interpro_id
string
interpro_numeric_id
int64
name
string
short_name
string
entry_type
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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
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int64
publication_ids
list
pubmed_ids
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publication_titles
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list
publication_count
int64
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child_count
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list
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list
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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
IPR001463
1,463
Sodium:alanine symporter
Na/Ala_symport
Family
27,527
false
false
Sodium symporters can be divided by sequence and functional similarity into various groups. One such group is the sodium/alanine symporter family, the members of which transport alanine in association with sodium ions. These transporters have between 10-14 transmembrane (TM) helices [ , , ], characterised by a five or ...
[ "GO:0005283", "GO:0006814", "GO:0006865", "GO:0016020" ]
[ "amino acid:sodium symporter activity", "sodium ion transport", "amino acid transport", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PFAM", "PRINTS", "PROSITE", "PANTHER", "NCBIFAM" ]
[ "PF01235", "PR00175", "PS00873", "PTHR30330", "TIGR00835" ]
[ "Na_Ala_symp", "NAALASMPORT", "NA_ALANINE_SYMP", "", "agcS" ]
[ 27189, 26797, 15997, 27022, 25928 ]
5
[ "PROSITEDOC" ]
[ "PDOC00681" ]
[ "PROSITEDOC:PDOC00681" ]
1
[ "6cse", "6csf" ]
2
[ "PUB00002744", "PUB00003824", "PUB00100661" ]
[ "1400476", "1447975", "30659158" ]
[ "Primary structure of the alanine carrier protein of thermophilic bacterium PS3.", "Identification and sequence of a Na(+)-linked gene from the marine bacterium Alteromonas haloplanktis which functionally complements the dagA gene of Escherichia coli.", "Structural basis for substrate binding and specificity of...
[ 1992, 1992, 2019 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 129, 26799, 188, 2, 409 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Sodium:alanine symporter
Sodium:alanine symporter
Na/Ala_symport
9
IPR001464
1,464
Annexin
Annexin
Family
28,116
false
false
The annexins (or lipocortins) are a family of proteins that bind to phospholipids in a calcium-dependent manner [ ]. The 12 annexins common to vertebrates are classified in the annexin A family and named as annexins A1-A13 (or ANXA1-ANXA13), leaving A12 unassigned in the official nomenclature. Annexins outside vertebra...
[ "GO:0005509", "GO:0005544" ]
[ "calcium ion binding", "calcium-dependent phospholipid binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS" ]
[ "PR00196" ]
[ "ANNEXIN" ]
[ 28116 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00195", "R-BTA-6798695", "R-BTA-75205", "R-BTA-9860927", "R-CFA-6798695", "R-CFA-75205", "R-CFA-9860927", "R-DDI-114608", "R-DDI-6798695", "R-DME-114608", "R-DME-6798695", "R-DME-9860927", "R-GGA-114608", "R-GGA-6798695", "R-GGA-75205", "R-GGA-9860927", "R-HSA-114608", "R-HSA-...
[ "PROSITEDOC:PDOC00195", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-75205", "REACTOME:R-BTA-9860927", "REACTOME:R-CFA-6798695", "REACTOME:R-CFA-75205", "REACTOME:R-CFA-9860927", "REACTOME:R-DDI-114608", "REACTOME:R-DDI-6798695", "REACTOME:R-DME-114608", "REACTOME:R-DME-6798695", "REACTOME:R-DME-...
41
[ "1a8a", "1a8b", "1aei", "1aii", "1ain", "1ala", "1ann", "1anw", "1anx", "1aow", "1avc", "1avh", "1avr", "1axn", "1bc0", "1bc1", "1bc3", "1bcw", "1bcy", "1bcz", "1bo9", "1dk5", "1dm5", "1g5n", "1hak", "1hm6", "1hvd", "1hve", "1hvf", "1hvg", "1i4a", "1m9i"...
114
[ "PUB00001395", "PUB00013921", "PUB00015121" ]
[ "1646719", "9797403", "15059252" ]
[ "Amino acid sequence analysis of the annexin super-gene family of proteins.", "Identification of the first fungal annexin: analysis of annexin gene duplications and implications for eukaryotic evolution.", "The annexins." ]
[ 1991, 1998, 2004 ]
3
[]
[ "IPR002388", "IPR002389", "IPR002390", "IPR002391", "IPR002392", "IPR002393", "IPR008156", "IPR008157", "IPR009115", "IPR009116", "IPR009117", "IPR009118", "IPR009166" ]
0
13
0
[ "Bacteria", "Eukaryota" ]
[ 16, 28100 ]
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", "Zea mays" ]
[ 30, 7, 45, 4, 110, 58, 2, 18, 71, 53 ]
10
true
Family
Annexin
Annexin
Annexin
8
IPR001466
1,466
Beta-lactamase-related
Beta-lactam-related
Domain
151,055
false
false
This entry represents the serine beta-lactamase-like superfamily. It is a group of diverse group of sequences that includes D-alanyl-D-alanine carboxypeptidase B, aminopeptidase (DmpB), alkaline D-peptidase, animal D-Ala-D-Ala carboxypeptidase homologues and the class A and C beta-lactamases and eukaryotic beta-lactama...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00144" ]
[ "Beta-lactamase" ]
[ 151055 ]
1
[]
[]
[]
0
[ "1bls", "1c3b", "1cef", "1ceg", "1ci8", "1ci9", "1ei5", "1fcm", "1fcn", "1fco", "1fr1", "1fr6", "1fsw", "1fsy", "1ga0", "1ga9", "1gce", "1hvb", "1i5q", "1iel", "1iem", "1ikg", "1iki", "1kds", "1kdw", "1ke0", "1ke3", "1ke4", "1kvl", "1kvm", "1l0d", "1l0e"...
379
[ "PUB00000464", "PUB00000477", "PUB00003270" ]
[ "3128280", "2788410", "1856867" ]
[ "The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.", "The phototrophic bacterium Rhodopseudomonas capsulata sp108 encodes an indigenous class A beta-lactamase.", "Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis...
[ 1988, 1989, 1991 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Plasmid pBWH77", "Viruses", "unclassified sequences" ]
[ 597, 124999, 23377, 1, 309, 1772 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 9, 13, 10, 3, 3, 8, 6, 4, 4, 9 ]
10
true
Domain
Beta-lactamase-related
Beta-lactamase-related
Beta-lactam-related
4
IPR001468
1,468
Indole-3-glycerol phosphate synthase, conserved site
Indole-3-GlycerolPSynthase_CS
Conserved_site
24,606
false
false
Indole-3-glycerol phosphate synthase ( ) (IGPS) catalyses the fourth step in the biosynthesis of tryptophan, the ring closure of 1-(2-carboxy-phenylamino)-1-deoxyribulose into indol-3-glycerol-phosphate. In some bacteria, IGPS is a single chain enzyme. In others, such as Escherichia coli, it is the N-terminal domain of...
[ "GO:0004425", "GO:0006568" ]
[ "indole-3-glycerol-phosphate synthase activity", "L-tryptophan metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00614" ]
[ "IGPS" ]
[ 24606 ]
1
[ "EC", "PROSITEDOC" ]
[ "4.1.1.48", "PDOC00536" ]
[ "EC:4.1.1.48", "PROSITEDOC:PDOC00536" ]
2
[ "1a53", "1i4n", "1igs", "1j5t", "1jcm", "1juk", "1jul", "1lbf", "1lbl", "1pii", "2c3z", "3qja", "3t40", "3t44", "3t55", "3t78", "3tc6", "3tsm", "4fb7", "4iww", "4ix0", "5k7j", "6bma", "6y88", "7etx", "7ety", "8w3y", "8w3z", "8w40" ]
29
[ "PUB00007146" ]
[ "8747452" ]
[ "How to make my blood boil." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 492, 21056, 2627, 431 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 11, 1, 1, 11, 1, 1, 12 ]
7
true
Conserved_site
Indole-3-glycerol phosphate synthase, conserved site
Indole-3-glycerol phosphate synthase, conserved site
Indole-3-GlycerolPSynthase_CS
7
IPR001469
1,469
ATP synthase, F1 complex, delta/epsilon subunit
ATP_synth_F1_dsu/esu
Family
44,078
false
false
This family represents subunits called delta (in mitochondrial ATPase) or epsilon (in bacteria or chloroplast ATPase). The interaction site of subunit C of the F0 complex with the delta or epsilon subunit of the F1 complex may be important for connecting the rotor of F1 (gamma subunit) to the rotor of F0 (C subunit) [ ...
[ "GO:0046933", "GO:0015986", "GO:0045259" ]
[ "proton-transporting ATP synthase activity, rotational mechanism", "proton motive force-driven ATP synthesis", "proton-transporting ATP synthase complex" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00530", "PTHR13822", "TIGR01216", "cd12152" ]
[ "ATP_synth_epsil_bac", "", "ATP_synt_epsi", "F1-ATPase_delta" ]
[ 38691, 40850, 37275, 43303 ]
4
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp0128", "R-BTA-163210", "R-BTA-8949613", "R-CEL-163210", "R-CEL-8949613", "R-HSA-163210", "R-HSA-8949613", "R-MMU-163210", "R-MMU-8949613", "R-RNO-163210", "R-RNO-8949613" ]
[ "GP:GenProp0128", "REACTOME:R-BTA-163210", "REACTOME:R-BTA-8949613", "REACTOME:R-CEL-163210", "REACTOME:R-CEL-8949613", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "REACTOME:R-MMU-163210", "REACTOME:R-MMU-8949613", "REACTOME:R-RNO-163210", "REACTOME:R-RNO-8949613" ]
11
[ "1aqt", "1bsh", "1bsn", "1e79", "1fs0", "1h8e", "1qo1", "2ck3", "2e5y", "2hld", "2jdi", "2qe7", "2rq6", "2rq7", "2v7q", "2w6h", "2w6i", "2w6j", "2wpd", "2wss", "2xnd", "2xok", "3fks", "3oaa", "3oe7", "3oee", "3oeh", "3ofn", "3zia", "3zry", "4asu", "4b2q"...
294
[ "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020606", "PUB00035968", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]
[ "11309608", "15473999", "15078220", "12887009", "16707672", "20450191", "18937357", "1385979", "9741106" ]
[ "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disciplinary approach.", "ATP synthases: insights int...
[ 2001, 2004, 2004, 2003, 2006, 2010, 2008, 1992, 1998 ]
9
[]
[ "IPR024037" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 28, 24105, 19459, 486 ]
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",...
[ 6, 1, 1, 1, 1, 2, 5, 1, 9, 7, 1, 1, 14 ]
13
true
Family
ATP synthase, F1 complex, delta/epsilon subunit
ATP synthase, F1 complex, delta/epsilon subunit
ATP_synth_F1_dsu/esu
3
IPR001471
1,471
AP2/ERF domain
AP2/ERF_dom
Domain
93,218
false
false
Ethylene is an endogenous plant hormone that influences many aspects of plant growth and development. Some defense related genes that are induced by ethylene contain a cis-regulatory element known as the Ethylene-Responsive Element (ERE) [ ]. Sequence analysis on various ERE regions has identified a short motif rich in...
[ "GO:0003700", "GO:0006355" ]
[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS", "PROFILE", "SMART", "CDD" ]
[ "PF00847", "PR00367", "PS51032", "SM00380", "cd00018" ]
[ "AP2", "ETHRSPELEMNT", "AP2_ERF", "AP2", "AP2" ]
[ 82311, 73521, 89907, 88561, 82981 ]
5
[ "PROSITEDOC" ]
[ "PDOC51032" ]
[ "PROSITEDOC:PDOC51032" ]
1
[ "1gcc", "2gcc", "3gcc", "3igm", "5wx9", "7et4", "7et5", "7wq5", "9g6k", "9i05" ]
10
[ "PUB00004522", "PUB00018481", "PUB00018482", "PUB00018483", "PUB00018484", "PUB00018485" ]
[ "7773013", "2535512", "10715325", "9756931", "9736626", "15319480" ]
[ "The APETALA2 domain is related to a novel type of DNA binding domain.", "Functional analysis of DNA sequences responsible for ethylene regulation of a bean chitinase gene in transgenic tobacco.", "Arabidopsis ethylene-responsive element binding factors act as transcriptional activators or repressors of GCC box...
[ 1995, 1989, 2000, 1998, 1998, 2004 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacterium", "Viruses", "metagenomes" ]
[ 791, 91975, 3, 341, 108 ]
5
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 635, 447, 728 ]
3
true
Domain
AP2/ERF domain
AP2/ERF domain
AP2/ERF_dom
2
IPR001474
1,474
GTP cyclohydrolase I
GTP_CycHdrlase_I
Family
30,380
false
false
GTP cyclohydrolase I ( ) catalyses the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP [ ]. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. The comparison of the sequenc...
[ "GO:0003934", "GO:0046654" ]
[ "GTP cyclohydrolase I activity", "tetrahydrofolate biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "NCBIFAM", "PANTHER", "NCBIFAM" ]
[ "MF_00223", "NF006826", "PTHR11109", "TIGR00063" ]
[ "FolE", "PRK09347.1-3", "", "folE" ]
[ 26505, 27315, 30332, 25841 ]
4
[ "EC", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.5.4.16", "GenProp0038", "GenProp1602", "GenProp1632", "PWY-5663", "PWY-6147", "PWY-6703", "PWY-6983", "PWY-7442", "PWY-7852", "PDOC00672", "R-CEL-1474151", "R-DDI-1474151", "R-DME-1474151", "R-HSA-1474151", "R-MMU-1474151", "R-RNO-1474151", "R-SCE-1474151", "R-SPO-1474151" ]
[ "EC:3.5.4.16", "GP:GenProp0038", "GP:GenProp1602", "GP:GenProp1632", "METACYC:PWY-5663", "METACYC:PWY-6147", "METACYC:PWY-6703", "METACYC:PWY-6983", "METACYC:PWY-7442", "METACYC:PWY-7852", "PROSITEDOC:PDOC00672", "REACTOME:R-CEL-1474151", "REACTOME:R-DDI-1474151", "REACTOME:R-DME-1474151",...
19
[ "1a8r", "1a9c", "1fb1", "1fbx", "1gtp", "1is7", "1is8", "1n3r", "1n3s", "1n3t", "1wm9", "1wpl", "1wuq", "1wur", "4du6", "4uqf", "6z80", "6z85", "6z86", "6z87", "6z88", "6z89", "7ala", "7alb", "7alc", "7alq", "9p8z" ]
27
[ "PUB00000247", "PUB00022220" ]
[ "7542887", "12559918" ]
[ "Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers.", "Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I." ]
[ 1995, 2003 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 239, 23494, 5892, 166, 589 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 4, 2, 2, 4, 1, 5, 3, 1, 4, 5, 1, 1, 8 ]
13
true
Family
GTP cyclohydrolase I
GTP cyclohydrolase I
GTP_CycHdrlase_I
4
IPR001475
1,475
ATP-binding cassette subfamily C member 9
ABCC9
Family
710
false
false
ATP-binding cassette subfamily C member 9 (ABCC9, also known as the sulphonylurea receptor SUR2) is an atypical member of the ABC transporter family. Although it has the requisite domains to function as a transporter, it is a regulator of a potassium channel to which it is directly coupled in a hetero-octameric complex...
[ "GO:0005524", "GO:0008281", "GO:0006813", "GO:0016020" ]
[ "ATP binding", "sulfonylurea receptor activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01094" ]
[ "SULFNYLUR2" ]
[ 710 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1296025", "R-HSA-382556", "R-HSA-5578775", "R-HSA-5678420", "R-MMU-1296025", "R-MMU-382556", "R-MMU-5578775", "R-RNO-1296025", "R-RNO-382556", "R-RNO-5578775" ]
[ "REACTOME:R-HSA-1296025", "REACTOME:R-HSA-382556", "REACTOME:R-HSA-5578775", "REACTOME:R-HSA-5678420", "REACTOME:R-MMU-1296025", "REACTOME:R-MMU-382556", "REACTOME:R-MMU-5578775", "REACTOME:R-RNO-1296025", "REACTOME:R-RNO-382556", "REACTOME:R-RNO-5578775" ]
10
[ "7mit", "7mjo", "7mjp", "7mjq", "7vlr", "7vls", "7vlt", "7vlu", "7y1j", "7y1k", "7y1l", "7y1m", "7y1n" ]
13
[ "PUB00072545", "PUB00072598" ]
[ "24700710", "23253866" ]
[ "Cantu syndrome resulting from activating mutation in the KCNJ8 gene.", "Tetrameric structure of SUR2B revealed by electron microscopy of oriented single particles." ]
[ 2014, 2013 ]
2
[ "IPR000388" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 710 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 2, 8 ]
3
true
Family
ATP-binding cassette subfamily C member 9
ATP-binding cassette subfamily C member 9
ABCC9
3
IPR001477
1,477
Viral small hydrophobic protein
SH
Family
941
false
false
The mumps virus SH protein is a membrane protein and not essential for virus growth [ ]. Its function is unknown.
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF01445", "PIRSF003923" ]
[ "SH", "SH" ]
[ 941, 925 ]
2
[]
[]
[]
0
[]
0
[ "PUB00005617" ]
[ "8918542" ]
[ "The mumps virus SH protein is a membrane protein and not essential for virus growth." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Orthorubulavirus" ]
[ 941 ]
1
[]
[]
0
true
Family
Viral small hydrophobic protein
Viral small hydrophobic protein
SH
7
IPR001478
1,478
PDZ domain
PDZ
Domain
452,596
false
false
PDZ domains (also known as Discs-large homologous regions (DHR) or GLGF)) are found in diverse signalling proteins in bacteria, yeasts, plants, insects and vertebrates [ , ]. PDZ domains can occur in one or multiple copies and are nearly always found in cytoplasmic proteins. They bind either the carboxyl-terminal seque...
[ "GO:0005515" ]
[ "protein binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PFAM", "PROFILE", "SMART" ]
[ "PF00595", "PF13180", "PS50106", "SM00228" ]
[ "PDZ", "PDZ_2", "PDZ", "PDZ" ]
[ 267437, 82496, 415120, 419635 ]
4
[ "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...
[ "GenProp1320", "GenProp1481", "PDOC50106", "R-BTA-196780", "R-BTA-199220", "R-BTA-212676", "R-BTA-425397", "R-BTA-5610787", "R-BTA-5666185", "R-BTA-5673001", "R-BTA-8853659", "R-BTA-8980692", "R-BTA-9013149", "R-BTA-9013404", "R-BTA-9013406", "R-BTA-9013408", "R-BTA-9013423", "R-BT...
[ "GP:GenProp1320", "GP:GenProp1481", "PROSITEDOC:PDOC50106", "REACTOME:R-BTA-196780", "REACTOME:R-BTA-199220", "REACTOME:R-BTA-212676", "REACTOME:R-BTA-425397", "REACTOME:R-BTA-5610787", "REACTOME:R-BTA-5666185", "REACTOME:R-BTA-5673001", "REACTOME:R-BTA-8853659", "REACTOME:R-BTA-8980692", "R...
460
[ "1b8q", "1be9", "1bfe", "1d5g", "1fc6", "1fc7", "1fc9", "1fcf", "1g9o", "1gm1", "1gq4", "1gq5", "1i16", "1i92", "1ihj", "1iu0", "1iu2", "1kef", "1kwa", "1ky9", "1l6o", "1lcy", "1m5z", "1mc7", "1mfg", "1mfl", "1n7e", "1n7f", "1n7t", "1n99", "1nf3", "1nte"...
834
[ "PUB00000735", "PUB00005049", "PUB00007292", "PUB00015313", "PUB00018122", "PUB00018590", "PUB00029812", "PUB00089563", "PUB00095156", "PUB00112911", "PUB00112912", "PUB00112913", "PUB00112914", "PUB00112915", "PUB00112916", "PUB00112917", "PUB00112918", "PUB00113569" ]
[ "9204764", "9041651", "7535955", "8674113", "9382826", "7482701", "8757139", "9434904", "20509869", "11591811", "11283303", "11158544", "8939589", "8974395", "9232802", "9425351", "9604925", "8625403" ]
[ "PDZ domains: targeting signalling molecules to sub-membranous sites.", "Evidence for PDZ domains in bacteria, yeast, and plants.", "DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins.", "Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecu...
[ 1997, 1997, 1995, 1996, 1997, 1995, 1996, 1997, 2010, 2001, 2001, 2001, 1996, 1997, 1997, 1997, 1998, 1996 ]
18
[]
[ "IPR039381", "IPR039382", "IPR061276" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1409, 138212, 310468, 19, 2488 ]
5
[ "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...
[ 75, 176, 2166, 327, 5, 781, 619, 46, 808, 2, 1, 78 ]
12
true
Domain
PDZ domain
PDZ domain
PDZ
8
IPR001479
1,479
Quinoprotein dehydrogenase, conserved site
Quinoprotein_DH_CS
Conserved_site
6,891
false
false
This entry represents two conserved regions found in mainly proteobacterial PQQ dehydrogenases. Pyrrolo-quinoline quinone (PQQ) is a redox coenzyme, which serves as a cofactor for a number of enzymes (quinoproteins) and particularly for some bacterial dehydrogenases [ , , ].
[ "GO:0030288" ]
[ "outer membrane-bounded periplasmic space" ]
[ "cellular_component" ]
1
[ "PROSITE", "PROSITE" ]
[ "PS00363", "PS00364" ]
[ "BACTERIAL_PQQ_1", "BACTERIAL_PQQ_2" ]
[ 1715, 6586 ]
2
[ "PROSITEDOC" ]
[ "PDOC00375" ]
[ "PROSITEDOC:PDOC00375" ]
1
[ "1flg", "1g72", "1h4i", "1h4j", "1kb0", "1kv9", "1lrw", "1w6s", "2ad6", "2ad7", "2ad8", "2d0v", "4aah", "4tqo", "5xm3", "6dam", "6oc5", "6oc6", "6zcv", "6zcw", "7cdl", "7ce5", "7ce9", "7ced", "7cfx", "8gy2", "9ism", "9iso" ]
28
[ "PUB00000066", "PUB00005344", "PUB00154592" ]
[ "2549854", "2572081", "32366463" ]
[ "Quinoproteins, enzymes with pyrrolo-quinoline quinone as cofactor.", "PQQ, the elusive coenzyme.", "Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function." ]
[ 1989, 1989, 2020 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteriales", "metagenomes" ]
[ 6822, 13, 2, 54 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Conserved_site
Quinoprotein dehydrogenase, conserved site
Quinoprotein dehydrogenase, conserved site
Quinoprotein_DH_CS
6
IPR001480
1,480
Bulb-type lectin domain
Bulb-type_lectin_dom
Domain
54,320
false
false
A bulb lectin super-family (Amaryllidaceae, Orchidaceae and Aliaceae) contains a ~115-residue-long domain whose overall three dimensional fold is very similar to that of [ , , ]: Dictyostelium discoideum comitin, an actin binding protein Curculigo latifolia curculin, a sweet tasting and taste-modifying protein This dom...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART", "CDD" ]
[ "PF01453", "PS50927", "SM00108", "cd00028" ]
[ "B_lectin", "BULB_LECTIN", "B_lectin", "B_lectin" ]
[ 46526, 52051, 48792, 39400 ]
4
[ "PROSITEDOC" ]
[ "PDOC50927" ]
[ "PROSITEDOC:PDOC50927" ]
1
[ "1b2p", "1bwu", "1dlp", "1jpc", "1kj1", "1msa", "1niv", "1npl", "1xd5", "1xd6", "2d04", "2dpf", "3a0c", "3a0d", "3a0e", "3dzw", "3m7h", "3m7j", "3mez", "3r0e", "4gc1", "4gc2", "4h3o", "4le7", "4lea", "4led", "4oit", "4oiz", "4okc", "4pdt", "4tkc", "5d5g"...
39
[ "PUB00008030", "PUB00018396", "PUB00095158" ]
[ "9132060", "7664110", "11522393" ]
[ "Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin.", "Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family.", "Mannose-binding plant lectins: different structural scaffolds for a common sugar-recognition...
