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IPR000001
1
Kringle
Kringle
Domain
21,741
false
false
Kringles are autonomous structural domains, found throughout the blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity [ , , ]. Kringle domains [ , , ] are characterised...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART", "CDD" ]
[ "PF00051", "PS50070", "SM00130", "cd00108" ]
[ "Kringle", "KRINGLE_2", "KR", "KR" ]
[ 20506, 21634, 21101, 17509 ]
4
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.4.21", "PDOC00020", "R-BTA-6798695", "R-BTA-75205", "R-CEL-5140745", "R-CFA-114608", "R-CFA-1257604", "R-CFA-5673001", "R-CFA-6806942", "R-CFA-6807004", "R-CFA-6811558", "R-CFA-8851805", "R-CFA-8851907", "R-CFA-8865999", "R-CFA-8874081", "R-CFA-8875513", "R-CFA-8875555", "R-CFA-...
[ "EC:3.4.21", "PROSITEDOC:PDOC00020", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-75205", "REACTOME:R-CEL-5140745", "REACTOME:R-CFA-114608", "REACTOME:R-CFA-1257604", "REACTOME:R-CFA-5673001", "REACTOME:R-CFA-6806942", "REACTOME:R-CFA-6807004", "REACTOME:R-CFA-6811558", "REACTOME:R-CFA-8851805", ...
133
[ "1a0h", "1b2i", "1bht", "1cea", "1ceb", "1gmn", "1gmo", "1gp9", "1hpj", "1hpk", "1i5k", "1i71", "1jfn", "1kdu", "1ki0", "1kiv", "1krn", "1nk1", "1nl1", "1nl2", "1pk2", "1pk4", "1pkr", "1pmk", "1pml", "1tpk", "1urk", "2doh", "2doi", "2fd6", "2feb", "2hpp"...
134
[ "PUB00000803", "PUB00001541", "PUB00001620", "PUB00002414", "PUB00003257", "PUB00003400" ]
[ "3891096", "6373375", "1879523", "3886654", "2157850", "3131537" ]
[ "Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules.", "Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases.", "Evolutionary origin of numerous kringles in human and simian apolip...
[ 1985, 1984, 1991, 1985, 1990, 1987 ]
6
[]
[]
0
0
null
[ "Eukaryota", "Mimiviridae sp. ChoanoV1", "Pseudoalteromonas amylolytica", "viral metagenome" ]
[ 21733, 2, 1, 5 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 39, 3, 87, 43, 68 ]
6
true
Domain
Kringle
Kringle
Kringle
8
IPR000003
3
Retinoid X receptor/HNF4
Retinoid-X_rcpt/HNF4
Family
8,170
false
false
Steroid or nuclear hormone receptors (NRs) constitute an important superfamily of transcription regulators that are involved in widely diverse physiological functions, including control of embryonic development, cell differentiation and homeostasis. Members of the superfamily include the steroid hormone receptors and r...
[ "GO:0003677", "GO:0003707", "GO:0008270", "GO:0006355", "GO:0005634" ]
[ "DNA binding", "nuclear steroid receptor activity", "zinc ion binding", "regulation of DNA-templated transcription", "nucleus" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
5
[ "PRINTS" ]
[ "PR00545" ]
[ "RETINOIDXR" ]
[ 8170 ]
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-383280", "R-BTA-5362517", "R-CEL-383280", "R-DME-159418", "R-DME-200425", "R-DME-381340", "R-DME-383280", "R-DME-400206", "R-DME-5362517", "R-DME-9029569", "R-DME-9616222", "R-DME-9623433", "R-DME-9707564", "R-DME-9841922", "R-DRE-159418", "R-DRE-381340", "R-DRE-400206", "R-...
[ "REACTOME:R-BTA-383280", "REACTOME:R-BTA-5362517", "REACTOME:R-CEL-383280", "REACTOME:R-DME-159418", "REACTOME:R-DME-200425", "REACTOME:R-DME-381340", "REACTOME:R-DME-383280", "REACTOME:R-DME-400206", "REACTOME:R-DME-5362517", "REACTOME:R-DME-9029569", "REACTOME:R-DME-9616222", "REACTOME:R-DME...
85
[ "1dkf", "1fby", "1fm6", "1fm9", "1g1u", "1g2n", "1g5y", "1h9u", "1hg4", "1k74", "1mv9", "1mvc", "1mzn", "1r1k", "1r20", "1rdt", "1uhl", "1xdk", "1xiu", "1xls", "1xv9", "1xvp", "1z5x", "2acl", "2gl8", "2nxx", "2p1t", "2p1u", "2p1v", "2q60", "2r40", "2zxz"...
