
74,
2,
6,
25,
1,
12,
13,
5,
34,
10,
3,
4,
163
] | 13 | true | Domain | Ribonuclease III domain | Ribonuclease III domain | RNase_III_dom | 5 |
IPR001000 | 1,000 | Glycoside hydrolase family 10 domain | GH10_dom | Domain | 23,296 | 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",
"PROFILE",
"SMART"
] | [
"PF00331",
"PR00134",
"PS51760",
"SM00633"
] | [
"Glyco_hydro_10",
"GLHYDRLASE10",
"GH10_2",
"Glyco_10"
] | [
23258,
17868,
22252,
21326
] | 4 | [
"CAZY",
"EC",
"EC",
"PROSITEDOC"
] | [
"GH10",
"3.2.1",
"3.2.1.8",
"PDOC00510"
] | [
"CAZY:GH10",
"EC:3.2.1",
"EC:3.2.1.8",
"PROSITEDOC:PDOC00510"
] | 4 | [
"1b30",
"1b31",
"1b3v",
"1b3w",
"1b3x",
"1b3y",
"1b3z",
"1bg4",
"1clx",
"1e0v",
"1e0w",
"1e0x",
"1e5n",
"1exp",
"1fh7",
"1fh8",
"1fh9",
"1fhd",
"1gok",
"1gom",
"1goo",
"1goq",
"1gor",
"1hiz",
"1i1w",
"1i1x",
"1isv",
"1isw",
"1isx",
"1isy",
"1isz",
"1it0"... | 246 | [
"PUB00000117",
"PUB00000503",
"PUB00001778",
"PUB00003608",
"PUB00004870",
"PUB00005266",
"PUB00048906",
"PUB00067124"
] | [
"2252383",
"1747104",
"2806912",
"1886523",
"7624375",
"8535779",
"17642511",
"23508990"
] | [
"Molecular biology of cellulose degradation.",
"A classification of glycosyl hydrolases based on amino acid sequence similarities.",
"Cellulase families revealed by hydrophobic cluster analysis.",
"Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.",
"Conserved ... | [
1990,
1991,
1989,
1991,
1995,
1995,
2007,
2013
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
12209,
10168,
143,
776
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
60,
4,
48,
59
] | 4 | true | Domain | Glycoside hydrolase family 10 domain | Glycoside hydrolase family 10 domain | GH10_dom | 7 |
IPR001001 | 1,001 | DNA polymerase III, beta sliding clamp | DNA_polIII_beta | Family | 30,008 | false | false | DNA polymerase III is a complex, multichain holoenzyme responsible for most of the replicative synthesis in bacteria [ ]. It functions by adding nucleotide triphosphate (dNTP) residues to the 5'-end of a growing DNA chain, using a complementary DNA as template. The elongation factor beta-clamp, also called beta subunit... | [
"GO:0003677",
"GO:0006260",
"GO:0009360"
] | [
"DNA binding",
"DNA replication",
"DNA polymerase III complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PANTHER",
"SMART",
"NCBIFAM",
"CDD"
] | [
"PIRSF000804",
"PTHR30478",
"SM00480",
"TIGR00663",
"cd00140"
] | [
"DNA_pol_III_b",
"",
"POL3Bc",
"dnan",
"beta_clamp"
] | [
25532,
29929,
29074,
27484,
28955
] | 5 | [
"GP",
"GP"
] | [
"GenProp0263",
"GenProp1162"
] | [
"GP:GenProp0263",
"GP:GenProp1162"
] | 2 | [
"1jqj",
"1jql",
"1mmi",
"1ok7",
"1unn",
"1vpk",
"2avt",
"2awa",
"2pol",
"2xur",
"3bep",
"3d1e",
"3d1f",
"3d1g",
"3f1v",
"3p16",
"3pwe",
"3q4j",
"3q4k",
"3q4l",
"3qsb",
"3rb9",
"3t0p",
"4k3k",
"4k3l",
"4k3m",
"4k3o",
"4k3p",
"4k3q",
"4k3r",
"4k3s",
"4k74"... | 133 | [
"PUB00050608",
"PUB00080350",
"PUB00080351",
"PUB00086412"
] | [
"18191219",
"8548826",
"1358275",
"27499105"
] | [
"Structure of a sliding clamp on DNA.",
"DNA polymerase III: running rings around the fork.",
"The sliding clamp of DNA polymerase III holoenzyme encircles DNA.",
"Structural insight into β-Clamp and its interaction with DNA Ligase in Helicobacter pylori."
] | [
2008,
1996,
1992,
2016
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3,
28942,
70,
178,
815
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | DNA polymerase III, beta sliding clamp | DNA polymerase III, beta sliding clamp | DNA_polIII_beta | 3 |
IPR001002 | 1,002 | Chitin-binding, type 1 | Chitin-bd_1 | Domain | 16,481 | false | false | A number of plant and fungal proteins that bind N-acetylglucosamine (e.g. solanaceous lectins of tomato and potato, plant endochitinases, the wound-induced proteins: hevein, win1 and win2, and the Kluyveromyces lactis killer toxin alpha subunit) contain this domain [ ]. The domain may occur in one or more copies and is... | [
"GO:0008061"
] | [
"chitin binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00187",
"PR00451",
"PS50941",
"SM00270"
] | [
"Chitin_bind_1",
"CHITINBINDNG",
"CHIT_BIND_I_2",
"ChtBD1"
] | [
11875,
3028,
15649,
13633
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00025"
] | [
"PROSITEDOC:PDOC00025"
] | 1 | [
"1ehd",
"1ehh",
"1eis",
"1en2",
"1enm",
"1hev",
"1iqb",
"1k7t",
"1k7u",
"1k7v",
"1mmc",
"1p9g",
"1p9z",
"1q9b",
"1t0w",
"1uha",
"1ulk",
"1ulm",
"1uln",
"1wgc",
"1wgt",
"1wkx",
"1znt",
"1zuv",
"1zwu",
"2cwg",
"2dkv",
"2kus",
"2lb7",
"2n1s",
"2uvo",
"2wgc"... | 55 | [
"PUB00001396",
"PUB00002707",
"PUB00003415"
] | [
"2070799",
"1375935",
"1757999"
] | [
"Kluyveromyces lactis toxin has an essential chitinase activity.",
"The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase.",
"Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin."
] | [
1991,
1992,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadota",
"viral metagenome"
] | [
16473,
6,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
38,
3,
3,
24,
40
] | 5 | true | Domain | Chitin-binding, type 1 | Chitin-binding, type 1 | Chitin-bd_1 | 6 |
IPR001003 | 1,003 | MHC class II, alpha chain, N-terminal | MHC_II_a_N | Domain | 8,971 | false | false | This entry represents the N-terminal domain (also called alpha-1 domain) of the alpha chain of class II MHC glycoproteins from vertebrates. Major Histocompatibility Complex (MHC) glycoproteins are heterodimeric cell surface receptors that function to present antigen peptide fragments to T cells responsible for cell-med... | [
"GO:0006955",
"GO:0019882",
"GO:0016020",
"GO:0042613"
] | [
"immune response",
"antigen processing and presentation",
"membrane",
"MHC class II protein complex"
] | [
"biological_process",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PFAM",
"SMART"
] | [
"PF00993",
"SM00920"
] | [
"MHC_II_alpha",
"MHC_II_alpha"
] | [
8921,
8655
] | 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-HSA-202424",
"R-HSA-202427",
"R-HSA-202430",
"R-HSA-202433",
"R-HSA-2132295",
"R-HSA-389948",
"R-HSA-877300",
"R-MMU-202424",
"R-MMU-202427",
"R-MMU-202430",
"R-MMU-202433",
"R-MMU-2132295",
"R-MMU-389948",
"R-RNO-202424",
"R-RNO-202427",
"R-RNO-202430",
"R-RNO-202433",
"R-RNO-2... | [
"REACTOME:R-HSA-202424",
"REACTOME:R-HSA-202427",
"REACTOME:R-HSA-202430",
"REACTOME:R-HSA-202433",
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-389948",
"REACTOME:R-HSA-877300",
"REACTOME:R-MMU-202424",
"REACTOME:R-MMU-202427",
"REACTOME:R-MMU-202430",
"REACTOME:R-MMU-202433",
"REACTOME:R-MMU-21... | 25 | [
"1a6a",
"1aqd",
"1bx2",
"1d5m",
"1d5x",
"1d5z",
"1d6e",
"1d9k",
"1dlh",
"1es0",
"1f3j",
"1fne",
"1fng",
"1fv1",
"1fyt",
"1h15",
"1hdm",
"1hqr",
"1hxy",
"1i3r",
"1iak",
"1iao",
"1iea",
"1ieb",
"1j8h",
"1jk8",
"1jl4",
"1jwm",
"1jws",
"1jwu",
"1k2d",
"1k8i"... | 280 | [
"PUB00015254",
"PUB00016273"
] | [
"7612235",
"15120183"
] | [
"The three-dimensional structure of peptide-MHC complexes.",
"Function and regulation of MHC class II molecules in T-lymphocytes: of mice and men."
] | [
1995,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
8971
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
718,
106,
42
] | 4 | true | Domain | MHC class II, alpha chain, N-terminal | MHC class II, alpha chain, N-terminal | MHC_II_a_N | 7 |
IPR001005 | 1,005 | SANT/Myb domain | SANT/Myb | Domain | 306,492 | false | false | The myb/SANT domains can be classified into three groups: the myb-type HTH domain, which binds DNA, the SANT domain, which is a protein-protein interaction module, and the myb-like domain that can be involved in either of these functions. This entry represents a myb-like domain. The retroviral oncogene v-myb, and its c... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00249",
"PF23082",
"PS50090",
"SM00717",
"cd00167"
] | [
"Myb_DNA-binding",
"Myb_DNA-binding_2",
"MYB_LIKE",
"SANT",
"SANT"
] | [
205909,
7776,
210926,
237396,
205990
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00037",
"R-BTA-3371453",
"R-BTA-72163",
"R-BTA-9772755",
"R-CEL-381340",
"R-CEL-383280",
"R-CEL-5250924",
"R-CEL-6807505",
"R-DDI-5689901",
"R-DDI-6807505",
"R-DDI-72163",
"R-DME-212300",
"R-DME-2559580",
"R-DME-3214815",
"R-DME-5689880",
"R-DME-8943724",
"R-DME-8953750",
"R-D... | [
"PROSITEDOC:PDOC00037",
"REACTOME:R-BTA-3371453",
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-9772755",
"REACTOME:R-CEL-381340",
"REACTOME:R-CEL-383280",
"REACTOME:R-CEL-5250924",
"REACTOME:R-CEL-6807505",
"REACTOME:R-DDI-5689901",
"REACTOME:R-DDI-6807505",
"REACTOME:R-DDI-72163",
"REACTOME:R-DME-... | 201 | [
"1a5j",
"1ba5",
"1guu",
"1gv2",
"1gv5",
"1gvd",
"1h88",
"1h89",
"1h8a",
"1idy",
"1idz",
"1ign",
"1irz",
"1ity",
"1iv6",
"1mbe",
"1mbf",
"1mbg",
"1mbh",
"1mbj",
"1mbk",
"1mse",
"1msf",
"1ofc",
"1ug2",
"1vf9",
"1vfc",
"1w0t",
"1w0u",
"1wgx",
"1x41",
"1x58"... | 410 | [
"PUB00001152",
"PUB00005459",
"PUB00029414",
"PUB00043689"
] | [
"2824190",
"8882580",
"14536084",
"15040448"
] | [
"The highly conserved amino-terminal region of the protein encoded by the v-myb oncogene functions as a DNA-binding domain.",
"The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB.",
"Crystal structure and functional analysis of a nuc... | [
1987,
1996,
2003,
2004
] | 4 | [] | [
"IPR017884",
"IPR017930",
"IPR039467",
"IPR041343"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
7,
2858,
303585,
22,
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... | [
1493,
42,
346,
63,
178,
152,
24,
827,
200,
19,
15,
1791
] | 12 | true | Domain | SANT/Myb domain | SANT/Myb domain | SANT/Myb | 7 |
IPR001006 | 1,006 | Procollagen-lysine 5-dioxygenase, conserved site | Procol_lys_dOase | Conserved_site | 3,723 | false | false | Procollagen-lysine 5-dioxygenase ( ) catalyses the hydroxylation of lysine residues in X-Lys-Gly sequences in collagens. The resulting hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen crosslinks. At least three isoforms are known in ve... | [
"GO:0008475"
] | [
"procollagen-lysine 5-dioxygenase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01325"
] | [
"LYS_HYDROXYLASE"
] | [
3723
] | 1 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.11.4",
"PWY-7894",
"PDOC01028",
"R-CEL-1650814",
"R-HSA-1650814",
"R-MMU-1650814",
"R-RNO-1650814"
] | [
"EC:1.14.11.4",
"METACYC:PWY-7894",
"PROSITEDOC:PDOC01028",
"REACTOME:R-CEL-1650814",
"REACTOME:R-HSA-1650814",
"REACTOME:R-MMU-1650814",
"REACTOME:R-RNO-1650814"
] | 7 | [
"6fxk",
"6fxm",
"6fxr",
"6fxt",
"6fxx",
"6fxy",
"6te3",
"6tec",
"6tes",
"6teu",
"6tex",
"6tez",
"8one",
"8zgc",
"8zge",
"8zgg",
"8zgh"
] | 17 | [
"PUB00002987",
"PUB00091103",
"PUB00091104",
"PUB00091105",
"PUB00091106",
"PUB00091107",
"PUB00091108"
] | [
"8621606",
"11956192",
"12475640",
"18298658",
"30089812",
"18834968",
"10934207"
] | [
"Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity.",
"Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-termin... | [
1996,
2002,
2002,
2009,
2018,
2008,
2000
] | 7 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
3723
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
15,
8,
12
] | 5 | true | Conserved_site | Procollagen-lysine 5-dioxygenase, conserved site | Procollagen-lysine 5-dioxygenase, conserved site | Procol_lys_dOase | 5 |
IPR001007 | 1,007 | VWFC domain | VWF_dom | Domain | 54,262 | false | false | The vWF domain is found in various plasma proteins: complement factors B, C2, CR3 and CR4; the integrins (I-domains); collagen types VI, VII, XII and XIV; and other extracellular proteins [ , , ]. Although the majority of VWA-containing proteins are extracellular, the most ancient ones present in all eukaryotes are all... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART",
"SMART"
] | [
"PF00093",
"PS01208",
"PS50184",
"SM00214",
"SM00215"
] | [
"VWC",
"VWFC_1",
"VWFC_2",
"VWC",
"VWC_out"
] | [
30149,
37536,
41083,
45155,
21191
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00928",
"R-BTA-114604",
"R-BTA-1442490",
"R-BTA-1566977",
"R-BTA-1650814",
"R-BTA-186797",
"R-BTA-198933",
"R-BTA-2022090",
"R-BTA-202733",
"R-BTA-216083",
"R-BTA-2243919",
"R-BTA-3000171",
"R-BTA-3000178",
"R-BTA-430116",
"R-BTA-75892",
"R-BTA-76009",
"R-BTA-8874081",
"R-BTA-... | [
"PROSITEDOC:PDOC00928",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1566977",
"REACTOME:R-BTA-1650814",
"REACTOME:R-BTA-186797",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-2022090",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-2243919",
"REACTOME:R-BTA... | 182 | [
"1u5m",
"5nb8",
"5nir",
"6n29",
"6tm2",
"7a5o",
"7kwo",
"7pmv",
"7pnf",
"7pov",
"7pp6",
"7qcl",
"7qcu",
"7wn3",
"7wn4",
"7wn6",
"7wpp",
"7wpq",
"7wpr",
"7wps",
"7wqt",
"7zwh",
"8d3c",
"8d3d",
"8oer",
"8oes",
"8r0t",
"8rde",
"9gvj",
"9gvq"
] | 30 | [
"PUB00000182",
"PUB00001619",
"PUB00003066",
"PUB00003322",
"PUB00003554"
] | [
"3495268",
"1864378",
"2007623",
"8145250",
"8412987"
] | [
"von Willebrand factor shares a distinctive cysteine-rich domain with thrombospondin and procollagen.",
"Shuffled domains in extracellular proteins.",
"Assembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acids.",... | [
1987,
1991,
1991,
1994,
1993
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
22,
54239,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
111,
29,
160,
127,
148
] | 6 | true | Domain | VWFC domain | VWFC domain | VWF_dom | 8 |
IPR001010 | 1,010 | Thionin | Thionin | Family | 904 | false | false | Thionins are small, basic plant proteins, 45 to 50 amino acids in length, which include three or four conserved disulphide linkages. The proteins are toxic to animal cells, presumably attacking the cell membrane and rendering it permeable: this results in the inhibition of sugar uptake and allows potassium and phosphat... | [
"GO:0006952"
] | [
"defense response"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PRINTS",
"PROSITE",
"PANTHER"
] | [
"PF00321",
"PR00287",
"PS00271",
"PTHR33920"
] | [
"Thionin",
"THIONIN",
"THIONIN",
""
] | [
669,
528,
733,
765
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00244"
] | [
"PROSITEDOC:PDOC00244"
] | 1 | [
"1ab1",
"1bhp",
"1cbn",
"1ccm",
"1ccn",
"1cnr",
"1crn",
"1cxr",
"1ed0",
"1ejg",
"1jmn",
"1jmp",
"1jxt",
"1jxu",
"1jxw",
"1jxx",
"1jxy",
"1nbl",
"1okh",
"1orl",
"1wuw",
"1yv8",
"1yva",
"2eya",
"2eyb",
"2eyc",
"2eyd",
"2fd7",
"2fd9",
"2plh",
"2v9b",
"3c8p"... | 40 | [
"PUB00000146",
"PUB00004552"
] | [
"3985614",
"1377959"
] | [
"A toxic thionin from Pyrularia pubera: purification, properties, and amino acid sequence.",
"The identification of leaf thionin as one of the main jasmonate-induced proteins of barley (Hordeum vulgare)."