[ 1997, 1995, 2001 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 24, 2807, 51429, 31, 29 ]
5
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 266, 1, 353, 236 ]
4
true
Domain
Bulb-type lectin domain
Bulb-type lectin domain
Bulb-type_lectin_dom
8
IPR001481
1,481
Prostanoid EP3 receptor, type 2
EP3_rcpt_2
Family
373
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004957", "GO:0007186", "GO:0016020" ]
[ "prostaglandin E receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00584" ]
[ "PRSTNOIDE32R" ]
[ 373 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-391908", "R-HSA-418594", "R-SSC-391908", "R-SSC-418594" ]
[ "REACTOME:R-HSA-391908", "REACTOME:R-HSA-418594", "REACTOME:R-SSC-391908", "REACTOME:R-SSC-418594" ]
4
[ "6ak3", "7wu9", "8gdc" ]
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
[ "IPR000265" ]
[]
1
0
1
[ "Eutheria" ]
[ 373 ]
1
[ "Homo sapiens" ]
[ 8 ]
1
true
Family
Prostanoid EP3 receptor, type 2
Prostanoid EP3 receptor, type 2
EP3_rcpt_2
2
IPR001482
1,482
Type II/IV secretion system domain
T2SS/T4SS_dom
Domain
92,982
false
false
This entry contains both type II and type IV pathway secretion proteins from bacteria. Proteins in this entry include VirB11 ATPase ( ), which is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cel...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00437" ]
[ "T2SSE" ]
[ 92982 ]
1
[ "PROSITEDOC" ]
[ "PDOC00567" ]
[ "PROSITEDOC:PDOC00567" ]
1
[ "1g6o", "1nly", "1nlz", "1opx", "1p9r", "1p9w", "2ewv", "2eww", "2eyu", "2gsz", "2gza", "2oap", "2oaq", "2pt7", "3jc8", "3jvu", "3jvv", "4ihq", "4ii7", "4ksr", "4kss", "4pht", "5fl3", "5it5", "5oiu", "5tsg", "5tsh", "5zfq", "5zfr", "6bge", "6ejf", "6f8l"...
54
[ "PUB00016812", "PUB00019657", "PUB00086434" ]
[ "15223057", "11566978", "28264910" ]
[ "The general secretory pathway: a general misnomer?", "Role of Agrobacterium VirB11 ATPase in T-pilus assembly and substrate selection.", "Expanding Role of Type II Secretion in Bacterial Pathogenesis and Beyond." ]
[ 2004, 2001, 2017 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "plasmids", "unclassified sequences" ]
[ 3608, 87063, 3, 229, 13, 2066 ]
6
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Domain
Type II/IV secretion system domain
Type II/IV secretion system domain
T2SS/T4SS_dom
4
IPR001483
1,483
Urotensin II, conserved site
Urotensin_II
Conserved_site
1,493
false
false
Urotensin II (UII) is a vasoactive somatostatin-like or cortistatin-like peptide hormone. However, despite the apparent structural similarity to these peptide hormones, they are not homologous to UII. Urotensin II was first identified in fish spinal cord but later found in humans and other mammals [ ]. In fish, UII is ...
[ "GO:0008217", "GO:0097746", "GO:0005576" ]
[ "regulation of blood pressure", "blood vessel diameter maintenance", "extracellular region" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "PFAM", "PROSITE" ]
[ "PF02083", "PS00984" ]
[ "Urotensin_II", "UROTENSIN_II" ]
[ 827, 1492 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00757", "R-HSA-375276", "R-HSA-416476", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476" ]
[ "PROSITEDOC:PDOC00757", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476" ]
7
[ "6hvb" ]
1
[ "PUB00007095", "PUB00007096", "PUB00063803", "PUB00063804" ]
[ "10499587", "11020490", "15102493", "3724202" ]
[ "Human urotensin-II is a potent vasoconstrictor and agonist for the orphan receptor GPR14.", "Human urotensin II mediates vasoconstriction via an increase in inositol phosphates.", "From 'gills to pills': urotensin-II as a regulator of mammalian cardiorenal function.", "Radioimmunoassays for fish tail neurope...
[ 1999, 2000, 2004, 1986 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Thermoproteota archaeon" ]
[ 4, 1488, 1 ]
3
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 3, 5, 4 ]
4
true
Conserved_site
Urotensin II, conserved site
Urotensin II, conserved site
Urotensin_II
9
IPR001489
1,489
Heat-stable enterotoxin, STa
Heat-stable_enterotox_STa
Family
71
false
false
This entry represents a group of heat-stable enterotoxins, such as STa from Escherichia coli, which is the cause of acute diarrhoea in infants and travellers in developing countries. The mature STa protein is a 19-residue peptide containing three disulphide bridges that are functionally important. STa contains an N-ter...
[ "GO:0090729", "GO:0005615" ]
[ "toxin activity", "extracellular space" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF02048" ]
[ "Enterotoxin_ST" ]
[ 71 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME" ]
[ "PDOC00246", "R-HSA-8942233", "R-HSA-9760173" ]
[ "PROSITEDOC:PDOC00246", "REACTOME:R-HSA-8942233", "REACTOME:R-HSA-9760173" ]
3
[ "1etn", "7css", "7d37" ]
3
[ "PUB00016492", "PUB00035778", "PUB00035779", "PUB00035780" ]
[ "15049831", "10799798", "17094787", "12813912" ]
[ "Structural features of Escherichia coli heat-stable enterotoxin that activates membrane-associated guanylyl cyclase.", "Characterization of the interaction of Escherichia coli heat-stable enterotoxin (STa) with its putative receptor on the intestinal tract of newborn calves.", "Interaction of Escherichia coli ...
[ 2004, 2000, 2007, 2003 ]
4
[]
[]
0
0
null
[ "Bacteria" ]
[ 71 ]
1
[]
[]
0
true
Family
Heat-stable enterotoxin, STa
Heat-stable enterotoxin, STa
Heat-stable_enterotox_STa
5
IPR001492
1,492
Flagellin
Flagellin
Family
44,343
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", "GO:0009288" ]
[ "structural molecule activity", "bacterial-type flagellum" ]
[ "molecular_function", "cellular_component" ]
2
[ "PANTHER" ]
[ "PTHR42792" ]
[ "" ]
[ 44343 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-GGA-433822", "R-GGA-451534", "R-GGA-977240", "R-HSA-168176", "R-HSA-5602680", "R-HSA-5603037", "R-HSA-844623", "R-HSA-975871" ]
[ "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" ]
8
[ "1io1", "1ory", "1ucu", "2d4x", "2zbi", "3a5x", "3k8v", "3k8w", "3pwx", "3v47", "4cfi", "4nx9", "5gy2", "5kay", "5maw", "5wjt", "5wju", "5wjv", "5wjw", "5wjx", "5wjy", "5wjz", "5wk5", "5wk6", "5yti", "5yud", "5z7q", "5ziy", "5ziz", "5zj0", "6b5b", "6gow"...
77
[ "PUB00002058", "PUB00002080", "PUB00002583", "PUB00099952", "PUB00099953", "PUB00099954", "PUB00099955" ]
[ "3536885", "2498283", "2211662", "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.", "Flagellin as a vaccin...
[ 1986, 1989, 1990, 2018, 2018, 2021, 2017 ]
7
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 43695, 67, 580, 1 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Flagellin
Flagellin
Flagellin
4
IPR001493
1,493
Peptidase A22A, presenilin 2
Pept_A22A_PS2
Family
720
false
false
This group of aspartic peptidases belong to MEROPS peptidase family A22 (presenilin family, clan AD): subfamily A22A, the type example being presenilin 1 from Homo sapiens (Human). Presenilins are polytopic transmembrane (TM) proteins, mutations in which are associated with the occurrence of early-onset familial Alzhei...
[ "GO:0042500", "GO:0035556", "GO:0042987", "GO:0016020" ]
[ "aspartic endopeptidase activity, intramembrane cleaving", "intracellular signal transduction", "amyloid precursor protein catabolic process", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01074" ]
[ "PRESENILIN2" ]
[ 720 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.4.23.-", "R-BTA-1251985", "R-BTA-193692", "R-BTA-205043", "R-BTA-3928665", "R-BTA-9839383", "R-HSA-1251985", "R-HSA-193692", "R-HSA-205043", "R-HSA-2122948", "R-HSA-2644606", "R-HSA-2894862", "R-HSA-2979096", "R-HSA-3928665", "R-HSA-9013507", "R-HSA-9013700", "R-HSA-9017802", "R...
[ "EC:3.4.23.-", "REACTOME:R-BTA-1251985", "REACTOME:R-BTA-193692", "REACTOME:R-BTA-205043", "REACTOME:R-BTA-3928665", "REACTOME:R-BTA-9839383", "REACTOME:R-HSA-1251985", "REACTOME:R-HSA-193692", "REACTOME:R-HSA-205043", "REACTOME:R-HSA-2122948", "REACTOME:R-HSA-2644606", "REACTOME:R-HSA-2894862...
36
[ "7y5x", "7y5z" ]
2
[ "PUB00000974", "PUB00000976", "PUB00002010", "PUB00004220" ]
[ "9791530", "9791533", "9521418", "7566091" ]
[ "Introduction: genetic determinants of mid- and late-life dementias.", "Monogenic determinants of familial Alzheimer's disease: presenilin-2 mutations.", "Presenilin mutations in Alzheimer's disease.", "Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gen...
[ 1998, 1998, 1998, 1995 ]
4
[ "IPR001108" ]
[]
1
0
1
[ "Amniota" ]
[ 720 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 19, 5, 2 ]
3
true
Family
Peptidase A22A, presenilin 2
Peptidase A22A, presenilin 2
Pept_A22A_PS2
8
IPR001494
1,494
Importin-beta, N-terminal domain
Importin-beta_N
Domain
57,801
false
false
This entry represents the N-terminal domain of importin-beta (also known as karyopherins-beta) that is important for the binding of the Ran GTPase protein [ ]. Members of the importin-beta (karyopherin-beta) family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha. As part of a he...
[ "GO:0031267", "GO:0006886" ]
[ "small GTPase binding", "intracellular protein transport" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE", "SMART" ]
[ "PF03810", "PS50166", "SM00913" ]
[ "IBN_N", "IMPORTIN_B_NT", "IBN_N" ]
[ 51898, 48233, 47748 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50166", "R-BTA-450513", "R-DDI-450513", "R-DDI-5687128", "R-DME-140342", "R-DME-1655829", "R-DME-3769402", "R-DME-450520", "R-DME-6798695", "R-DME-68616", "R-DME-69273", "R-DME-909733", "R-DME-9634638", "R-DME-9707616", "R-DME-9856649", "R-HSA-1169408", "R-HSA-140342", "R-HSA-...
[ "PROSITEDOC:PDOC50166", "REACTOME:R-BTA-450513", "REACTOME:R-DDI-450513", "REACTOME:R-DDI-5687128", "REACTOME:R-DME-140342", "REACTOME:R-DME-1655829", "REACTOME:R-DME-3769402", "REACTOME:R-DME-450520", "REACTOME:R-DME-6798695", "REACTOME:R-DME-68616", "REACTOME:R-DME-69273", "REACTOME:R-DME-90...
102
[ "1f59", "1gcj", "1ibr", "1m5n", "1o6o", "1o6p", "1qbk", "1qgk", "1qgr", "1ukl", "1wa5", "1z3h", "2bku", "2h4m", "2ot8", "2p8q", "2q5d", "2qmr", "2x19", "2x1g", "2xwu", "2z5j", "2z5k", "2z5m", "2z5n", "2z5o", "3a6p", "3ea5", "3gb8", "3gjx", "3lww", "3m1i"...
168
[ "PUB00009772", "PUB00018160", "PUB00034676", "PUB00034678" ]
[ "12372823", "10367892", "17170104", "17161424" ]
[ "GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta.", "Structural view of the Ran-Importin beta interaction at 2.3 A resolution.", "Classical nuclear localization signals: definition, function, and interaction with importin alpha.", "Association of nuclear pore FG-repeat domains to NTF2 im...
[ 2002, 1999, 2007, 2007 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Dipodfec virus UA23Rod_1340", "Eukaryota", "metagenomes" ]
[ 7, 88, 1, 57700, 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...
[ 61, 6, 35, 37, 84, 46, 11, 40, 78, 9, 8, 198 ]
12
true
Domain
Importin-beta, N-terminal domain
Importin-beta, N-terminal domain
Importin-beta_N
5
IPR001496
1,496
SOCS box domain
SOCS_box
Domain
41,251
false
false
The SOCS box was first identified in SH2-domain-containing proteins of the suppressor of cytokines signalling (SOCS) family [ ] but was later also found in: the WSB (WD-40-repeat-containing proteins with a SOCS box) family, the SSB (SPRY domain-containing proteins with a SOCS box) family, the ASB (ankyrin-repeat-contai...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART", "SMART" ]
[ "PF07525", "PS50225", "SM00253", "SM00969" ]
[ "SOCS_box", "SOCS", "SOCS", "SOCS_box" ]
[ 36923, 39923, 18302, 37423 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50225", "R-BTA-1059683", "R-BTA-877300", "R-BTA-877312", "R-BTA-8849474", "R-BTA-8951664", "R-BTA-909733", "R-BTA-9705462", "R-BTA-9706369", "R-BTA-983168", "R-DME-8951664", "R-DME-983168", "R-DRE-8951664", "R-DRE-983168", "R-HSA-1059683", "R-HSA-1266695", "R-HSA-1433559", "R-...
[ "PROSITEDOC:PDOC50225", "REACTOME:R-BTA-1059683", "REACTOME:R-BTA-877300", "REACTOME:R-BTA-877312", "REACTOME:R-BTA-8849474", "REACTOME:R-BTA-8951664", "REACTOME:R-BTA-909733", "REACTOME:R-BTA-9705462", "REACTOME:R-BTA-9706369", "REACTOME:R-BTA-983168", "REACTOME:R-DME-8951664", "REACTOME:R-DM...
57
[ "2c9w", "2izv", "2jz3", "3zkj", "3zng", "4jgh", "5bo4", "6c5x", "6i4x", "6i5j", "6i5n", "6v9h", "7m6t", "7zlm", "7zln", "7zlo", "7zlp", "7zlr", "7zls", "8okx", "8ol1", "8y1u" ]
22
[ "PUB00006611", "PUB00006612", "PUB00006613", "PUB00006614", "PUB00060101" ]
[ "9202125", "9419338", "9869640", "10051596", "15601820" ]
[ "A family of cytokine-inducible inhibitors of signalling.", "Twenty proteins containing a C-terminal SOCS box form five structural classes.", "The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families.", "The conserved SOC...
[ 1997, 1998, 1998, 1999, 2004 ]
5
[]
[ "IPR028410", "IPR028414", "IPR037326", "IPR037327", "IPR037328", "IPR037329", "IPR037330", "IPR037331", "IPR037332", "IPR037333", "IPR037334", "IPR037340", "IPR037342", "IPR037343", "IPR037345", "IPR037346" ]
0
16
0
[ "Bacteria", "Eukaryota", "Viruses", "bird metagenome" ]
[ 123, 41120, 7, 1 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 11, 141, 26, 85, 96, 124 ]
6
true
Domain
SOCS box domain
SOCS box domain
SOCS_box
6
IPR001497
1,497
Methylated-DNA-[protein]-cysteine S-methyltransferase, active site
MethylDNA_cys_MeTrfase_AS
Active_site
38,868
false
false
Synonym(s): 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase, Methylated-DNA-[protein]-cysteine S-methyltransferase. This entry represents the active site of 6-O-methylguanine-DNA methyltransferases. The repair of DNA containing O6-alkylated guanine is carried out by DNA-[protein]-cystein...
[ "GO:0003908", "GO:0006281" ]
[ "methylated-DNA-[protein]-cysteine S-methyltransferase activity", "DNA repair" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00374" ]
[ "MGMT" ]
[ 38868 ]
1
[ "EC", "PROSITEDOC", "REACTOME" ]
[ "2.1.1.63", "PDOC00320", "R-HSA-5657655" ]
[ "EC:2.1.1.63", "PROSITEDOC:PDOC00320", "REACTOME:R-HSA-5657655" ]
3
[ "1eh6", "1eh7", "1eh8", "1mgt", "1qnt", "1sfe", "1t39", "1wrj", "1yfh", "2g7h", "3kzy", "3l00", "4bhb", "4bhc", "4wx9", "4wxc", "4wxd", "4zye", "4zyg", "6ga0", "6rla", "6rlb", "6sc2", "6y8p", "7dkn", "7dqr", "7dqt", "7wz8", "8aes", "8bbe", "8bbg", "8dd7"...
58
[ "PUB00000053", "PUB00004404" ]
[ "3052269", "1579490" ]
[ "Regulation and expression of the adaptive response to alkylating agents.", "Isolation and partial characterisation of a Chinese hamster O6-alkylguanine-DNA alkyltransferase cDNA." ]
[ 1988, 1992 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Megaviricetes", "unclassified sequences" ]
[ 682, 34706, 2863, 28, 589 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 2, 7, 1, 2, 5, 2, 5, 1 ]
8
true
Active_site
Methylated-DNA-[protein]-cysteine S-methyltransferase, active site
Methylated-DNA-[protein]-cysteine S-methyltransferase, active site
MethylDNA_cys_MeTrfase_AS
1
IPR001498
1,498
Impact, N-terminal
Impact_N
Domain
25,396
false
false
This entry represents the N-terminal domain of the Impact proteins. The Impact protein is a translational regulator that ensures constant high levels of translation under amino acid starvation. It acts by interacting with Gcn1/Gcn1L1, thereby preventing activation of Gcn2 protein kinases (EIF2AK1 to 4) and subsequent d...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01205" ]
[ "Impact_N" ]
[ 25396 ]
1
[ "PROSITEDOC", "REACTOME" ]
[ "PDOC00707", "R-HSA-9633012" ]
[ "PROSITEDOC:PDOC00707", "REACTOME:R-HSA-9633012" ]
2
[ "1vi7", "2cve", "6bqi", "6u1l", "6u1o" ]
5
[ "PUB00046141" ]
[ "11116084" ]
[ "Comparative genome analysis of the mouse imprinted gene impact and its nonimprinted human homolog IMPACT: toward the structural basis for species-specific imprinting." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Microviridae sp. ctNWS1", "unclassified sequences" ]
[ 496, 18550, 6196, 1, 153 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae ...
[ 7, 1, 12, 1, 3, 1, 2, 3, 5, 2, 2, 6 ]
12
true
Domain
Impact, N-terminal
Impact, N-terminal
Impact_N
1
IPR001499
1,499
GPCR fungal pheromone mating factor, STE3
GPCR_STE3
Family
4,113
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:0004932", "GO:0007186", "GO:0016020" ]
[ "mating-type factor pheromone receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF02076", "PR00899", "PTHR28097" ]
[ "STE3", "GPCRSTE3", "" ]
[ 4109, 3693, 4011 ]
3
[]
[]
[]
0
[]
0
[ "PUB00001139", "PUB00004338", "PUB00004657", "PUB00004961", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "16453635", "3001640", "2836861", "8170923", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Nucleotide sequences of STE2 and STE3, cell type-specific sterile genes from Saccharomyces cerevisiae.", "The yeast alpha-factor receptor: structural properties deduced from the sequence of the STE2 gene.", "STE2 protein of Saccharomyces kluyveri is a member of the rhodopsin/beta-adrenergic receptor family and...
[ 1985, 1985, 1988, 1994, 2003, 1994, 2005, 2009, 2006, 2013 ]
10
[]
[ "IPR000481", "IPR001546" ]
0
2
0
[ "Aurantiacibacter atlanticus", "Opisthokonta" ]
[ 1, 4112 ]
2
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1, 1, 1 ]
3
true
Family
GPCR fungal pheromone mating factor, STE3
GPCR fungal pheromone mating factor, STE3
GPCR_STE3
9
IPR001500
1,500
Alpha-1-acid glycoprotein
A1A_glycop
Family
273
false
false
null
[ "GO:0002682", "GO:0005615" ]
[ "regulation of immune system process", "extracellular space" ]
[ "biological_process", "cellular_component" ]
2
[ "PIRSF", "PRINTS" ]
[ "PIRSF036899", "PR00708" ]
[ "AGP", "A1AGLPROTEIN" ]
[ 155, 268 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-114608", "R-HSA-6798695", "R-MMU-114608", "R-MMU-6798695", "R-RNO-114608", "R-RNO-6798695" ]
[ "REACTOME:R-HSA-114608", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-114608", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-114608", "REACTOME:R-RNO-6798695" ]
6
[ "3apu", "3apv", "3apw", "3apx", "3kq0", "7oub" ]
6
[ "PUB00000205", "PUB00001391", "PUB00001451", "PUB00001491", "PUB00002020", "PUB00002777", "PUB00003097", "PUB00003778", "PUB00004508", "PUB00004899", "PUB00005013", "PUB00005238", "PUB00005379" ]
[ "1834059", "2026162", "7514123", "3622999", "8886858", "8486691", "7866554", "1707134", "3064105", "8755512", "7684291", "8069623", "1723819" ]
[ "Mouse oncogene protein 24p3 is a member of the lipocalin protein family.", "Complete sequence and model for the A2 subunit of the carotenoid pigment complex, crustacyanin.", "Structural organization of the genes for rat von Ebner's gland proteins 1 and 2 reveals their close relationship to lipocalins.", "Hom...
[ 1991, 1991, 1994, 1987, 1996, 1993, 1994, 1991, 1988, 1996, 1993, 1993, 1991 ]
13
[]
[]
0
0
null
[ "Bilateria" ]
[ 273 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 8, 4 ]
3
true
Family
Alpha-1-acid glycoprotein
Alpha-1-acid glycoprotein
A1A_glycop
7
IPR001501
1,501
Nickel-dependent hydrogenase, large subunit
Ni-dep_hyd_lsu
Family
15,185
false
false
Hydrogenases are enzymes that catalyse the reversible oxidation of hydrogen and are important in anaerobic metabolism. There are various types of metal-containing hydrogenases and can be broadly divided into three groups: Fe ('iron only') hydrogenases; Ni-Fe hydrogenases; and Ni-Fe-Se hydrogenases [ ]. The [NiFe] and [...
[ "GO:0016151" ]
[ "nickel cation binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00374" ]
[ "NiFeSe_Hases" ]
[ 15185 ]
1
[ "GP", "PROSITEDOC" ]
[ "GenProp1209", "PDOC00400" ]
[ "GP:GenProp1209", "PROSITEDOC:PDOC00400" ]
2
[ "1cc1", "1e3d", "1frf", "1frv", "1h2a", "1h2r", "1ubh", "1ubj", "1ubk", "1ubl", "1ubm", "1ubo", "1ubr", "1ubt", "1ubu", "1wuh", "1wui", "1wuj", "1wuk", "1wul", "1yq9", "1yqw", "1yrq", "2frv", "2wpn", "3ayx", "3ayz", "3cur", "3cus", "3h3x", "3myr", "3rgw"...
177
[ "PUB00001739", "PUB00002102", "PUB00004672", "PUB00020978", "PUB00099872" ]
[ "3078655", "2180913", "2521386", "7854413", "24778258" ]
[ "The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio.", "Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames.", "Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases...
[ 1988, 1990, 1989, 1995, 2014 ]
5
[]
[ "IPR017682" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1461, 13273, 15, 436 ]
4
[ "Escherichia coli (strain K12)" ]
[ 4 ]
1
true
Family
Nickel-dependent hydrogenase, large subunit
Nickel-dependent hydrogenase, large subunit
Ni-dep_hyd_lsu
5
IPR001503
1,503
Glycosyl transferase family 10
Glyco_trans_10
Family
17,998
false
false
The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferas...
[ "GO:0008417", "GO:0009101", "GO:0016020" ]
[ "fucosyltransferase activity", "glycoprotein biosynthetic process", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PANTHER", "PANTHER" ]
[ "PTHR11929", "PTHR48438" ]
[ "", "" ]
[ 12023, 5975 ]
2
[ "CAZY", "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GT10", "2.4.1", "GenProp1444", "R-BTA-9037629", "R-CEL-9037629", "R-CEL-975578", "R-CFA-9037629", "R-DME-9037629", "R-DME-975578", "R-HSA-5173105", "R-HSA-9037629", "R-HSA-975578", "R-MMU-5173105", "R-MMU-9037629", "R-RNO-5173105", "R-RNO-9037629", "R-XTR-5173105" ]
[ "CAZY:GT10", "EC:2.4.1", "GP:GenProp1444", "REACTOME:R-BTA-9037629", "REACTOME:R-CEL-9037629", "REACTOME:R-CEL-975578", "REACTOME:R-CFA-9037629", "REACTOME:R-DME-9037629", "REACTOME:R-DME-975578", "REACTOME:R-HSA-5173105", "REACTOME:R-HSA-9037629", "REACTOME:R-HSA-975578", "REACTOME:R-MMU-51...
17
[ "2nzw", "2nzx", "2nzy", "5zoi", "7yro", "8d0o", "8d0p", "8d0q", "8d0r", "8d0s", "8d0u", "8d0w", "8d0x" ]
13
[ "PUB00001989", "PUB00006364", "PUB00009409" ]
[ "9451017", "9042366", "9334165" ]
[ "Conserved structural features in eukaryotic and prokaryotic fucosyltransferases.", "Chemical modification of an alpha 3-fucosyltransferase; definition of amino acid residues essential for enzyme activity.", "A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence simila...