127
[ "PUB00004464", "PUB00006168", "PUB00015853", "PUB00057400" ]
[ "7899080", "8165128", "14747695", "19440305" ]
[ "Vitamin D receptor contains multiple dimerization interfaces that are functionally different.", "Human androgen receptor expressed in HeLa cells activates transcription in vitro.", "Nuclear receptors: the evolution of diversity.", "Identification of an endogenous ligand bound to a native orphan nuclear recep...
[ 1995, 1994, 2004, 2009 ]
4
[ "IPR001723" ]
[]
1
0
1
[ "Metazoa" ]
[ 8170 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 40, 4, 22, 20, 24 ]
6
true
Family
Retinoid X receptor/HNF4
Retinoid X receptor/HNF4
Retinoid-X_rcpt/HNF4
9
IPR000006
6
Metallothionein, vertebrate
Metalthion_vert
Family
2,444
false
false
Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , ]. An empirical classification into three classes has been proposed by Fowler and coworkers [ ] and K...
[ "GO:0046872" ]
[ "metal ion binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF00131", "PR00860", "PTHR23299" ]
[ "Metallothio", "MTVERTEBRATE", "" ]
[ 2435, 2038, 2252 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00180", "R-BTA-5661231", "R-CFA-5661231", "R-DRE-5661231", "R-GGA-5661231", "R-HSA-5661231", "R-HSA-877300", "R-MMU-5661231", "R-RNO-5661231", "R-SSC-5661231" ]
[ "PROSITEDOC:PDOC00180", "REACTOME:R-BTA-5661231", "REACTOME:R-CFA-5661231", "REACTOME:R-DRE-5661231", "REACTOME:R-GGA-5661231", "REACTOME:R-HSA-5661231", "REACTOME:R-HSA-877300", "REACTOME:R-MMU-5661231", "REACTOME:R-RNO-5661231", "REACTOME:R-SSC-5661231" ]
10
[ "1dfs", "1dft", "1ji9", "1m0g", "1mhu", "1mrb", "1mrt", "2f5h", "2fj4", "2fj5", "2mhu", "2mrb", "2mrt", "4mt2" ]
14
[ "PUB00001490", "PUB00003570", "PUB00003571", "PUB00005944", "PUB00078698" ]
[ "2959513", "1779825", "1779826", "2959504", "21633816" ]
[ "Chemistry and biochemistry of metallothionein.", "Overview of metallothionein.", "Definitions and nomenclature of metallothioneins.", "Nomenclature of metallothionein.", "Metallothionein protein evolution: a miniassay." ]
[ 1987, 1991, 1991, 1987, 2011 ]
5
[]
[]
0
0
null
[ "Vertebrata" ]
[ 2444 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 35, 13, 14 ]
4
true
Family
Metallothionein, vertebrate
Metallothionein, vertebrate
Metalthion_vert
1
IPR000007
7
Tubby, C-terminal
Tubby_C
Domain
15,382
false
false
Tubby, an autosomal recessive mutation, mapping to mouse chromosome 7, was recently found to be the result of a splicing defect in a novel gene with unknown function. This mutation maps to the tub gene [ , ]. The mouse tubby mutation is the cause of maturity-onset obesity, insulin resistance and sensory deficits. By co...
[]
[]
[]
0
[ "PFAM", "PRINTS" ]
[ "PF01167", "PR01573" ]
[ "Tub", "SUPERTUBBY" ]
[ 15378, 12899 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00923", "R-CEL-5610787", "R-HSA-5610787", "R-HSA-8951664", "R-MMU-5610787", "R-MMU-8951664" ]
[ "PROSITEDOC:PDOC00923", "REACTOME:R-CEL-5610787", "REACTOME:R-HSA-5610787", "REACTOME:R-HSA-8951664", "REACTOME:R-MMU-5610787", "REACTOME:R-MMU-8951664" ]
6
[ "1c8z", "1i7e", "1s31", "2fim", "3c5n", "8fh3" ]
6
[ "PUB00000932", "PUB00004232", "PUB00007281", "PUB00014197" ]
[ "8612280", "8606774", "10591637", "14708010" ]
[ "Identification and characterization of the mouse obesity gene tubby: a member of a novel gene family.", "A candidate gene for the mouse mutation tubby.", "Implication of tubby proteins as transcription factors by structure-based functional analysis.", "Tubby proteins: the plot thickens." ]
[ 1996, 1996, 1999, 2004 ]
4
[]
[]
0
0
null
[ "Eukaryota", "marine metagenome" ]
[ 15380, 2 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 53, 3, 34, 5, 22, 20, 34, 22, 85 ]
9
true
Domain
Tubby, C-terminal
Tubby, C-terminal
Tubby_C
8
IPR000009
9
Protein phosphatase 2A regulatory subunit PR55
PP2A_PR55
Family
14,179
false
false
Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase implicated in many cellular processes, including the regulation of metabolic enzymes and proteins involved in signal transduction [ , ]. PP2A is a trimer composed of a 36kDa catalytic subunit, a 65kDa regulatory subunit (subunit A) and a variable third sub...