] | [
1985,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Riboviria sp.",
"marine metagenome"
] | [
5,
897,
1,
1
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
16,
25,
1
] | 3 | true | Family | Thionin | Thionin | Thionin | 2 |
IPR001011 | 1,011 | Acid phosphatase, class A, bacterial | Acid_Pase_classA_bac | Family | 4,433 | false | false | This group represents nonspecific acid phosphatases, class A [ , ]. Non-specific acid phosphatases are bacterial enzymes that catalyse the dephosphorylation of orthophosphoric monoesters to alcohol and phosphate, in addition to being able to catalyse transphosphorylation. As their name suggests, they show broad specifi... | [
"GO:0003993",
"GO:0030288"
] | [
"acid phosphatase activity",
"outer membrane-bounded periplasmic space"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PIRSF",
"PRINTS",
"CDD"
] | [
"PIRSF000897",
"PR00483",
"cd03397"
] | [
"Acid_Ptase_ClsA",
"BACPHPHTASE",
"PAP2_acid_phosphatase"
] | [
2202,
2874,
3759
] | 3 | [
"EC",
"METACYC",
"PROSITEDOC"
] | [
"3.1.3.2",
"PWY-6348",
"PDOC00891"
] | [
"EC:3.1.3.2",
"METACYC:PWY-6348",
"PROSITEDOC:PDOC00891"
] | 3 | [
"1d2t",
"1eoi",
"1iw8",
"2a96",
"2akc",
"2ipb",
"7f17",
"7f18",
"8yc1",
"9htz",
"9jq0"
] | 11 | [
"PUB00003588",
"PUB00014389",
"PUB00014807"
] | [
"8081499",
"8755883",
"12968332"
] | [
"Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii.",
"Identification and characterization of phoN-Sf, a gene on the large plasmid of Shigella flexneri 2a encoding a nonspecific phosphatase.",
"Phosphorylation and dephosphorylation of polyhydrox... | [
1994,
1996,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4417,
7,
9
] | 3 | [] | [] | 0 | true | Family | Acid phosphatase, class A, bacterial | Acid phosphatase, class A, bacterial | Acid_Pase_classA_bac | 3 |
IPR001012 | 1,012 | UBX domain | UBX_dom | Domain | 35,448 | false | false | The UBX domain is found in ubiquitin-regulatory proteins, which are members of the ubiquitination pathway, as well as a number of other proteins including FAF-1 (FAS-associated factor 1), the human Rep-8 reproduction protein and several hypothetical proteins from yeast. The function of the UBX domain is not known altho... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00789",
"PS50033",
"SM00166"
] | [
"UBX",
"UBX",
"UBX"
] | [
33966,
34187,
23001
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50033",
"R-BTA-532668",
"R-BTA-5693565",
"R-BTA-6798695",
"R-BTA-8980692",
"R-BTA-9013407",
"R-CEL-532668",
"R-CEL-9013407",
"R-DDI-8951664",
"R-DDI-9013407",
"R-DDI-9755511",
"R-DRE-532668",
"R-GGA-9013407",
"R-HSA-1445148",
"R-HSA-532668",
"R-HSA-5693565",
"R-HSA-6798695",
"... | [
"PROSITEDOC:PDOC50033",
"REACTOME:R-BTA-532668",
"REACTOME:R-BTA-5693565",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8980692",
"REACTOME:R-BTA-9013407",
"REACTOME:R-CEL-532668",
"REACTOME:R-CEL-9013407",
"REACTOME:R-DDI-8951664",
"REACTOME:R-DDI-9013407",
"REACTOME:R-DDI-9755511",
"REACTOME:R-... | 53 | [
"1h8c",
"1i42",
"1jru",
"1s3s",
"1wj4",
"2cr5",
"2dzk",
"2kxj",
"3qc8",
"3qca",
"3qq8",
"3qwz",
"3qx1",
"3r3m",
"5ifs",
"5ifw",
"5x3p",
"5x4l",
"6hd0",
"6opc",
"7oat",
"7r7s",
"7r7t",
"8b5r",
"8fcl",
"8fcm",
"8fcn",
"8fco",
"8fcp",
"8fcq",
"8fcr",
"8fct"... | 36 | [] | [] | [] | [] | 0 | [] | [
"IPR033043"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota"
] | [
18,
35430
] | 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... | [
68,
7,
32,
17,
37,
27,
4,
55,
71,
7,
4,
87
] | 12 | true | Domain | UBX domain | UBX domain | UBX_dom | 9 |
IPR001013 | 1,013 | Neurokinin NK3 receptor | NK3_rcpt | Family | 1,302 | 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:0004995",
"GO:0007186",
"GO:0005886",
"GO:0016020"
] | [
"tachykinin receptor activity",
"G protein-coupled receptor signaling pathway",
"plasma membrane",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01026"
] | [
"NEUROKININ3R"
] | [
1302
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"362",
"R-HSA-380095",
"R-HSA-416476",
"R-MMU-380095",
"R-MMU-416476",
"R-RNO-380095",
"R-RNO-416476"
] | [
"IUPHAR:362",
"REACTOME:R-HSA-380095",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-380095",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-380095",
"REACTOME:R-RNO-416476"
] | 7 | [
"8jbf"
] | 1 | [
"PUB00000131",
"PUB00002477",
"PUB00002518",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"2478537",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Molecular characterization of a functional cDNA for rat substance P receptor.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G pr... | [
1990,
1988,
1989,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 11 | [
"IPR001681"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
1302
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
42,
4,
2,
2
] | 4 | true | Family | Neurokinin NK3 receptor | Neurokinin NK3 receptor | NK3_rcpt | 5 |
IPR001014 | 1,014 | Large ribosomal subunit protein uL23, conserved site | Ribosomal_uL23_CS | Conserved_site | 27,111 | false | false | This entry represents a small conserved region in the C-terminal section of the large ribosomal subunit protein uL23, previously known as Ribosomal protein L23 in bacteria, archaea, animals and plants, and as L25 in yeast. uL23 binds to a specific region on either the 23S or 26S rRNA [ , , ]. Ribosomes are the particle... | [
"GO:0019843"
] | [
"rRNA binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00050"
] | [
"RIBOSOMAL_L23"
] | [
27111
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00049",
"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-HSA-156827",
"R-HSA-156902",
"R-HSA-1799339",
"R-HSA-192823",
"R-HSA-2408557... | [
"PROSITEDOC:PDOC00049",
"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-72689",
"REACTOME:R-DDI-72706",
"REACTOME:R-DDI-975956... | 45 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql"... | 1,128 | [
"PUB00003403",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00059102",
"PUB00080279"
] | [
"2501503",
"11297922",
"11290319",
"11114498",
"22096102",
"24524803"
] | [
"Structural comparison of 26S rRNA-binding ribosomal protein L25 from two different yeast strains and the equivalent proteins from three eubacteria and two chloroplasts.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal p... | [
1989,
2001,
2001,
2000,
2011,
2014
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
526,
10153,
16280,
152
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (s... | [
12,
2,
2,
4,
1,
6,
4,
8,
6,
1,
2,
21
] | 12 | true | Conserved_site | Large ribosomal subunit protein uL23, conserved site | Large ribosomal subunit protein uL23, conserved site | Ribosomal_uL23_CS | 9 |
IPR001015 | 1,015 | Ferrochelatase | Ferrochelatase | Family | 28,341 | false | false | null | [
"GO:0004325",
"GO:0006783"
] | [
"ferrochelatase activity",
"heme biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00323",
"PF00762",
"PTHR11108",
"TIGR00109"
] | [
"Ferrochelatase",
"Ferrochelatase",
"",
"hemH"
] | [
25549,
28279,
28026,
24641
] | 4 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.98.1.1",
"GenProp0222",
"GenProp1421",
"GenProp1470",
"GenProp1663",
"GenProp1686",
"PDOC00462",
"R-BTA-189451",
"R-BTA-9837999",
"R-DDI-189451",
"R-DDI-9837999",
"R-DME-189451",
"R-DME-9837999",
"R-GGA-421984",
"R-HSA-189451",
"R-HSA-9837999",
"R-MMU-189451",
"R-MMU-9837999",
... | [
"EC:4.98.1.1",
"GP:GenProp0222",
"GP:GenProp1421",
"GP:GenProp1470",
"GP:GenProp1663",
"GP:GenProp1686",
"PROSITEDOC:PDOC00462",
"REACTOME:R-BTA-189451",
"REACTOME:R-BTA-9837999",
"REACTOME:R-DDI-189451",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-189451",
"REACTOME:R-DME-9837999",
"REACTOM... | 22 | [
"1ak1",
"1c1h",
"1c9e",
"1doz",
"1hrk",
"1l8x",
"1lbq",
"1ld3",
"1n0i",
"2ac2",
"2ac4",
"2c8j",
"2h1v",
"2h1w",
"2hk6",
"2hrc",
"2hre",
"2pnj",
"2po5",
"2po7",
"2q2n",
"2q2o",
"2q3j",
"2qd1",
"2qd2",
"2qd3",
"2qd4",
"2qd5",
"3aqi",
"3goq",
"3hcn",
"3hco"... | 54 | [
"PUB00002620",
"PUB00004754",
"PUB00006691",
"PUB00006693",
"PUB00012956",
"PUB00021315",
"PUB00022076",
"PUB00026989",
"PUB00079463",
"PUB00079464",
"PUB00079465",
"PUB00079466",
"PUB00079467"
] | [
"2185242",
"1704134",
"9384565",
"11175906",
"12196143",
"10704318",
"12427010",
"12761666",
"11215517",
"10582332",
"7592569",
"8122254",
"6390167"
] | [
"The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption, and expression of its structural gene HEM15.",
"Cloning of murine ferrochelatase.",
"Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis.",
"The 2.0 A structure of human ferrochelatase, the terminal enzyme of he... | [
1990,
1991,
1997,
2001,
2002,
2000,
2002,
2003,
2000,
1999,
1995,
1993,
1984
] | 13 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
108,
21671,
6258,
304
] | 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",... | [
8,
1,
3,
1,
1,
10,
11,
1,
7,
6,
1,
2,
19
] | 13 | true | Family | Ferrochelatase | Ferrochelatase | Ferrochelatase | 1 |
IPR001017 | 1,017 | Dehydrogenase, E1 component | DH_E1 | Domain | 85,278 | false | false | null | [
"GO:0016624"
] | [
"oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00676"
] | [
"E1_dh"
] | [
85278
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"1.2.4",
"GenProp1408",
"R-BTA-6783984",
"R-BTA-9837999",
"R-BTA-9853506",
"R-CEL-204174",
"R-CEL-5362517",
"R-CEL-6783984",
"R-CEL-9837999",
"R-CEL-9853506",
"R-CEL-9858328",
"R-CEL-9859138",
"R-CEL-9861559",
"R-CFA-204174",
"R-CFA-5362517",
"R-CFA-9837999",
"R-CFA-9861559",
"R-DD... | [
"EC:1.2.4",
"GP:GenProp1408",
"REACTOME:R-BTA-6783984",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9853506",
"REACTOME:R-CEL-204174",
"REACTOME:R-CEL-5362517",
"REACTOME:R-CEL-6783984",
"REACTOME:R-CEL-9837999",
"REACTOME:R-CEL-9853506",
"REACTOME:R-CEL-9858328",
"REACTOME:R-CEL-9859138",
"RE... | 71 | [
"1dtw",
"1ni4",
"1ols",
"1olu",
"1olx",
"1qs0",
"1u5b",
"1um9",
"1umb",
"1umc",
"1umd",
"1v11",
"1v16",
"1v1m",
"1v1r",
"1w85",
"1w88",
"1wci",
"1x7w",
"1x7x",
"1x7y",
"1x7z",
"1x80",
"2beu",
"2bev",
"2bew",
"2bfb",
"2bfc",
"2bfd",
"2bfe",
"2bff",
"2bp7"... | 84 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1188,
57115,
25775,
6,
1194
] | 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",... | [
44,
8,
25,
15,
1,
42,
13,
3,
17,
32,
2,
2,
80
] | 13 | true | Domain | Dehydrogenase, E1 component | Dehydrogenase, E1 component | DH_E1 | 9 |
IPR001018 | 1,018 | Beta-lactamase, class-B, conserved site | Beta-lactamase_class-B_CS | Conserved_site | 3,957 | false | false | null | [
"GO:0008270",
"GO:0008800",
"GO:0017001"
] | [
"zinc ion binding",
"beta-lactamase activity",
"antibiotic catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00743",
"PS00744"
] | [
"BETA_LACTAMASE_B_1",
"BETA_LACTAMASE_B_2"
] | [
3206,
1402
] | 2 | [
"EC",
"PROSITEDOC"
] | [
"3.5.2.6",
"PDOC00606"
] | [
"EC:3.5.2.6",
"PROSITEDOC:PDOC00606"
] | 2 | [
"1a7t",
"1a8t",
"1bc2",
"1bmc",
"1bvt",
"1dd6",
"1ddk",
"1dxk",
"1hlk",
"1jje",
"1jjt",
"1kr3",
"1m2x",
"1mqo",
"1sml",
"1vgn",
"1wuo",
"1wup",
"1x8g",
"1x8h",
"1x8i",
"1znb",
"2aio",
"2bc2",
"2bfk",
"2bfl",
"2bfz",
"2bg2",
"2bg6",
"2bg7",
"2bg8",
"2bga"... | 195 | [
"PUB00000136",
"PUB00005282"
] | [
"8141584",
"8805566"
] | [
"Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance.",
"Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis."