[ 1998, 1997, 1997 ]
3
[]
[ "IPR016646", "IPR017176", "IPR017177" ]
0
3
0
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Viruses", "unclassified sequences" ]
[ 1267, 16536, 11, 55, 129 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 23, 5, 40, 9, 37, 18, 11, 20, 23 ]
9
true
Family
Glycosyl transferase family 10
Glycosyl transferase family 10
Glyco_trans_10
2
IPR001504
1,504
Bradykinin receptor B2
Brdyknn_2_rcpt
Family
897
false
false
Bradykinins are a family of short, structurally similar peptides that activate sensory fibres, contract venous smooth muscle, stimulate release of cytokines, induce connective tissue proliferation and mediate endothelium-dependent vasodilation [ , ]. Bradykinin antagonists are used in the treatment of inflammation, ast...
[ "GO:0004947", "GO:0006939", "GO:0007186", "GO:0042310", "GO:0016020" ]
[ "bradykinin receptor activity", "smooth muscle contraction", "G protein-coupled receptor signaling pathway", "vasoconstriction", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "cellular_component" ]
5
[ "PRINTS" ]
[ "PR00994" ]
[ "BRADYKINNB2R" ]
[ 897 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "42", "R-HSA-375276", "R-HSA-416476", "R-HSA-418594", "R-MMU-375276", "R-MMU-416476", "R-MMU-418594", "R-RNO-375276", "R-RNO-416476", "R-RNO-418594" ]
[ "IUPHAR:42", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476", "REACTOME:R-RNO-418594" ]
10
[ "7f2o" ]
1
[ "PUB00063406", "PUB00063407", "PUB00063408", "PUB00063409", "PUB00063410", "PUB00063420", "PUB00063421", "PUB00063422", "PUB00063424", "PUB00063425", "PUB00063426", "PUB00066864", "PUB00066865", "PUB00066866", "PUB00066867" ]
[ "10812256", "12755382", "9112069", "9650825", "8075864", "7835885", "8846417", "10653985", "15734727", "17077303", "11904521", "2560387", "8458876", "8227332", "7895328" ]
[ "Increased mRNA expression of the B1 and B2 bradykinin receptors and antinociceptive effects of their antagonists in an animal model of neuropathic pain.", "Amelioration of hyperalgesia by kinin receptor antagonists or kininogen deficiency in chronic constriction nerve injury in rats.", "Bradykinin receptors.",...
[ 2000, 2003, 1997, 1998, 1994, 1994, 1995, 2000, 2005, 2006, 2002, 1989, 1993, 1993, 1995 ]
15
[ "IPR000496" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 897 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 3, 2, 5 ]
4
true
Family
Bradykinin receptor B2
Bradykinin receptor B2
Brdyknn_2_rcpt
4
IPR001505
1,505
Copper centre Cu(A)
Copper_CuA
Binding_site
74,106
false
false
The Cu(A) centre contains a mixed valence binuclear copper binding site formed of about 50 amino acids containing two cysteines and histidines and one glutamate and methionine [ ]. The Cu(A) centre has been identified in subunit II of cytochrome c oxidase and nitrous oxide reductase [ , ]. Cytochrome c oxidase ( ) [ , ...
[ "GO:0005507" ]
[ "copper ion binding" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00078" ]
[ "COX2" ]
[ 74106 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...
[ "7.1.1.9", "PWY-3781", "PWY-4521", "PWY-6692", "PWY-7279", "PWY-7429", "PWY-8271", "PDOC00075", "R-BTA-5419276", "R-BTA-5628897", "R-BTA-611105", "R-BTA-9707564", "R-BTA-9864848", "R-CEL-5419276", "R-DDI-9837999", "R-DME-5419276", "R-DME-5628897", "R-DME-611105", "R-DME-9707564",...
[ "EC:7.1.1.9", "METACYC:PWY-3781", "METACYC:PWY-4521", "METACYC:PWY-6692", "METACYC:PWY-7279", "METACYC:PWY-7429", "METACYC:PWY-8271", "PROSITEDOC:PDOC00075", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-5628897", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-9707564", "REACTOME:R-BTA-9864848", "RE...
45
[ "1ar1", "1cyx", "1ehk", "1m56", "1m57", "1occ", "1oco", "1ocr", "1ocz", "1qle", "1qni", "1v54", "1v55", "1xme", "2cua", "2dyr", "2dys", "2eij", "2eik", "2eil", "2eim", "2ein", "2fwl", "2gsm", "2lln", "2occ", "2qpd", "2qpe", "2y69", "2ybb", "2yev", "2zxw"...
249
[ "PUB00000581", "PUB00001225", "PUB00001426", "PUB00002253", "PUB00006585" ]
[ "6307356", "1324168", "1324835", "8083153", "7592701" ]
[ "Structure of cytochrome c oxidase.", "Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex.", "Derived amino acid sequences of the nosZ gene (respiratory N2O reductase) from Alcaligenes eutrophus, Pseudomonas aeru...
[ 1983, 1992, 1992, 1994, 1995 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 946, 19888, 52776, 496 ]
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)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizo...
[ 1, 2, 2, 7, 434, 3, 1, 6, 1, 1, 2 ]
11
true
Binding_site
Copper centre Cu(A)
Copper centre Cu(A)
Copper_CuA
1
IPR001507
1,507
Zona pellucida domain
ZP_dom
Domain
42,638
false
false
The zona pellucida (ZP) domain is a protein polymerisation module of ~260 amino acid module, which is found at the C terminus of many secreted eukaryotic glycoproteins that play fundamental roles in development, hearing, immunity, and cancer [ , , , ]. Proteins containing a ZP domain include: Sperm receptor proteins ZP...
[]
[]
[]
0
[ "PROFILE", "SMART" ]
[ "PS51034", "SM00241" ]
[ "ZP_2", "ZP" ]
[ 42276, 34938 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00577", "R-BTA-2534343", "R-HSA-1502540", "R-HSA-163125", "R-HSA-190370", "R-HSA-190373", "R-HSA-201451", "R-HSA-2173789", "R-HSA-2534343", "R-HSA-446203", "R-HSA-5683826", "R-HSA-9839383", "R-HSA-9839389", "R-HSA-9839394", "R-HSA-9839397", "R-HSA-9839406", "R-HSA-9925561", "R...
[ "PROSITEDOC:PDOC00577", "REACTOME:R-BTA-2534343", "REACTOME:R-HSA-1502540", "REACTOME:R-HSA-163125", "REACTOME:R-HSA-190370", "REACTOME:R-HSA-190373", "REACTOME:R-HSA-201451", "REACTOME:R-HSA-2173789", "REACTOME:R-HSA-2534343", "REACTOME:R-HSA-446203", "REACTOME:R-HSA-5683826", "REACTOME:R-HSA...
42
[ "3d4c", "3d4g", "3ef7", "3nk3", "3nk4", "3qw9", "4ajv", "4wrn", "5bup", "5osq", "6tqk", "6tql", "6zs5", "6zya", "7lbg", "7pfp", "7q3n", "8bqu", "8dc0", "8rki", "8xc5", "9nu1", "9nu2", "9nu3" ]
24
[ "PUB00001633", "PUB00017980", "PUB00017982", "PUB00017983", "PUB00163198" ]
[ "1313375", "12021773", "12878193", "15079052", "40550004" ]
[ "A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor.", "The ZP domain is a conserved module for polymerization of extracellular proteins.", "Identification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC.", "A duplicated motif controls assembly of...
[ 1992, 2002, 2003, 2004, 2025 ]
5
[]
[ "IPR048290" ]
0
1
0
[ "Bacteria", "Eukaryota", "Proteus phage Myduc", "hydrothermal vent metagenome" ]
[ 7, 42629, 1, 1 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 61, 151, 57, 38, 44, 70 ]
6
true
Domain
Zona pellucida domain
Zona pellucida domain
ZP_dom
3
IPR001508
1,508
Ionotropic glutamate receptor, metazoa
Iono_Glu_rcpt_met
Family
36,326
false
false
Ionotropic glutamate receptors (iGluRs) are a highly conserved family of ligand-gated ion channels present in animals, plants, and bacteria, which are best characterised for their roles in synaptic communication in vertebrate nervous systems [ ]. A variant subfamily of iGluRs, the Ionotropic Receptors (IRs), consist of...
[ "GO:0005216", "GO:0038023", "GO:0006811", "GO:0016020" ]
[ "monoatomic ion channel activity", "signaling receptor activity", "monoatomic ion transport", "membrane" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR00177" ]
[ "NMDARECEPTOR" ]
[ 36326 ]
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-204005", "R-CEL-399710", "R-CEL-438066", "R-CEL-5694530", "R-CEL-8849932", "R-CFA-3928662", "R-CFA-438066", "R-CFA-5673001", "R-CFA-8849932", "R-CFA-9609736", "R-DME-204005", "R-DME-3928662", "R-DME-399710", "R-DME-416993", "R-DME-438066", "R-DME-5694530", "R-DME-8849932", "...
[ "REACTOME:R-CEL-204005", "REACTOME:R-CEL-399710", "REACTOME:R-CEL-438066", "REACTOME:R-CEL-5694530", "REACTOME:R-CEL-8849932", "REACTOME:R-CFA-3928662", "REACTOME:R-CFA-438066", "REACTOME:R-CFA-5673001", "REACTOME:R-CFA-8849932", "REACTOME:R-CFA-9609736", "REACTOME:R-DME-204005", "REACTOME:R-D...
63
[ "3kg2", "4pe5", "4tll", "4tlm", "4u1w", "4u1x", "4u1y", "4u2p", "4u2q", "4u4f", "4u4g", "4u5b", "4u5c", "4u5d", "4u5e", "4u5f", "4uq6", "4uqj", "4uqk", "4uqq", "5fxg", "5fxh", "5fxi", "5fxj", "5fxk", "5ide", "5idf", "5iou", "5iov", "5ipq", "5ipr", "5ips"...
317
[ "PUB00001634", "PUB00072709", "PUB00072710" ]
[ "1532151", "14977400", "20808886" ]
[ "Cloning, expression and modulation of a mouse NMDA receptor subunit.", "Structure and function of glutamate receptor ion channels.", "Ancient protostome origin of chemosensory ionotropic glutamate receptors and the evolution of insect taste and olfaction." ]
[ 1992, 2004, 2010 ]
3
[ "IPR015683" ]
[]
1
0
1
[ "Bacteria", "Eukaryota" ]
[ 18, 36308 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 14, 222, 37, 91, 71, 102 ]
6
true
Family
Ionotropic glutamate receptor, metazoa
Ionotropic glutamate receptor, metazoa
Iono_Glu_rcpt_met
1
IPR001509
1,509
NAD-dependent epimerase/dehydratase
Epimerase_deHydtase
Domain
304,090
false
false
This domain is found in proteins that utilise NAD as a cofactor and use nucleotide-sugar substrates for a variety of chemical reactions [ ]. One of the best studied of these proteins is UDP-galactose 4-epimerase which catalyses the conversion of UDP-galactose to UDP-glucose during galactose metabolism [ , ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF01370" ]
[ "Epimerase" ]
[ 304090 ]
1
[ "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1260", "GenProp1429", "GenProp1546", "R-BTA-611105", "R-BTA-6799198", "R-CEL-6787639", "R-CEL-70370", "R-DDI-6787639", "R-DME-6787639", "R-HSA-611105", "R-HSA-6787639", "R-HSA-6799198", "R-MMU-6787639" ]
[ "GP:GenProp1260", "GP:GenProp1429", "GP:GenProp1546", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-6799198", "REACTOME:R-CEL-6787639", "REACTOME:R-CEL-70370", "REACTOME:R-DDI-6787639", "REACTOME:R-DME-6787639", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-6787639", "REACTOME:R-HSA-6799198", "REACTOM...
13
[ "1a9y", "1a9z", "1bsv", "1bws", "1e6u", "1e7q", "1e7r", "1e7s", "1eq2", "1fxs", "1gfs", "1gy8", "1i24", "1i2b", "1i2c", "1kvq", "1kvr", "1kvs", "1kvt", "1kvu", "1lrj", "1lrk", "1lrl", "1nah", "1nai", "1qrr", "1sb8", "1sb9", "1u9j", "1uda", "1udb", "1udc"...
450
[ "PUB00000446", "PUB00024593", "PUB00025849" ]
[ "9174344", "10801319", "11279032" ]
[ "Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli.", "Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.", "Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site." ]
[ 1997, 2000, 2001 ]
3
[]
[ "IPR045869" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 6011, 218928, 73870, 211, 5070 ]
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",...
[ 199, 6, 19, 19, 7, 27, 13, 12, 182, 14, 5, 4, 337 ]
13
true
Domain
NAD-dependent epimerase/dehydratase
NAD-dependent epimerase/dehydratase
Epimerase_deHydtase
3
IPR001510
1,510
Zinc finger, PARP-type
Znf_PARP
Domain
9,557
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:0003677", "GO:0008270" ]
[ "DNA binding", "zinc ion binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "PROSITE", "PROFILE", "SMART" ]
[ "PF00645", "PS00347", "PS50064", "SM01336" ]
[ "zf-PARP", "ZF_PARP_1", "ZF_PARP_2", "zf-PARP" ]
[ 7456, 3024, 9013, 8395 ]
4
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.4.2.-", "2.4.2.30", "PWY-5381", "PWY-5800", "PWY-6148", "PWY-6720", "PWY-7018", "PWY-7025", "PWY-7450", "PWY-7817", "PWY-7981", "PDOC00360", "R-CEL-5696394", "R-CEL-5696395", "R-CEL-5696400", "R-DME-110362", "R-DME-2173795", "R-DME-3108214", "R-DME-5685939", "R-DME-5696394",...
[ "EC:2.4.2.-", "EC:2.4.2.30", "METACYC:PWY-5381", "METACYC:PWY-5800", "METACYC:PWY-6148", "METACYC:PWY-6720", "METACYC:PWY-7018", "METACYC:PWY-7025", "METACYC:PWY-7450", "METACYC:PWY-7817", "METACYC:PWY-7981", "PROSITEDOC:PDOC00360", "REACTOME:R-CEL-5696394", "REACTOME:R-CEL-5696395", "RE...
57
[ "1uw0", "1v9x", "2cs2", "2dmj", "2l30", "2l31", "2n8a", "3od8", "3oda", "3odc", "3ode", "4av1", "4dqy", "4opx", "4oqa", "4oqb", "7s68", "7s6h", "7s6m", "7s81", "8g0h" ]
21
[ "PUB00003624", "PUB00003699", "PUB00005417", "PUB00014077", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]
[ "3118181", "7760816", "8016868", "12665246", "17210253", "15963892", "15718139", "10529348", "11179890" ]
[ "ADP-ribosylation of proteins. Enzymology and biological significance.", "Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination.", "Poly(ADP-ribose) polymerase: a molecular nick-sensor.", "Zinc fingers--folds for man...
[ 1987, 1995, 1994, 2002, 2007, 2005, 2005, 1999, 2001 ]
9
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 2, 82, 9456, 11, 6 ]
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", "Schizosaccharomyces pombe (stra...
[ 11, 2, 54, 1, 14, 18, 1, 4, 9, 2, 14 ]
11
true
Domain
Zinc finger, PARP-type
Zinc finger, PARP-type
Znf_PARP
5
IPR001512
1,512
Somatostatin receptor 4
Somatstn_rcpt_4
Family
404
false
false
Somatostatin (SST), also known as somatotropin release-inhibiting factor (SRIF), is a hypothalamic hormone, a pancreatic hormone, and a central and peripheral neurotransmitter. Somatostatin has a wide distribution throughout the central nervous system (CNS) as well as in peripheral tissues, for example in the pituitary...
[ "GO:0004994", "GO:0007186", "GO:0016020" ]
[ "somatostatin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00590" ]
[ "SOMATOSTTN4R" ]
[ 404 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "358", "R-HSA-375276", "R-HSA-418594", "R-MMU-375276", "R-MMU-418594", "R-RNO-375276", "R-RNO-418594" ]
[ "IUPHAR:358", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594" ]
7
[ "7xms", "7xmt" ]
2
[ "PUB00013316", "PUB00063572", "PUB00063590", "PUB00063595", "PUB00063596", "PUB00063597", "PUB00063598", "PUB00063599", "PUB00063600", "PUB00063601", "PUB00063602", "PUB00063603", "PUB00063604", "PUB00063605", "PUB00063619", "PUB00063626", "PUB00063627" ]
[ "14507421", "10433861", "7792934", "8243278", "8078491", "7907795", "1346068", "8483934", "15361490", "10598790", "1328199", "7538774", "9426226", "8684611", "8034040", "14966206", "10804219" ]
[ "Somatostatin receptors.", "Somatostatin and its receptor family.", "Classification and nomenclature of somatostatin receptors.", "Tissue distribution of somatostatin receptor subtype messenger ribonucleic acid in the rat.", "Characterization of cloned human somatostatin receptor SSTR5.", "Stimulation of ...
[ 2003, 1999, 1995, 1993, 1994, 1994, 1992, 1993, 2004, 1999, 1992, 1995, 1997, 1996, 1994, 2004, 2000 ]
17
[ "IPR000586" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 404 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 2, 2 ]
3
true
Family
Somatostatin receptor 4
Somatostatin receptor 4
Somatstn_rcpt_4
3
IPR001513
1,513
Adenosine A2A receptor
Adeno_A2A_rcpt
Family
1,015
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor signaling pathway", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR00553" ]
[ "ADENOSINA2AR" ]
[ 1015 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "19", "R-CFA-417973", "R-CFA-5683826", "R-HSA-187024", "R-HSA-417973", "R-HSA-418555", "R-HSA-5683826", "R-MMU-417973", "R-MMU-418555", "R-MMU-5683826", "R-RNO-417973", "R-RNO-5683826" ]
[ "IUPHAR:19", "REACTOME:R-CFA-417973", "REACTOME:R-CFA-5683826", "REACTOME:R-HSA-187024", "REACTOME:R-HSA-417973", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-5683826", "REACTOME:R-MMU-417973", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-5683826", "REACTOME:R-RNO-417973", "REACTOME:R-RNO-5683826" ]
12
[ "2ydo", "2ydv", "3pwh", "3rey", "3rfm", "3uza", "3uzc", "3vg9", "3vga", "4eiy", "4ug2", "4uhr", "5g53", "5iu4", "5iu7", "5iu8", "5iua", "5iub", "5jtb", "5k2a", "5k2b", "5k2c", "5k2d", "5mzj", "5mzp", "5n2r", "5nlx", "5nm2", "5nm4", "5olg", "5olh", "5olo"...
89
[ "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
[ "IPR001634" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 1015 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 11, 3, 4 ]
4
true
Family
Adenosine A2A receptor
Adenosine A2A receptor
Adeno_A2A_rcpt
4
IPR001514
1,514
DNA-directed RNA polymerase, 30-40kDa subunit, conserved site
DNA-dir_RNA_pol_30-40kDasu_CS
Conserved_site
8,020
false
false
DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerase...
[ "GO:0003677", "GO:0003899", "GO:0006351" ]
[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PROSITE" ]
[ "PS00446" ]
[ "RNA_POL_D_30KD" ]
[ 8020 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.7.6", "PDOC00411", "R-BTA-112382", "R-BTA-113418", "R-BTA-5250924", "R-BTA-5578749", "R-BTA-674695", "R-BTA-6781823", "R-BTA-6782135", "R-BTA-6782210", "R-BTA-6796648", "R-BTA-6803529", "R-BTA-6807505", "R-BTA-72086", "R-BTA-72163", "R-BTA-72165", "R-BTA-72203", "R-BTA-73762",...
[ "EC:2.7.7.6", "PROSITEDOC:PDOC00411", "REACTOME:R-BTA-112382", "REACTOME:R-BTA-113418", "REACTOME:R-BTA-5250924", "REACTOME:R-BTA-5578749", "REACTOME:R-BTA-674695", "REACTOME:R-BTA-6781823", "REACTOME:R-BTA-6782135", "REACTOME:R-BTA-6782210", "REACTOME:R-BTA-6796648", "REACTOME:R-BTA-6803529",...
153
[ "1i3q", "1i50", "1i6h", "1k83", "1nik", "1nt9", "1pqv", "1r5u", "1r9s", "1r9t", "1sfo", "1twa", "1twc", "1twf", "1twg", "1twh", "1wcm", "1y1v", "1y1w", "1y1y", "1y77", "2b63", "2b8k", "2e2h", "2e2i", "2e2j", "2ja5", "2ja6", "2ja7", "2ja8", "2nvq", "2nvt"...
533
[ "PUB00000061", "PUB00002623", "PUB00004429", "PUB00013994", "PUB00013995", "PUB00033173" ]
[ "3052291", "2187864", "8367291", "12860379", "12694606", "10499798" ]
[ "Structure and function of bacterial sigma factors.", "The amino acid sequence of the human RNA polymerase II 33-kDa subunit hRPB 33 is highly conserved among eukaryotes.", "Subunits of the Schizosaccharomyces pombe RNA polymerase II: enzyme purification and structure of the subunit 3 gene.", "Functional inte...
[ 1988, 1990, 1993, 2003, 2003, 1999 ]
6
[]
[]
0
0
null
[ "Archaea", "Eukaryota", "metagenomes" ]
[ 652, 7351, 17 ]
3
[ "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)", "...
[ 14, 2, 2, 14, 7, 1, 7, 9, 2, 2, 8 ]
11
true
Conserved_site
DNA-directed RNA polymerase, 30-40kDa subunit, conserved site
DNA-directed RNA polymerase, 30-40kDa subunit, conserved site
DNA-dir_RNA_pol_30-40kDasu_CS
6
IPR001515
1,515
Large ribosomal subunit protein eL32
Ribosomal_eL32
Family
7,692
false
false
eL32 is a protein from the large ribosomal subunit that contains a surface-exposed globular domain and a finger-like projection that extends into the RNA core to stabilize the tertiary structure. eL32 does not appear to play a role in forming the A (aminacyl), P (peptidyl) or E (exit) sites of the ribosome, but does in...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER", "SMART", "CDD" ]
[ "PF01655", "PTHR23413", "SM01393", "cd00513" ]
[ "Ribosomal_L32e", "", "Ribosomal_L32e", "Ribosomal_L32_L32e" ]
[ 7682, 7413, 7633, 7051 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00502", "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CFA-156827", "R-CFA-1799339", "R-CFA-6791226", "R-CFA-72689", "R-CFA-72706", "R-CFA-975956", "R-CFA-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-72689...
[ "PROSITEDOC:PDOC00502", "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-CFA-156827", "REACTOME:R-CFA-1799339", "REACTOME:R-CFA-6791226", "REACTOME:R-CFA-72...
73
[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...
680
[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00028498", "PUB00079483", "PUB00079521", "PUB00079522", "PUB00079523", "PUB00079524" ]
[ "11297922", "11290319", "11114498", "10937989", "10937990", "12082018", "16452584", "16516201", "11904172" ]
[ "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.", "The structural basis of ribosome activity in peptide bond synthesis.", ...
[ 2001, 2001, 2000, 2000, 2000, 2002, 2006, 2006, 2002 ]
9
[]
[ "IPR023654" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 947, 5, 6708, 32 ]
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...
[ 4, 2, 2, 4, 5, 3, 1, 11, 8, 1, 2, 16 ]
12
true
Family
Large ribosomal subunit protein eL32
Large ribosomal subunit protein eL32
Ribosomal_eL32
2
IPR001516
1,516
NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal
Proton_antipo_N
Domain
98,427
false
false
Mrp-type antiporters comprise the cation/proton antiporter family 3 (CPA3), commonly referred to as Mrp. They are the products of operons that carry either six or seven genes (mrpA-G), and form complexes containing all subunits [ , ]. They have Na(+)/H(+) antiporter activity [ ]. Two of the Mrp proteins, MrpA and MrpD,...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00662" ]
[ "Proton_antipo_N" ]
[ 98427 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "7.1.1", "R-DME-5419276", "R-DME-611105", "R-DME-6799198", "R-DRE-611105", "R-GGA-5419276", "R-GGA-611105", "R-GGA-6799198", "R-HSA-5419276", "R-HSA-611105", "R-HSA-6799198", "R-HSA-9837999", "R-MMU-5419276", "R-MMU-611105", "R-MMU-6799198", "R-RNO-5419276", "R-RNO-611105", "R-RNO-...
[ "EC:7.1.1", "REACTOME:R-DME-5419276", "REACTOME:R-DME-611105", "REACTOME:R-DME-6799198", "REACTOME:R-DRE-611105", "REACTOME:R-GGA-5419276", "REACTOME:R-GGA-611105", "REACTOME:R-GGA-6799198", "REACTOME:R-HSA-5419276", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-6799198", "REACTOME:R-HSA-9837999", ...