[ "GO:0019888", "GO:0000159" ]
[ "protein phosphatase regulator activity", "protein phosphatase type 2A complex" ]
[ "molecular_function", "cellular_component" ]
2
[ "PIRSF", "PRINTS", "PANTHER" ]
[ "PIRSF037309", "PR00600", "PTHR11871" ]
[ "PP2A_PR55", "PP2APR55", "" ]
[ 11746, 13709, 14038 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00785", "R-CEL-2995383", "R-CEL-69231", "R-CEL-69273", "R-CEL-975957", "R-CEL-9860927", "R-DDI-69231", "R-DDI-69273", "R-DME-209155", "R-DME-209190", "R-DME-209214", "R-DME-209360", "R-DME-209396", "R-DME-209413", "R-DME-209440", "R-DME-209461", "R-DME-2995383", "R-DME-432553"...
[ "PROSITEDOC:PDOC00785", "REACTOME:R-CEL-2995383", "REACTOME:R-CEL-69231", "REACTOME:R-CEL-69273", "REACTOME:R-CEL-975957", "REACTOME:R-CEL-9860927", "REACTOME:R-DDI-69231", "REACTOME:R-DDI-69273", "REACTOME:R-DME-209155", "REACTOME:R-DME-209190", "REACTOME:R-DME-209214", "REACTOME:R-DME-209360...
42
[ "3dw8", "8so0", "8ttb", "8twe", "8uo5", "9c6b", "9c7t", "9mzw", "9n0y", "9n0z" ]
10
[ "PUB00000344", "PUB00003499", "PUB00075288", "PUB00075290" ]
[ "1849734", "1370560", "23886942", "21852958" ]
[ "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform.", "The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton protein which is apparently substituted for by T antigens in complexes with the 36- and 63-kilodalton PP2A subunits, bears little ...
[ 1991, 1992, 2013, 2011 ]
4
[]
[]
0
0
null
[ "Bacillati", "Eukaryota" ]
[ 20, 14159 ]
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...
[ 18, 1, 20, 3, 21, 17, 2, 14, 30, 1, 1, 43 ]
12
true
Family
Protein phosphatase 2A regulatory subunit PR55
Protein phosphatase 2A regulatory subunit PR55
PP2A_PR55
9
IPR000010
10
Cystatin domain
Cystatin_dom
Domain
22,591
false
false
This entry represents the cystatin domain. Cystatins occur mainly as single-domain proteins. However, some extracellular proteins such as kininogen, His-rich glycoprotein and fetuin also contain these domains. Cystatins are cysteine proteinase inhibitors belonging to MEROPS inhibitor family I25, clan IH [ , , ]. They m...
[ "GO:0004869" ]
[ "cysteine-type endopeptidase inhibitor activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PFAM", "SMART", "CDD" ]
[ "PF00031", "PF16845", "SM00043", "cd00042" ]
[ "Cystatin", "SQAPI", "CY", "CY" ]
[ 14944, 6776, 16798, 20038 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00259", "R-BTA-114608", "R-BTA-381426", "R-BTA-6798695", "R-BTA-8957275", "R-CEL-381426", "R-CEL-6798695", "R-CEL-8957275", "R-DDI-6798695", "R-HSA-114608", "R-HSA-140837", "R-HSA-375276", "R-HSA-381426", "R-HSA-416476", "R-HSA-418594", "R-HSA-6798695", "R-HSA-6809371", "R-HSA...
[ "PROSITEDOC:PDOC00259", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8957275", "REACTOME:R-CEL-381426", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-8957275", "REACTOME:R-DDI-6798695", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-140837", "REACTOME:R-HSA...
37
[ "1a67", "1a90", "1cew", "1cyu", "1cyv", "1dvc", "1dvd", "1eqk", "1g96", "1gd3", "1gd4", "1m9g", "1mnl", "1mol", "1n9j", "1nb3", "1nb5", "1r4c", "1rn7", "1roa", "1stf", "1tij", "1yvb", "2ch9", "2kxg", "2l4v", "2mzv", "2oct", "2w9p", "2w9q", "3gax", "3ima"...
126
[ "PUB00001614", "PUB00003412", "PUB00014312" ]
[ "1855589", "2107324", "14587292" ]
[ "The cystatins: protein inhibitors of cysteine proteinases.", "Evolution of proteins of the cystatin superfamily.", "Cystatins." ]
[ 1991, 1990, 2003 ]
3
[]
[ "IPR025760", "IPR025764", "IPR027358" ]
0
3
0
[ "Bacteria", "Bracoviriform", "Eukaryota", "viral metagenome" ]
[ 274, 43, 22273, 1 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 44, 4, 33, 5, 39, 71, 32, 102, 73 ]
9
true
Domain
Cystatin domain
Cystatin domain
Cystatin_dom
6
IPR000011
11
Ubiquitin/SUMO-activating enzyme E1-like
UBQ/SUMO-activ_enz_E1-like
Family
11,773
false
false
This entry includes Ubiquitin-activating enzyme E1 (Uba1), SUMO-activating enzyme subunit 1 (Sae1) and similar proteins from eukaryotes. Sae1 is an heterodimer that acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4 and mediates ATP-dependent activation of SUMO proteins [ , , ]. The post-translational att...