] | [
1994,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacillus phage G",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
11,
1,
3576,
319,
50
] | 5 | [
"Arabidopsis thaliana"
] | [
6
] | 1 | true | Conserved_site | Beta-lactamase, class-B, conserved site | Beta-lactamase, class-B, conserved site | Beta-lactamase_class-B_CS | 2 |
IPR001019 | 1,019 | Guanine nucleotide binding protein, alpha subunit | Gprotein_alpha_su | Family | 42,599 | false | false | This family consists of the G protein alpha subunit, which acts as a weak GTPase. G protein classes are defined based on the sequence and function of their alpha subunits, which in mammals fall into four main categories: G alpha-S ( ), G alpha-Q ( ), G alpha-I ( ) and G alpha-12 ( ); there are also fungal ( ) and plant... | [
"GO:0003924",
"GO:0019001",
"GO:0031683",
"GO:0007186"
] | [
"GTPase activity",
"guanyl nucleotide binding",
"G-protein beta/gamma-subunit complex binding",
"G protein-coupled receptor signaling pathway"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PFAM",
"PRINTS",
"PROFILE",
"PANTHER",
"SMART",
"CDD"
] | [
"PF00503",
"PR00318",
"PS51882",
"PTHR10218",
"SM00275",
"cd00066"
] | [
"G-alpha",
"GPROTEINA",
"G_ALPHA",
"",
"G_alpha",
"G-alpha"
] | [
42138,
37283,
41826,
40958,
40450,
34020
] | 6 | [
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"GenProp2089",
"GenProp2092",
"GenProp2093",
"GenProp2094",
"R-BTA-112043",
"R-BTA-170670",
"R-BTA-202040",
"R-BTA-2485179",
"R-BTA-2514859",
"R-BTA-381771",
"R-BTA-392170",
"R-BTA-399997",
"R-BTA-400042",
"R-BTA-4086398",
"R-BTA-416476",
"R-BTA-418592",
"R-BTA-418594",
"R-BTA-4289... | [
"GP:GenProp2089",
"GP:GenProp2092",
"GP:GenProp2093",
"GP:GenProp2094",
"REACTOME:R-BTA-112043",
"REACTOME:R-BTA-170670",
"REACTOME:R-BTA-202040",
"REACTOME:R-BTA-2485179",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-381771",
"REACTOME:R-BTA-392170",
"REACTOME:R-BTA-399997",
"REACTOME:R-BTA-40... | 230 | [
"1agr",
"1as0",
"1as2",
"1as3",
"1azs",
"1azt",
"1bh2",
"1bof",
"1cip",
"1cjk",
"1cjt",
"1cju",
"1cjv",
"1cs4",
"1cul",
"1fqj",
"1fqk",
"1gdd",
"1gfi",
"1gg2",
"1gia",
"1gil",
"1git",
"1got",
"1gp2",
"1kjy",
"1shz",
"1svk",
"1svs",
"1tad",
"1tag",
"1tl7"... | 1,362 | [
"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 | [] | [
"IPR000367",
"IPR000469",
"IPR000654",
"IPR001408",
"IPR002975",
"IPR002976"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Orpheovirus IHUMI-LCC2"
] | [
2,
7,
42588,
2
] | 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... | [
20,
31,
53,
12,
88,
59,
3,
26,
74,
2,
2,
19
] | 12 | true | Family | Guanine nucleotide binding protein, alpha subunit | Guanine nucleotide binding protein, alpha subunit | Gprotein_alpha_su | 9 |
IPR001020 | 1,020 | Phosphotransferase system, HPr histidine phosphorylation site | PTS_HPr_His_P_site | PTM | 27,366 | false | false | The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is as follows: a phosphoryl gro... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00369"
] | [
"PTS_HPR_HIS"
] | [
27366
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00318"
] | [
"PROSITEDOC:PDOC00318"
] | 1 | [
"1fu0",
"1ggr",
"1hdn",
"1j6t",
"1jem",
"1ka5",
"1kkl",
"1kkm",
"1opd",
"1pch",
"1pfh",
"1poh",
"1ptf",
"1qfr",
"1qr5",
"1rzr",
"1sph",
"1vrc",
"1y4y",
"1y50",
"1y51",
"2fep",
"2hid",
"2hpr",
"2jel",
"2lrk",
"2lrl",
"2nzu",
"2nzv",
"2oen",
"2xdf",
"3eza"... | 51 | [
"PUB00000073",
"PUB00003612"
] | [
"2197982",
"8246840"
] | [
"The bacterial phosphoenolpyruvate: glycose phosphotransferase system.",
"Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria."
] | [
1990,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
232,
26846,
91,
196,
1
] | 5 | [
"Escherichia coli (strain K12)",
"Zea mays"
] | [
5,
3
] | 2 | true | PTM | Phosphotransferase system, HPr histidine phosphorylation site | Phosphotransferase system, HPr histidine phosphorylation site | PTS_HPr_His_P_site | 2 |
IPR001021 | 1,021 | Ribosomal protein bL25, long-form | Ribosomal_bL25_long | Family | 20,881 | false | false | This entry represents the full-length form of ribosomal protein bL25 (previously known as L25), such as ribosomal protein TL5 of Thermus thermophilus. It has homology to the general stress protein Ctc of Bacillus subtilis, which has now been localised to ribosomes and can be viewed as the long form, or Ctc form, of L25... | [
"GO:0003735",
"GO:0008097",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"5S rRNA binding",
"translation",
"ribosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01334",
"TIGR00731"
] | [
"Ribosomal_bL25_CTC",
"bL25_bact_ctc"
] | [
20211,
20865
] | 2 | [] | [] | [] | 0 | [
"1feu",
"1njm",
"1njp",
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"2zjp",
"2zjq",
"2zjr",
"3cf5",
"3dll",
"3pio",
"3pip",
"4io9",
"4ioa",
"4ioc",
"4l47",
"4l71",
"4lel",
"4lfz",
"4lnt",
"4lsk",
"4lt8",
"4p6f",
"4p70"... | 438 | [
"PUB00020992",
"PUB00070727"
] | [
"12432960",
"15236599"
] | [
"The general stress protein Ctc of Bacillus subtilis is a ribosomal protein.",
"General stress protein CTC from Bacillus subtilis specifically binds to ribosomal 5S RNA."
] | [
2002,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"candidate division MSBL1 archaeon SCGC-AAA382N08",
"unclassified sequences"
] | [
20248,
137,
1,
1,
494
] | 5 | [] | [] | 0 | true | Family | Ribosomal protein bL25, long-form | Ribosomal protein bL25, long-form | Ribosomal_bL25_long | 5 |
IPR001022 | 1,022 | Tobamoviral movement protein | TMV_movement | Family | 362 | false | false | The movement protein of tobamoviruses is necessary for the initial cell-to-cell movement during the early stages of a viral infection. This movement is active, and involves the interaction of the movement protein with the plasmodesmata. The movement protein possesses the ability to bind to RNA to achieve its role [ ]. ... | [
"GO:0003676"
] | [
"nucleic acid binding"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00964"
] | [
"MOVEMENT"
] | [
362
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005565",
"PUB00005584"
] | [
"3201760",
"1546450"
] | [
"Interviral homologies of the 30K proteins of tobamoviruses.",
"Effects of terminal deletion mutations on function of the movement protein of tobacco mosaic virus."
] | [
1988,
1992
] | 2 | [
"IPR028919"
] | [] | 1 | 0 | 1 | [
"Kitrinoviricota"
] | [
362
] | 1 | [] | [] | 0 | true | Family | Tobamoviral movement protein | Tobamoviral movement protein | TMV_movement | 6 |
IPR001024 | 1,024 | PLAT/LH2 domain | PLAT/LH2_dom | Domain | 37,961 | false | false | This entry represents a domain found in a variety of membrane or lipid associated proteins. It is known as the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain, is found in a variety of membrane or lipid associated proteins. Structurally, this domain forms a β-sandwich compose... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01477",
"PS50095",
"SM00308"
] | [
"PLAT",
"PLAT",
"LH2"
] | [
35138,
36788,
26527
] | 3 | [
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"GenProp1588",
"GenProp1653",
"GenProp1703",
"PDOC50095",
"R-BTA-192456",
"R-BTA-2142691",
"R-BTA-2142712",
"R-BTA-2142770",
"R-BTA-8963889",
"R-BTA-8963901",
"R-BTA-8964026",
"R-BTA-9018677",
"R-BTA-9018681",
"R-BTA-9018896",
"R-BTA-9023661",
"R-BTA-9025106",
"R-BTA-9026286",
"R-B... | [
"GP:GenProp1588",
"GP:GenProp1653",
"GP:GenProp1703",
"PROSITEDOC:PDOC50095",
"REACTOME:R-BTA-192456",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-2142712",
"REACTOME:R-BTA-2142770",
"REACTOME:R-BTA-8963889",
"REACTOME:R-BTA-8963901",
"REACTOME:R-BTA-8964026",
"REACTOME:R-BTA-9018677",
"REACTO... | 113 | [
"1bu8",
"1ca1",
"1eth",
"1f8n",
"1fgm",
"1fgo",
"1fgq",
"1fgr",
"1fgt",
"1gpl",
"1gyg",
"1hpl",
"1hu9",
"1ik3",
"1jnq",
"1kho",
"1lnh",
"1lox",
"1lpa",
"1lpb",
"1n8q",
"1n8s",
"1no3",
"1olp",
"1qm6",
"1qmd",
"1rov",
"1rp1",
"1rrh",
"1rrl",
"1w52",
"1y4k"... | 101 | [
"PUB00016270",
"PUB00018111",
"PUB00018112"
] | [
"11412104",
"10469604",
"11985859"
] | [
"Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1.",
"The PLAT domain: a new piece in the PKD1 puzzle.",
"PSLAP, a protein with multiple adhesive motifs, is expressed in Plasmodium falciparum gametocytes."