21
[ "3rko", "4he8", "4hea", "4wz7", "5gpn", "5gup", "5lc5", "5ldw", "5ldx", "5lnk", "5o31", "5xtc", "5xtd", "5xth", "5xti", "6cfw", "6g2j", "6g72", "6gcs", "6h8k", "6hum", "6i0d", "6i1p", "6khi", "6khj", "6l7o", "6l7p", "6nbq", "6nbx", "6nby", "6q8o", "6q8w"...
308
[ "PUB00009994", "PUB00072925", "PUB00072926", "PUB00072927", "PUB00072928", "PUB00072929", "PUB00072930", "PUB00072931", "PUB00072932" ]
[ "10751389", "24142251", "15980940", "18408029", "12914915", "20826797", "12460669", "20595580", "9387241" ]
[ "The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases.", "Purification and functional reconstitution of a seven-subunit mrp-type na+/h+ antiporter.", "The Mrp system: a giant among monovalent cation/proton antiporters?", "Single gene deletions...
[ 2000, 2014, 2005, 2008, 2003, 2010, 2002, 2010, 1997 ]
9
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1380, 33886, 62480, 681 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 15, 1, 11, 3, 1668, 11, 3, 4, 9, 8 ]
10
true
Domain
NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal
NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal
Proton_antipo_N
6
IPR001518
1,518
Argininosuccinate synthase
Arginosuc_synth
Family
29,901
false
false
Argininosuccinate synthase ( ) (AS) is a urea cycle enzyme that catalyses the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate [ , ]. In humans, a defect in the AS gene causes citrullinemia, a genetic disease characterised ...
[ "GO:0004055", "GO:0005524", "GO:0006526" ]
[ "argininosuccinate synthase activity", "ATP binding", "L-arginine biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PANTHER", "NCBIFAM" ]
[ "PTHR11587", "TIGR00032" ]
[ "", "argG" ]
[ 29880, 26535 ]
2
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.3.4.5", "GenProp0117", "GenProp1300", "GenProp1320", "GenProp1481", "PWY-4983", "PWY-4984", "PWY-5", "PWY-5154", "PWY-7400", "PDOC00488", "R-BTA-70635", "R-HSA-70635", "R-MMU-70635" ]
[ "EC:6.3.4.5", "GP:GenProp0117", "GP:GenProp1300", "GP:GenProp1320", "GP:GenProp1481", "METACYC:PWY-4983", "METACYC:PWY-4984", "METACYC:PWY-5", "METACYC:PWY-5154", "METACYC:PWY-7400", "PROSITEDOC:PDOC00488", "REACTOME:R-BTA-70635", "REACTOME:R-HSA-70635", "REACTOME:R-MMU-70635" ]
14
[ "1j1z", "1j20", "1j21", "1k92", "1k97", "1kh1", "1kh2", "1kh3", "1kor", "1kp2", "1kp3", "1vl2", "2nz2", "4nzp", "4u7j", "4xfj", "5us8", "6e5y", "6xnq", "7k5z" ]
20
[ "PUB00001799", "PUB00002066" ]
[ "2123815", "3133361" ]
[ "Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals.", "Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina bark...
[ 1990, 1988 ]
2
[]
[ "IPR023434", "IPR023437" ]
0
2
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 843, 23367, 2, 5027, 662 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae...
[ 4, 1, 1, 1, 10, 3, 2, 6, 3, 1, 1, 11 ]
12
true
Family
Argininosuccinate synthase
Argininosuccinate synthase
Arginosuc_synth
3
IPR001519
1,519
Ferritin
Ferritin
Family
21,213
false
false
Ferritin is one of the major non-haem iron storage proteins in animals, plants, and microorganisms [ , ]. It consists of a mineral core of hydrated ferric oxide, and a multi-subunit protein shell which encloses the former and assures its solubility in an aqueous environment. In animals the protein is mainly cytoplasmic...
[ "GO:0008199", "GO:0006826", "GO:0006879" ]
[ "ferric iron binding", "iron ion transport", "intracellular iron ion homeostasis" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PANTHER" ]
[ "PTHR11431" ]
[ "" ]
[ 21213 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.16.3", "R-BTA-6798695", "R-BTA-917937", "R-CFA-432722", "R-CFA-6798695", "R-CFA-917937", "R-GGA-432722", "R-GGA-6798695", "R-GGA-917937", "R-HSA-1222449", "R-HSA-3000480", "R-HSA-432722", "R-HSA-6798695", "R-HSA-917937", "R-MMU-432722", "R-MMU-6798695", "R-MMU-917937", "R-RNO-43...
[ "EC:1.16.3", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-917937", "REACTOME:R-CFA-432722", "REACTOME:R-CFA-6798695", "REACTOME:R-CFA-917937", "REACTOME:R-GGA-432722", "REACTOME:R-GGA-6798695", "REACTOME:R-GGA-917937", "REACTOME:R-HSA-1222449", "REACTOME:R-HSA-3000480", "REACTOME:R-HSA-432722", ...
20
[ "1aew", "1bg7", "1dat", "1eum", "1fha", "1gwg", "1h96", "1hrs", "1ier", "1ies", "1krq", "1lb3", "1mfr", "1r03", "1rcc", "1rcd", "1rce", "1rcg", "1rci", "1s3q", "1sq3", "1vlg", "1xz1", "1xz3", "1z4a", "1z6o", "2cei", "2chi", "2cih", "2clu", "2cn6", "2cn7"...
541
[ "PUB00000049", "PUB00001349", "PUB00002586" ]
[ "3304136", "3032619", "2211706" ]
[ "Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms.", "Iron transport and storage.", "Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean." ]
[ 1987, 1987, 1990 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 266, 8995, 11848, 2, 102 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 19, 2, 15, 7, 1, 26, 24, 9, 44, 16 ]
10
true
Family
Ferritin
Ferritin
Ferritin
6
IPR001521
1,521
Opsin, blue sensitive
Opsin_blue
Family
2,367
false
false
Opsins are the photoreceptors of animal retinas: vertebrate rhodopsin is found in rod cells and mediates scotopic vision; red, green and blue opsins are found in cone cells and mediate photopic vision. Blue-sensitive opsin has an absorption maximum at 420nm. The ratio of blue cones to rods is ~1:200. Deficiency in blue...
[ "GO:0007186", "GO:0007602", "GO:0016020" ]
[ "G protein-coupled receptor signaling pathway", "phototransduction", "membrane" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00574" ]
[ "OPSINBLUE" ]
[ 2367 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-2187335", "R-BTA-418594", "R-BTA-419771", "R-DRE-2187335", "R-DRE-418594", "R-DRE-419771", "R-HSA-2187335", "R-HSA-418594", "R-HSA-419771", "R-HSA-9918443", "R-MMU-2187335", "R-MMU-418594", "R-MMU-419771", "R-RNO-2187335", "R-RNO-418594", "R-RNO-419771" ]
[ "REACTOME:R-BTA-2187335", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-419771", "REACTOME:R-DRE-2187335", "REACTOME:R-DRE-418594", "REACTOME:R-DRE-419771", "REACTOME:R-HSA-2187335", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-419771", "REACTOME:R-HSA-9918443", "REACTOME:R-MMU-2187335", "REACTOME:R-MM...
16
[ "8y02" ]
1
[]
[]
[]
[]
0
[ "IPR001760" ]
[]
1
0
1
[ "Bilateria" ]
[ 2367 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 2, 3, 4 ]
4
true
Family
Opsin, blue sensitive
Opsin, blue sensitive
Opsin_blue
5
IPR001522
1,522
Fatty acid desaturase type 1, conserved site
FADS-1_CS
Conserved_site
5,972
false
false
Fatty acid desaturases are enzymes that catalyse the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related. Family 1 is composed of: Stearoyl-CoA desaturase (SCD) ( ) [ ]. Family 2 is composed of: Ba...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00476" ]
[ "FATTY_ACID_DESATUR_1" ]
[ 5972 ]
1
[ "EC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.14.19.1", "PWY-5987", "PWY-5996", "PDOC00399", "R-BTA-75105", "R-HSA-2426168", "R-HSA-75105", "R-HSA-9029558", "R-HSA-9619665", "R-HSA-9841922", "R-MMU-75105", "R-RNO-75105", "R-SCE-75105", "R-SPO-75105", "R-SSC-75105" ]
[ "EC:1.14.19.1", "METACYC:PWY-5987", "METACYC:PWY-5996", "PROSITEDOC:PDOC00399", "REACTOME:R-BTA-75105", "REACTOME:R-HSA-2426168", "REACTOME:R-HSA-75105", "REACTOME:R-HSA-9029558", "REACTOME:R-HSA-9619665", "REACTOME:R-HSA-9841922", "REACTOME:R-MMU-75105", "REACTOME:R-RNO-75105", "REACTOME:R-...
15
[ "4ymk", "4zyo", "6wf2" ]
3
[ "PUB00002505", "PUB00004074", "PUB00004734", "PUB00098457", "PUB00098458" ]
[ "2570068", "2118597", "2006187", "32470559", "26098317" ]
[ "Differentiation-induced gene expression in 3T3-L1 preadipocytes. A second differentially expressed gene encoding stearoyl-CoA desaturase.", "Enhancement of chilling tolerance of a cyanobacterium by genetic manipulation of fatty acid desaturation.", "Stearoyl-acyl-carrier-protein desaturase from higher plants i...
[ 1989, 1990, 1991, 2020, 2015 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "hydrothermal vent metagenome" ]
[ 22, 5949, 1 ]
3
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 3, 5, 4, 6, 11, 1, 1 ]
7
true
Conserved_site
Fatty acid desaturase type 1, conserved site
Fatty acid desaturase type 1, conserved site
FADS-1_CS
5
IPR001523
1,523
Paired domain
Paired_dom
Domain
20,359
false
false
The paired domain is an approximately 126 amino acid DNA-binding domain, which is found in eukaryotic transcription regulatory proteins involved in embryogenesis. The domain was originally described as the 'paired box' in the Drosophila protein paired (prd) [ , ]. The paired domain is generally located in the N-termina...
[ "GO:0003677", "GO:0006355" ]
[ "DNA binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS", "PROFILE", "SMART", "CDD" ]
[ "PF00292", "PR00027", "PS51057", "SM00351", "cd00131" ]
[ "PAX", "PAIREDBOX", "PAIRED_2", "PAX", "PAX" ]
[ 19862, 17936, 19885, 19060, 14194 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00034", "R-CEL-8939245", "R-DME-3214847", "R-DME-8939245", "R-HSA-210745", "R-HSA-210746", "R-HSA-3214847", "R-HSA-381771", "R-HSA-400511", "R-HSA-5617472", "R-HSA-8939245", "R-HSA-9761174", "R-HSA-9823739", "R-HSA-9830364", "R-HSA-9830674", "R-HSA-9834899", "R-HSA-9856649", "...
[ "PROSITEDOC:PDOC00034", "REACTOME:R-CEL-8939245", "REACTOME:R-DME-3214847", "REACTOME:R-DME-8939245", "REACTOME:R-HSA-210745", "REACTOME:R-HSA-210746", "REACTOME:R-HSA-3214847", "REACTOME:R-HSA-381771", "REACTOME:R-HSA-400511", "REACTOME:R-HSA-5617472", "REACTOME:R-HSA-8939245", "REACTOME:R-HS...
19
[ "1k78", "1mdm", "1pdn", "2k27", "6pax" ]
5
[ "PUB00000810", "PUB00001887", "PUB00017868", "PUB00017869", "PUB00017870" ]
[ "2877747", "3123319", "10811620", "11103953", "15148315" ]
[ "Conservation of a large protein domain in the segmentation gene paired and in functionally related genes of Drosophila.", "Structure of two genes at the gooseberry locus related to the paired gene and their spatial expression during Drosophila embryogenesis.", "Transcriptional repression by Pax5 (BSAP) through...
[ 1986, 1987, 2000, 2000, 2004 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 338, 20015, 6 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 10, 150, 35, 69, 60, 40 ]
6
true
Domain
Paired domain
Paired domain
Paired_dom
7
IPR001524
1,524
Glycoside hydrolase, family 6, conserved site
Glyco_hydro_6_CS
Conserved_site
6,568
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
[ "PROSITE", "PROSITE" ]
[ "PS00655", "PS00656" ]
[ "GLYCOSYL_HYDROL_F6_1", "GLYCOSYL_HYDROL_F6_2" ]
[ 4690, 3714 ]
2
[ "CAZY", "EC", "METACYC", "PROSITEDOC" ]
[ "GH6", "3.2.1.91", "PWY-6788", "PDOC00563" ]
[ "CAZY:GH6", "EC:3.2.1.91", "METACYC:PWY-6788", "PROSITEDOC:PDOC00563" ]
4
[ "1bvw", "1cb2", "1dys", "1gz1", "1hgw", "1hgy", "1oc5", "1oc6", "1oc7", "1ocb", "1ocj", "1ocn", "1qjw", "1qk0", "1qk2", "1tml", "2bod", "2boe", "2bof", "2bog", "2bvw", "3a64", "3a9b", "3abx", "3cbh", "3vog", "3voh", "3voi", "3voj", "4a05", "4au0", "4avo"...
67
[ "PUB00004870", "PUB00005130", "PUB00005266" ]
[ "7624375", "2377893", "8535779" ]
[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei.", "Structures and mechanisms of glycosyl hydrolases." ]
[ 1995, 1990, 1995 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Streptomyces phage Gilgamesh", "unclassified sequences" ]
[ 4577, 1986, 1, 4 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 3 ]
1
true
Conserved_site
Glycoside hydrolase, family 6, conserved site
Glycoside hydrolase, family 6, conserved site
Glyco_hydro_6_CS
5
IPR001525
1,525
C-5 cytosine methyltransferase
C5_MeTfrase
Family
57,486
false
false
C-5 cytosine-specific DNA methylases ( ) (C5 Mtase) are enzymes that specifically methylate the C-5 carbon of cytosines in DNA to produce C5-methylcytosine [ , , ]. In mammalian cells, cytosine-specific methyltransferases methylate certain CpG sequences, which are believed to modulate gene expression and cell different...
[ "GO:0008168" ]
[ "methyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROFILE", "NCBIFAM" ]
[ "PF00145", "PR00105", "PS51679", "TIGR00675" ]
[ "DNA_methylase", "C5METTRFRASE", "SAM_MT_C5", "dcm" ]
[ 57449, 37703, 47436, 28338 ]
4
[ "EC", "EC", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.1.1", "2.1.1.37", "GenProp0767", "PDOC00089", "R-HSA-212300", "R-HSA-3214858", "R-HSA-427413", "R-HSA-4655427", "R-HSA-5334118", "R-HSA-6782315", "R-HSA-9701898", "R-HSA-9710421", "R-HSA-9725371", "R-HSA-9845323", "R-MMU-212300", "R-MMU-3214858", "R-MMU-4655427", "R-RNO-212300",...
[ "EC:2.1.1", "EC:2.1.1.37", "GP:GenProp0767", "PROSITEDOC:PDOC00089", "REACTOME:R-HSA-212300", "REACTOME:R-HSA-3214858", "REACTOME:R-HSA-427413", "REACTOME:R-HSA-4655427", "REACTOME:R-HSA-5334118", "REACTOME:R-HSA-6782315", "REACTOME:R-HSA-9701898", "REACTOME:R-HSA-9710421", "REACTOME:R-HSA-9...
20
[ "10mh", "1dct", "1fjx", "1g55", "1hmy", "1m0e", "1mht", "1skm", "1svu", "2c7o", "2c7p", "2c7q", "2c7r", "2hmy", "2hr1", "2i9k", "2qrv", "2uyc", "2uyh", "2uz4", "2z6a", "2z6q", "2z6u", "2zcj", "3av4", "3av5", "3av6", "3eeo", "3g7u", "3lx6", "3me5", "3mht"...
140
[ "PUB00000896", "PUB00001090", "PUB00001771", "PUB00003244", "PUB00004446", "PUB00058132" ]
[ "8343957", "7773746", "3248729", "2716049", "8127644", "16424344" ]
[ "Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine.", "DNA modification by methyltransferases.", "Sequence motifs specific for cytosine methyltransferases.", "Cytosine-specific type II DNA methyltransferases. A conserved enzyme core with variable target-recognizing dom...
[ 1993, 1995, 1988, 1989, 1994, 2006 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 634, 32550, 22113, 1150, 1039 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pomb...
[ 54, 56, 3, 1, 34, 16, 2, 16, 20, 1, 85 ]
11
true
Family
C-5 cytosine methyltransferase
C-5 cytosine methyltransferase
C5_MeTfrase
3
IPR001528
1,528
Flavivirus non-structural protein NS4B
Flavi_NS4B
Domain
11,522
false
false
Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. The NS4B protein is small and poorly conserved among the Flaviviruses. NS4B contains multiple hydrophobic potential membrane spanning regions [ ]. NS4B may form membrane components of the viral replication...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01349" ]
[ "Flavi_NS4B" ]
[ 11522 ]
1
[ "EC", "EC", "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.1.1.56", "2.1.1.57", "2.7.7.48", "3.4.21.91", "3.6.1.15", "3.6.4.13", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210", "PWY-7375", "PWY-7379" ]
[ "EC:2.1.1.56", "EC:2.1.1.57", "EC:2.7.7.48", "EC:3.4.21.91", "EC:3.6.1.15", "EC:3.6.4.13", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7185", "METACYC:PWY-7198", "METACYC:PWY-7210", "METACYC:PWY-7375", "METACYC:PWY-7379" ]
13
[ "8cxg", "8cxh", "8cxi" ]
3
[ "PUB00000118" ]
[ "2174669" ]
[ "Flavivirus genome organization, expression, and replication." ]
[ 1990 ]
1
[]
[]
0
0
null
[ "Levilactobacillus bambusae", "Orthornavirae" ]
[ 1, 11521 ]
2
[]
[]
0
true
Domain
Flavivirus non-structural protein NS4B
Flavivirus non-structural protein NS4B
Flavi_NS4B
6
IPR001529
1,529
DNA-directed RNA polymerase II subunit RPB9-like, zinc ribbon
Zn_ribbon_RPB9
Domain
10,102
false
false
This entry represents a zinc ribbon domain found at the terminal of DNA-directed RNA polymerase II subunit RPB9, DNA-directed RNA polymerase III subunit RPC10, archaeal Transcription factor S and similar sequences. RPB9 is the core component of RNA polymerase II, the central component of the basal RNA polymerase II tra...
[ "GO:0006351" ]
[ "DNA-templated transcription" ]
[ "biological_process" ]
1
[ "PFAM", "SMART" ]
[ "PF02150", "SM00661" ]
[ "Zn_ribbon_RPB9", "RPOL9" ]
[ 8655, 9551 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00790", "R-CEL-112382", "R-CEL-113418", "R-CEL-5578749", "R-CEL-674695", "R-CEL-6781823", "R-CEL-6782135", "R-CEL-6782210", "R-CEL-6796648", "R-CEL-6803529", "R-CEL-6807505", "R-CEL-72086", "R-CEL-72163", "R-CEL-72165", "R-CEL-72203", "R-CEL-73776", "R-CEL-73779", "R-CEL-75953...
[ "PROSITEDOC:PDOC00790", "REACTOME:R-CEL-112382", "REACTOME:R-CEL-113418", "REACTOME:R-CEL-5578749", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-6781823", "REACTOME:R-CEL-6782135", "REACTOME:R-CEL-6782210", "REACTOME:R-CEL-6796648", "REACTOME:R-CEL-6803529", "REACTOME:R-CEL-6807505", "REACTOME:R-C...
173
[ "1i3q", "1i50", "1i6h", "1k83", "1nik", "1nt9", "1pqv", "1r5u", "1r9s", "1r9t", "1sfo", "1twa", "1twc", "1twf", "1twg", "1twh", "1wcm", "1y1v", "1y1w", "1y1y", "1y77", "2b63", "2b8k", "2e2h", "2e2i", "2e2j", "2ja5", "2ja6", "2ja7", "2ja8", "2nvq", "2nvt"...
501
[ "PUB00000061", "PUB00003685", "PUB00004438", "PUB00009536", "PUB00033173", "PUB00078615", "PUB00099662", "PUB00099663", "PUB00103730", "PUB00155993" ]
[ "3052291", "8417319", "8265347", "10777522", "10499798", "15130130", "33335104", "33558764", "30190596", "30584594" ]
[ "Structure and function of bacterial sigma factors.", "Gene RRN4 in Saccharomyces cerevisiae encodes the A12.2 subunit of RNA polymerase I and is essential only at high temperatures.", "Structure of the gene encoding the 14.5 kDa subunit of human RNA polymerase II.", "Transcription factor S, a cleavage induct...
[ 1988, 1993, 1993, 2000, 1999, 2004, 2020, 2021, 2018, 2018 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Imitervirales", "metagenomes" ]
[ 1333, 236, 8453, 3, 77 ]
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...
[ 15, 2, 2, 5, 3, 6, 3, 13, 7, 3, 3, 17 ]
12
true
Domain
DNA-directed RNA polymerase II subunit RPB9-like, zinc ribbon
DNA-directed RNA polymerase II subunit RPB9-like, zinc ribbon
Zn_ribbon_RPB9
5
IPR001530
1,530
Geminivirus BR1 coat protein
Gemini_BR1
Family
1,521
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:0003697", "GO:0051027", "GO:0043657" ]
[ "single-stranded DNA binding", "DNA transport", "host cell" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00225" ]
[ "GEMCOATBR1" ]
[ 1521 ]
1
[]
[]
[]
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
[ "IPR000263" ]
[]
1
0
1
[ "Pentapetalae", "Pilimelia anulata", "Viruses" ]
[ 16, 2, 1503 ]
3
[]
[]
0
true
Family
Geminivirus BR1 coat protein
Geminivirus BR1 coat protein
Gemini_BR1
3
IPR001531
1,531
Zinc-dependent phospholipase C
Zn_PLipaseC
Domain
1,440
false
false
Bacillus cereus contains a monomeric phospholipase C (PLC) of 245 amino-acid residues that binds three zinc ions [ ]. Although PLC prefers to act on phosphatidylcholine, it also shows weak catalytic activity with sphingomyelin and phosphatidylinositol [ ]. Sequence studies have shown the PLC protein to be similar to th...
[ "GO:0004629", "GO:0008270" ]
[ "C-type glycerophospholipase activity", "zinc ion binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS", "PROSITE", "PROFILE", "SMART", "CDD" ]
[ "PR00479", "PS00384", "PS51346", "SM00770", "cd11009" ]
[ "PRPHPHLPASEC", "PROKAR_ZN_DEPEND_PLPC_1", "PROKAR_ZN_DEPEND_PLPC_2", "Zn_dep_PLPC", "Zn_dep_PLPC" ]
[ 811, 605, 1300, 1172, 951 ]
5
[ "EC", "METACYC", "METACYC", "METACYC", "PROSITEDOC" ]
[ "3.1.4.3", "PWY-7782", "PWY-7783", "PWY-8052", "PDOC00357" ]
[ "EC:3.1.4.3", "METACYC:PWY-7782", "METACYC:PWY-7783", "METACYC:PWY-8052", "PROSITEDOC:PDOC00357" ]
5
[ "1ah7", "1ca1", "1gyg", "1kho", "1olp", "1p5x", "1p6d", "1p6e", "1qm6", "1qmd", "2ffz", "2fgn", "2huc", "2wxt", "2wxu", "2wy6", "8cqm" ]
17
[ "PUB00001364", "PUB00001724", "PUB00002023", "PUB00002026", "PUB00004043", "PUB00023881" ]
[ "2841128", "2111259", "2536355", "1309513", "2493587", "9699639" ]
[ "Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus.", "The role of histidine residues in the alpha toxin of Clostridium perfringens.", "Molecular cloning and nucleotide sequence of the alpha-toxin (phospholipase C) of Clostridium perfringens.", "...
[ 1988, 1990, 1989, 1992, 1989, 1998 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Myoviridae sp. ctYA416", "metagenomes" ]
[ 45, 1364, 21, 1, 9 ]
5
[]
[]
0
true
Domain
Zinc-dependent phospholipase C
Zinc-dependent phospholipase C
Zn_PLipaseC
1
IPR001534
1,534
Transthyretin-like
Transthyretin-like
Family
5,415
false
false
Transthyretin-related proteins form a nematode-specific expanded protein family that comprises 59 members, 54 of which are predicted to be secreted. The proteins show weak similarity to transthyretin (formerly called prealbumin) which transports thyroid hormones. [ ]. Some transthyretin-related genes are induced in res...