[ "GO:0008641", "GO:0036211" ]
[ "ubiquitin-like modifier activating enzyme activity", "protein modification process" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR01849" ]
[ "UBIQUITINACT" ]
[ 11773 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00463", "R-BTA-3065676", "R-BTA-3065678", "R-BTA-8866652", "R-BTA-983168", "R-DDI-1169408", "R-DDI-3065676", "R-DDI-3065678", "R-DDI-8866652", "R-DDI-936440", "R-DDI-983168", "R-DDI-9909505", "R-DRE-3065676", "R-DRE-3065678", "R-HSA-1169408", "R-HSA-168928", "R-HSA-3065676", "...
[ "PROSITEDOC:PDOC00463", "REACTOME:R-BTA-3065676", "REACTOME:R-BTA-3065678", "REACTOME:R-BTA-8866652", "REACTOME:R-BTA-983168", "REACTOME:R-DDI-1169408", "REACTOME:R-DDI-3065676", "REACTOME:R-DDI-3065678", "REACTOME:R-DDI-8866652", "REACTOME:R-DDI-936440", "REACTOME:R-DDI-983168", "REACTOME:R-D...
42
[ "1y8q", "1y8r", "3cmm", "3kyc", "3kyd", "4ii2", "4ii3", "4nnj", "4p22", "5knl", "5l6h", "5l6i", "5l6j", "5tr4", "5um6", "6cwy", "6cwz", "6dc6", "6nya", "6o82", "6o83", "6xog", "6xoh", "6xoi", "6zhs", "6zht", "6zhu", "6zqh", "7k5j", "7pvn", "7pyv", "7sol"...
78
[ "PUB00015619", "PUB00015620", "PUB00015621", "PUB00015625", "PUB00038452", "PUB00058677", "PUB00063223" ]
[ "15454246", "14998368", "15556404", "15196553", "15660128", "20164921", "11451954" ]
[ "The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications.", "Getting into position: the catalytic mechanisms of protein ubiquitylation.", "Polyubiquitin chains: polymeric protein signals.", "The novel functions of ubiquitination in signaling.", "Structures of the SUMO E1 provi...
[ 2004, 2004, 2004, 2004, 2005, 2010, 2001 ]
7
[ "IPR045886" ]
[ "IPR018075" ]
1
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Mimiviridae", "metagenomes" ]
[ 13, 12, 11729, 11, 8 ]
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...
[ 12, 3, 7, 10, 14, 12, 2, 15, 24, 1, 2, 44 ]
12
true
Family
Ubiquitin/SUMO-activating enzyme E1-like
Ubiquitin/SUMO-activating enzyme E1-like
UBQ/SUMO-activ_enz_E1-like
9
IPR000012
12
Retroviral VpR/VpX protein
RetroV_VpR/X
Family
14,653
false
false
null
[ "GO:0019058", "GO:0042025" ]
[ "viral life cycle", "host cell nucleus" ]
[ "biological_process", "cellular_component" ]
2
[ "HAMAP", "PFAM", "PRINTS" ]
[ "MF_04080", "PF00522", "PR00444" ]
[ "HIV_VPR", "VPR", "HIVVPRVPX" ]
[ 12451, 14650, 13505 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "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-180897", "R-HSA-180910" ]
[ "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-HSA-175474", "REACTOME:R-HSA-175567", "REACTOME:R-HSA-177539", "REACTOME:R-HSA-180...
14
[ "1bde", "1ceu", "1dsj", "1dsk", "1esx", "1fi0", "1m8l", "1vpc", "1x9v", "4cc9", "4z8l", "5aja", "5jk7", "6xqi", "6xqj", "6zx9", "7v7c" ]
17
[ "PUB00000018", "PUB00004048" ]
[ "2611042", "2797181" ]
[ "Genomic divergence of HIV-2 from Ghana.", "Sequence of a novel simian immunodeficiency virus from a wild-caught African mandrill." ]
[ 1989, 1989 ]
2
[]
[]
0
0
null
[ "Actinomycetes", "Lentivirus" ]
[ 2, 14651 ]
2
[]
[]
0
true
Family
Retroviral VpR/VpX protein
Retroviral VpR/VpX protein
RetroV_VpR/X
9
IPR000013
13
Peptidase M7, snapalysin
Peptidase_M7
Family
2,055
false
false
This group of metallopeptidases belong to the MEROPS peptidase family M7 (snapalysin 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. With a molecular weight of around 16kDa, Streptomyces extracellular neutral protease ...