] | [
2001,
1999,
2002
] | 3 | [] | [
"IPR042057",
"IPR042060",
"IPR042062",
"IPR047277"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
17,
684,
37242,
3,
15
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
37,
6,
82,
6,
95,
68,
56,
80,
91
] | 9 | true | Domain | PLAT/LH2 domain | PLAT/LH2 domain | PLAT/LH2_dom | 5 |
IPR001025 | 1,025 | Bromo adjacent homology (BAH) domain | BAH_dom | Domain | 41,478 | false | false | The BAH (bromo-adjacent homology) is commonly found in chromatin-associated proteins [ ]. It is found in proteins such as eukaryotic DNA (cytosine-5) methyltransferases , the origin recognition complex 1 (Orc1) proteins, as well as several proteins involved in transcriptional regulation. The BAH domain appears to act a... | [
"GO:0003682"
] | [
"chromatin binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01426",
"PS51038",
"SM00439"
] | [
"BAH",
"BAH",
"BAH"
] | [
36985,
41362,
34578
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51038",
"R-DME-176187",
"R-DME-68616",
"R-DME-68689",
"R-DME-68949",
"R-DME-68962",
"R-HSA-113507",
"R-HSA-176187",
"R-HSA-212300",
"R-HSA-3214815",
"R-HSA-3214841",
"R-HSA-3214858",
"R-HSA-3232118",
"R-HSA-427389",
"R-HSA-427413",
"R-HSA-4655427",
"R-HSA-5334118",
"R-HSA-6804... | [
"PROSITEDOC:PDOC51038",
"REACTOME:R-DME-176187",
"REACTOME:R-DME-68616",
"REACTOME:R-DME-68689",
"REACTOME:R-DME-68949",
"REACTOME:R-DME-68962",
"REACTOME:R-HSA-113507",
"REACTOME:R-HSA-176187",
"REACTOME:R-HSA-212300",
"REACTOME:R-HSA-3214815",
"REACTOME:R-HSA-3214841",
"REACTOME:R-HSA-321485... | 72 | [
"1m4z",
"1w4s",
"1zbx",
"1zhi",
"2fl7",
"2fvu",
"3av4",
"3av5",
"3av6",
"3pt6",
"3pt9",
"3pta",
"3swr",
"3tu4",
"4bb7",
"4da4",
"4dov",
"4dow",
"4fsx",
"4ft2",
"4ft4",
"4jjn",
"4kud",
"4kui",
"4kul",
"4ld9",
"4wxx",
"4yoc",
"5gut",
"5guv",
"5hh7",
"5v8f"... | 111 | [
"PUB00001720",
"PUB00068988"
] | [
"10100640",
"23907388"
] | [
"The BAH (bromo-adjacent homology) domain: a link between DNA methylation, replication and transcriptional regulation.",
"The BAH domain of Rsc2 is a histone H3 binding domain."
] | [
1999,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)",
"metagenomes"
] | [
118,
27,
41327,
1,
5
] | 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... | [
115,
17,
70,
19,
49,
53,
5,
46,
56,
5,
3,
158
] | 12 | true | Domain | Bromo adjacent homology (BAH) domain | Bromo adjacent homology (BAH) domain | BAH_dom | 1 |
IPR001028 | 1,028 | Glycoprotein phospholipase D | Gprt_PLipase_D | Family | 818 | false | false | Phosphatidylinositol-glycan-specific phospholipase D is an extracellular amphiphilic glycoprotein [ , ]. It hydrolyses the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans, releasing these proteins from the membrane. The enzyme catalyses the reaction: glycoprotein phosphatidylinositol + H... | [
"GO:0004621",
"GO:0005576"
] | [
"GPI anchor phospholipase D activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00718"
] | [
"PHPHLIPASED"
] | [
818
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.4.50",
"R-HSA-163125",
"R-MMU-163125",
"R-RNO-163125"
] | [
"EC:3.1.4.50",
"REACTOME:R-HSA-163125",
"REACTOME:R-MMU-163125",
"REACTOME:R-RNO-163125"
] | 4 | [] | 0 | [
"PUB00001419",
"PUB00005141"
] | [
"1606959",
"2017684"
] | [
"Phosphatidylinositol-glycan-specific phospholipase D is an amphiphilic glycoprotein that in serum is associated with high-density lipoproteins.",
"Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D."
] | [
1992,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
33,
785
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
4
] | 3 | true | Family | Glycoprotein phospholipase D | Glycoprotein phospholipase D | Gprt_PLipase_D | 9 |
IPR001029 | 1,029 | Flagellin, N-terminal domain | Flagellin_N | Domain | 43,148 | false | false | Bacterial flagella are responsible for motility and chemotaxis [ ]. They comprise a basal body, a hook and a filament, the latter accounting for 98% of the mass [ ]. Flagellin is the subunit protein that polymerises to form the flagella [ ], the subunits being transported through the centre of the filament to the tip, ... | [
"GO:0005198"
] | [
"structural molecule activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF00669",
"PR00207"
] | [
"Flagellin_N",
"FLAGELLIN"
] | [
43147,
26348
] | 2 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp0882",
"R-GGA-433822",
"R-GGA-451534",
"R-GGA-977240",
"R-HSA-168176",
"R-HSA-5602680",
"R-HSA-5603037",
"R-HSA-844623",
"R-HSA-975871"
] | [
"GP:GenProp0882",
"REACTOME:R-GGA-433822",
"REACTOME:R-GGA-451534",
"REACTOME:R-GGA-977240",
"REACTOME:R-HSA-168176",
"REACTOME:R-HSA-5602680",
"REACTOME:R-HSA-5603037",
"REACTOME:R-HSA-844623",
"REACTOME:R-HSA-975871"
] | 9 | [
"1io1",
"1ucu",
"2d4x",
"2zbi",
"3a5x",
"3k8v",
"3k8w",
"3pwx",
"3v47",
"4cfi",
"4mn8",
"4nx9",
"5gy2",
"5kay",
"5maw",
"5wjt",
"5wju",
"5wjv",
"5wjw",
"5wjx",
"5wjy",
"5wjz",
"5wk5",
"5wk6",
"5yti",
"5z7q",
"5ziy",
"5ziz",
"5zj0",
"6b5b",
"6gow",
"6jy0"... | 75 | [
"PUB00002058",
"PUB00002080",
"PUB00002583",
"PUB00031736",
"PUB00099952",
"PUB00099953",
"PUB00099954",
"PUB00099955"
] | [
"3536885",
"2498283",
"2211662",
"12904785",
"29580106",
"29643437",
"34299141",
"28827825"
] | [
"Nucleotide sequence of the hag gene encoding flagellin of Escherichia coli.",
"Cloning of the flagellin gene from Bacillus subtilis and complementation studies of an in vitro-derived deletion mutation.",
"Structural and functional analysis of two Campylobacter jejuni flagellin genes.",
"Complete atomic model... | [
1986,
1989,
1990,
2003,
2018,
2018,
2021,
2017
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
42574,
62,
511,
1
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Flagellin, N-terminal domain | Flagellin, N-terminal domain | Flagellin_N | 1 |
IPR001030 | 1,030 | Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain | Acoase/IPM_deHydtase_lsu_aba | Domain | 86,602 | false | false | This entry represents a region containing 3 domains, each with a 3-layer α/β/α topology. This region represents the [4Fe-4S] cluster-binding region found at the N-terminal of eukaryotic mAcn, cAcn/IPR1 and IRP2, and bacterial AcnA, but in the C-terminal of bacterial AcnB. This domain is also found in the large subunit ... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS"
] | [
"PF00330",
"PR00415"
] | [
"Aconitase",
"ACONITASE"
] | [
86598,
74721
] | 2 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"4.2.1",
"4.2.1.33",
"PDOC00423",
"R-BTA-71403",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-389542",
"R-CEL-71403",
"R-CEL-917937",
"R-CEL-9837999",
"R-CEL-9854311",
"R-DDI-389542",
"R-DDI-71403",
"R-DDI-917937",
"R-DDI-9837999",
"R-DDI-9854311",
"R-HSA-1268020",
"R-HSA-389542",
"R... | [
"EC:4.2.1",
"EC:4.2.1.33",
"PROSITEDOC:PDOC00423",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-389542",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-917937",
"REACTOME:R-CEL-9837999",
"REACTOME:R-CEL-9854311",
"REACTOME:R-DDI-389542",
"REACTOME:R-DD... | 40 | [
"1aco",
"1ami",
"1amj",
"1b0j",
"1b0k",
"1b0m",
"1c96",
"1c97",
"1fgh",
"1l5j",
"1nis",
"1nit",
"2b3x",
"2b3y",
"3sn2",
"3snp",
"4kp1",
"4kp2",
"4nqy",
"5acn",
"6acn",
"6vcd",
"7acn",
"8acn"
] | 24 | [
"PUB00005471",
"PUB00016210",
"PUB00032014",
"PUB00033924",
"PUB00036012",
"PUB00036013",
"PUB00036014",
"PUB00036015",
"PUB00036016",
"PUB00036017",
"PUB00036018",
"PUB00036019",
"PUB00036021",
"PUB00036023",
"PUB00082326"
] | [
"9020582",
"9813279",
"15522288",
"1400210",
"16850017",
"10087914",
"15877277",
"17513696",
"15882410",
"15009904",
"17185597",
"16407072",
"15604397",
"16524361",
"20663849"
] | [
"The aconitase family: three structural variations on a common theme.",
"The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus.",
"Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specifici... | [
1997,
1998,
2004,
1992,
2006,
1999,
2005,
2007,
2005,
2004,
2006,
2006,
2004,
2006,
2010
] | 15 | [] | [
"IPR033941"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2136,
63577,
19374,
1515
] | 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",... | [
16,
2,
5,
11,
4,
29,
6,
4,
11,
15,
4,
5,
102
] | 13 | true | Domain | Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain | Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain | Acoase/IPM_deHydtase_lsu_aba | 5 |
IPR001031 | 1,031 | Thioesterase | Thioesterase | Domain | 53,053 | false | false | Thioesterase (TE) domains often occur integrated in or associated with peptide synthetases which are involved in the non-ribosomal synthesis of peptide antibiotics [ ]. Thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Next to the operons ... | [
"GO:0009058"
] | [
"biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00975"
] | [
"Thioesterase"
] | [
53053
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1",
"GenProp1220",
"R-HSA-163765",
"R-HSA-199220",
"R-HSA-2426168",
"R-HSA-75105",
"R-HSA-9029558",
"R-MMU-199220",
"R-MMU-75105",
"R-RNO-199220",
"R-RNO-75105"
] | [
"EC:2.3.1",
"GP:GenProp1220",
"REACTOME:R-HSA-163765",
"REACTOME:R-HSA-199220",
"REACTOME:R-HSA-2426168",
"REACTOME:R-HSA-75105",
"REACTOME:R-HSA-9029558",
"REACTOME:R-MMU-199220",
"REACTOME:R-MMU-75105",
"REACTOME:R-RNO-199220",
"REACTOME:R-RNO-75105"
] | 11 | [
"1jmk",
"1kez",
"1mn6",
"1mna",
"1mnq",
"1mo2",
"1xkt",
"2cb9",
"2cbg",
"2h7x",
"2h7y",
"2hfj",
"2hfk",
"2k2q",
"2px6",
"2ron",
"2roq",
"2vsq",
"2vz8",
"2vz9",
"3fla",
"3flb",
"3ils",
"3lcr",
"3qmv",
"3qmw",
"3tej",
"3tjm",
"4xjv",
"4z49",
"4zxh",
"4zxi"... | 114 | [
"PUB00000169",
"PUB00095142"
] | [
"9560421",
"23822773"
] | [
"Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis.",
"Thioesterase domains of fungal nonreducing polyketide synthases act as decision gates during combinatorial biosynthesis."