[ "GO:0009986" ]
[ "cell surface" ]
[ "cellular_component" ]
1
[ "PFAM", "PANTHER" ]
[ "PF01060", "PTHR21700" ]
[ "TTR-52", "" ]
[ 5328, 4904 ]
2
[]
[]
[]
0
[ "3uaf" ]
1
[ "PUB00001984", "PUB00088242", "PUB00093975" ]
[ "9417907", "20526330", "29346382" ]
[ "Analysis of protein domain families in Caenorhabditis elegans.", "Caenorhabditis elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor.", "6-OHDA-induced dopaminergic neurodegeneration in Caenorhabditis elegans is promoted by the engulfment pathway an...
[ 1997, 2010, 2018 ]
3
[]
[]
0
0
null
[ "Bacteria", "Protostomia", "ecological metagenomes" ]
[ 4, 5409, 2 ]
3
[ "Caenorhabditis elegans" ]
[ 67 ]
1
true
Family
Transthyretin-like
Transthyretin-like
Transthyretin-like
5
IPR001537
1,537
tRNA/rRNA methyltransferase, SpoU type
SpoU_MeTrfase
Domain
113,970
false
false
This entry represents a domain found in the spoU protein from E. coli that shows strong similarities to previously characterised 2'-O-methyltransferases [ , ]. The Mrm1 protein of Saccharomyces cerevisiae has been shown to be required for ribose methylation at a universally conserved nucleotide in the peptidyl transfer...
[ "GO:0003723", "GO:0008173", "GO:0006396" ]
[ "RNA binding", "RNA methyltransferase activity", "RNA processing" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF00588" ]
[ "SpoU_methylase" ]
[ 113970 ]
1
[ "EC", "REACTOME" ]
[ "2.1.1", "R-HSA-6793080" ]
[ "EC:2.1.1", "REACTOME:R-HSA-6793080" ]
2
[ "1gz0", "1ipa", "1j85", "1mxi", "1v2x", "1x7o", "1x7p", "1zjr", "2ha8", "2i6d", "3e5y", "3gyq", "3ic6", "3ilk", "3kty", "3l8u", "3n4j", "3n4k", "3nk6", "3nk7", "3onp", "4cnd", "4cne", "4cnf", "4cng", "4jak", "4jal", "4kdz", "4kgn", "4pzk", "4x3l", "4x3m"...
63
[ "PUB00004439", "PUB00004481", "PUB00006298" ]
[ "8265370", "9321663", "8266080" ]
[ "SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases.", "The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2'-O-methyltransferase activity.", "Functional requirement of a site-specific ribose methylation in ribosomal RNA." ]
[ 1993, 1997, 1993 ]
3
[]
[ "IPR044748", "IPR047261" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 830, 98998, 12277, 10, 1855 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 37, 2, 13, 3, 6, 4, 3, 1, 19, 7, 2, 1, 48 ]
13
true
Domain
tRNA/rRNA methyltransferase, SpoU type
tRNA/rRNA methyltransferase, SpoU type
SpoU_MeTrfase
1
IPR001538
1,538
Mannose-6-phosphate isomerase, type II, C-terminal
Man6P_isomerase-2_C
Domain
15,476
false
false
The type II phosphomannose isomerases are bifunctional enzymes . This entry covers the isomerase region of the protein [ ]. The guanosine diphospho-D-mannose pyrophosphorylase region is described in another InterPro entry (see ). Mannose-6-phosphate isomerase or phosphomannose isomerase ( ) (PMI) is the enzyme that cat...
[ "GO:0016779", "GO:0005976" ]
[ "nucleotidyltransferase activity", "polysaccharide metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF01050" ]
[ "MannoseP_isomer" ]
[ 15476 ]
1
[ "EC", "METACYC" ]
[ "2.7.7.13", "PWY-5659" ]
[ "EC:2.7.7.13", "METACYC:PWY-5659" ]
2
[]
0
[ "PUB00000676", "PUB00001448", "PUB00007419" ]
[ "9507048", "8307007", "11165500" ]
[ "Domain organisation in phosphomannose isomerases (types I and II).", "Purification, cDNA cloning and heterologous expression of human phosphomannose isomerase.", "JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta." ]
[ 1998, 1994, 2001 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 270, 14788, 30, 19, 369 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Mannose-6-phosphate isomerase, type II, C-terminal
Mannose-6-phosphate isomerase, type II, C-terminal
Man6P_isomerase-2_C
2
IPR001539
1,539
Peptidase U32
Peptidase_U32
Family
30,673
false
false
This is a group of peptidases belonging to MEROPS peptidase family U32 (clan U-). They are classified as collagenases as they are present in bacterial collagenases, involved in bacterial infection. For example, Porphyromonas gingivalis PrtC (Bacteroides gingivalis) [ ], is an enzyme that degrades type I collagen and th...
[]
[]
[]
0
[ "PROSITE", "PANTHER" ]
[ "PS01276", "PTHR30217" ]
[ "PEPTIDASE_U32", "" ]
[ 19247, 30669 ]
2
[ "PROSITEDOC" ]
[ "PDOC00982" ]
[ "PROSITEDOC:PDOC00982" ]
1
[]
0
[ "PUB00002182", "PUB00094342", "PUB00094343", "PUB00094522" ]
[ "1317840", "29069499", "31289180", "31253794" ]
[ "Sequence analysis and characterization of the Porphyromonas gingivalis prtC gene, which expresses a novel collagenase activity.", "Biogenesis and iron-dependency of ribosomal RNA hydroxylation.", "Ubiquinone Biosynthesis over the Entire O2 Range: Characterization of a Conserved O2-Independent Pathway.", "Dua...
[ 1992, 2017, 2019, 2019 ]
4
[]
[ "IPR043692", "IPR043693" ]
0
2
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 560, 29449, 53, 149, 462 ]
5
[ "Escherichia coli (strain K12)" ]
[ 4 ]
1
true
Family
Peptidase U32
Peptidase U32
Peptidase_U32
7
IPR001542
1,542
Defensin, invertebrate/fungal
Defensin_invertebrate/fungal
Domain
1,482
false
false
Arthropod defensins are a family of insect and scorpion cysteine-rich antibacterial peptides, primarily active against Gram-positive bacteria [ , , , , ]. All these peptides range in length from 38 to 51 amino acids. There are six conserved cysteines all involved in intrachain disulphide bonds. A schematic representati...
[ "GO:0006952" ]
[ "defense response" ]
[ "biological_process" ]
1
[ "PFAM", "PROFILE" ]
[ "PF01097", "PS51378" ]
[ "Defensin_2", "INVERT_DEFENSINS" ]
[ 1344, 1272 ]
2
[]
[]
[]
0
[ "1fjn", "1i2u", "1i2v", "1ica", "1l4v", "1ozz", "1p00", "1p0a", "1zfu", "2b68", "2e3e", "2e3f", "2e3g", "2koz", "2lld", "2ln4", "2lr5", "2lt8", "2ny8", "2ny9", "2nz3", "2rty", "2ru0", "3e7r", "3e7u", "5xa6", "6b9w", "6bam", "6bb6", "6k50", "6k51", "6px8"...
40
[ "PUB00000525", "PUB00001431", "PUB00001593", "PUB00002559", "PUB00002677", "PUB00004678" ]
[ "8471044", "1425705", "2401368", "2358464", "1761552", "2911573" ]
[ "Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin.", "A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata).", "1H nuclear ma...
[ 1993, 1992, 1990, 1990, 1991, 1989 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanofollis aquaemaris" ]
[ 43, 1438, 1 ]
3
[ "Caenorhabditis elegans", "Drosophila melanogaster", "Zea mays" ]
[ 1, 2, 4 ]
3
true
Domain
Defensin, invertebrate/fungal
Defensin, invertebrate/fungal
Defensin_invertebrate/fungal
1
IPR001543
1,543
Flagellar motor switch protein FliN-like, C-terminal domain
FliN-like_C
Domain
31,053
false
false
This entry represents the C-terminal region of Flagellar motor switch proteins FliN and FliM and similar proteins mainly found in bacteria. This domain seems to play a key role in flagellation [ ]. The flagellar motor switch in Escherichia coli and Salmonella typhimurium regulates the direction of flagellar rotation an...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01052" ]
[ "FliMN_C" ]
[ 31053 ]
1
[]
[]
[]
0
[ "1o6a", "1o9y", "1yab", "3uep", "4tt9", "4yx1", "4yx5", "4yx7", "4yxa", "4yxb", "4yxc", "5xrw", "8umd", "8umx", "8uox", "8upl", "8vib", "8vid", "8vkq", "8vkr", "8wiw", "8wo5", "8woe", "8xp0", "8xp1", "8yjt", "9n49", "9n4z" ]
28
[ "PUB00001834", "PUB00002083", "PUB00002290", "PUB00003825", "PUB00003876", "PUB00004790", "PUB00006273", "PUB00099915" ]
[ "8224881", "2656645", "8631704", "1447979", "8885278", "1631122", "1312536", "29991595" ]
[ "Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG.", "Flagellar switch of Salmonella typhimurium: gene sequences and deduced protein sequences.", "A mutational analysis of the interaction between FliG and FliM, two compone...
[ 1993, 1989, 1996, 1992, 1996, 1992, 1992, 2018 ]
8
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 30642, 36, 375 ]
3
[ "Escherichia coli (strain K12)", "Zea mays" ]
[ 2, 1 ]
2
true
Domain
Flagellar motor switch protein FliN-like, C-terminal domain
Flagellar motor switch protein FliN-like, C-terminal domain
FliN-like_C
8
IPR001544
1,544
Aminotransferase class IV
Aminotrans_IV
Family
81,107
false
false
Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [ ] into subfamilies. This entry represents a subfamily of a...
[ "GO:0003824" ]
[ "catalytic activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF01063" ]
[ "Aminotran_4" ]
[ 81107 ]
1
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.6.1", "GenProp1328", "GenProp1332", "GenProp1334", "GenProp1467", "GenProp1533", "GenProp1667", "GenProp1673", "GenProp1708", "GenProp1727", "PDOC00618", "R-BTA-70895", "R-CEL-70895", "R-DDI-70895", "R-HSA-70895", "R-MMU-70895", "R-RNO-70895", "R-SCE-70895", "R-SPO-70895" ]
[ "EC:2.6.1", "GP:GenProp1328", "GP:GenProp1332", "GP:GenProp1334", "GP:GenProp1467", "GP:GenProp1533", "GP:GenProp1667", "GP:GenProp1673", "GP:GenProp1708", "GP:GenProp1727", "PROSITEDOC:PDOC00618", "REACTOME:R-BTA-70895", "REACTOME:R-CEL-70895", "REACTOME:R-DDI-70895", "REACTOME:R-HSA-70...
19
[ "1a0g", "1a3g", "1daa", "1ekf", "1ekp", "1ekv", "1et0", "1g2w", "1i1k", "1i1l", "1i1m", "1i2k", "1i2l", "1iyd", "1iye", "1kt8", "1kta", "1wrv", "2a1h", "2abj", "2cog", "2coi", "2coj", "2daa", "2dab", "2eiy", "2ej0", "2ej2", "2ej3", "2hdk", "2hg8", "2hgw"...
164
[ "PUB00000425", "PUB00002195", "PUB00002360", "PUB00088724", "PUB00089640", "PUB00151494" ]
[ "7626635", "1644759", "9163511", "22998630", "27705900", "33950161" ]
[ "Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity.", "Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme.", "Three-dimensional structure of Escherichia coli branched-chain a...
[ 1995, 1992, 1997, 2012, 2017, 2021 ]
6
[]
[ "IPR005784", "IPR017824", "IPR033939" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1194, 60023, 18461, 9, 1420 ]
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",...
[ 73, 2, 15, 1, 2, 8, 11, 4, 39, 19, 3, 2, 49 ]
13
true
Family
Aminotransferase class IV
Aminotransferase class IV
Aminotrans_IV
1
IPR001545
1,545
Gonadotropin, beta subunit
Gonadotropin_bsu
Family
4,588
false
false
The crystal structures of four growth factors; nerve growth factor, transforming growth factor-beta, platelet-derived growth factor, and human chorionic gonadotropin from four separate superfamilies revealed that these proteins are structurally related and share a common overall topology [ ]. These proteins show very l...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PANTHER", "SMART", "CDD" ]
[ "PTHR11515", "SM00068", "cd00069" ]
[ "", "GHB", "GHB_like" ]
[ 4461, 4202, 4418 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00234", "R-BTA-193048", "R-BTA-193993", "R-BTA-209822", "R-BTA-209968", "R-BTA-375281", "R-BTA-418555", "R-BTA-8866910", "R-BTA-975578", "R-GGA-209822", "R-GGA-209968", "R-GGA-375281", "R-GGA-418555", "R-HSA-193048", "R-HSA-193993", "R-HSA-209822", "R-HSA-209968", "R-HSA-37528...
[ "PROSITEDOC:PDOC00234", "REACTOME:R-BTA-193048", "REACTOME:R-BTA-193993", "REACTOME:R-BTA-209822", "REACTOME:R-BTA-209968", "REACTOME:R-BTA-375281", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-8866910", "REACTOME:R-BTA-975578", "REACTOME:R-GGA-209822", "REACTOME:R-GGA-209968", "REACTOME:R-GGA-375...
43
[ "1fl7", "1hcn", "1hrp", "1qfw", "1xwd", "4ay9", "4mqw", "6p57", "7fig", "7fih", "7fii", "7t9i", "7utz", "7xw5", "8enb", "8end", "8enf", "8i2g" ]
18
[ "PUB00000033", "PUB00000091", "PUB00000517", "PUB00000890", "PUB00001089", "PUB00004177" ]
[ "6267989", "7663117", "1445230", "8490958", "7583638", "8202136" ]
[ "Glycoprotein hormones: structure and function.", "The cystine-knot growth-factor superfamily.", "Molecular structures of glycoprotein hormones and functions of their carbohydrate components.", "A structural superfamily of growth factors containing a cystine knot motif.", "Cystine knots.", "Crystal struct...
[ 1981, 1995, 1992, 1993, 1995, 1994 ]
6
[]
[]
0
0
null
[ "Eumetazoa" ]
[ 4588 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 11, 5, 26, 11, 14 ]
6
true
Family
Gonadotropin, beta subunit
Gonadotropin, beta subunit
Gonadotropin_bsu
4
IPR001546
1,546
GPCR fungal pheromone A receptor
GPCR_Pheromne_A_rcpt
Family
769
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:0004933", "GO:0007186", "GO:0016020" ]
[ "mating-type a-factor pheromone receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00900" ]
[ "PHEROMONEAR" ]
[ 769 ]
1
[]
[]
[]
0
[]
0
[ "PUB00000868", "PUB00001139", "PUB00004338", "PUB00004657", "PUB00004961", "PUB00005669", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "1310895", "16453635", "3001640", "2836861", "8170923", "7913746", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "The a mating type locus of U. maydis specifies cell signaling components.", "Nucleotide sequences of STE2 and STE3, cell type-specific sterile genes from Saccharomyces cerevisiae.", "The yeast alpha-factor receptor: structural properties deduced from the sequence of the STE2 gene.", "STE2 protein of Saccharo...
[ 1992, 1985, 1985, 1988, 1994, 1994, 2003, 1994, 2005, 2009, 2006, 2013 ]
12
[ "IPR001499" ]
[]
1
0
1
[ "Fungi" ]
[ 769 ]
1
[]
[]
0
true
Family
GPCR fungal pheromone A receptor
GPCR fungal pheromone A receptor
GPCR_Pheromne_A_rcpt
4
IPR001548
1,548
Peptidase M2, peptidyl-dipeptidase A
Peptidase_M2
Family
9,027
false
false
This group of metallopeptidases belong to the MEROPS peptidase family M2 (clan MA(E)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA. The catalytic residues and zinc ligands have been identified, the zinc ion being ligated to two His resi...
[ "GO:0008237", "GO:0008241", "GO:0006508", "GO:0016020" ]
[ "metallopeptidase activity", "peptidyl-dipeptidase activity", "proteolysis", "membrane" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PRINTS", "PROFILE", "PANTHER", "CDD" ]
[ "PF01401", "PR00791", "PS52011", "PTHR10514", "cd06461" ]
[ "Peptidase_M2", "PEPDIPTASEA", "PEPTIDASE_M2", "", "M2_ACE" ]
[ 8984, 7657, 8702, 8779, 7447 ]
5
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp2085", "R-BTA-2022377", "R-CEL-2022377", "R-DME-2022377", "R-GGA-2022377", "R-HSA-2022377", "R-HSA-9678110", "R-HSA-9679191", "R-HSA-9694614", "R-HSA-9733458", "R-MMU-2022377", "R-RNO-2022377", "R-SSC-2022377" ]
[ "GP:GenProp2085", "REACTOME:R-BTA-2022377", "REACTOME:R-CEL-2022377", "REACTOME:R-DME-2022377", "REACTOME:R-GGA-2022377", "REACTOME:R-HSA-2022377", "REACTOME:R-HSA-9678110", "REACTOME:R-HSA-9679191", "REACTOME:R-HSA-9694614", "REACTOME:R-HSA-9733458", "REACTOME:R-MMU-2022377", "REACTOME:R-RNO-...
13
[ "1j36", "1j37", "1j38", "1o86", "1o8a", "1r42", "1r4l", "1uze", "1uzf", "2ajf", "2c6f", "2c6n", "2iul", "2iux", "2oc2", "2x8y", "2x8z", "2x90", "2x91", "2x92", "2x93", "2x94", "2x95", "2x96", "2x97", "2xhm", "2xy9", "2xyd", "2ydm", "3bkk", "3bkl", "3d0g"...
547
[ "PUB00000029", "PUB00002699", "PUB00003579", "PUB00021878", "PUB00029342", "PUB00034625", "PUB00039907", "PUB00042150", "PUB00050670", "PUB00082168", "PUB00120172", "PUB00153259", "PUB00153260", "PUB00153261", "PUB00153262", "PUB00153263", "PUB00153264", "PUB00153265" ]
[ "9629165", "1851160", "7674922", "12633854", "12540854", "14754895", "16476442", "17439247", "18457420", "17464936", "15175004", "16329762", "18464595", "14559923", "33146371", "19021774", "16403023", "26380810" ]
[ "Toward a role for angiotensin-converting enzyme in insects.", "The two homologous domains of human angiotensin I-converting enzyme are both catalytically active.", "Evolutionary families of metallopeptidases.", "Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril...
[ 1998, 1991, 1995, 2003, 2003, 2004, 2006, 2007, 2008, 2007, 2004, 2005, 2008, 2003, 2020, 2008, 2006, 2015 ]
18
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 1662, 7319, 46 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 5, 12, 26, 16, 15 ]
6
true
Family
Peptidase M2, peptidyl-dipeptidase A
Peptidase M2, peptidyl-dipeptidase A
Peptidase_M2
2
IPR001550
1,550
Transcription antiterminator, conserved site
Transcrpt_antitermin_CS
Conserved_site
1,800
false
false
This is a family of bacterial proteins related to the Escherichia coli BglG protein. E. coli BglG protein mediates the positive regulation of the beta-glucoside (bgl) operon by functioning as a transcriptional antiterminator [ ]. BglG is an RNA-binding protein that recognises a specific sequence located just upstream o...
[ "GO:0003723", "GO:0045893" ]
[ "RNA binding", "positive regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00654" ]
[ "PRD_1" ]
[ 1800 ]
1
[ "PROSITEDOC" ]
[ "PDOC00562" ]
[ "PROSITEDOC:PDOC00562" ]
1
[ "1h99", "1tlv", "3rio" ]
3
[ "PUB00000837", "PUB00005131" ]
[ "1698125", "2200123" ]
[ "Transcriptional antitermination in the bgl operon of E. coli is modulated by a specific RNA binding protein.", "Regulation of activity of a transcriptional anti-terminator in E. coli by phosphorylation in vivo." ]
[ 1990, 1990 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 1795, 2, 3 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Conserved_site
Transcription antiterminator, conserved site
Transcription antiterminator, conserved site
Transcrpt_antitermin_CS
2
IPR001551
1,551
Cannabinoid receptor type 2
Canbinoid_rcpt_2
Family
198
false
false
Cannabinoid receptors are a class of cell membrane receptors that belong to the rhodopsin-like G-protein coupled receptor (GPCR) family [ , , ]. Typical of G protein-coupled receptors, cannabinoid receptors contain seven transmembrane spanning domains [ ]. Cannabinoid receptors are activated by three major groups of li...
[ "GO:0004949", "GO:0007186", "GO:0016020" ]
[ "cannabinoid receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00523" ]
[ "CANABINOID2R" ]
[ 198 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "57", "R-HSA-373076", "R-HSA-418594", "R-MMU-373076", "R-MMU-418594", "R-RNO-373076", "R-RNO-418594" ]
[ "IUPHAR:57", "REACTOME:R-HSA-373076", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-373076", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-373076", "REACTOME:R-RNO-418594" ]
7
[ "6kpf", "6pt0", "8guq", "8gur", "8gus", "8gut", "8x3l" ]
7
[ "PUB00068045", "PUB00068114", "PUB00068115", "PUB00068116", "PUB00068117", "PUB00068118", "PUB00068119", "PUB00068120", "PUB00068121", "PUB00068126", "PUB00068127", "PUB00068139", "PUB00068140", "PUB00068141", "PUB00068142", "PUB00068143", "PUB00068144", "PUB00068145", "PUB000681...
[ "21079038", "12432948", "18426493", "19273110", "6268916", "5538858", "7565624", "2165569", "7689702", "8819477", "9721036", "21295074", "7556170", "8647116", "7651369", "7605349", "22048769", "10022233", "8937419", "14657172", "18291574" ]
[ "International Union of Basic and Clinical Pharmacology. LXXIX. Cannabinoid receptors and their ligands: beyond CB₁ and CB₂.", "The cannabinoid receptors.", "Cannabinoid receptors: where they are and what they do.", "Cannabinoid receptors: a brief history and \"what's hot\".", "Behavioral comparisons of the...
[ 2010, 2002, 2008, 2009, 1981, 1971, 1995, 1990, 1993, 1996, 1998, 2011, 1995, 1996, 1995, 1995, 2011, 1998, 1996, 2003, 2008 ]
21
[ "IPR002230" ]
[]
1
0
1
[ "Theria" ]
[ 198 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 4 ]
3
true
Family
Cannabinoid receptor type 2
Cannabinoid receptor type 2
Canbinoid_rcpt_2
7
IPR001554
1,554
Glycoside hydrolase, family 14
Glyco_hydro_14
Family
7,511
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:0016161", "GO:0000272" ]
[ "beta-amylase activity", "polysaccharide catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF01373", "PR00750", "PTHR31352" ]
[ "Glyco_hydro_14", "BETAAMYLASE", "" ]
[ 7453, 6904, 7396 ]
3
[ "CAZY", "EC", "GP", "METACYC", "METACYC", "PROSITEDOC" ]
[ "GH14", "3.2.1.2", "GenProp1726", "PWY-6724", "PWY-842", "PDOC00414" ]
[ "CAZY:GH14", "EC:3.2.1.2", "GP:GenProp1726", "METACYC:PWY-6724", "METACYC:PWY-842", "PROSITEDOC:PDOC00414" ]
6
[ "1b1y", "1b90", "1b9z", "1bfn", "1btc", "1bya", "1byb", "1byc", "1byd", "1fa2", "1itc", "1j0y", "1j0z", "1j10", "1j11", "1j12", "1j18", "1q6c", "1q6d", "1q6e", "1q6f", "1q6g", "1uko", "1ukp", "1v3h", "1v3i", "1vem", "1ven", "1veo", "1vep", "1wdp", "1wdq"...
52
[ "PUB00001450", "PUB00002337", "PUB00002354", "PUB00004870", "PUB00005062", "PUB00005234", "PUB00005266" ]
[ "8174545", "2474529", "1491009", "7624375", "2464171", "2457058", "8535779" ]
[ "Residues essential for catalytic activity of soybean beta-amylase.", "Identification of glutamic acid 186 affinity-labeled by 2,3-epoxypropyl alpha-D-glucopyranoside in soybean beta-amylase.", "Three-dimensional structure of soybean beta-amylase determined at 3.0 A resolution: preliminary chain tracing of the ...