[ "GO:0004222", "GO:0008270", "GO:0006508", "GO:0005576" ]
[ "metalloendopeptidase activity", "zinc ion binding", "proteolysis", "extracellular region" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "NCBIFAM", "PFAM", "PIRSF", "PRINTS" ]
[ "NF033628", "PF02031", "PIRSF016573", "PR00787" ]
[ "snapalysin", "Peptidase_M7", "Peptidase_M7", "NEUTRALPTASE" ]
[ 758, 2055, 1003, 2007 ]
4
[ "EC" ]
[ "3.4.24.77" ]
[ "EC:3.4.24.77" ]
1
[ "1c7k", "1kuh", "4hx3" ]
3
[ "PUB00003579" ]
[ "7674922" ]
[ "Evolutionary families of metallopeptidases." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Bacillati" ]
[ 2055 ]
1
[]
[]
0
true
Family
Peptidase M7, snapalysin
Peptidase M7, snapalysin
Peptidase_M7
1
IPR000014
14
PAS domain
PAS
Domain
531,533
false
false
PAS domains are involved in many signalling proteins where they are used as a signal sensor domain [ ]. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in dif...
[]
[]
[]
0
[ "PFAM", "PFAM", "PROFILE", "SMART", "NCBIFAM", "CDD" ]
[ "PF13188", "PF13426", "PS50112", "SM00091", "TIGR00229", "cd00130" ]
[ "PAS_8", "PAS_9", "PAS", "PAS", "sensory_box", "PAS" ]
[ 44079, 155740, 399400, 379344, 388190, 473527 ]
6
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50112", "R-BTA-1296072", "R-CEL-1234158", "R-CEL-1234176", "R-CEL-5689880", "R-CEL-8951664", "R-CEL-9768919", "R-CFA-1296072", "R-CFA-5576890", "R-DME-1234158", "R-DME-1234176", "R-DME-1296072", "R-DME-211945", "R-DME-418555", "R-DME-432395", "R-DME-432408", "R-DME-432490", "R...
[ "PROSITEDOC:PDOC50112", "REACTOME:R-BTA-1296072", "REACTOME:R-CEL-1234158", "REACTOME:R-CEL-1234176", "REACTOME:R-CEL-5689880", "REACTOME:R-CEL-8951664", "REACTOME:R-CEL-9768919", "REACTOME:R-CFA-1296072", "REACTOME:R-CFA-5576890", "REACTOME:R-DME-1234158", "REACTOME:R-DME-1234176", "REACTOME:...
150
[ "1byw", "1d06", "1d7e", "1dp6", "1dp8", "1dp9", "1drm", "1ew0", "1f98", "1f9i", "1g28", "1gsv", "1gsw", "1gsx", "1jnu", "1kou", "1ll8", "1lsv", "1lsw", "1lsx", "1lt0", "1mzu", "1n9l", "1n9n", "1n9o", "1nwz", "1odv", "1ot6", "1ot9", "1ota", "1otb", "1otd"...
546
[ "PUB00005472", "PUB00014500", "PUB00014501", "PUB00015791" ]
[ "9301332", "15009198", "12377121", "10357859" ]
[ "PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox.", "The PAS fold. A redefinition of the PAS domain based upon structural prediction.", "Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation.", "PAS domains: internal sensors of oxyg...
[ 1997, 2004, 2002, 1999 ]
4
[]
[ "IPR013655", "IPR013656", "IPR013767", "IPR059127" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 16268, 413505, 96392, 84, 5284 ]
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",...
[ 149, 13, 207, 64, 14, 152, 123, 14, 66, 165, 3, 7, 111 ]
13
true
Domain
PAS domain
PAS domain
PAS
3
IPR000015
15
Outer membrane usher protein
Fimb_usher
Family
29,210
false
false
In Gram-negative bacteria the biogenesis of fimbriae (or pili) requires a two-component assembly and transport system which is composed of a periplasmic chaperone and an outer membrane protein which has been termed a molecular 'usher' [ , , ]. The usher protein is rather large (from 86 to 100kDa) and seems to be mainly...