] | [
1998,
2013
] | 2 | [] | [
"IPR020802"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
42020,
10915,
2,
116
] | 4 | [
"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)",
"Rattus norvegicus"
] | [
3,
8,
11,
1,
6,
4,
1,
6
] | 8 | true | Domain | Thioesterase | Thioesterase | Thioesterase | 7 |
IPR001032 | 1,032 | Leghaemoglobin-like | Leghaemoglobin-like | Family | 1,546 | false | false | This entry includes plant proteins that bind oxygen through a penta- or hexa-coordinated heme iron and are required for general plant development and during nodulation. Members of this family are leghemoglobins that facilitates the diffusion of O2 to bacteroids in nodules [ , ]. Other members are non-symbiotic plant he... | [
"GO:0019825",
"GO:0020037"
] | [
"oxygen binding",
"heme binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PANTHER"
] | [
"PTHR22924"
] | [
""
] | [
1546
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00183"
] | [
"PROSITEDOC:PDOC00183"
] | 1 | [
"1bin",
"1d8u",
"1fsl",
"1gdi",
"1gdj",
"1gdk",
"1gdl",
"1lh1",
"1lh2",
"1lh3",
"1lh5",
"1lh6",
"1lh7",
"2gdm",
"2gnv",
"2gnw",
"2lh1",
"2lh2",
"2lh3",
"2lh5",
"2lh6",
"2lh7",
"2oif",
"2r50",
"3qqq",
"3qqr",
"3zhw",
"7z1u",
"7zos"
] | 29 | [
"PUB00004012",
"PUB00006066",
"PUB00016016",
"PUB00029465",
"PUB00035865",
"PUB00035866",
"PUB00035867",
"PUB00035868",
"PUB00035869",
"PUB00035870",
"PUB00035871",
"PUB00035872",
"PUB00035873",
"PUB00035877",
"PUB00035889",
"PUB00035890",
"PUB00035891",
"PUB00035892",
"PUB000358... | [
"2448639",
"1118009",
"15096613",
"12962627",
"16600051",
"17540514",
"11092893",
"11481493",
"15598488",
"16888280",
"15598493",
"15339940",
"15804833",
"17084861",
"15797009",
"12927972",
"11835502",
"6854938",
"16377734",
"17540516",
"17701548",
"21495624",
"15797021",... | [
"Functioning haemoglobin genes in non-nodulating plants.",
"Structure of leghaemoglobin from lupin root nodules at 5 angstrom resolution.",
"Ancestral hemoglobins in Archaea.",
"Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity.",
"A phylogenomic profile of globins.",
... | [
1988,
1975,
2004,
2003,
2006,
2007,
2001,
2001,
2005,
2006,
2005,
2004,
2004,
2007,
2005,
2003,
2002,
1983,
2006,
2007,
2007,
2011,
2005,
2020,
1997
] | 25 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1546
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
8,
7,
9
] | 3 | true | Family | Leghaemoglobin-like | Leghaemoglobin-like | Leghaemoglobin-like | 6 |
IPR001033 | 1,033 | Alpha-catenin | Alpha_catenin | Family | 7,782 | false | false | Catenins associate with the cytoplasmic domains of a variety of cadherins [ ] producing a complex that links to the actin filament network. This association appears to be indispensable for tight cell-cell adhesion. Dysfunction of the complex causes dissociation of cancer cells from primary tumours, possibly contributin... | [
"GO:0045296",
"GO:0051015",
"GO:0007155"
] | [
"cadherin binding",
"actin filament binding",
"cell adhesion"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS"
] | [
"PR00805"
] | [
"ALPHACATENIN"
] | [
7782
] | 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-CEL-5218920",
"R-CEL-9764561",
"R-DME-418990",
"R-DME-5218920",
"R-DME-525793",
"R-DME-9764561",
"R-DME-9766229",
"R-DRE-5218920",
"R-DRE-525793",
"R-DRE-5626467",
"R-DRE-9764561",
"R-HSA-418990",
"R-HSA-5218920",
"R-HSA-525793",
"R-HSA-5626467",
"R-HSA-9762292",
"R-HSA-9764302",
... | [
"REACTOME:R-CEL-5218920",
"REACTOME:R-CEL-9764561",
"REACTOME:R-DME-418990",
"REACTOME:R-DME-5218920",
"REACTOME:R-DME-525793",
"REACTOME:R-DME-9764561",
"REACTOME:R-DME-9766229",
"REACTOME:R-DRE-5218920",
"REACTOME:R-DRE-525793",
"REACTOME:R-DRE-5626467",
"REACTOME:R-DRE-9764561",
"REACTOME:R... | 27 | [
"1dov",
"1dow",
"1h6g",
"1l7c",
"4ehp",
"4igg",
"4k1n",
"4k1o",
"4ons",
"4p9t",
"5h5m",
"5xfl",
"6duw",
"6duy",
"6dv1",
"6o3e",
"6upv",
"6wvt",
"7utj",
"7uuw",
"9dva"
] | 21 | [
"PUB00000225",
"PUB00000237",
"PUB00004758",
"PUB00071468"
] | [
"8323564",
"7945318",
"1924379",
"23739176"
] | [
"Cloning of the human alpha-catenin cDNA and its aberrant mRNA in a human cancer cell line.",
"Molecular cloning reveals alternative splice forms of human alpha(E)-catenin.",
"The uvomorulin-anchorage protein alpha catenin is a vinculin homologue.",
"α-catenin, vinculin, and F-actin in strengthening E-cadheri... | [
1993,
1994,
1991,
2013
] | 4 | [
"IPR006077"
] | [
"IPR030045"
] | 1 | 1 | 0 | [
"Opisthokonta"
] | [
7782
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
10,
4,
32,
16,
21
] | 6 | true | Family | Alpha-catenin | Alpha-catenin | Alpha_catenin | 1 |
IPR001034 | 1,034 | DeoR-type HTH domain | DeoR_HTH | Domain | 101,300 | false | false | The deoR-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain ofvabout 50-60 amino acids present in transcription regulators of the deoR family, involved in sugar catabolism. This family of prokaryotic regulators is named after the Escherichia coli protein DeoR, a repressor of the deo operon, which encodes n... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF08220",
"PR00037",
"PS51000",
"SM00420"
] | [
"HTH_DeoR",
"HTHLACR",
"HTH_DEOR_2",
"HTH_DEOR"
] | [
74979,
59079,
95863,
74769
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00696"
] | [
"PROSITEDOC:PDOC00696"
] | 1 | [] | 0 | [
"PUB00004793",
"PUB00015413",
"PUB00067928"
] | [
"1731335",
"14731281",
"10714997"
] | [
"Opine catabolism and conjugal transfer of the nopaline Ti plasmid pTiC58 are coordinately regulated by a single repressor.",
"Application of AgaR repressor and dominant repressor variants for verification of a gene cluster involved in N-acetylgalactosamine metabolism in Escherichia coli K-12.",
"Purification a... | [
1992,
2004,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
323,
100518,
60,
12,
387
] | 5 | [
"Escherichia coli (strain K12)"
] | [
13
] | 1 | true | Domain | DeoR-type HTH domain | DeoR-type HTH domain | DeoR_HTH | 3 |
IPR001036 | 1,036 | Acriflavin resistance protein | Acrflvin-R | Family | 156,320 | false | false | The Escherichia coli acrA and acrB genes encode a multi-drug efflux system that is believed to protect the bacterium against hydrophobic inhibitors [ ]. The E. coli AcrB protein is a transporter that is energized by proton-motive force and that shows the widest substrate specificity among all known multidrug pumps, ran... | [
"GO:0022857",
"GO:0055085",
"GO:0016020"
] | [
"transmembrane transporter activity",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00873",
"PR00702",
"PTHR32063"
] | [
"ACR_tran",
"ACRIFLAVINRP",
""
] | [
146287,
148377,
145620
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-9638334",
"R-HSA-9760173",
"R-HSA-9913143",
"R-SCE-8963678",
"R-SCE-8964038"
] | [
"REACTOME:R-HSA-9638334",
"REACTOME:R-HSA-9760173",
"REACTOME:R-HSA-9913143",
"REACTOME:R-SCE-8963678",
"REACTOME:R-SCE-8964038"
] | 5 | [
"1iwg",
"1oy6",
"1oy8",
"1oy9",
"1oyd",
"1oye",
"1t9t",
"1t9u",
"1t9v",
"1t9w",
"1t9x",
"1t9y",
"2dhh",
"2dr6",
"2drd",
"2gif",
"2hqc",
"2hqd",
"2hqf",
"2hqg",
"2hrt",
"2i6w",
"2j8s",
"2rdd",
"2v50",
"2w1b",
"3aoa",
"3aob",
"3aoc",
"3aod",
"3d9b",
"3k07"... | 200 | [
"PUB00002229"
] | [
"8407802"
] | [
"Molecular cloning and characterization of acrA and acrE genes of Escherichia coli."
] | [
1993
] | 1 | [] | [
"IPR004763",
"IPR004764",
"IPR022831",
"IPR023931"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid pMCBF1",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
138,
152249,
1082,
1,
2,
2848
] | 6 | [
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
2,
7,
1
] | 3 | true | Family | Acriflavin resistance protein | Acriflavin resistance protein | Acrflvin-R | 2 |
IPR001038 | 1,038 | Glycoprotein C/glycoprotein A | GA_GC | Family | 725 | false | false | Equid herpesvirus 1 (Equine herpesvirus 1, EHV-1) glycoprotein 13 (EHV-1 gp13) has the characteristic features of a membrane-spanning protein: an N-terminal signal sequence; a hydrophobic membrane anchor region; a charged C-terminal cytoplasmic tail; and an exterior domain with nine potential N-glycosylation sites [ ].... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS"
] | [
"PF02124",
"PR00668"
] | [
"Marek_A",
"GLYCPROTEINC"
] | [
717,
673
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00003483",
"PUB00003484",
"PUB00005634"
] | [
"2836620",
"2455821",
"2543160"
] | [
"Structure and complete nucleotide sequence of the Marek's disease herpesvirus gp57-65 gene.",
"Characterization of an equine herpesvirus type 1 gene encoding a glycoprotein (gp13) with homology to herpes simplex virus glycoprotein C.",
"Nucleotide sequence of the Marek's disease virus (MDV) RB-1B A antigen gen... | [
1988,
1988,
1989
] | 3 | [] | [
"IPR001654"
] | 0 | 1 | 0 | [
"Alphaherpesvirinae",
"Oryzias latipes"
] | [
723,
2
] | 2 | [] | [] | 0 | true | Family | Glycoprotein C/glycoprotein A | Glycoprotein C/glycoprotein A | GA_GC | 4 |
IPR001039 | 1,039 | MHC class I alpha chain, alpha1 alpha2 domains | MHC_I_a_a1/a2 | Domain | 63,095 | false | false | This entry represents the alpha chain domains alpha1 and alpha2 that make up this recognition region (the alpha3 domain is represented by ( ). Major Histocompatibility Complex (MHC) glycoproteins are heterodimeric cell surface receptors that function to present antigen peptide fragments to T cells responsible for cell-... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR01638"
] | [
"MHCCLASSI"
] | [
63095
] | 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-HSA-1236974",
"R-HSA-1236977",
"R-HSA-164940",
"R-HSA-198933",
"R-HSA-2172127",
"R-HSA-2424491",
"R-HSA-5223345",
"R-HSA-6798695",
"R-HSA-877300",
"R-HSA-8866654",
"R-HSA-909733",
"R-HSA-917977",
"R-HSA-9705671",
"R-HSA-983170",
"R-MMU-1236974",
"R-MMU-1236977",
"R-MMU-198933",
... | [
"REACTOME:R-HSA-1236974",
"REACTOME:R-HSA-1236977",
"REACTOME:R-HSA-164940",
"REACTOME:R-HSA-198933",
"REACTOME:R-HSA-2172127",
"REACTOME:R-HSA-2424491",
"REACTOME:R-HSA-5223345",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-877300",
"REACTOME:R-HSA-8866654",
"REACTOME:R-HSA-909733",
"REACTOME:R-... | 24 | [
"1a1m",
"1a1n",
"1a1o",
"1a6z",
"1a9b",
"1a9e",
"1agb",
"1agc",
"1agd",
"1age",
"1agf",
"1akj",
"1ao7",
"1b0g",
"1b0r",
"1bd2",
"1bii",
"1bqh",
"1bz9",
"1c16",
"1ce6",
"1cg9",
"1ddh",
"1de4",
"1duy",
"1duz",
"1e27",
"1e28",
"1ed3",
"1eey",
"1eez",
"1efx"... | 1,515 | [
"PUB00007109",
"PUB00016272"
] | [
"9485452",
"15526153"
] | [
"Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding.",
"Evolutionary and functional perspectives of the major histocompatibility complex class I antigen-processing machinery."
] | [
1998,
2004
] | 2 | [
"IPR011161"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Bilateria",
"Viruses"
] | [
5,
63082,
8
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
28132,
313,
236
] | 4 | true | Domain | MHC class I alpha chain, alpha1 alpha2 domains | MHC class I alpha chain, alpha1 alpha2 domains | MHC_I_a_a1/a2 | 1 |
IPR001041 | 1,041 | 2Fe-2S ferredoxin-type iron-sulfur binding domain | 2Fe-2S_ferredoxin-type | Domain | 220,642 | false | false | Ferredoxins are small, acidic, electron transfer proteins that are ubiquitous in biological redox systems. They have either 4Fe-4S, 3Fe-4S, or 2Fe-2S cluster. Among them, ferredoxin with one 2Fe-2S cluster per molecule are present in plants, animals, and bacteria, and form a distinct Ferredoxin family [ ]. They are pro... | [
"GO:0051536"
] | [
"iron-sulfur cluster binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"CDD"
] | [
"PF00111",
"PS51085",
"cd00207"
] | [
"Fer2",
"2FE2S_FER_2",
"fer2"
] | [
158219,
210005,
188131
] | 3 | [
"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... | [
"GenProp1236",
"GenProp1255",
"GenProp1469",
"GenProp1753",
"PDOC00175",
"R-BTA-1362409",
"R-BTA-196108",
"R-BTA-211976",
"R-BTA-2395516",
"R-BTA-611105",
"R-BTA-6799198",
"R-BTA-9837999",
"R-BTA-9857492",
"R-CEL-71403",
"R-CEL-964975",
"R-DDI-6799198",
"R-DDI-71403",
"R-DDI-74259"... | [
"GP:GenProp1236",
"GP:GenProp1255",
"GP:GenProp1469",
"GP:GenProp1753",
"PROSITEDOC:PDOC00175",
"REACTOME:R-BTA-1362409",
"REACTOME:R-BTA-196108",
"REACTOME:R-BTA-211976",
"REACTOME:R-BTA-2395516",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9... | 92 | [
"1a70",
"1awd",
"1ayf",
"1b9r",
"1c4a",
"1c4c",
"1cje",
"1czp",
"1dgj",
"1doi",
"1dox",
"1doy",
"1e0z",
"1e10",
"1e6e",
"1e7p",
"1e9m",
"1ewy",
"1feh",
"1ffu",
"1ffv",
"1fiq",
"1fo4",
"1frd",
"1frr",
"1fxa",
"1fxi",
"1gaq",
"1gpx",
"1i7h",
"1iue",
"1j7a"... | 748 | [
"PUB00001617",
"PUB00017893"
] | [
"2065785",
"8586613"
] | [
"Divergent evolution of chloroplast-type ferredoxins.",
"Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis refined at 2.5 A resolution: structural comparisons of plant-type ferredoxins and an electrostatic potential analysis."