[ 1994, 1989, 1992, 1995, 1988, 1988, 1995 ]
7
[]
[ "IPR000125", "IPR001371" ]
0
2
0
[ "Bacteria", "Eukaryota" ]
[ 264, 7247 ]
2
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 39, 30, 84 ]
3
true
Family
Glycoside hydrolase, family 14
Glycoside hydrolase, family 14
Glyco_hydro_14
3
IPR001555
1,555
Phosphoribosylglycinamide formyltransferase, active site
GART_AS
Active_site
33,531
false
false
Phosphoribosylglycinamide formyltransferase ( ) (GART) [ ] catalyses the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. In higher eukaryotes, GART is part of a multifunctional enzyme polypeptide that catalyses three of the steps of purine biosynthesis. In bact...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00373" ]
[ "GART" ]
[ 33531 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.1.2.9", "PDOC00319", "R-BTA-73817", "R-DME-73817", "R-GGA-419140", "R-HSA-196757", "R-HSA-73817", "R-MMU-196757", "R-MMU-73817", "R-RNO-196757", "R-XTR-196757" ]
[ "EC:2.1.2.9", "PROSITEDOC:PDOC00319", "REACTOME:R-BTA-73817", "REACTOME:R-DME-73817", "REACTOME:R-GGA-419140", "REACTOME:R-HSA-196757", "REACTOME:R-HSA-73817", "REACTOME:R-MMU-196757", "REACTOME:R-MMU-73817", "REACTOME:R-RNO-196757", "REACTOME:R-XTR-196757" ]
11
[ "1c2t", "1c3e", "1cdd", "1cde", "1fmt", "1gar", "1grc", "1jkx", "1mej", "1men", "1meo", "1njs", "1rbm", "1rbq", "1rby", "1rbz", "1rc0", "1rc1", "1s3i", "1zlx", "1zly", "2bw0", "2cfi", "2fmt", "2gar", "3auf", "3av3", "3gar", "3p9x", "3q0i", "3r8x", "3tqq"...
74
[ "PUB00000327", "PUB00002186", "PUB00002683" ]
[ "2204419", "1624424", "1848231" ]
[ "Active-site mapping and site-specific mutagenesis of glycinamide ribonucleotide transformylase from Escherichia coli.", "Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli.", "Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofol...
[ 1990, 1992, 1991 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 396, 27221, 5498, 6, 410 ]
5
[ "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...
[ 7, 1, 6, 5, 2, 18, 8, 7, 11, 1, 1, 2 ]
12
true
Active_site
Phosphoribosylglycinamide formyltransferase, active site
Phosphoribosylglycinamide formyltransferase, active site
GART_AS
3
IPR001556
1,556
Bombesin receptor-like
Bombsn_rcpt-like
Family
3,026
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:0008528", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled peptide receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00358" ]
[ "BOMBESINR" ]
[ 3026 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-416476", "R-HSA-375276", "R-HSA-416476", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476", "R-SSC-375276", "R-SSC-416476" ]
[ "REACTOME:R-DME-416476", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476", "REACTOME:R-SSC-375276", "REACTOME:R-SSC-416476" ]
9
[ "7w41", "8h0p", "8h0q", "8y51", "8y52", "8y53", "9jf4", "9k07", "9lwp" ]
9
[ "PUB00000131", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816", "PUB00099716", "PUB00099719" ]
[ "2111655", "2830256", "8386361", "8170923", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293", "34539578", "25517020" ]
[ "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, 2021, 2015 ]
12
[ "IPR000276" ]
[ "IPR000401", "IPR001560", "IPR001642", "IPR001966" ]
1
4
0
[ "Eumetazoa" ]
[ 3026 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 3, 5, 6, 7 ]
5
true
Family
Bombesin receptor-like
Bombesin receptor-like
Bombsn_rcpt-like
1
IPR001558
1,558
HIV negative factor Nef
HIV_Nef
Family
43,152
false
false
Human immunodeficiency virus 1 (HIV-1) negative factor (Nef protein) accelerates virulent progression of acquired immunodeficiency syndrome (AIDS) by its interaction with specific cellular proteins involved in signal transduction and host cell activation. Nef has been shown to bind specifically to a subset of the Src f...
[ "GO:0005525" ]
[ "GTP binding" ]
[ "molecular_function" ]
1
[ "HAMAP", "PFAM" ]
[ "MF_04078", "PF00469" ]
[ "NEF_HIV", "F-protein" ]
[ 28656, 43152 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-162585", "R-HSA-162588", "R-HSA-162599", "R-HSA-164939", "R-HSA-164940", "R-HSA-164944", "R-HSA-167590", "R-HSA-173107", "R-HSA-175474", "R-HSA-182218" ]
[ "REACTOME:R-HSA-162585", "REACTOME:R-HSA-162588", "REACTOME:R-HSA-162599", "REACTOME:R-HSA-164939", "REACTOME:R-HSA-164940", "REACTOME:R-HSA-164944", "REACTOME:R-HSA-167590", "REACTOME:R-HSA-173107", "REACTOME:R-HSA-175474", "REACTOME:R-HSA-182218" ]
10
[ "1avv", "1avz", "1efn", "2nef", "2xi1", "3ik5", "3ioz", "3rbb", "3rea", "3reb", "3tb8", "4d8d", "4emz", "4en2", "4nee", "4orz", "4u5w", "5nuh", "5nui", "6b72", "6cm9", "6cri", "6d83", "6d84", "6dff", "6k6m", "6k6n", "6owt", "6uri", "7d7s", "7ux3", "8d4c"...
43
[ "PUB00005286" ]
[ "9351809" ]
[ "The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Cercopithecus neglectus", "Qipengyuania pelagi", "Retroviridae" ]
[ 1, 1, 43150 ]
3
[]
[]
0
true
Family
HIV negative factor Nef
HIV negative factor Nef
HIV_Nef
9
IPR001559
1,559
Phosphotriesterase
Phosphotriesterase
Family
8,264
false
false
Bacteria such as Brevundimonas diminuta (Pseudomonas diminuta) harbour a plasmid that carries the gene for phosphotriesterase (PTE also known as parathion hydrolase; ). This enzyme has attracted interest because of its potential use in the detoxification of chemical waste and organophosphate warfare agents such as VX, ...
[ "GO:0008270", "GO:0009056" ]
[ "zinc ion binding", "catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "PROFILE", "PANTHER", "CDD" ]
[ "PF02126", "PIRSF016839", "PS51347", "PTHR10819", "cd00530" ]
[ "PTE", "PhP", "PHOSPHOTRIESTERASE_2", "", "PTE" ]
[ 8224, 3514, 8124, 8153, 3110 ]
5
[ "PROSITEDOC" ]
[ "PDOC01026" ]
[ "PROSITEDOC:PDOC01026" ]
1
[ "1bf6", "1dpm", "1eyw", "1ez2", "1hzy", "1i0b", "1i0d", "1jgm", "1p6b", "1p6c", "1psc", "1pta", "1qw7", "2d2g", "2d2h", "2d2j", "2o4m", "2o4q", "2ob3", "2oql", "2r1k", "2r1l", "2r1m", "2r1n", "2r1p", "2vc5", "2vc7", "2zc1", "3a3w", "3a3x", "3a4j", "3c86"...
174
[ "PUB00000454", "PUB00000987", "PUB00080091", "PUB00080092", "PUB00080093", "PUB00080094", "PUB00080095", "PUB00085013", "PUB00085014" ]
[ "9548740", "9383406", "10858282", "8396425", "9314115", "11170459", "7867909", "24955762", "15909078" ]
[ "Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family.", "Evolution in action.", "Self-assembly of the binuclear metal center of phosphotriesterase.", "Structural characterization of the divalent cation sites of bacterial phosphotri...
[ 1998, 1995, 2000, 1993, 1997, 2001, 1994, 2014, 2005 ]
9
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 53, 6413, 1650, 148 ]
4
[ "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 1, 1, 2, 3, 4 ]
6
true
Family
Phosphotriesterase
Phosphotriesterase
Phosphotriesterase
1
IPR001560
1,560
Bombesin receptor type 3
Bombesin_rcpt_3
Family
435
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:0004946", "GO:0031989", "GO:0016020" ]
[ "bombesin receptor activity", "bombesin receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00637" ]
[ "BOMBESIN3R" ]
[ 435 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "40", "R-HSA-375276", "R-HSA-416476", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476" ]
[ "IUPHAR:40", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476" ]
7
[ "8y51", "8y52", "8y53", "9k07", "9lwp" ]
5
[ "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
[ "IPR001556" ]
[]
1
0
1
[ "Amniota" ]
[ 435 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 3 ]
3
true
Family
Bombesin receptor type 3
Bombesin receptor type 3
Bombesin_rcpt_3
7
IPR001561
1,561
Influenza matrix M1, N-terminal
Flu_matrix_M1_N
Domain
70,262
false
false
Matrix protein (M1) of influenza virus is a bifunctional membrane/RNA-binding protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. It is therefore required that M1 binds both membrane and RNA simultaneously [ ]. M1 is comprised of two domains connected by a linker sequence. The...
[ "GO:0003723", "GO:0005198" ]
[ "RNA binding", "structural molecule activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF00598" ]
[ "Flu_M1" ]
[ 70262 ]
1
[ "GP", "REACTOME", "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-168316", "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-168316", "REACTOME:R-HSA-168330", "REACTOME:R-HSA-168333", "REACTOME:R-HSA-168336", "REACTOME:R-HSA-192823" ]
12
[ "1aa7", "1ea3", "2z16", "3md2", "3vdx", "4d9j", "4iq4", "4itv", "4ivj", "4pus", "4qes", "4qf0", "4qff", "5cqe", "5v6g", "5v7b", "5v7s", "5v8a", "6i3h", "6z5j", "6z5l", "7jm3" ]
22
[ "PUB00003941", "PUB00024486" ]
[ "9164466", "11162800" ]
[ "Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1.", "Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer." ]
[ 1997, 2001 ]
2
[]
[]
0
0
null
[ "Bacteria", "Capsicum baccatum", "Orthomyxoviridae" ]
[ 12, 1, 70249 ]
3
[]
[]
0
true
Domain
Influenza matrix M1, N-terminal
Influenza matrix M1, N-terminal
Flu_matrix_M1_N
7
IPR001562
1,562
Zinc finger, Btk motif
Znf_Btk_motif
Conserved_site
9,215
false
false
The Btk-type zinc finger or Btk motif (BM) is a conserved zinc-binding motif containing conserved cysteines and a histidine that is present in certain eukaryotic signalling proteins. The motif is named after Bruton's tyrosine kinase (Btk), an enzyme which is essential for B cell maturation in humans and mice [ , ]. Btk...
[ "GO:0035556" ]
[ "intracellular signal transduction" ]
[ "biological_process" ]
1
[ "PFAM", "PRINTS", "PROFILE", "SMART" ]
[ "PF00779", "PR00402", "PS51113", "SM00107" ]
[ "BTK", "TECBTKDOMAIN", "ZF_BTK", "BTK" ]
[ 8732, 3074, 9169, 8110 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC51113", "R-DME-111465", "R-DME-1660499", "R-DME-202433", "R-DME-2424491", "R-DME-2871809", "R-DME-416476", "R-DME-416482", "R-DME-512988", "R-DME-5658442", "R-DME-8964315", "R-HSA-111465", "R-HSA-1236974", "R-HSA-1433557", "R-HSA-1660499", "R-HSA-166058", "R-HSA-202433", "R-HS...
[ "PROSITEDOC:PDOC51113", "REACTOME:R-DME-111465", "REACTOME:R-DME-1660499", "REACTOME:R-DME-202433", "REACTOME:R-DME-2424491", "REACTOME:R-DME-2871809", "REACTOME:R-DME-416476", "REACTOME:R-DME-416482", "REACTOME:R-DME-512988", "REACTOME:R-DME-5658442", "REACTOME:R-DME-8964315", "REACTOME:R-HSA...
46
[ "1b55", "1btk", "1bwn", "2e6i", "2lul", "2ys2", "2z0p", "4y93", "4y94", "6tse", "6tt2", "6tuh", "6tvn", "6yyf", "6yyg", "6yyk", "8gmb", "8s93" ]
18
[ "PUB00001301", "PUB00001677", "PUB00001711", "PUB00016999", "PUB00018545" ]
[ "9218782", "8070576", "9280283", "9796816", "15661031" ]
[ "Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: molecular explanations for X-linked agammaglobulinaemia.", "Tec homology (TH) adjacent to the PH domain.", "Missense mutations affecting a conserved cysteine pair in the TH domain of Btk.", "The G protein G alpha12 stimulates Bruton's ty...
[ 1997, 1994, 1997, 1998, 2005 ]
5
[]
[]
0
0
null
[ "Candidatus Accumulibacter phosphatis", "Eukaryota" ]
[ 1, 9214 ]
2
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 19, 3, 33, 27, 30 ]
5
true
Conserved_site
Zinc finger, Btk motif
Zinc finger, Btk motif
Znf_Btk_motif
6
IPR001564
1,564
Nucleoside diphosphate kinase
Nucleoside_diP_kinase
Family
39,866
false
false
Nucleoside diphosphate kinases ( ) (NDK) are enzymes required for the synthesis of nucleoside triphosphates (NTP) other than ATP. They provide NTPs for nucleic acid synthesis, CTP for lipid synthesis, UTP for polysaccharide synthesis and GTP for protein elongation, signal transduction and microtubule polymerisation. ND...
[ "GO:0004550", "GO:0006183", "GO:0006228", "GO:0006241" ]
[ "nucleoside diphosphate kinase activity", "GTP biosynthetic process", "UTP biosynthetic process", "CTP biosynthetic process" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process" ]
4
[ "HAMAP", "PRINTS" ]
[ "MF_00451", "PR01243" ]
[ "NDP_kinase", "NUCDPKINASE" ]
[ 28829, 39719 ]
2
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITED...
[ "2.7.4.6", "GenProp1227", "GenProp1262", "GenProp1343", "GenProp1446", "GenProp1484", "GenProp1494", "GenProp1586", "GenProp1607", "GenProp1617", "GenProp1621", "GenProp1634", "GenProp1650", "GenProp1755", "PWY-6545", "PWY-7176", "PWY-7184", "PWY-7187", "PWY-7197", "PWY-7198", ...
[ "EC:2.7.4.6", "GP:GenProp1227", "GP:GenProp1262", "GP:GenProp1343", "GP:GenProp1446", "GP:GenProp1484", "GP:GenProp1494", "GP:GenProp1586", "GP:GenProp1607", "GP:GenProp1617", "GP:GenProp1621", "GP:GenProp1634", "GP:GenProp1650", "GP:GenProp1755", "METACYC:PWY-6545", "METACYC:PWY-7176"...
83
[ "1b4s", "1b99", "1be4", "1bhn", "1bux", "1ehw", "1f3f", "1f6t", "1hhq", "1hiy", "1hlw", "1jxv", "1k44", "1kdn", "1leo", "1lwx", "1mn7", "1mn9", "1nb2", "1ncl", "1ndc", "1ndk", "1ndl", "1ndp", "1nhk", "1nlk", "1npk", "1nsk", "1nsp", "1nsq", "1nue", "1pae"...
218
[ "PUB00000847", "PUB00002696" ]
[ "2175255", "1851158" ]
[ "A Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase.", "Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme." ]
[ 1990, 1991 ]
2
[]
[ "IPR011410", "IPR012410", "IPR037994" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 892, 21027, 17360, 32, 555 ]
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",...
[ 26, 1, 28, 10, 1, 29, 27, 1, 15, 26, 1, 1, 36 ]
13
true
Family
Nucleoside diphosphate kinase
Nucleoside diphosphate kinase
Nucleoside_diP_kinase
2
IPR001565
1,565
Synaptotagmin
Synaptotagmin
Domain
23,082
false
false
Synaptotagmins are synaptic vesicle membrane proteins found in abundance in nerve cells and some endocrine cells [ , ]. The amino acid sequence of synaptotagmin comprises a single transmembrane region with a short vesicular N-terminal region, and a cytoplasmic C-terminal region containing 2 internal repeats similar to ...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR00399" ]
[ "SYNAPTOTAGMN" ]
[ 23082 ]
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-181429", "R-BTA-181430", "R-BTA-210500", "R-BTA-212676", "R-BTA-264642", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-888590", "R-CEL-181429", "R-CEL-181430", "R-CEL-210500", "R-CEL-212676", "R-CEL-264642", "R-CEL-8856825", "R-CEL-8856828", "R-CEL-888590", "R-DME-181429", "R-DME...
[ "REACTOME:R-BTA-181429", "REACTOME:R-BTA-181430", "REACTOME:R-BTA-210500", "REACTOME:R-BTA-212676", "REACTOME:R-BTA-264642", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-888590", "REACTOME:R-CEL-181429", "REACTOME:R-CEL-181430", "REACTOME:R-CEL-210500", "REACTOME:R-CEL-2...
58
[ "1byn", "1dqv", "1k5w", "1rsy", "1tjm", "1tjx", "1ugk", "1uov", "1uow", "1w15", "1w16", "2chd", "2cm5", "2cm6", "2d8k", "2enp", "2k3h", "2k45", "2k4a", "2k8m", "2ki6", "2lha", "2n1t", "2r83", "2yoa", "3f00", "3f01", "3f04", "3f05", "3fdw", "3hn8", "3n5a"...
73
[ "PUB00000918", "PUB00002879" ]
[ "7697723", "7961887" ]
[ "Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold.", "Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II." ]
[ 1995, 1994 ]
2
[]
[]
0
0
null
[ "Eukaryota", "bird metagenome" ]
[ 23081, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 14, 146, 24, 62, 56, 75 ]
6
true
Domain
Synaptotagmin
Synaptotagmin
Synaptotagmin
4
IPR001566
1,566
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD
23S_rRNA_MeTrfase_RlmD
Family
6,409
false
false
This family represents the RlmD (also known as rumA / ygcA) RNA uridine methyltransferase. In E. coli, methyltransferases are responsible for converting uridine to thymidine in rRNA and tRNAs. Among them, TrmA is responsible for tRNA U54 methylation. RlmD (assigned as YgcA previously) was first identified as a methyltr...
[ "GO:0003723", "GO:0008173", "GO:0006396" ]
[ "RNA binding", "RNA methyltransferase activity", "RNA processing" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP" ]
[ "MF_01010" ]
[ "23SrRNA_methyltr_RlmD" ]
[ 6409 ]
1
[ "EC" ]
[ "2.1.1.190" ]
[ "EC:2.1.1.190" ]
1
[ "1uwv", "2bh2" ]
2
[ "PUB00015406", "PUB00015471" ]
[ "11779873", "12907714" ]
[ "Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli.", "Identifying the methyltransferases for m(5)U747 and m(5)U1939 in 23S rRNA using MALDI mass spectrometry." ]
[ 2002, 2003 ]
2
[ "IPR010280" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 6343, 6, 60 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD
23S_rRNA_MeTrfase_RlmD
4
IPR001567
1,567
Peptidase M3A/M3B catalytic domain
Pept_M3A_M3B_dom
Domain
56,836
false
false
This group of metallopeptidases belong to MEROPS peptidase family M3 (clan MA(E)), subfamilies M3A and M3B. The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA. The Thimet oligopeptidase family, is a large family of archaeal, bacterial and euka...
[ "GO:0004222", "GO:0006508" ]
[ "metalloendopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF01432" ]
[ "Peptidase_M3" ]
[ 56836 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.24", "R-DDI-983168", "R-HSA-375276", "R-HSA-983168", "R-MMU-375276", "R-MMU-983168", "R-RNO-375276", "R-RNO-983168", "R-SCE-983168", "R-SSC-375276" ]
[ "EC:3.4.24", "REACTOME:R-DDI-983168", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-983168", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-983168", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-983168", "REACTOME:R-SCE-983168", "REACTOME:R-SSC-375276" ]
10
[ "1i1i", "1s4b", "1y79", "2h1j", "2h1n", "2o36", "2o3e", "2qr4", "3ce2", "4fxy", "4ka7", "4ka8", "4put", "5l43", "5l44", "5luz", "5lv0", "8vju", "8vjv", "8vjw", "8vjx", "8vjy" ]
22
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 492, 38838, 16951, 17, 538 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 17, 3, 12, 3, 2, 17, 10, 2, 14, 20, 2, 1, 25 ]
13
true
Domain
Peptidase M3A/M3B catalytic domain
Peptidase M3A/M3B catalytic domain
Pept_M3A_M3B_dom
3
IPR001568
1,568
Ribonuclease T2-like
RNase_T2-like
Family
18,437
false
false
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases) [ , , , , ]. Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleot...
[ "GO:0003723", "GO:0033897" ]
[ "RNA binding", "ribonuclease T2 activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "PANTHER" ]
[ "PF00445", "PTHR11240" ]
[ "Ribonuclease_T2", "" ]
[ 18419, 17270 ]
2
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.6.1.19", "PDOC00459", "R-CEL-6798695", "R-DDI-6798695", "R-DRE-6798695", "R-HSA-6798695", "R-MMU-6798695", "R-SCE-6798695" ]
[ "EC:4.6.1.19", "PROSITEDOC:PDOC00459", "REACTOME:R-CEL-6798695", "REACTOME:R-DDI-6798695", "REACTOME:R-DRE-6798695", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-6798695", "REACTOME:R-SCE-6798695" ]
8
[ "1bk7", "1bol", "1dix", "1ioo", "1iqq", "1iyb", "1j1f", "1j1g", "1jy5", "1sgl", "1uca", "1ucc", "1ucd", "1ucg", "1v9h", "1vcz", "1vd1", "1vd3", "2ea1", "2pqx", "2pqy", "2z70", "3d3z", "3t0o", "3tbj", "9iot" ]
26
[ "PUB00001381", "PUB00001640", "PUB00002342", "PUB00022764", "PUB00036440", "PUB00080049", "PUB00080050", "PUB00080051" ]
[ "2298207", "1633875", "2229029", "12731868", "10446375", "12109772", "11582795", "11158587" ]
[ "Identification of two essential histidine residues of ribonuclease T2 from Aspergillus oryzae.", "Crystal and molecular structure of RNase Rh, a new class of microbial ribonuclease from Rhizopus niveus.", "Primary structure of a base non-specific and adenylic acid preferential ribonuclease from Aspergillus sai...
[ 1990, 1992, 1990, 2003, 1999, 2002, 2001, 2001 ]
8
[]
[ "IPR033697", "IPR039378" ]
0
2
0
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 4857, 13520, 12, 48 ]
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",...
[ 24, 1, 8, 4, 1, 11, 6, 1, 27, 5, 1, 31 ]
12
true
Family
Ribonuclease T2-like
Ribonuclease T2-like
RNase_T2-like
8
IPR001569
1,569
Large ribosomal subunit protein eL37
Ribosomal_eL37
Family
6,398
false
false
A number of eukaryotic and archaeal ribosomal proteins can be grouped on the basis of sequence similarities. This family represents the large ribosomal subunit protein eL37 (also known as L37) [ ], which consists of proteins of 56 to 96 amino-acid residues that share a highly conserved region located in the N-terminal ...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PFAM" ]
[ "MF_00547", "PF01907" ]
[ "Ribosomal_eL37", "Ribosomal_L37e" ]
[ 4527, 6395 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00827", "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72706", "R-DDI-975956", "R-DDI-975957", "R-DME-156827", "R-DME-1799339", "R-DME-72689", "R-DME-72706",...
[ "PROSITEDOC:PDOC00827", "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-DDI-156827", "REACTOME:R-DDI-1799339", "REACTOME:R-DDI-72689", "REACTOME:R-DDI-7270...
59
[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...
680
[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00080279" ]
[ "11297922", "11290319", "11114498", "24524803" ]
[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "A new system for naming ribosomal proteins." ]
[ 2001, 2001, 2000, 2014 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 787, 3, 5598, 10 ]
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...
[ 11, 2, 1, 5, 3, 1, 1, 6, 5, 2, 2, 16 ]
12
true
Family
Large ribosomal subunit protein eL37
Large ribosomal subunit protein eL37
Ribosomal_eL37
3
IPR001570
1,570
Peptidase M4, C-terminal
Peptidase_M4_C_domain
Domain
15,800
false
false
This entry represents a domain found in the C-terminal of the peptidase M4 family members. This group of metallopeptidases that belong to the MEROPS peptidase family M4 (thermolysin family, clan MA(E)). The protein fold of the peptidase domain of thermolysin (MEROPS identifier M04.001), is the type example for members ...
[ "GO:0004222" ]
[ "metalloendopeptidase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02868" ]
[ "Peptidase_M4_C" ]
[ 15800 ]
1
[ "EC" ]
[ "3.4.24" ]
[ "EC:3.4.24" ]
1
[ "1bqb", "1esp", "1ezm", "1fj3", "1fjo", "1fjq", "1fjt", "1fju", "1fjv", "1fjw", "1gxw", "1hyt", "1kei", "1kjo", "1kjp", "1kkk", "1kl6", "1kr6", "1kro", "1ks7", "1kto", "1l3f", "1lna", "1lnb", "1lnc", "1lnd", "1lne", "1lnf", "1npc", "1os0", "1pe5", "1pe7"...