[ "GO:0015473", "GO:0009297", "GO:0016020" ]
[ "fimbrial usher porin activity", "pilus assembly", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER" ]
[ "PF00577", "PTHR30451" ]
[ "Usher", "" ]
[ 27974, 29124 ]
2
[ "PROSITEDOC" ]
[ "PDOC00886" ]
[ "PROSITEDOC:PDOC00886" ]
1
[ "1zdv", "1zdx", "1ze3", "2kt6", "2vqi", "2xet", "3bwu", "3fcg", "3fip", "3l48", "3ohn", "3rfz", "4b0e", "4b0m", "4j3o", "6cd2", "6e14", "6e15", "7b0x", "7lhg", "7lhh", "7lhi", "9bog", "9fw9", "9fwb", "9fwz", "9fx8", "9fxb", "9fxs", "9fy9" ]
30
[ "PUB00002237", "PUB00002841", "PUB00005083", "PUB00049856", "PUB00052911" ]
[ "7906265", "7909802", "7906046", "18485872", "19380723" ]
[ "Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli.", "Chaperone-assisted self-assembly of pili independent of cellular energy.", "Structural and evolutionary relationships between two families of bacterial extracytoplasmic chaperone proteins which function coo...
[ 1994, 1994, 1993, 2008, 2009 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 29088, 57, 65 ]
3
[ "Escherichia coli (strain K12)" ]
[ 11 ]
1
true
Family
Outer membrane usher protein
Outer membrane usher protein
Fimb_usher
3
IPR000018
18
P2Y purinoceptor 4
P2Y4
Family
710
false
false
There are three distinct families of extracellular receptors for purine and pyrimidine nucleotides [ ], known as P1, P2X and P2Y purinoceptors [ ]. These receptors induce a wide variety of biological effects and are involved in many different cellular functions [ , , ]. P2X receptors are ligand-gated ion channels, wher...
[ "GO:0045028", "GO:0007186", "GO:0030321", "GO:0016020" ]
[ "G protein-coupled purinergic nucleotide receptor activity", "G protein-coupled receptor signaling pathway", "transepithelial chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01066" ]
[ "P2Y4PRNOCPTR" ]
[ 710 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "325", "R-HSA-417957", "R-HSA-418594", "R-MMU-417957", "R-MMU-418594", "R-RNO-417957", "R-RNO-418594" ]
[ "IUPHAR:325", "REACTOME:R-HSA-417957", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-417957", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-417957", "REACTOME:R-RNO-418594" ]
7
[ "9k0k" ]
1
[ "PUB00002940", "PUB00007054", "PUB00028347", "PUB00033968", "PUB00066193", "PUB00066194", "PUB00066195", "PUB00066196", "PUB00066197", "PUB00066198", "PUB00066203", "PUB00066204", "PUB00066205", "PUB00066206", "PUB00066207", "PUB00066208", "PUB00066209", "PUB00066210", "PUB000662...
[ "8537336", "12270951", "8872457", "11111826", "10629443", "20471713", "11099464", "19921464", "11734617", "16257449", "9364468", "7724657", "16968944", "8508924", "19386608", "8921391", "8702478", "12724320", "18404483", "9755289", "11794691", "16914897", "16934527", "1...
[ "Cloning and functional expression of a human uridine nucleotide receptor.", "Molecular physiology of P2X receptors.", "Modelling the P2Y purinoceptor using rhodopsin as template.", "Molecular pharmacology of P2Y-receptors.", "Renal vascular reactivity to P(2)-purinoceptor activation in spontaneously hypert...
[ 1995, 2002, 1995, 2000, 2000, 2011, 2000, 2010, 2001, 2006, 1997, 1994, 2006, 1993, 2009, 1996, 1996, 2003, 2006, 1998, 2001, 2006, 2006, 2000, 2001, 2005, 2009, 2001, 2009, 2006, 1995, 2000, 1998, 2008, 2006, 2006, 2003 ]
37
[ "IPR000276" ]
[]
1
0
1
[ "Vertebrata" ]
[ 710 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 2, 2 ]
4
true
Family
P2Y purinoceptor 4
P2Y purinoceptor 4
P2Y4
8
IPR000020
20
Anaphylatoxin/fibulin
Anaphylatoxin/fibulin
Domain
8,581
false
false
This entry represents C3a, C4a and C5a anaphylatoxins, which are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins. Complement components C3, C4 and C5 are ...
[ "GO:0005576" ]
[ "extracellular region" ]
[ "cellular_component" ]
1
[ "PFAM", "PROSITE", "PROFILE", "SMART", "CDD" ]
[ "PF01821", "PS01177", "PS01178", "SM00104", "cd00017" ]
[ "ANATO", "ANAPHYLATOXIN_1", "ANAPHYLATOXIN_2", "ANATO", "ANATO" ]
[ 7322, 6418, 8103, 7807, 6578 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00906", "R-BTA-173736", "R-BTA-174577", "R-BTA-198933", "R-BTA-375276", "R-BTA-381426", "R-BTA-418594", "R-BTA-6798695", "R-BTA-8957275", "R-BTA-977606", "R-CEL-2129379", "R-HSA-166663", "R-HSA-166665", "R-HSA-173736", "R-HSA-174577", "R-HSA-198933", "R-HSA-2129379", "R-HSA-37...