] | [
1991,
1995
] | 2 | [] | [
"IPR010241",
"IPR025192"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"plasmids",
"unclassified sequences"
] | [
3568,
180336,
57,
33765,
4,
2912
] | 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",... | [
77,
7,
13,
18,
11,
24,
34,
6,
51,
37,
2,
2,
137
] | 13 | true | Domain | 2Fe-2S ferredoxin-type iron-sulfur binding domain | 2Fe-2S ferredoxin-type iron-sulfur binding domain | 2Fe-2S_ferredoxin-type | 2 |
IPR001044 | 1,044 | XPG/Rad2 endonuclease, eukaryotes | XPG/Rad2_eukaryotes | Family | 4,114 | false | false | This entry represents XPG (ERCC-5, also known as Rad2 in budding yeast, AtRAD2 or UVH3 in Arabidopsis and Rad13 in fission yeast), a single-stranded structure-specific DNA endonuclease, which cleaves single-stranded DNA during nucleotide excision repair to excise damaged DNA [ ]. It makes the 3' incision in DNA nucleot... | [
"GO:0003697",
"GO:0004519",
"GO:0006289",
"GO:0005634"
] | [
"single-stranded DNA binding",
"endonuclease activity",
"nucleotide-excision repair",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS",
"NCBIFAM"
] | [
"PR00066",
"TIGR00600"
] | [
"XRODRMPGMNTG",
"rad2"
] | [
4113,
256
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5696395",
"R-HSA-5696400",
"R-HSA-6782135",
"R-MMU-5696395",
"R-MMU-5696400",
"R-MMU-6782135",
"R-SCE-6782135",
"R-SPO-5696395",
"R-SPO-5696400",
"R-SPO-6782135"
] | [
"REACTOME:R-HSA-5696395",
"REACTOME:R-HSA-5696400",
"REACTOME:R-HSA-6782135",
"REACTOME:R-MMU-5696395",
"REACTOME:R-MMU-5696400",
"REACTOME:R-MMU-6782135",
"REACTOME:R-SCE-6782135",
"REACTOME:R-SPO-5696395",
"REACTOME:R-SPO-5696400",
"REACTOME:R-SPO-6782135"
] | 10 | [
"4q0r",
"4q0w",
"4q0z",
"4q10",
"6tur",
"6tus",
"6tuw",
"6tux",
"6vbh"
] | 9 | [
"PUB00062819",
"PUB00062820",
"PUB00062833",
"PUB00062834",
"PUB00097845",
"PUB00097846",
"PUB00097847"
] | [
"22863773",
"7951246",
"8855246",
"12110180",
"32821917",
"32522879",
"26833090"
] | [
"Generation of DNA single-strand displacement by compromised nucleotide excision repair.",
"Mutations that disable the DNA repair gene XPG in a xeroderma pigmentosum group G patient.",
"Transcription factor TFIIH and DNA endonuclease Rad2 constitute yeast nucleotide excision repair factor 3: implications for nu... | [
2012,
1994,
1996,
2002,
2020,
2020,
2016
] | 7 | [
"IPR006084"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
4114
] | 1 | [
"Arabidopsis thaliana",
"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 (strain ATCC 204508 / S288c)",
"... | [
4,
2,
4,
10,
9,
1,
4,
2,
1,
1,
6
] | 11 | true | Family | XPG/Rad2 endonuclease, eukaryotes | XPG/Rad2 endonuclease, eukaryotes | XPG/Rad2_eukaryotes | 4 |
IPR001045 | 1,045 | Spermidine/spermine synthases | Spermi_synthase | Family | 22,565 | false | false | The nearly ubiquitous polyamines (putrescine, spermidine and spermine) are polycationic mediators of cell proliferation and differentiation whose functions likely provide both stability and neutralisation for nucleic acids. The following polyamine biosynthetic enzymes are evolutionary related [ ]: Spermidine synthase (... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_00198",
"PTHR11558",
"TIGR00417"
] | [
"Spermidine_synth",
"",
"speE"
] | [
21132,
14615,
12445
] | 3 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.5.1",
"2.5.1.16",
"GenProp0641",
"GenProp1433",
"GenProp1571",
"GenProp1596",
"PDOC01033",
"R-DDI-351202",
"R-HSA-351202",
"R-MMU-351202",
"R-SCE-351202",
"R-SPO-351202"
] | [
"EC:2.5.1",
"EC:2.5.1.16",
"GP:GenProp0641",
"GP:GenProp1433",
"GP:GenProp1571",
"GP:GenProp1596",
"PROSITEDOC:PDOC01033",
"REACTOME:R-DDI-351202",
"REACTOME:R-HSA-351202",
"REACTOME:R-MMU-351202",
"REACTOME:R-SCE-351202",
"REACTOME:R-SPO-351202"
] | 12 | [
"1inl",
"1iy9",
"1jq3",
"1mjf",
"1uir",
"1xj5",
"2b2c",
"2cmg",
"2cmh",
"2e5w",
"2hte",
"2i7c",
"2o05",
"2o06",
"2o07",
"2o0l",
"2pss",
"2pt6",
"2pt9",
"2pwp",
"2q41",
"2zsu",
"3anx",
"3b7p",
"3bwb",
"3bwc",
"3o4f",
"3rie",
"3rw9",
"4bp1",
"4bp3",
"4cwa"... | 64 | [
"PUB00004525",
"PUB00015422"
] | [
"9517003",
"11731804"
] | [
"Molecular cloning of plant spermidine synthases.",
"The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor."
] | [
1998,
2002
] | 2 | [] | [
"IPR015576",
"IPR025803",
"IPR030668"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
416,
13178,
8736,
5,
230
] | 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",... | [
18,
2,
2,
7,
1,
6,
5,
1,
10,
5,
2,
1,
45
] | 13 | true | Family | Spermidine/spermine synthases | Spermidine/spermine synthases | Spermi_synthase | 9 |
IPR001046 | 1,046 | NRAMP family | NRAMP_fam | Family | 41,325 | false | false | The natural resistance-associated macrophage protein (NRAMP) family consists of animal NRAMP1, NRAMP2 (DMT1), yeast proteins Smf1 and Smf2 and bacterial homologues such as divalent metal cation transporters (MntH) [ , , , , , , ]. The NRAMP family includes functional related proteins defined by a conserved hydrophobic ... | [
"GO:0046873",
"GO:0030001",
"GO:0016020"
] | [
"metal ion transmembrane transporter activity",
"metal ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"MF_00221",
"PF01566",
"PR00447",
"PTHR11706",
"TIGR01197"
] | [
"NRAMP",
"Nramp",
"NATRESASSCMP",
"",
"nramp"
] | [
16016,
41214,
25957,
38592,
20240
] | 5 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-1222556",
"R-CEL-425410",
"R-CEL-6798695",
"R-CEL-6803544",
"R-CEL-917937",
"R-DDI-1222556",
"R-DDI-425410",
"R-DDI-6798695",
"R-DDI-6803544",
"R-DDI-917937",
"R-DME-1222556",
"R-DME-425410",
"R-DME-6798695",
"R-DME-6803544",
"R-DME-917937",
"R-GGA-1222556",
"R-GGA-425410",
... | [
"REACTOME:R-CEL-1222556",
"REACTOME:R-CEL-425410",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-6803544",
"REACTOME:R-CEL-917937",
"REACTOME:R-DDI-1222556",
"REACTOME:R-DDI-425410",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-6803544",
"REACTOME:R-DDI-917937",
"REACTOME:R-DME-1222556",
"REACTOME:R-... | 40 | [
"5kte",
"5m87",
"5m8a",
"5m8j",
"5m8k",
"5m94",
"5m95",
"6c3i",
"6d91",
"6d9w",
"6tl2",
"7phq",
"7pij",
"7qia",
"7qic",
"7qji",
"7qjj",
"8e5s",
"8e5v",
"8e60",
"8e6h",
"8e6i",
"8e6l",
"8e6m",
"8e6n",
"8ont",
"9f6n",
"9f6o",
"9f6p",
"9f6q"
] | 30 | [
"PUB00002034",
"PUB00003001",
"PUB00004854",
"PUB00005530",
"PUB00101160",
"PUB00101161",
"PUB00101162",
"PUB00101163"
] | [
"9719491",
"9360964",
"7479731",
"8928221",
"25326704",
"30714568",
"28059071",
"24968120"
] | [
"Macrophage NRAMP1 and its role in resistance to microbial infections.",
"Functional complementation of the yeast divalent cation transporter family SMF by NRAMP2, a member of the mammalian natural resistance-associated macrophage protein family.",
"Nramp defines a family of membrane proteins.",
"Resistance t... | [
1998,
1997,
1995,
1996,
2014,
2019,
2017,
2014
] | 8 | [] | [
"IPR017187"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
746,
26581,
13636,
362
] | 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",... | [
33,
3,
2,
9,
1,
25,
5,
2,
34,
18,
3,
1,
97
] | 13 | true | Family | NRAMP family | NRAMP family | NRAMP_fam | 5 |
IPR001047 | 1,047 | Small ribosomal subunit protein eS8 | Ribosomal_eS8 | Family | 7,467 | false | false | This entry represents the small ribosomal subunit protein eS8 from archaea and eukaryotes [ , ], which consists of a number of proteins with either about 220 amino acids (in eukaryotes) or about 125 amino acids (in archaea). Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR10394",
"TIGR00307"
] | [
"",
"eS8"
] | [
7330,
6890
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00918",
"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-CEL-156827",
"R-CEL-1799339",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R... | [
"PROSITEDOC:PDOC00918",
"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",
"REACTOME:R-CEL-156827"... | 93 | [
"2kco",
"2kcp",
"2kcy",
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7a",
"3j7p",
"3j7r",
"3j80",
"3j81",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jam",
"3jan",
"3jap",
"3jbn",
"3jbo",
"3jbp",
"4bts",
"4d5l",
"4d61",
"4kzx",
"4kzy",
"4kzz",
"4u3m",
"4u3n",
"4u3u",
"4u4n"... | 629 | [
"PUB00003471",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00110894"
] | [
"7662106",
"11297922",
"11290319",
"11114498",
"23636399"
] | [
"Amino acid sequence of the ribosomal protein HS23 from the halophilic Haloarcula marismortui and homology studies to other ribosomal proteins.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Structures o... | [
1995,
2001,
2001,
2000,
2013
] | 5 | [
"IPR022309"
] | [
"IPR020919"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
888,
8,
6538,
33
] | 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... | [
6,
2,
2,
2,
5,
7,
1,
3,
7,
2,
2,
31
] | 12 | true | Family | Small ribosomal subunit protein eS8 | Small ribosomal subunit protein eS8 | Ribosomal_eS8 | 6 |
IPR001048 | 1,048 | Aspartate/glutamate/uridylate kinase | Asp/Glu/Uridylate_kinase | Domain | 152,384 | false | false | This entry contains proteins with various specificities and includes the aspartate, glutamate and uridylate kinase families. In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed-back inhibition of aspartate kinase (AK) and dihydrodipicolinate synth... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00696"
] | [
"AA_kinase"
] | [
152384
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.2",
"GenProp1358",
"GenProp1419",
"GenProp1475",
"GenProp1553",
"GenProp1581",
"R-CEL-8964539",
"R-CEL-9837999",
"R-DDI-70635",
"R-HSA-70635",
"R-HSA-8964539",
"R-HSA-9837999",
"R-MMU-8964539",
"R-MMU-9837999",
"R-SCE-70635",
"R-SPO-70635"
] | [
"EC:2.7.2",
"GP:GenProp1358",
"GP:GenProp1419",
"GP:GenProp1475",
"GP:GenProp1553",
"GP:GenProp1581",
"REACTOME:R-CEL-8964539",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-70635",
"REACTOME:R-HSA-70635",
"REACTOME:R-HSA-8964539",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-8964539",
"REACTOME:... | 16 | [
"1b7b",
"1e19",
"1gs5",
"1gsj",
"1oh9",
"1oha",
"1ohb",
"1ybd",
"1z9d",
"2a1f",
"2ako",
"2ap9",
"2bmu",
"2bnd",
"2bne",
"2bnf",
"2bri",
"2brx",
"2bty",
"2buf",
"2cdq",
"2e9y",
"2hmf",
"2ij9",
"2j0w",
"2j0x",
"2j4j",
"2j4k",
"2j4l",
"2j5t",
"2j5v",
"2ji5"... | 178 | [
"PUB00006409",
"PUB00006443",
"PUB00006598"
] | [
"9584993",
"10220897",
"9501134"
] | [
"Subunit structure of lysine sensitive aspartate kinase from spinach leaves.",
"Mutational analysis of the feedback sites of lysine-sensitive aspartokinase of Escherichia coli.",
"Expression of an arabidopsis aspartate Kinase/Homoserine dehydrogenase gene is metabolically regulated by photosynthesis-related sig... | [
1998,
1999,
1998
] | 3 | [] | [
"IPR033719",
"IPR035804",
"IPR041734",
"IPR041739",
"IPR041740",
"IPR041743",
"IPR041744",
"IPR041745",
"IPR041746",
"IPR041747",
"IPR041748"
] | 0 | 11 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4333,
125995,
19380,
5,
2671
] | 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",... | [
65,
1,
4,
1,
10,
4,
5,
3,
53,
2,
4,
3,
141
] | 13 | true | Domain | Aspartate/glutamate/uridylate kinase | Aspartate/glutamate/uridylate kinase | Asp/Glu/Uridylate_kinase | 7 |
IPR001050 | 1,050 | Syndecan | Syndecan | Family | 4,635 | false | false | The syndecans are multifunctional transmembrane heparan sulphate bearing cell surface receptors [ ]. There are four syndecans in mammals (syndecan1-4), but only one syndecan in C. elegans or D. melanogaster. These homologues have similar protein structure that consists of four separate domains: A signal sequence; An ex... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PANTHER"
] | [
"PTHR10915"
] | [
""
] | [
4635
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00745",
"R-BTA-1971475",
"R-BTA-2022928",
"R-BTA-2024096",
"R-BTA-202733",
"R-BTA-3000170",
"R-BTA-381426",
"R-BTA-3928662",
"R-BTA-449836",
"R-BTA-8957275",
"R-BTA-975634",
"R-CEL-1971475",
"R-CEL-2022928",
"R-CEL-2024096",
"R-CEL-3000170",
"R-CEL-381426",
"R-CEL-3928662",
"R... | [
"PROSITEDOC:PDOC00745",
"REACTOME:R-BTA-1971475",
"REACTOME:R-BTA-2022928",
"REACTOME:R-BTA-2024096",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-3000170",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-3928662",
"REACTOME:R-BTA-449836",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-975634",
"REACTOME:R-CE... | 73 | [
"1ejp",
"1ejq",
"6ith"
] | 3 | [
"PUB00072903",
"PUB00072904",
"PUB00072905",
"PUB00072906",
"PUB00072907"
] | [
"23559542",
"15886101",
"16176946",
"17097330",
"24237141"
] | [
"Novel insight into the biological functions of syndecan ectodomain core proteins.",
"The heparan sulfate proteoglycans Dally-like and Syndecan have distinct functions in axon guidance and visual-system assembly in Drosophila.",
"Syndecan regulates cell migration and axon guidance in C. elegans.",
"Syndecans ... | [
2013,
2005,
2005,
2007,
2013
] | 5 | [] | [] | 0 | 0 | null | [
"Eumetazoa",