265
[ "PUB00003579" ]
[ "7674922" ]
[ "Evolutionary families of metallopeptidases." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 27, 15004, 716, 53 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Domain
Peptidase M4, C-terminal
Peptidase M4, C-terminal
Peptidase_M4_C_domain
6
IPR001571
1,571
GPCR, family 2, vasoactive intestinal peptide receptor
GPCR_2_VIP_rcpt
Family
1,545
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004999", "GO:0007186", "GO:0016020" ]
[ "vasoactive intestinal polypeptide receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00491" ]
[ "VASOACTVEIPR" ]
[ 1545 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-418555", "R-HSA-420092", "R-MMU-418555", "R-MMU-420092", "R-RNO-420092" ]
[ "REACTOME:R-HSA-418555", "REACTOME:R-HSA-420092", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-420092", "REACTOME:R-RNO-420092" ]
5
[ "2x57", "6vn7", "7vqx", "7wbj", "8e3y", "8e3z" ]
6
[ "PUB00001208", "PUB00003458", "PUB00003459", "PUB00004310", "PUB00004822", "PUB00004961", "PUB00005147", "PUB00005148", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "1646711", "8933357", "8784257", "1314625", "8392197", "8170923", "1658940", "1658941", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Molecular cloning and expression of a cDNA encoding the secretin receptor.", "Tissue specific expression of different human receptor types for pituitary adenylate cyclase activating polypeptide and vasoactive intestinal polypeptide: implications for their role in human physiology.", "Differential expression of...
[ 1991, 1996, 1996, 1992, 1993, 1994, 1991, 1991, 2003, 1994, 2005, 2009, 2006, 2013 ]
14
[]
[ "IPR001771", "IPR002284" ]
0
2
0
[ "Gnathostomata" ]
[ 1545 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 8, 4, 9 ]
4
true
Family
GPCR, family 2, vasoactive intestinal peptide receptor
GPCR, family 2, vasoactive intestinal peptide receptor
GPCR_2_VIP_rcpt
2
IPR001573
1,573
A kinase-anchoring protein AKAP5 and AKAP12, calmodulin (CaM)-binding motif
AKAP_WSK
Domain
1,726
false
false
The AKAP CaM-binding motif (also known as the WSK motif) is short motif, named after three conserved residues found in the WXSXK motif, found in protein kinase A anchoring proteins. The A kinase-anchoring proteins AKAP-5 and AKAP-12 (Gravin) bind calmodulin (CaM), a Ca(2+)-sensing protein that is expressed in all eukar...
[ "GO:0005516" ]
[ "calmodulin binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF03832", "PS51893" ]
[ "WSK", "AKAP_CAM_BD" ]
[ 1329, 1724 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-381676", "R-HSA-399719", "R-HSA-9010642", "R-HSA-9013405", "R-HSA-9035034", "R-MMU-399719", "R-MMU-9013405", "R-MMU-9035034", "R-RNO-399719", "R-RNO-9013405", "R-RNO-9035034" ]
[ "REACTOME:R-HSA-381676", "REACTOME:R-HSA-399719", "REACTOME:R-HSA-9010642", "REACTOME:R-HSA-9013405", "REACTOME:R-HSA-9035034", "REACTOME:R-MMU-399719", "REACTOME:R-MMU-9013405", "REACTOME:R-MMU-9035034", "REACTOME:R-RNO-399719", "REACTOME:R-RNO-9013405", "REACTOME:R-RNO-9035034" ]
11
[ "5nin" ]
1
[ "PUB00094791" ]
[ "29162807" ]
[ "Molecular basis of AKAP79 regulation by calmodulin." ]
[ 2017 ]
1
[]
[]
0
0
null
[ "Vertebrata" ]
[ 1726 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 4, 7, 10 ]
4
true
Domain
A kinase-anchoring protein AKAP5 and AKAP12, calmodulin (CaM)-binding motif
A kinase-anchoring protein AKAP5 and AKAP12, calmodulin (CaM)-binding motif
AKAP_WSK
7
IPR001574
1,574
Ribosome-inactivating protein
Ribosome_inactivat_prot
Family
3,722
false
false
A number of bacterial and plant toxins act by inhibiting protein synthesis in eukaryotic cells. The toxins of the shiga and ricin family inactivate 60S ribosomal subunits by an N-glycosidic cleavage which releases a specific adenine base from the sugar-phosphate backbone of 28S rRNA [ , , ]. Members of the family inclu...
[ "GO:0030598", "GO:0017148" ]
[ "rRNA N-glycosylase activity", "negative regulation of translation" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PANTHER" ]
[ "PF00161", "PTHR33453" ]
[ "RIP", "" ]
[ 3704, 2803 ]
2
[ "EC", "PROSITEDOC" ]
[ "3.2.2.22", "PDOC00248" ]
[ "EC:3.2.2.22", "PROSITEDOC:PDOC00248" ]
2
[ "1abr", "1aha", "1ahb", "1ahc", "1apa", "1br5", "1br6", "1bry", "1ce7", "1cf5", "1d6a", "1d8v", "1dm0", "1f8q", "1ggp", "1gik", "1gis", "1giu", "1hwm", "1hwn", "1hwo", "1hwp", "1ifs", "1ift", "1ifu", "1il3", "1il4", "1il5", "1il9", "1j1m", "1j1q", "1j1r"...
309
[ "PUB00000690", "PUB00001175", "PUB00001357", "PUB00003312", "PUB00004654", "PUB00004990" ]
[ "1742358", "2714255", "3276522", "8411176", "3357883", "8066085" ]
[ "Conserved amino acid residues in ribosome-inactivating proteins from plants.", "Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides.", "Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosome...
[ 1991, 1989, 1988, 1993, 1988, 1994 ]
6
[]
[ "IPR016331", "IPR017989" ]
0
2
0
[ "Bacteria", "Eukaryota", "Viruses" ]
[ 658, 2967, 97 ]
3
[ "Oryza sativa subsp. japonica", "Zea mays" ]
[ 115, 36 ]
2
true
Family
Ribosome-inactivating protein
Ribosome-inactivating protein
Ribosome_inactivat_prot
3
IPR001576
1,576
Phosphoglycerate kinase
Phosphoglycerate_kinase
Family
38,226
false
false
Phosphoglycerate kinase ( ) (PGK) is an enzyme that catalyses the formation of ATP to ADP and vice versa. In the second step of the second phase in glycolysis, 1,3-diphosphoglycerate is converted to 3-phosphoglycerate, forming one molecule of ATP. If the reverse were to occur, one molecule of ADP would be formed. This ...
[ "GO:0004618", "GO:0006096" ]
[ "phosphoglycerate kinase activity", "glycolytic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "PIRSF", "PRINTS", "PANTHER", "CDD" ]
[ "MF_00145", "PF00162", "PIRSF000724", "PR00477", "PTHR11406", "cd00318" ]
[ "Phosphoglyc_kinase", "PGK", "Pgk", "PHGLYCKINASE", "", "Phosphoglycerate_kinase" ]
[ 32055, 38195, 32004, 37370, 37913, 18031 ]
6
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...
[ "2.7.2.3", "GenProp0691", "GenProp1306", "GenProp1344", "GenProp1407", "GenProp1599", "GenProp1612", "PWY-1042", "PWY-5484", "PWY-6886", "PWY-6901", "PWY-7003", "PWY-8004", "PWY-8404", "R-BTA-70171", "R-BTA-70263", "R-CEL-70171", "R-CEL-70263", "R-DDI-70171", "R-DDI-70263", "...
[ "EC:2.7.2.3", "GP:GenProp0691", "GP:GenProp1306", "GP:GenProp1344", "GP:GenProp1407", "GP:GenProp1599", "GP:GenProp1612", "METACYC:PWY-1042", "METACYC:PWY-5484", "METACYC:PWY-6886", "METACYC:PWY-6901", "METACYC:PWY-7003", "METACYC:PWY-8004", "METACYC:PWY-8404", "REACTOME:R-BTA-70171", ...
39
[ "13pk", "16pk", "1fw8", "1hdi", "1kf0", "1ltk", "1php", "1qpg", "1v6s", "1vjc", "1vjd", "1vpe", "1zmr", "2cun", "2ie8", "2p9q", "2p9t", "2paa", "2wzb", "2wzc", "2wzd", "2x13", "2x14", "2x15", "2xe6", "2xe7", "2xe8", "2y3i", "2ybe", "2zgv", "3c39", "3c3a"...
68
[ "PUB00006255", "PUB00006482", "PUB00006511" ]
[ "2124145", "6689547", "10593256" ]
[ "Flexibility and folding of phosphoglycerate kinase.", "Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects.", "Folding funnels and conformational transitions via hinge-bending motions." ]
[ 1990, 1983, 1999 ]
3
[]
[ "IPR027250" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 959, 26614, 9809, 2, 842 ]
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",...
[ 8, 1, 1, 6, 1, 10, 4, 1, 16, 8, 1, 1, 33 ]
13
true
Family
Phosphoglycerate kinase
Phosphoglycerate kinase
Phosphoglycerate_kinase
8
IPR001577
1,577
Peptidase M8, leishmanolysin
Peptidase_M8
Family
7,547
false
false
This group of metallopeptidases belong to the MEROPS peptidase family M8 (leishmanolysin family, clan MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA. Leishmanolysin ( ) is an enzyme found in eukaryotes including Leishmania and rela...
[ "GO:0004222", "GO:0006508", "GO:0007155", "GO:0016020" ]
[ "metalloendopeptidase activity", "proteolysis", "cell adhesion", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF01457", "PR00782", "PTHR10942" ]
[ "Peptidase_M8", "LSHMANOLYSIN", "" ]
[ 7433, 2787, 6689 ]
3
[ "EC" ]
[ "3.4.24" ]
[ "EC:3.4.24" ]
1
[ "1lml" ]
1
[ "PUB00003579", "PUB00090184", "PUB00101066" ]
[ "7674922", "19706689", "34903892" ]
[ "Evolutionary families of metallopeptidases.", "The conserved metalloprotease invadolysin localizes to the surface of lipid droplets.", "Discovery of a genetic module essential for assigning left-right asymmetry in humans and ancestral vertebrates." ]
[ 1995, 2009, 2022 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 371, 7165, 11 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 5, 2, 5, 1, 7, 3, 3, 6, 8 ]
9
true
Family
Peptidase M8, leishmanolysin
Peptidase M8, leishmanolysin
Peptidase_M8
4
IPR001579
1,579
Glycosyl hydrolase family 18, active site
Glyco_hydro_18_chit_AS
Active_site
53,275
false
false
The glycosyl hydrolase family 18 (GH18) is widely distributed in all domains of life. The GH18 family contains hydrolytic enzymes with chitinase or endo-N-acetyl-beta-D-glucosaminidase (ENGase) activity as well as chitinase like lectins (chi-lectins/proteins (CLPs). Chitinases (EC 3.2.1.14) are hydrolytic enzymes that ...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS01095" ]
[ "GH18_1" ]
[ 53275 ]
1
[ "CAZY", "EC", "EC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GH18", "3.2.1", "3.2.1.14", "PWY-6855", "PWY-6902", "PWY-7822", "PDOC00839", "R-CEL-189085", "R-CEL-6798695", "R-DME-189085", "R-DME-6798695", "R-HSA-189085", "R-HSA-6798695", "R-MMU-189085", "R-MMU-6798695", "R-RNO-189085", "R-SCE-189085", "R-SCE-6798695" ]
[ "CAZY:GH18", "EC:3.2.1", "EC:3.2.1.14", "METACYC:PWY-6855", "METACYC:PWY-6902", "METACYC:PWY-7822", "PROSITEDOC:PDOC00839", "REACTOME:R-CEL-189085", "REACTOME:R-CEL-6798695", "REACTOME:R-DME-189085", "REACTOME:R-DME-6798695", "REACTOME:R-HSA-189085", "REACTOME:R-HSA-6798695", "REACTOME:R-M...
18
[ "1c3f", "1ctn", "1d2k", "1e15", "1e6r", "1e6z", "1edq", "1edt", "1ffq", "1ffr", "1goi", "1gpf", "1guv", "1h0g", "1h0i", "1hki", "1hkj", "1hkk", "1hkm", "1hvq", "1itx", "1k9t", "1kfw", "1lg1", "1lg2", "1ll4", "1ll6", "1llo", "1lq0", "1o6i", "1ogb", "1ogg"...
241
[ "PUB00023089", "PUB00061053", "PUB00093758", "PUB00093759", "PUB00093760", "PUB00093761", "PUB00093762", "PUB00093763", "PUB00093764" ]
[ "8831791", "22742450", "22796096", "20868765", "22859955", "23717482", "24380021", "25232743", "20553502" ]
[ "The 1.8 A resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18.", "Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding properties.", "Functional analysis of glycoside hydrolase family ...
[ 1996, 2012, 2012, 2011, 2012, 2013, 2013, 2014, 2010 ]
9
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 123, 19061, 33742, 173, 176 ]
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...
[ 10, 5, 35, 18, 12, 5, 7, 33, 13, 2, 36 ]
11
true
Active_site
Glycosyl hydrolase family 18, active site
Glycosyl hydrolase family 18, active site
Glyco_hydro_18_chit_AS
8
IPR001580
1,580
Calreticulin/calnexin
Calret/calnex
Family
14,747
false
false
null
[ "GO:0005509", "GO:0051082", "GO:0006457", "GO:0005783" ]
[ "calcium ion binding", "unfolded protein binding", "protein folding", "endoplasmic reticulum" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF00262", "PR00626", "PTHR11073" ]
[ "Calreticulin", "CALRETICULIN", "" ]
[ 14582, 13935, 14474 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00636", "R-CEL-901042", "R-DDI-901042", "R-DME-901042", "R-HSA-1236974", "R-HSA-168316", "R-HSA-2132295", "R-HSA-3000480", "R-HSA-3000484", "R-HSA-381183", "R-HSA-8984722", "R-HSA-901042", "R-HSA-9020956", "R-HSA-9683686", "R-HSA-9694548", "R-HSA-9768727", "R-HSA-983170", "R-M...
[ "PROSITEDOC:PDOC00636", "REACTOME:R-CEL-901042", "REACTOME:R-DDI-901042", "REACTOME:R-DME-901042", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-168316", "REACTOME:R-HSA-2132295", "REACTOME:R-HSA-3000480", "REACTOME:R-HSA-3000484", "REACTOME:R-HSA-381183", "REACTOME:R-HSA-8984722", "REACTOME:R-HSA...
39
[ "1hhn", "1jhn", "1k91", "1k9c", "3ici", "3o0v", "3o0w", "3o0x", "3pos", "3pow", "3rg0", "5hca", "5hcb", "5hcf", "5lk5", "5v8z", "5v90", "6eny", "7qpd", "8rjc", "8rjd", "8tzo", "8tzr", "8xvf" ]
24
[ "PUB00000513", "PUB00002891", "PUB00005415", "PUB00063812" ]
[ "1497605", "8126001", "8203019", "12401114" ]
[ "Calreticulin.", "Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development.", "Calnexin: a membrane-bound chaperone of the endoplasmic reticulum.", "Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss o...
[ 1992, 1994, 1994, 2003 ]
4
[]
[ "IPR009169" ]
0
1
0
[ "Bacteria", "Eukaryota" ]
[ 2, 14745 ]
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...
[ 34, 3, 11, 12, 39, 14, 1, 25, 22, 1, 2, 62 ]
12
true
Family
Calreticulin/calnexin
Calreticulin/calnexin
Calret/calnex
6
IPR001581
1,581
Leukemia inhibitory factor /oncostatin
Leukemia_IF/oncostatin
Family
1,000
false
false
On the basis of functional and structural similarities, the small cytokines leukemia inhibitory factor (LIF) and oncostatin (OSM) can be classified into a single family [ , ]. It has been said [ ] that LIF and OSM can be included in the IL-6 family of cytokines, but while all these cytokines seem to be structurally rel...
[ "GO:0005125", "GO:0006955", "GO:0005576" ]
[ "cytokine activity", "immune response", "extracellular region" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "SMART" ]
[ "PF01291", "SM00080" ]
[ "LIF_OSM", "LIF_OSM" ]
[ 987, 867 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00509", "R-BTA-6788467", "R-HSA-6783783", "R-HSA-6785807", "R-HSA-6788467", "R-MMU-6788467", "R-RNO-6788467" ]
[ "PROSITEDOC:PDOC00509", "REACTOME:R-BTA-6788467", "REACTOME:R-HSA-6783783", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-6788467", "REACTOME:R-MMU-6788467", "REACTOME:R-RNO-6788467" ]
7
[ "1a7m", "1emr", "1evs", "1lki", "1pvh", "2q7n", "7n0a", "8d6a", "8v29", "8v2a", "8v2b", "8v2c" ]
12
[ "PUB00004755", "PUB00005395" ]
[ "1717982", "1566332" ]
[ "Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6.", "LIF: lots of interesting functions." ]
[ 1991, 1992 ]
2
[]
[ "IPR003624", "IPR039578" ]
0
2
0
[ "Eukaryota" ]
[ 1000 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 5, 15 ]
3
true
Family
Leukemia inhibitory factor /oncostatin
Leukemia inhibitory factor /oncostatin
Leukemia_IF/oncostatin
2
IPR001584
1,584
Integrase, catalytic core
Integrase_cat-core
Domain
466,959
false
false
The retroviral integrase is the enzyme responsible for the insertion of a DNA copy of the viral genome into host DNA, an essential step in the replication cycle of viruses [ ]. Integrases comprise three functional and structural domains: the central core domain, which contains the catalytic residues, an N-terminal zinc...
[ "GO:0015074" ]
[ "DNA integration" ]
[ "biological_process" ]
1
[ "PFAM", "PFAM", "PFAM", "PROFILE" ]
[ "PF00665", "PF13333", "PF13683", "PS50994" ]
[ "rve", "rve_2", "rve_3", "INTEGRASE" ]
[ 254611, 37429, 35986, 450455 ]
4
[ "EC", "EC", "EC", "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.7.49", "2.7.7.7", "3.1.26", "3.4.23", "PDOC50994", "R-HSA-162585", "R-HSA-162588", "R-HSA-162592", "R-HSA-162594", "R-HSA-164516", "R-HSA-164525", "R-HSA-164843", "R-HSA-173107", "R-HSA-175474", "R-HSA-175567", "R-HSA-177539", "R-HSA-180689", "R-HSA-180910" ]
[ "EC:2.7.7.49", "EC:2.7.7.7", "EC:3.1.26", "EC:3.4.23", "PROSITEDOC:PDOC50994", "REACTOME:R-HSA-162585", "REACTOME:R-HSA-162588", "REACTOME:R-HSA-162592", "REACTOME:R-HSA-162594", "REACTOME:R-HSA-164516", "REACTOME:R-HSA-164525", "REACTOME:R-HSA-164843", "REACTOME:R-HSA-173107", "REACTOME:R...
18
[ "1a5v", "1a5w", "1a5x", "1asu", "1asv", "1asw", "1b92", "1b9d", "1b9f", "1bhl", "1bi4", "1bis", "1biu", "1biz", "1bl3", "1c0m", "1c1a", "1c6v", "1cxq", "1cxu", "1cz9", "1czb", "1ex4", "1exq", "1hyv", "1hyz", "1itg", "1k6y", "1qs4", "1vsd", "1vse", "1vsf"...
386
[ "PUB00005191", "PUB00016297", "PUB00018337", "PUB00018338", "PUB00018343" ]
[ "7801124", "8696976", "9759480", "10384240", "7526778" ]
[ "Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases.", "Retroviral integrases and their cousins.", "HIV-1: fifteen proteins and an RNA.", "HIV integrase structure and function.", "The retroviral enzymes." ]
[ 1994, 1996, 1998, 1999, 1994 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "other sequences", "unclassified sequences" ]
[ 589, 148138, 252704, 63001, 17, 2510 ]
6
[ "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...
[ 189, 3, 217, 68, 25, 45, 31, 2212, 9, 50, 13, 64 ]
12
true
Domain
Integrase, catalytic core
Integrase, catalytic core
Integrase_cat-core
7
IPR001585
1,585
Transaldolase/Fructose-6-phosphate aldolase
TAL/FSA
Family
38,849
false
false
Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA) [ ]. They both belong to the class I aldolase ...
[ "GO:0005975" ]
[ "carbohydrate metabolic process" ]
[ "biological_process" ]
1
[ "PFAM", "PANTHER" ]
[ "PF00923", "PTHR10683" ]
[ "TAL_FSA", "" ]
[ 38819, 38125 ]
2
[ "EC", "GP", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "2.2.1.2", "GenProp1294", "PWY-1861", "PWY-5723", "PDOC00741", "R-DDI-163754", "R-DDI-71336", "R-DME-163754", "R-DME-71336", "R-HSA-163754", "R-HSA-6791055", "R-HSA-6791462", "R-HSA-71336", "R-HSA-8950505", "R-HSA-9818028", "R-MMU-163754", "R-MMU-71336", "R-RNO-163754", "R-RNO-71...
[ "EC:2.2.1.2", "GP:GenProp1294", "METACYC:PWY-1861", "METACYC:PWY-5723", "PROSITEDOC:PDOC00741", "REACTOME:R-DDI-163754", "REACTOME:R-DDI-71336", "REACTOME:R-DME-163754", "REACTOME:R-DME-71336", "REACTOME:R-HSA-163754", "REACTOME:R-HSA-6791055", "REACTOME:R-HSA-6791462", "REACTOME:R-HSA-71336...
25
[ "1f05", "1i2n", "1i2o", "1i2p", "1i2q", "1i2r", "1l6w", "1onr", "1ucw", "1vpx", "1wx0", "2cwn", "2e1d", "3clm", "3cq0", "3cwn", "3hjz", "3igx", "3kof", "3m16", "3r5e", "3r8r", "3s0c", "3s1u", "3s1v", "3s1w", "3s1x", "3te9", "3tk7", "3tkf", "3tno", "3upb"...
72
[ "PUB00005649", "PUB00053971", "PUB00076745", "PUB00076746" ]
[ "8109173", "11120740", "25267444", "26131847" ]
[ "Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase.", "Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases.", "Sweet siblings with different faces: the mechanisms of FBP and F6P aldo...
[ 1993, 2001, 2014, 2015 ]
4
[]
[ "IPR004730", "IPR004732", "IPR033919" ]
0
3
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 206, 30142, 125, 7747, 629 ]
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, 1, 2, 4, 5, 2, 2, 6, 9, 2, 1, 13 ]
13
true
Family
Transaldolase/Fructose-6-phosphate aldolase
Transaldolase/Fructose-6-phosphate aldolase
TAL/FSA
6
IPR001586
1,586
Beta-lactamase, class-C active site
Beta-lactam_class-C_AS
Active_site
5,193
false
false
This active site signature detects all class C Beta-lactamases. The class C beta-lactamases are serine hydrolases belonging to MEROPS peptidase family S12 (D-Ala-D-Ala carboxypeptidase B family, clan SE). They are classed as non-peptidase homologues. Beta-lactamases ( ) [ , ] are enzymes which catalyse the hydrolysis o...
[ "GO:0008800", "GO:0017001", "GO:0030288" ]
[ "beta-lactamase activity", "antibiotic catabolic process", "outer membrane-bounded periplasmic space" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PROSITE" ]
[ "PS00336" ]
[ "BETA_LACTAMASE_C" ]
[ 5193 ]
1
[ "EC", "PROSITEDOC" ]
[ "3.5.2.6", "PDOC00134" ]
[ "EC:3.5.2.6", "PROSITEDOC:PDOC00134" ]
2
[ "1bls", "1c3b", "1fcm", "1fcn", "1fco", "1fr1", "1fr6", "1fsw", "1fsy", "1ga0", "1ga9", "1gce", "1i5q", "1iel", "1iem", "1kds", "1kdw", "1ke0", "1ke3", "1ke4", "1kvm", "1l0f", "1l2s", "1ll5", "1ll9", "1llb", "1mxo", "1my8", "1o07", "1onh", "1pi4", "1pi5"...
260
[ "PUB00000133", "PUB00000464", "PUB00003800", "PUB00004510" ]
[ "2658779", "3128280", "2082152", "6109327" ]
[ "Characterization of beta-lactamases.", "The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.", "Molecular evolution of class A beta-lactamases: phylogeny and patterns of sequence conservation.", "The structure of beta-lactamases." ]
[ 1989, 1988, 1990, 1980 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanospirillum", "unclassified sequences" ]
[ 5154, 15, 4, 20 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Active_site
Beta-lactamase, class-C active site
Beta-lactamase, class-C active site
Beta-lactam_class-C_AS
7
IPR001587
1,587
Ribonuclease J, conserved site
RNase_J_CS
Conserved_site
8,336
false
false
This conserved region is found in proteins characterised as RNase J. They are about 50 to 77kDa. The central region is well conserved and contains three conserved histidines. Most of these proteins are related at the N-terminal region to the beta-lactamase family. RNase J cleaves the 5'-leader sequence of certain mRNAs...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01292" ]
[ "UPF0036" ]
[ 8336 ]
1
[ "PROSITEDOC" ]
[ "PDOC00994" ]
[ "PROSITEDOC:PDOC00994" ]
1
[ "3zq4", "6k6s", "7pcr", "8cgl" ]
4
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctSwt2", "metagenomes" ]
[ 105, 8125, 41, 1, 64 ]
5
[]
[]
0
true
Conserved_site
Ribonuclease J, conserved site
Ribonuclease J, conserved site
RNase_J_CS
3
IPR001588
1,588
Casein, alpha/beta
Casein
Family
635
false
false
Caseins [ ] are the major protein constituent of milk. In milk, caseins interact with calcium phosphate, forming large stable colloidal particles termed micelles. These micelles make it possible to maintain a supersaturated calcium phosphate concentration in milk, providing the newborn with sufficient calcium phosphate...