[ "PROSITEDOC:PDOC00906", "REACTOME:R-BTA-173736", "REACTOME:R-BTA-174577", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8957275", "REACTOME:R-BTA-977606", "REACTOME:R-CEL-2129379", "REACTOME:R-HSA-1...
47
[ "1c5a", "1cfa", "1kjs", "2a73", "3cu7", "3hqa", "3hqb", "3kls", "3km9", "3prx", "3pvm", "4e0s", "4hw5", "4hwj", "4i6o", "4p39", "4p3a", "4p3b", "4uu9", "4wb2", "4wb3", "5b4p", "5hcc", "5hcd", "5hce", "5i5k", "5jpm", "5jpn", "6jv7", "6jv8", "6rqj", "6ru5"...
58
[ "PUB00001343", "PUB00002512", "PUB00003065", "PUB00003073", "PUB00003181", "PUB00011223" ]
[ "3081348", "2777798", "2269669", "8245130", "1431125", "12778127" ]
[ "C5a fragment of bovine complement. Purification, bioassays, amino-acid sequence and other structural studies.", "Sequence of the gene for murine complement component C4.", "Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure.", "Structure and expression of fibulin-2, a n...
[ 1986, 1989, 1990, 1993, 1992, 2003 ]
6
[]
[ "IPR001840" ]
0
1
0
[ "Eukaryota", "Pseudomonadati" ]
[ 8578, 3 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 25, 35, 23, 29 ]
5
true
Domain
Anaphylatoxin/fibulin
Anaphylatoxin/fibulin
Anaphylatoxin/fibulin
4
IPR000023
23
Phosphofructokinase domain
Phosphofructokinase_dom
Domain
47,419
false
false
The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes [ ]. One enzyme that utilises this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the...
[ "GO:0003872", "GO:0006096" ]
[ "6-phosphofructokinase activity", "glycolytic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF00365" ]
[ "PFK" ]
[ 47419 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.1.11", "PWY-1042", "PWY-1861", "PWY-5484", "PWY-7385", "R-BTA-6798695", "R-BTA-70171", "R-CEL-6798695", "R-CEL-70171", "R-DME-6798695", "R-DME-70171", "R-HSA-6798695", "R-HSA-70171", "R-MMU-6798695", "R-MMU-70171", "R-RNO-6798695", "R-RNO-70171", "R-SCE-6798695", "R-SCE-7017...
[ "EC:2.7.1.11", "METACYC:PWY-1042", "METACYC:PWY-1861", "METACYC:PWY-5484", "METACYC:PWY-7385", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-70171", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-70171", "REACTOME:R-DME-6798695", "REACTOME:R-DME-70171", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-70171...
21
[ "1kzh", "1mto", "1pfk", "1zxx", "2f48", "2hig", "2pfk", "3f5m", "3hno", "3k2q", "3o8l", "3o8n", "3o8o", "3opy", "3pfk", "3u39", "4a3s", "4i36", "4i4i", "4i7e", "4omt", "4pfk", "4rh3", "4u1r", "4wl0", "4xyj", "4xyk", "4xz2", "5xoe", "5xz6", "5xz7", "5xz8"...
54
[ "PUB00000020", "PUB00003237", "PUB00004002", "PUB00014238" ]
[ "7825568", "2975709", "2953977", "12023862" ]
[ "Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency.", "Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products.", "Mutations in the active site of Escheric...
[ 1995, 1988, 1987, 2002 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 87, 27375, 19185, 5, 767 ]
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",...
[ 42, 2, 28, 6, 1, 43, 14, 1, 45, 23, 2, 1, 116 ]
13
true
Domain
Phosphofructokinase domain
Phosphofructokinase domain
Phosphofructokinase_dom
6
IPR000025
25
Melatonin receptor family
Melatonin_rcpt
Family
3,216
false
false
Melatonin is a naturally occurring compound found in animals, plants, and microbes [ , ]. In animals melatonin is secreted by the pineal gland during darkness [ , ]. It regulates a variety of neuroendocrine functions and is thought to play an essential role in circadian rhythms [ ]. Drugs that modify the action of mela...
[ "GO:0008502", "GO:0007186", "GO:0016020" ]
[ "melatonin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00857" ]
[ "MELATONINR" ]
[ 3216 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "288", "R-DRE-373076", "R-DRE-418594", "R-GGA-373076", "R-GGA-418594", "R-HSA-373076", "R-HSA-418594", "R-MMU-373076", "R-MMU-418594", "R-RNO-373076", "R-RNO-418594" ]
[ "IUPHAR:288", "REACTOME:R-DRE-373076", "REACTOME:R-DRE-418594", "REACTOME:R-GGA-373076", "REACTOME:R-GGA-418594", "REACTOME:R-HSA-373076", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-373076", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-373076", "REACTOME:R-RNO-418594" ]
11
[ "6me2", "6me3", "6me4", "6me5", "6me6", "6me7", "6me8", "6me9", "6ps8", "7db6", "7vgy", "7vgz", "7vh0" ]
13
[ "PUB00066873", "PUB00066874", "PUB00066875", "PUB00066876", "PUB00066877", "PUB00066878", "PUB00066879", "PUB00066880", "PUB00066881", "PUB00066882" ]
[ "15206778", "19033551", "1649044", "17901231", "17298593", "16473858", "15992934", "8936344", "15357831", "9933574" ]
[ "Melatonin in plants.", "Phytomelatonin: a review.", "Pineal melatonin: cell biology of its synthesis and of its physiological interactions.", "Minireview: Entrainment of the suprachiasmatic clockwork in diurnal and nocturnal mammals.", "Melatonin: therapeutic and clinical utilization.", "Efficacy and saf...