"Kangiella spongicola"
] | [
4634,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
6,
7,
15,
10,
12
] | 6 | true | Family | Syndecan | Syndecan | Syndecan | 9 |
IPR001053 | 1,053 | CXC chemokine receptor 5 | Chemokine_CXCR5 | Family | 440 | false | false | Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang... | [
"GO:0016494",
"GO:0006935",
"GO:0006955",
"GO:0007186",
"GO:0042113",
"GO:0048535",
"GO:0016020"
] | [
"C-X-C chemokine receptor activity",
"chemotaxis",
"immune response",
"G protein-coupled receptor signaling pathway",
"B cell activation",
"lymph node development",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 7 | [
"PRINTS"
] | [
"PR00564"
] | [
"CXCCHMKINER5"
] | [
440
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"72",
"R-HSA-380108",
"R-HSA-418594",
"R-MMU-380108",
"R-MMU-418594",
"R-RNO-380108",
"R-RNO-418594"
] | [
"IUPHAR:72",
"REACTOME:R-HSA-380108",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-380108",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-380108",
"REACTOME:R-RNO-418594"
] | 7 | [] | 0 | [
"PUB00007112",
"PUB00009401",
"PUB00064589",
"PUB00064621",
"PUB00064622",
"PUB00064905",
"PUB00064906",
"PUB00064907",
"PUB00064908",
"PUB00064909",
"PUB00064910",
"PUB00064939",
"PUB00067945",
"PUB00067946"
] | [
"9463416",
"11544102",
"10714678",
"10601351",
"9500790",
"16214223",
"12171958",
"8978608",
"12851649",
"12732661",
"23281399",
"15969628",
"9689100",
"7592998"
] | [
"B cell-attracting chemokine 1, a human CXC chemokine expressed in lymphoid tissues, selectively attracts B lymphocytes via BLR1/CXCR5.",
"Chemokine receptors.",
"Chemokines: a new classification system and their role in immunity.",
"Macrophage inflammatory protein 3alpha is involved in the constitutive traff... | [
1998,
2001,
2000,
1999,
1998,
2005,
2002,
1996,
2003,
2003,
2013,
2005,
1998,
1995
] | 14 | [
"IPR000355"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
440
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
3,
3
] | 3 | true | Family | CXC chemokine receptor 5 | CXC chemokine receptor 5 | Chemokine_CXCR5 | 7 |
IPR001054 | 1,054 | Adenylyl cyclase class-3/4/guanylyl cyclase | A/G_cyclase | Domain | 109,848 | false | false | Guanylate cyclases ( ) catalyse the formation of cyclic GMP (cGMP) from GTP. cGMP acts as an intracellular messenger, activating cGMP-dependent kinases and regulating cGMP-sensitive ion channels. The role of cGMP as a second messenger in vascular smooth muscle relaxation and retinal photo-transduction is well establish... | [
"GO:0009190",
"GO:0035556"
] | [
"cyclic nucleotide biosynthetic process",
"intracellular signal transduction"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00211",
"PS50125",
"SM00044",
"cd07302"
] | [
"Guanylate_cyc",
"GUANYLATE_CYCLASE_2",
"CYCc",
"CHD"
] | [
105015,
108172,
91460,
102929
] | 4 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"4.6.1",
"PDOC00425",
"R-BTA-163615",
"R-BTA-170660",
"R-BTA-170670",
"R-BTA-418597",
"R-BTA-445355",
"R-BTA-5578768",
"R-BTA-5610787",
"R-CEL-2514859",
"R-CFA-445355",
"R-DDI-163615",
"R-DDI-170660",
"R-DDI-170670",
"R-DDI-2514859",
"R-DDI-418597",
"R-DDI-5610787",
"R-DME-163615",... | [
"EC:4.6.1",
"PROSITEDOC:PDOC00425",
"REACTOME:R-BTA-163615",
"REACTOME:R-BTA-170660",
"REACTOME:R-BTA-170670",
"REACTOME:R-BTA-418597",
"REACTOME:R-BTA-445355",
"REACTOME:R-BTA-5578768",
"REACTOME:R-BTA-5610787",
"REACTOME:R-CEL-2514859",
"REACTOME:R-CFA-445355",
"REACTOME:R-DDI-163615",
"RE... | 71 | [
"1ab8",
"1azs",
"1cjk",
"1cjt",
"1cju",
"1cjv",
"1cs4",
"1cul",
"1fx2",
"1fx4",
"1tl7",
"1u0h",
"1wc0",
"1wc1",
"1wc3",
"1wc4",
"1wc5",
"1wc6",
"1y10",
"1y11",
"1ybt",
"1ybu",
"1yk9",
"2bw7",
"2gvd",
"2gvz",
"2w01",
"2wz1",
"3c14",
"3c15",
"3c16",
"3et6"... | 167 | [
"PUB00000129",
"PUB00000877",
"PUB00001511",
"PUB00004322",
"PUB00100705"
] | [
"1349465",
"1356629",
"1680765",
"1982420",
"34644530"
] | [
"Guanylyl cyclase-linked receptors.",
"Guanylyl cyclase receptors and their endocrine, paracrine, and autocrine ligands.",
"Guanylyl cyclases, a growing family of signal-transducing enzymes.",
"The guanylyl cyclase receptor family.",
"Cyclic CMP and cyclic UMP mediate bacterial immunity against phages."
] | [
1992,
1992,
1991,
1990,
2021
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
205,
48905,
59748,
89,
901
] | 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)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizo... | [
1,
50,
162,
73,
89,
67,
2,
101,
1,
1
] | 10 | true | Domain | Adenylyl cyclase class-3/4/guanylyl cyclase | Adenylyl cyclase class-3/4/guanylyl cyclase | A/G_cyclase | 9 |
IPR001055 | 1,055 | Adrenodoxin-like | Adrenodoxin-like | Family | 24,405 | false | false | Adrenodoxin, putidaredoxin, rhodocoxin and terpredoxin are soluble 2Fe-2S iron-sulphur proteins that act as single electron carriers. They are a subgroup of the ferredoxin family of iron-sulphur proteins. In mitochondrial monooxygenase systems, adrenodoxin transfers an electron from NADPH:adrenodoxin reductase to membr... | [
"GO:0051537",
"GO:0140647"
] | [
"2 iron, 2 sulfur cluster binding",
"P450-containing electron transport chain"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS",
"PANTHER"
] | [
"PR00355",
"PTHR23426"
] | [
"ADRENODOXIN",
""
] | [
18543,
24249
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00642",
"R-BTA-1362409",
"R-BTA-196108",
"R-BTA-211976",
"R-BTA-2395516",
"R-BTA-9857492",
"R-DME-1362409",
"R-DME-2395516",
"R-DME-9857492",
"R-DRE-1362409",
"R-DRE-196108",
"R-DRE-211976",
"R-DRE-2395516",
"R-HSA-1362409",
"R-HSA-196108",
"R-HSA-211976",
"R-HSA-2395516",
"R-... | [
"PROSITEDOC:PDOC00642",
"REACTOME:R-BTA-1362409",
"REACTOME:R-BTA-196108",
"REACTOME:R-BTA-211976",
"REACTOME:R-BTA-2395516",
"REACTOME:R-BTA-9857492",
"REACTOME:R-DME-1362409",
"REACTOME:R-DME-2395516",
"REACTOME:R-DME-9857492",
"REACTOME:R-DRE-1362409",
"REACTOME:R-DRE-196108",
"REACTOME:R-D... | 37 | [
"1ayf",
"1b9r",
"1cje",
"1e6e",
"1e9m",
"1gpx",
"1i7h",
"1l6u",
"1l6v",
"1oqq",
"1oqr",
"1pdx",
"1put",
"1r7s",
"1uwm",
"1xln",
"1xlo",
"1xlp",
"1xlq",
"1yji",
"1yjj",
"2bt6",
"2jqr",
"2m56",
"2mj3",
"2mjd",
"2mje",
"2wlb",
"2y5c",
"3ah7",
"3hui",
"3lb8"... | 68 | [
"PUB00002613",
"PUB00002723",
"PUB00016350",
"PUB00097471"
] | [
"2180940",
"1629218",
"12069587",
"22556163"
] | [
"Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins.",
"Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon.",
"A new electron transport mechanism in mitochondrial steroid hydroxylase system... | [
1990,
1992,
2002,
2012
] | 4 | [] | [
"IPR011536"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5,
15279,
8940,
181
] | 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",... | [
17,
1,
7,
4,
1,
4,
8,
1,
13,
8,
1,
1,
39
] | 13 | true | Family | Adrenodoxin-like | Adrenodoxin-like | Adrenodoxin-like | 4 |
IPR001056 | 1,056 | Photosystem II reaction centre protein H | PSII_PsbH | Family | 15,148 | 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:0042301",
"GO:0015979",
"GO:0050821",
"GO:0009523",
"GO:0016020"
] | [
"phosphate ion binding",
"photosynthesis",
"protein stabilization",
"photosystem II",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component",
"cellular_component"
] | 5 | [
"HAMAP",
"NCBIFAM",
"PFAM",
"PANTHER"
] | [
"MF_00752",
"NF002728",
"PF00737",
"PTHR34469"
] | [
"PSII_PsbH",
"PRK02624.1",
"PsbH",
""
] | [
13979,
14167,
14850,
15017
] | 4 | [
"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"... | 163 | [
"PUB00015357",
"PUB00015358",
"PUB00015359",
"PUB00015365",
"PUB00097583",
"PUB00152828",
"PUB00159457",
"PUB00159458",
"PUB00159459"
] | [
"12518057",
"15100025",
"14871485",
"12909614",
"30076221",
"33846594",
"26164101",
"2106663",
"15970599"
] | [
"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.",
"Role of the PSII-H subunit in photop... | [
2003,
2004,
2004,
2003,
2018,
2021,
2015,
1990,
2005
] | 9 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
396,
14751,
1
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
5,
2
] | 3 | true | Family | Photosystem II reaction centre protein H | Photosystem II reaction centre protein H | PSII_PsbH | 4 |
IPR001057 | 1,057 | Glutamate/acetylglutamate kinase | Glu/AcGlu_kinase | Family | 46,844 | false | false | Glutamate 5-kinase ( ) catalyses the first step in the biosynthesis of proline, the ATP-dependent phosphorylation of glutamate to glutamate 5-phosphate [ , ]. This entry also includes N-acetylglutamate kinase ( ), which catalyses the phosphorylation of N-acetylglutamate to N-acetylglutamate-5P in the pathway for argini... | [
"GO:0005524",
"GO:0016301"
] | [
"ATP binding",
"kinase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PRINTS"
] | [
"PR00474"
] | [
"GLU5KINASE"
] | [
46844
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.2",
"PDOC00701",
"R-CEL-8964539",
"R-CEL-9837999",
"R-HSA-8964539",
"R-HSA-9837999",
"R-MMU-8964539",
"R-MMU-9837999"
] | [
"EC:2.7.2",
"PROSITEDOC:PDOC00701",
"REACTOME:R-CEL-8964539",
"REACTOME:R-CEL-9837999",
"REACTOME:R-HSA-8964539",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-8964539",
"REACTOME:R-MMU-9837999"
] | 8 | [
"2ako",
"2bty",
"2buf",
"2j5t",
"2j5v",
"2jj4",
"2rd5",
"2v5h",
"2w21",
"3k4o",
"3k4y",
"3k52",
"3k56",
"3l86",
"3u6u",
"3wwm",
"3wwn",
"4q1t",
"4usj",
"7f5t",
"7f5u",
"7f5v",
"7f5x",
"7lnt",
"7lnu",
"7lnv",
"7lnw",
"7lnx",
"7n9d",
"7wx3",
"7wx4",
"7wxf"... | 44 | [
"PUB00002185",
"PUB00002254"
] | [
"1350780",
"8083159"
] | [
"Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase.",
"Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis."
] | [
1992,
1994
] | 2 | [] | [
"IPR005715"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Hyperionvirus sp.",
"unclassified sequences"
] | [
872,
37272,
7793,
1,
906
] | 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",... | [
15,
1,
4,
1,
1,
1,
5,
1,
10,
2,
2,
1,
35
] | 13 | true | Family | Glutamate/acetylglutamate kinase | Glutamate/acetylglutamate kinase | Glu/AcGlu_kinase | 4 |
IPR001058 | 1,058 | Synuclein | Synuclein | Family | 3,466 | false | false | Synucleins are small, soluble proteins expressed primarily in neural tissue and in certain tumours [ , ]. The family includes three known proteins: alpha-synuclein, beta-synuclein, and gamma-synuclein. All synucleins have in common a highly conserved α-helical lipid-binding motif with similarity to the class-A2 lipid-b... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF01387",
"PR01211",
"PTHR13820"
] | [
"Synuclein",
"SYNUCLEIN",
""
] | [
3433,
3312,
3374
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-9833482",
"R-HSA-5660489",
"R-HSA-977225",
"R-HSA-9833482",
"R-MMU-9833482",
"R-RNO-9833482",
"R-SSC-9833482"
] | [
"REACTOME:R-BTA-9833482",
"REACTOME:R-HSA-5660489",
"REACTOME:R-HSA-977225",
"REACTOME:R-HSA-9833482",
"REACTOME:R-MMU-9833482",
"REACTOME:R-RNO-9833482",
"REACTOME:R-SSC-9833482"
] | 7 | [
"1xq8",
"2kkw",
"2m55",
"2n0a",
"3q25",
"3q26",
"3q27",
"3q29",
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"6l1u",
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"6rtb",
"6sst",
"6ssx",
"6ufr",
"6xyo",
"6xyp",
"6xyq",
"7c1d",
"7e0f"... | 187 | [
"PUB00001947",
"PUB00007113",
"PUB00007114",
"PUB00007115",
"PUB00007116",
"PUB00007117",
"PUB00007118"
] | [
"9750188",
"11806835",
"10952980",
"7857654",
"7877458",
"9044857",
"11433374"
] | [
"The synuclein family.",
"The synucleins.",
"Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis.",
"The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central ne... | [
1998,
2002,
2000,
1995,
1994,
1997,
2001
] | 7 | [] | [
"IPR002460",
"IPR002461",
"IPR002462"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota"
] | [
40,
3426
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
18,
4,
19
] | 4 | true | Family | Synuclein | Synuclein | Synuclein | 5 |
IPR001059 | 1,059 | Translation elongation factor P/YeiP, central | Transl_elong_P/YeiP_cen | Domain | 29,457 | false | false | Elongation factor P (EF-P) is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet [ , ]. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF... | [
"GO:0003746",
"GO:0006414"
] | [
"translation elongation factor activity",
"translational elongation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART",
"CDD"
] | [
"PF01132",
"SM01185",
"cd04470"
] | [
"EFP",
"EFP",
"S1_EF-P_repeat_1"
] | [
29407,
29320,
27046
] | 3 | [] | [] | [] | 0 | [
"1ueb",
"1yby",
"3a5z",
"3oyy",
"3tre",
"4v6a",
"5j3b",
"6enj",
"6enu",
"6j7m",
"6rji",
"6rk3",
"6s8z",
"8s8u",
"8vwq",
"8w2n"
] | 16 | [
"PUB00000702",
"PUB00015919",
"PUB00081045"
] | [
"9195040",
"15210970",
"9405429"
] | [
"Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction.",
"Crystal structure of elongation factor P from Thermus thermophilus HB8.",
"The gene encoding the elongation factor P protein is essential for viability and is required for protein synthesis."