[ "GO:0005576" ]
[ "extracellular region" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF00363" ]
[ "Casein" ]
[ 635 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00277", "R-BTA-5223345", "R-HSA-1251985", "R-MMU-5223345", "R-RNO-5223345" ]
[ "PROSITEDOC:PDOC00277", "REACTOME:R-BTA-5223345", "REACTOME:R-HSA-1251985", "REACTOME:R-MMU-5223345", "REACTOME:R-RNO-5223345" ]
5
[ "6fs4", "6fs5", "7ttr", "7tts" ]
4
[ "PUB00004950", "PUB00062158", "PUB00062170", "PUB00062171" ]
[ "3074304", "7619062", "16386026", "3952000" ]
[ "Primary and predicted secondary structures of the caseins in relation to their biological functions.", "Characterization of three types of human alpha s1-casein mRNA transcripts.", "Comparative study of the amino acid sequences of the caseinomacropeptides from seven species.", "Evolution of the casein multig...
[ 1988, 1995, 1976, 1986 ]
4
[]
[ "IPR011175", "IPR016345", "IPR026999" ]
0
3
0
[ "Eutheria" ]
[ 635 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 12, 13 ]
3
true
Family
Casein, alpha/beta
Casein, alpha/beta
Casein
2
IPR001589
1,589
Actinin-type actin-binding domain, conserved site
Actinin_actin-bd_CS
Conserved_site
51,549
false
false
Alpha-actinin is a F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures [ ]. The actin-binding domain of alpha-actinin seems to reside in the first 250 residues of the protein. A similar actin-binding domain has been found in the N-terminal region of many different act...
[]
[]
[]
0
[ "PROSITE", "PROSITE" ]
[ "PS00019", "PS00020" ]
[ "ACTININ_1", "ACTININ_2" ]
[ 43765, 47085 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00019", "R-BTA-114608", "R-BTA-390522", "R-BTA-438066", "R-BTA-446388", "R-BTA-5673001", "R-BTA-9013405", "R-BTA-9013418", "R-BTA-9035034", "R-CEL-9913351", "R-DDI-114608", "R-DDI-1169408", "R-DDI-446353", "R-DDI-5627123", "R-DDI-6798695", "R-DDI-6807878", "R-DDI-9013418", "R-...
[ "PROSITEDOC:PDOC00019", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-390522", "REACTOME:R-BTA-438066", "REACTOME:R-BTA-446388", "REACTOME:R-BTA-5673001", "REACTOME:R-BTA-9013405", "REACTOME:R-BTA-9013418", "REACTOME:R-BTA-9035034", "REACTOME:R-CEL-9913351", "REACTOME:R-DDI-114608", "REACTOME:R-DDI...
124
[ "1aoa", "1dxx", "1mb8", "1pxy", "1qag", "1rt8", "1sh5", "1sh6", "1sjj", "1tjt", "1wku", "2eyi", "2eyn", "2r0o", "2wa5", "2wa6", "2wa7", "2wfn", "3byh", "3f7p", "3fer", "3hoc", "3hop", "3hor", "3lue", "4b7l", "4d1e", "4q57", "4q58", "4q59", "4z6g", "5a36"...
57
[ "PUB00000716", "PUB00001105", "PUB00005381" ]
[ "1892474", "3243032", "2058002" ]
[ "Structure and evolution of the actin crosslinking proteins.", "Actin-binding proteins are conserved from slime molds to man.", "Modular organization of actin crosslinking proteins." ]
[ 1991, 1988, 1991 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 177, 51369, 3 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 18, 35, 279, 59, 168, 115, 2, 6, 147, 1, 2, 20 ]
12
true
Conserved_site
Actinin-type actin-binding domain, conserved site
Actinin-type actin-binding domain, conserved site
Actinin_actin-bd_CS
7
IPR001590
1,590
Peptidase M12B, ADAM/reprolysin
Peptidase_M12B
Domain
62,228
false
false
This group of metallopeptidases belong to the MEROPS peptidase family M12, subfamily M12B (adamalysin family, clan (MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA and the predicted active site residues for members of this family an...
[ "GO:0004222", "GO:0006508" ]
[ "metalloendopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE" ]
[ "PF01421", "PS50215" ]
[ "Reprolysin", "ADAM_MEPRO" ]
[ 48873, 61890 ]
2
[ "EC", "EC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REAC...
[ "3.4.24", "3.4.24.-", "PWY-8119", "PDOC50215", "R-BTA-1474228", "R-BTA-1650814", "R-BTA-381426", "R-BTA-5173214", "R-BTA-6798695", "R-BTA-8957275", "R-CEL-1474228", "R-CEL-381426", "R-CEL-5173214", "R-CEL-6798695", "R-CEL-8957275", "R-HSA-1251985", "R-HSA-1442490", "R-HSA-1474228",...
[ "EC:3.4.24", "EC:3.4.24.-", "METACYC:PWY-8119", "PROSITEDOC:PDOC50215", "REACTOME:R-BTA-1474228", "REACTOME:R-BTA-1650814", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-5173214", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8957275", "REACTOME:R-CEL-1474228", "REACTOME:R-CEL-381426", "REACTOME:R-CE...
76
[ "1atl", "1bkc", "1bsw", "1bud", "1dth", "1htd", "1iag", "1kuf", "1kug", "1kui", "1kuk", "1nd1", "1qua", "1r54", "1r55", "1wni", "1yp1", "1zxc", "2a8h", "2aig", "2ddf", "2dw0", "2dw1", "2dw2", "2e3x", "2ero", "2erp", "2erq", "2fv5", "2fv9", "2i47", "2jih"...
97
[ "PUB00003579", "PUB00082630", "PUB00082631" ]
[ "7674922", "27196928", "15922769" ]
[ "Evolutionary families of metallopeptidases.", "ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview.", "Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases." ]
[ 1995, 2016, 2005 ]
3
[]
[ "IPR033817", "IPR034025", "IPR034027", "IPR034028", "IPR034030" ]
0
5
0
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "ecological metagenomes" ]
[ 864, 61347, 10, 7 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 14, 149, 39, 137, 161, 1, 169, 1 ]
8
true
Domain
Peptidase M12B, ADAM/reprolysin
Peptidase M12B, ADAM/reprolysin
Peptidase_M12B
6
IPR001591
1,591
Influenza RNA-dependent RNA polymerase subunit PB2
INV_PB2
Family
61,847
false
false
Orthomyxoviridae RNA polymerase with the subunit composition of PB1-PB2-PA is a unique multifunctional enzyme with the activities of both synthesis and cleavage of RNA, and is involved in both transcription and replication of the RNA genome. Transcription is initiated by using capped RNA fragments, which are generated ...
[ "GO:0003723", "GO:0039694" ]
[ "RNA binding", "viral RNA genome replication" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP" ]
[ "MF_04062" ]
[ "INV_PB2" ]
[ 61847 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1012", "R-HSA-168255", "R-HSA-168271", "R-HSA-168275", "R-HSA-168288", "R-HSA-168298", "R-HSA-168302", "R-HSA-168303", "R-HSA-168325", "R-HSA-168330", "R-HSA-168333", "R-HSA-168336", "R-HSA-192814", "R-HSA-192823", "R-HSA-192869", "R-HSA-192905" ]
[ "GP:GenProp1012", "REACTOME:R-HSA-168255", "REACTOME:R-HSA-168271", "REACTOME:R-HSA-168275", "REACTOME:R-HSA-168288", "REACTOME:R-HSA-168298", "REACTOME:R-HSA-168302", "REACTOME:R-HSA-168303", "REACTOME:R-HSA-168325", "REACTOME:R-HSA-168330", "REACTOME:R-HSA-168333", "REACTOME:R-HSA-168336", ...
16
[ "4wrt", "4wsa", "5d98", "5d9a", "5epi", "5fmz", "5m3j", "5msg", "6f5o", "6f5p", "6qcs", "6qct", "6qcv", "6qcw", "6qcx", "6qnw", "6qpf", "6qpg", "6qwl", "6qx3", "6qx8", "6qxe", "6rr7", "6t0w", "6xzd", "6xzg", "6xzp", "6xzq", "6xzr", "6y0c", "7nha", "7nhc"...
96
[ "PUB00005639", "PUB00006567", "PUB00087126" ]
[ "8806170", "10526235", "10393191" ]
[ "Recombinant-baculovirus-expressed PB2 subunit of the influenza A virus RNA polymerase binds cap groups as an isolated subunit.", "Two separate sequences of PB2 subunit constitute the RNA cap-binding site of influenza virus RNA polymerase.", "Distinct regions of influenza virus PB1 polymerase subunit recognize ...
[ 1996, 1999, 1999 ]
3
[]
[]
0
0
null
[ "Bacillati", "Orthomyxoviridae" ]
[ 4, 61843 ]
2
[]
[]
0
true
Family
Influenza RNA-dependent RNA polymerase subunit PB2
Influenza RNA-dependent RNA polymerase subunit PB2
INV_PB2
8
IPR001592
1,592
Potyvirus coat protein
Poty_coat
Family
16,870
false
false
This protease is found in genome polyproteins of potyviruses. The genome polyprotein contains: N-terminal protein (P1), helper component protease ( , HC-PRO), protein P3, 6KD protein (6K1), cytoplasmic inclusion protein (CI), 6KD protein 2 (6K2), genome-linked protein (VPG), nuclear inclusion protein A ( ), nuclear inc...
[ "GO:0019028" ]
[ "viral capsid" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF00767" ]
[ "Poty_coat" ]
[ 16870 ]
1
[ "EC", "EC", "EC", "METACYC" ]
[ "2.7.7.48", "3.4.22.44", "3.6.4.-", "PWY-7250" ]
[ "EC:2.7.7.48", "EC:3.4.22.44", "EC:3.6.4.-", "METACYC:PWY-7250" ]
4
[ "5odv", "6hxx", "6hxz", "6t34", "8acb", "8acc", "8opa", "8opb", "8opc", "8opd", "8ope", "8opf", "8opg", "8oph", "8opj", "8opk", "8opl" ]
17
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Pentapetalae", "Viruses" ]
[ 2, 16868 ]
2
[]
[]
0
true
Family
Potyvirus coat protein
Potyvirus coat protein
Poty_coat
4
IPR001593
1,593
Small ribosomal subunit protein eS1
Ribosomal_eS1
Family
7,824
false
false
A number of eukaryotic and archaebacterial ribosomal proteins can be grouped on the basis of sequence similarities. This family represents the small ribosomal subunit protein eS1, previously known as S1 in yeast and S3A in archaea and mammals [ ], which consists of proteins that have from 220 to 250 amino acids. Riboso...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "SMART" ]
[ "PF01015", "SM01397" ]
[ "Ribosomal_S3Ae", "Ribosomal_S3Ae" ]
[ 7813, 7585 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00917", "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:PDOC00917", "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"...
123
[ "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", "4u4o", "4u4q", "4u4r"...
622
[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00080279" ]
[ "11297922", "11290319", "11114498", "24524803" ]
[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "A new system for naming ribosomal proteins." ]
[ 2001, 2001, 2000, 2014 ]
4
[]
[ "IPR027500", "IPR030838" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 919, 8, 6844, 53 ]
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...
[ 7, 1, 1, 1, 16, 6, 1, 9, 9, 2, 2, 19 ]
12
true
Family
Small ribosomal subunit protein eS1
Small ribosomal subunit protein eS1
Ribosomal_eS1
2
IPR001594
1,594
Palmitoyltransferase, DHHC domain
Palmitoyltrfase_DHHC
Domain
69,421
false
false
This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases [ ]. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of pa...
[ "GO:0016409" ]
[ "palmitoyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF01529" ]
[ "DHHC" ]
[ 69421 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.3.1.225", "PDOC50216", "R-BTA-203615", "R-BTA-9009391", "R-BTA-9648002", "R-DME-8963896", "R-DME-9648002", "R-DRE-5683826", "R-DRE-8963896", "R-DRE-9009391", "R-HSA-203615", "R-HSA-5683826", "R-HSA-8963896", "R-HSA-9009391", "R-HSA-9648002", "R-HSA-9694548", "R-MMU-203615", "R-M...
[ "EC:2.3.1.225", "PROSITEDOC:PDOC50216", "REACTOME:R-BTA-203615", "REACTOME:R-BTA-9009391", "REACTOME:R-BTA-9648002", "REACTOME:R-DME-8963896", "REACTOME:R-DME-9648002", "REACTOME:R-DRE-5683826", "REACTOME:R-DRE-8963896", "REACTOME:R-DRE-9009391", "REACTOME:R-HSA-203615", "REACTOME:R-HSA-568382...
23
[ "6bml", "6bmm", "6bmn", "6bms", "7khm", "8hf3", "8hfc", "9oa6" ]
8
[ "PUB00001882", "PUB00005678", "PUB00033761", "PUB00033762", "PUB00053955", "PUB00072195", "PUB00082711", "PUB00082712", "PUB00082716" ]
[ "10231582", "10490616", "12370247", "16100337", "15603741", "16000296", "23034182", "26224664", "12021275" ]
[ "The Drosophila STAM gene homolog is in a tight gene cluster, and its expression correlates to that of the adjacent gene ial.", "Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae.", "The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl tr...
[ 1999, 1999, 2002, 2005, 2004, 2005, 2012, 2015, 2002 ]
9
[]
[]
0
0
null
[ "Eukaryota" ]
[ 69421 ]
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...
[ 103, 22, 115, 51, 78, 43, 6, 102, 104, 7, 5, 234 ]
12
true
Domain
Palmitoyltransferase, DHHC domain
Palmitoyltransferase, DHHC domain
Palmitoyltrfase_DHHC
8
IPR001595
1,595
Mycoplasma-specific lipoprotein, type 3
Lipoprotein_3
Family
80
false
false
This family of lipoproteins is Mycoplasma specific, and includes a variety of hypothetical proteins [ ]. They all have a prokaryotic membrane lipoprotein lipid attachment site which is probable acts as a membrane anchor.
[]
[]
[]
0
[ "PFAM" ]
[ "PF00938" ]
[ "Lipoprotein_3" ]
[ 80 ]
1
[]
[]
[]
0
[]
0
[ "PUB00004470" ]
[ "8948633" ]
[ "Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Mycoplasmoides" ]
[ 80 ]
1
[]
[]
0
true
Family
Mycoplasma-specific lipoprotein, type 3
Mycoplasma-specific lipoprotein, type 3
Lipoprotein_3
9
IPR001597
1,597
Aromatic amino acid beta-eliminating lyase/threonine aldolase
ArAA_b-elim_lyase/Thr_aldolase
Domain
34,474
false
false
This domain is found in many tryptophanases (tryptophan indole-lyase, TNase), tyrosine phenol-lyases (TPL) and threonine aldolases. It is involved in the degradation of amino acids. The glycine cleavage system is composed of four proteins: P, T, L and H. In Bacillus subtilis, the P 'protein' is an heterodimer of two su...
[ "GO:0016829", "GO:0006520" ]
[ "lyase activity", "amino acid metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF01212" ]
[ "Beta_elim_lyase" ]
[ 34474 ]
1
[ "EC", "GP", "REACTOME", "REACTOME" ]
[ "4.1.99.1", "GenProp1445", "R-HSA-6783984", "R-MMU-6783984" ]
[ "EC:4.1.99.1", "GP:GenProp1445", "REACTOME:R-HSA-6783984", "REACTOME:R-MMU-6783984" ]
4
[ "1ax4", "1c7g", "1jg8", "1lw4", "1lw5", "1m6s", "1svv", "1tpl", "1v72", "2c44", "2ez1", "2ez2", "2fm1", "2oqx", "2tpl", "2v0y", "2v1p", "2vlf", "2vlh", "2ycn", "2ycp", "2yct", "2yhk", "3lws", "3pj0", "3wgb", "3wgc", "3wlx", "4lnj", "4lnl", "4lnm", "4rjy"...
75
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 475, 25405, 7957, 637 ]
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",...
[ 10, 3, 5, 1, 2, 2, 4, 1, 4, 4, 1, 1, 39 ]
13
true
Domain
Aromatic amino acid beta-eliminating lyase/threonine aldolase
Aromatic amino acid beta-eliminating lyase/threonine aldolase
ArAA_b-elim_lyase/Thr_aldolase
4
IPR001598
1,598
Transposase, IS30, conserved site
Transposase_IS30_CS
Conserved_site
5,452
false
false
Autonomous mobile genetic elements such as transposon or insertion sequences (IS) encode an enzyme, called transposase, required for excising and inserting the mobile element. On the basis of sequence similarities, transposases can be grouped into various families. One of these families has been shown [ , ] to consist ...
[ "GO:0003677", "GO:0004803", "GO:0006313" ]
[ "DNA binding", "transposase activity", "DNA transposition" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PROSITE" ]
[ "PS01043" ]
[ "TRANSPOSASE_IS30" ]
[ 5452 ]
1
[ "PROSITEDOC" ]
[ "PDOC00801" ]
[ "PROSITEDOC:PDOC00801" ]
1
[]
0
[ "PUB00002208", "PUB00003122" ]
[ "1334071", "8393068" ]
[ "Cloning and sequencing of IS1086, an Alcaligenes eutrophus insertion element related to IS30 and IS4351.", "The ftf gene encoding the cell-bound fructosyltransferase of Streptococcus salivarius ATCC 25975 is preceded by an insertion sequence and followed by FUR1 and clpP homologues." ]
[ 1992, 1993 ]
2
[]
[]
0
0
null
[ "Bacteria", "Bronfenbrennervirinae", "Halobaculum halobium", "Opisthokonta", "unclassified sequences" ]
[ 5358, 2, 1, 12, 79 ]
5
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Conserved_site
Transposase, IS30, conserved site
Transposase, IS30, conserved site
Transposase_IS30_CS
5
IPR001602
1,602
UPF0047 protein YjbQ-like
UPF0047_YjbQ-like
Family
18,959
false
false
This family contains small uncharacterised proteins of 14 to 16kDa mainly from bacteria although the signatures also occur in a hypothetical protein from archaea and eukaryotes. Members of this protein family, designated YjbQ in E. coli, have been studied extensively by crystallography. Members from several different s...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PROSITE", "PANTHER", "NCBIFAM" ]
[ "PF01894", "PIRSF004681", "PS01314", "PTHR30615", "TIGR00149" ]
[ "YjbQ", "UCP004681", "UPF0047", "", "TIGR00149_YjbQ" ]
[ 18922, 15853, 7855, 18483, 16685 ]
5
[ "PROSITEDOC" ]
[ "PDOC01018" ]
[ "PROSITEDOC:PDOC01018" ]
1
[ "1ve0", "1vmf", "1vmh", "1vmj", "1vph", "1xbf", "2cu5", "2p6c", "2p6h" ]
9
[ "PUB00101019", "PUB00101020" ]
[ "21119630", "18178222" ]
[ "Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis.", "Sensitive genome-wide screen for low secondary enzymatic activities: the YjbQ family shows thiamin phosphate synthase activity." ]
[ 2010, 2008 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "uncultured marine phage" ]
[ 933, 14345, 3239, 441, 1 ]
5
[ "Arabidopsis thaliana", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 7, 3, 1, 1, 7, 1, 9 ]
7
true
Family
UPF0047 protein YjbQ-like
UPF0047 protein YjbQ-like
UPF0047_YjbQ-like
5
IPR001605
1,605
Pleckstrin homology domain, spectrin-type
PH_dom-spectrin-type
Domain
14,319
false
false
Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane; it associates with band 4.1 and actin to form the cytoskeletal super-structure. The native spectrin molecule is a tetramer comprising two anti-parallel heterodimers joined head to head, such that the C terminus of ...
[ "GO:0005515", "GO:0005543" ]
[ "protein binding", "phospholipid binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS" ]
[ "PR00683" ]
[ "SPECTRINPH" ]
[ 14319 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-DME-375165", "R-DME-5673001", "R-DME-6807878", "R-DME-9013420", "R-DME-9013424", "R-HSA-2132295", "R-HSA-373753", "R-HSA-375165", "R-HSA-445095", "R-HSA-5673001", "R-HSA-6807878", "R-HSA-9013420", "R-HSA-9013424", "R-HSA-9662360", "R-HSA-9662361", "R-HSA-9703465", "R-MMU-375165", ...
[ "REACTOME:R-DME-375165", "REACTOME:R-DME-5673001", "REACTOME:R-DME-6807878", "REACTOME:R-DME-9013420", "REACTOME:R-DME-9013424", "REACTOME:R-HSA-2132295", "REACTOME:R-HSA-373753", "REACTOME:R-HSA-375165", "REACTOME:R-HSA-445095", "REACTOME:R-HSA-5673001", "REACTOME:R-HSA-6807878", "REACTOME:R-...
27
[ "1btn", "1dro", "1mph", "1wjm", "2dhj", "2j59", "3a8p", "3a8q" ]
8
[ "PUB00003928", "PUB00004179", "PUB00004180" ]
[ "8599766", "8208296", "8208297" ]
[ "Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain.", "Solution structure of a pleckstrin-homology domain.", "Structure of the pleckstrin homology domain from beta-spectrin." ]
[ 1996, 1994, 1994 ]
3
[ "IPR001849" ]
[]
1
0
1
[ "Eukaryota", "Kangiella spongicola" ]
[ 14318, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 11, 76, 10, 23, 22, 33 ]
6
true
Domain
Pleckstrin homology domain, spectrin-type
Pleckstrin homology domain, spectrin-type
PH_dom-spectrin-type
4
IPR001606
1,606
ARID DNA-binding domain
ARID_dom
Domain
39,019
false
false
The AT-rich interaction domain (ARID) is an ~100-amino acid DNA-binding module found in a large number of eukaryotic transcription factors that regulate cell proliferation, differentiation, and development [ , ]. The ARID domain appears as a single-copy motif and can be found in association with other domains, such as ...
[ "GO:0003677" ]
[ "DNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF01388", "PS51011", "SM00501" ]
[ "ARID", "ARID", "BRIGHT" ]
[ 38375, 38660, 36221 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC51011", "R-CEL-3214842", "R-DME-212300", "R-DME-3214858", "R-DME-8866911", "R-DME-8939243", "R-DME-9933937", "R-DME-9933946", "R-DME-9934037", "R-DRE-212300", "R-DRE-8866911", "R-GGA-8866911", "R-HSA-212300", "R-HSA-3214815", "R-HSA-3214842", "R-HSA-3214858", "R-HSA-427413", "...
[ "PROSITEDOC:PDOC51011", "REACTOME:R-CEL-3214842", "REACTOME:R-DME-212300", "REACTOME:R-DME-3214858", "REACTOME:R-DME-8866911", "REACTOME:R-DME-8939243", "REACTOME:R-DME-9933937", "REACTOME:R-DME-9933946", "REACTOME:R-DME-9934037", "REACTOME:R-DRE-212300", "REACTOME:R-DRE-8866911", "REACTOME:R-...
42
[ "1c20", "1ig6", "1kkx", "1kn5", "1kqq", "1ryu", "2cxy", "2eh9", "2eqy", "2jrz", "2jxj", "2kk0", "2li6", "2lm1", "2oeh", "2rq5", "2yqe", "4ljx", "5ceh", "5k4l", "5v9p", "5v9t", "6l87", "6lqf", "6lth", "6ltj", "6uxv", "6uxw", "7c4j", "7egm", "7egp", "7kso"...
38
[ "PUB00018453", "PUB00018454", "PUB00018455", "PUB00018456" ]
[ "10545119", "11867548", "11959810", "14722072" ]
[ "Solution structure of the DNA binding domain from Dead ringer, a sequence-specific AT-rich interaction domain (ARID).", "The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA.", "ARID proteins: a diverse family of DNA binding proteins implicated in the contr...
[ 1999, 2002, 2002, 2004 ]
4
[]
[ "IPR028853", "IPR030094", "IPR030408", "IPR038040", "IPR045303", "IPR047974" ]
0
6
0
[ "Bacteria", "Eukaryota", "bird metagenome" ]
[ 7, 39011, 1 ]
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...
[ 48, 9, 115, 16, 71, 48, 4, 24, 60, 2, 4, 112 ]
12
true
Domain
ARID DNA-binding domain
ARID DNA-binding domain
ARID_dom
1