] | [
1997,
2004,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences",
"uncultured crenarchaeote MCG"
] | [
27123,
1740,
1,
592,
1
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
10,
2,
9,
8
] | 4 | true | Domain | Translation elongation factor P/YeiP, central | Translation elongation factor P/YeiP, central | Transl_elong_P/YeiP_cen | 4 |
IPR001060 | 1,060 | FCH domain | FCH_dom | Domain | 45,831 | false | false | FCH domain is a short conserved region of around 60 amino acids first described as a region of homology between FER and CIP4 proteins [ ]. In the CIP4 protein the FCH domain binds to microtubules [ ]. The FCH domain is always found N-terminally and is followed by a coiled-coil region. The FCH and coiled-coil domains ar... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00611",
"SM00055"
] | [
"FCH",
"FCH"
] | [
40202,
43021
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50133",
"R-BTA-8856828",
"R-CEL-8856828",
"R-CEL-9013406",
"R-DDI-8856828",
"R-DDI-9013148",
"R-DDI-9013149",
"R-DDI-9013404",
"R-DDI-9013423",
"R-DME-399954",
"R-DME-399956",
"R-DRE-5663220",
"R-DRE-9013148",
"R-DRE-9013149",
"R-DRE-9013406",
"R-DRE-9013420",
"R-DRE-9013423",
... | [
"PROSITEDOC:PDOC50133",
"REACTOME:R-BTA-8856828",
"REACTOME:R-CEL-8856828",
"REACTOME:R-CEL-9013406",
"REACTOME:R-DDI-8856828",
"REACTOME:R-DDI-9013148",
"REACTOME:R-DDI-9013149",
"REACTOME:R-DDI-9013404",
"REACTOME:R-DDI-9013423",
"REACTOME:R-DME-399954",
"REACTOME:R-DME-399956",
"REACTOME:R-... | 81 | [
"2efk",
"2efl",
"2v0o",
"2x3v",
"2x3w",
"2x3x",
"3abh",
"3aco",
"3hah",
"3hai",
"3haj",
"3i2w",
"3lll",
"3m3w",
"3q0k",
"3q84",
"3qe6",
"3qni",
"3syv",
"4bne",
"4dyl",
"4wpc",
"4wpe",
"5c1f",
"5i6j",
"5i6r",
"5i7d",
"6ikn",
"6iko",
"6xj1",
"7aal",
"7aam"... | 34 | [
"PUB00001037",
"PUB00018146",
"PUB00018147",
"PUB00068608"
] | [
"9210375",
"10713100",
"11994747",
"18525024"
] | [
"A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton.",
"Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules.",
"Closing in on the biological functions of Fps/Fes and Fer.",
"F-BAR domai... | [
1997,
2000,
2002,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Orthoretrovirinae"
] | [
45821,
10
] | 2 | [
"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... | [
12,
179,
28,
135,
97,
5,
104,
4,
6
] | 9 | true | Domain | FCH domain | FCH domain | FCH_dom | 3 |
IPR001062 | 1,062 | Transcription antitermination protein, NusG | Transcrpt_antiterm_NusG | Family | 24,486 | false | false | Bacterial transcription antitermination protein, NusG, is a component of the transcription complex and interacts with the termination factor Rho and RNA polymerase [ , ]. NusG is a bacterial transcriptional elongation factor involved in transcription termination and antitermination [ , ]. | [
"GO:0032784"
] | [
"regulation of DNA-templated transcription elongation"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"PRINTS",
"NCBIFAM"
] | [
"MF_00948",
"PR00338",
"TIGR00922"
] | [
"NusG",
"NUSGTNSCPFCT",
"nusG"
] | [
23881,
24245,
23759
] | 3 | [
"GP"
] | [
"GenProp0132"
] | [
"GP:GenProp0132"
] | 1 | [
"1m1g",
"1m1h",
"1npp",
"1npr",
"1nz9",
"2jvv",
"2kvq",
"2lq8",
"2mi6",
"2xhc",
"5ms0",
"5tbz",
"6c6u",
"6duq",
"6gov",
"6tqn",
"6tqo",
"6vu3",
"6vyq",
"6vyr",
"6vys",
"6vyt",
"6vyu",
"6vyw",
"6vyx",
"6vyy",
"6vyz",
"6vz2",
"6vz5",
"6x6t",
"6x7f",
"6x7k"... | 98 | [
"PUB00001884",
"PUB00001911",
"PUB00002759",
"PUB00100966"
] | [
"7505669",
"8422985",
"1532577",
"33488562"
] | [
"NusG alters rho-dependent termination of transcription in vitro independent of kinetic coupling.",
"Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription.",
"NusG, a new Escherichia coli elongation factor involved in transcriptional antitermin... | [
1993,
1993,
1992,
2020
] | 4 | [
"IPR043425"
] | [
"IPR010216"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2,
23924,
83,
2,
475
] | 5 | [
"Escherichia coli (strain K12)",
"Zea mays"
] | [
1,
2
] | 2 | true | Family | Transcription antitermination protein, NusG | Transcription antitermination protein, NusG | Transcrpt_antiterm_NusG | 9 |
IPR001063 | 1,063 | Large ribosomal subunit protein uL22 | Ribosomal_uL22 | Family | 50,029 | false | false | Large ribosomal subunit protein uL22 (also known as L22 in bacteria and previously known as L17 in eukaryotes) is a core protein of the large ribosomal subunit [ ]. It is the only ribosomal protein that interacts with all six domains of 23S rRNA, and is one of the proteins important for directing the proper folding and... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"CDD"
] | [
"PF00237",
"cd00336"
] | [
"Ribosomal_L22",
"Ribosomal_L22"
] | [
50023,
45851
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00387",
"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-17993... | [
"PROSITEDOC:PDOC00387",
"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-17... | 74 | [
"1bxe",
"1ffk",
"1i4j",
"1j5a",
"1jj2",
"1jzx",
"1jzy",
"1jzz",
"1k01",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1ond",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1"... | 1,965 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00025895",
"PUB00028498",
"PUB00080279"
] | [
"11297922",
"11290319",
"11114498",
"12225755",
"10937989",
"24524803"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin.",
"The complete atomic structure of the large ribosomal subunit at 2.... | [
2001,
2001,
2000,
2002,
2000,
2014
] | 6 | [] | [
"IPR005721",
"IPR047867"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
926,
24008,
24621,
474
] | 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,
2,
2,
3,
1,
18,
7,
2,
11,
18,
3,
3,
39
] | 13 | true | Family | Large ribosomal subunit protein uL22 | Large ribosomal subunit protein uL22 | Ribosomal_uL22 | 9 |
IPR001064 | 1,064 | Beta/gamma crystallin | Beta/gamma_crystallin | Domain | 23,934 | false | false | The crystallins are water-soluble structural proteins that occur in high concentration in the cytoplasm of eye lens fibre cells. Four major groups of crystallin have been distinguished on the basis of size, charge and immunological properties: alpha-, beta- and gamma-crystallins occur in all vertebrate classes (though ... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00030",
"PR01367",
"PS50915",
"SM00247"
] | [
"Crystall",
"BGCRYSTALLIN",
"CRYSTALLIN_BETA_GAMMA",
"XTALbg"
] | [
22487,
18774,
23021,
23160
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00197"
] | [
"PROSITEDOC:PDOC00197"
] | 1 | [
"1a45",
"1a5d",
"1a7h",
"1ag4",
"1amm",
"1bd7",
"1blb",
"1dsl",
"1e7n",
"1elp",
"1gam",
"1gcs",
"1h4a",
"1ha4",
"1hdf",
"1hk0",
"1i5i",
"1m8u",
"1nps",
"1oki",
"1prr",
"1prs",
"1ytq",
"1zgt",
"1zie",
"1ziq",
"1zir",
"1zwm",
"1zwo",
"2a5m",
"2bb2",
"2bv2"... | 93 | [
"PUB00003409",
"PUB00003917",
"PUB00004933",
"PUB00005345"
] | [
"2107329",
"7634077",
"3064189",
"2688200"
] | [
"Evolution of a protein superfamily: relationships between vertebrate lens crystallins and microorganism dormancy proteins.",
"The structure of avian eye lens delta-crystallin reveals a new fold for a superfamily of oligomeric enzymes.",
"The evolution of lenticular proteins: the beta- and gamma-crystallin supe... | [
1990,
1994,
1988,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
6,
1935,
21965,
5,
23
] | 5 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
89,
50,
47,
52
] | 4 | true | Domain | Beta/gamma crystallin | Beta/gamma crystallin | Beta/gamma_crystallin | 5 |
IPR001065 | 1,065 | Muscarinic acetylcholine receptor M2 | Musac_Ach_M2_rcpt | Family | 817 | false | false | Muscarinic acetylcholine receptors are members of rhodopsin-like G-protein coupled receptor family. They play several important roles; they mediate many of the effects of acetylcholine in the central and peripheral nervous system and modulate a variety of physiological functions, such as airway, eye and intestinal smoo... | [
"GO:0016907",
"GO:0007186",
"GO:0008016",
"GO:0016020"
] | [
"G protein-coupled acetylcholine receptor activity",
"G protein-coupled receptor signaling pathway",
"regulation of heart contraction",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00539"
] | [
"MUSCRINICM2R"
] | [
817
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"14",
"R-BTA-390648",
"R-BTA-418594",
"R-BTA-8856825",
"R-BTA-8856828",
"R-GGA-390648",
"R-GGA-418594",
"R-HSA-390648",
"R-HSA-418594",
"R-HSA-8856825",
"R-HSA-8856828",
"R-MMU-390648",
"R-MMU-418594",
"R-MMU-8856825",
"R-MMU-8856828",
"R-RNO-390648",
"R-RNO-418594",
"R-RNO-8856825... | [
"IUPHAR:14",
"REACTOME:R-BTA-390648",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-GGA-390648",
"REACTOME:R-GGA-418594",
"REACTOME:R-HSA-390648",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-MMU-390648",
... | 23 | [
"6u1n"
] | 1 | [
"PUB00064316",
"PUB00064317",
"PUB00064318",
"PUB00064319",
"PUB00064320",
"PUB00064321",
"PUB00064322",
"PUB00064323",
"PUB00064324",
"PUB00064325",
"PUB00064326",
"PUB00064327",
"PUB00064336",
"PUB00064337",
"PUB00064340",
"PUB00064341",
"PUB00064342",
"PUB00064343",
"PUB000643... | [
"3443095",
"3272174",
"3037705",
"9647869",
"2470172",
"8853955",
"10841527",
"14641022",
"12725869",
"17762886",
"15850824",
"3753655",
"14744253",
"15474550",
"7504306",
"10581327",
"8981565",
"11714883",
"9990086"
] | [
"Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors.",
"Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes.",
"Identification of a family of muscarinic acetylcholine receptor genes.",
"Inter... | [
1987,
1988,
1987,
1998,
1989,
1996,
2000,
2003,
2003,
2007,
2005,
1986,
2004,
2004,
1993,
1999,
1996,
2001,
1999
] | 19 | [
"IPR000995"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
817
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
1,
3
] | 4 | true | Family | Muscarinic acetylcholine receptor M2 | Muscarinic acetylcholine receptor M2 | Musac_Ach_M2_rcpt | 6 |
IPR001067 | 1,067 | Nuclear translocator | Nuc_translocat | Family | 16,704 | false | false | null | [
"GO:0003700",
"GO:0006355",
"GO:0005634",
"GO:0005667",
"GO:0005737"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription",
"nucleus",
"transcription regulator complex",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00785"
] | [
"NCTRNSLOCATR"
] | [
16704
] | 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-CEL-1234158",
"R-CEL-9768919",
"R-DME-1234158",
"R-DME-211945",
"R-DME-432395",
"R-DME-432408",
"R-DME-432501",
"R-DME-432524",
"R-DME-432560",
"R-DME-432620",
"R-DME-432626",
"R-DME-8937144",
"R-DME-9768919",
"R-DRE-211945",
"R-DRE-211976",
"R-DRE-211981",
"R-DRE-8937144",
"R-D... | [
"REACTOME:R-CEL-1234158",
"REACTOME:R-CEL-9768919",
"REACTOME:R-DME-1234158",
"REACTOME:R-DME-211945",
"REACTOME:R-DME-432395",
"REACTOME:R-DME-432408",
"REACTOME:R-DME-432501",
"REACTOME:R-DME-432524",
"REACTOME:R-DME-432560",
"REACTOME:R-DME-432620",
"REACTOME:R-DME-432626",
"REACTOME:R-DME-... | 57 | [
"4f3l",
"4h10",
"4zp4",
"4zph",
"4zpk",
"4zpr",
"4zqd",
"5nj8",
"5sy5",
"5sy7",
"5v0l",
"5y7y",
"6e3s",
"6e3t",
"6e3u",
"7v7l",
"7v7w",
"7w80",
"7xhv",
"7xi3",
"7xi4",
"8osj",
"8osk",
"8osl",
"8vhg",
"8xs6",
"8xs7",
"8xs8",
"8xs9",
"8xsa",
"8xsb",
"9ljx"... | 38 | [
"PUB00003697",
"PUB00005150"
] | [
"8065341",
"1317062"
] | [
"Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT).",
"Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor."
] | [
1994,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
16704
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
61,
8,
40,
39,
46
] | 6 | true | Family | Nuclear translocator | Nuclear translocator | Nuc_translocat | 4 |
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