[ 2003, 2009, 1991, 2007, 2007, 2006, 2005, 1996, 2004, 1999 ]
10
[ "IPR000276" ]
[ "IPR002278", "IPR002280" ]
1
2
0
[ "Bilateria" ]
[ 3216 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 7, 6, 11 ]
4
true
Family
Melatonin receptor family
Melatonin receptor family
Melatonin_rcpt
9
IPR000026
26
Guanine-specific ribonuclease N1-like
N1-like
Family
8,591
false
false
This entry represents Guanyl-specific ribonuclease N1 from Neurospora crassa [ ], and similar sequences from fungi and bacteria, including Ribonuclease from Bacillus amyloliquefaciens (also known as Barnase) and Ribonuclease clavin from Aspergillus clavatus. Barnase hydrolyses the phosphodiester bonds in RNA and oligor...
[ "GO:0003723", "GO:0004521" ]
[ "RNA binding", "RNA endonuclease activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF00545" ]
[ "Ribonuclease" ]
[ 8591 ]
1
[ "EC" ]
[ "4.6.1.24" ]
[ "EC:4.6.1.24" ]
1
[ "1a2p", "1aqz", "1ay7", "1b20", "1b21", "1b27", "1b2m", "1b2s", "1b2u", "1b2x", "1b2z", "1b3s", "1ban", "1bao", "1bgs", "1bir", "1bne", "1bnf", "1bng", "1bni", "1bnj", "1bnr", "1bns", "1box", "1brg", "1brh", "1bri", "1brj", "1brk", "1brn", "1brs", "1bsa"...
187
[ "PUB00000397", "PUB00075293", "PUB00094167" ]
[ "8110767", "2977130", "8706730" ]
[ "Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution.", "The amino acid sequence of ribonuclease N1, a guanine-specific ribonuclease from the fungus Neurospora crassa.", "Clavin, a type-1 ribosome-inactivating protein from Aspergillus clavatus IFO 8605. cDNA isolatio...
[ 1994, 1988, 1996 ]
3
[]
[ "IPR001887" ]
0
1
0
[ "Bacteria", "Eukaryota", "Methanobacteriota", "metagenomes" ]
[ 5833, 2722, 17, 19 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Family
Guanine-specific ribonuclease N1-like
Guanine-specific ribonuclease N1-like
N1-like
6
IPR000028
28
Chloroperoxidase
Chloroperoxidase
Domain
9,007
false
false
Chloroperoxidase (CPO), also known as Heme haloperoxidase, is a ~250 residue heme-containing glycoprotein that is secreted by various fungi. Chloroperoxidase was first identified in Caldariomyces fumago where it catalyses the hydrogen peroxide-dependent chlorination of cyclopentanedione during the biosynthesis of the a...
[ "GO:0004601" ]
[ "peroxidase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF01328", "PS51405" ]
[ "Peroxidase_2", "HEME_HALOPEROXIDASE" ]
[ 8999, 8880 ]
2
[ "GP" ]
[ "GenProp0213" ]
[ "GP:GenProp0213" ]
1
[ "1cpo", "2civ", "2ciw", "2cix", "2ciy", "2ciz", "2cj0", "2cj1", "2cj2", "2cpo", "2j18", "2j19", "2j5m", "2yor", "2yp1", "5fuj", "5fuk", "5oxt", "5oxu", "5oy1", "5oy2", "6ekw", "6ekx", "6eky", "6ekz", "6el0", "6el4", "7o1r", "7o1x", "7o1z", "7o2d", "7o2g"...
68
[ "PUB00005255", "PUB00040032", "PUB00052607", "PUB00052608" ]
[ "8747463", "16790441", "16628447", "18220360" ]
[ "The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.", "Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate.", "Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental...
[ 1995, 2006, 2006, 2008 ]
4
[]
[]
0
0
null
[ "Eukaryota", "viral metagenome" ]
[ 9006, 1 ]
2
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 2 ]
1
true
Domain
Chloroperoxidase
Chloroperoxidase
Chloroperoxidase
8
IPR000030
30
PPE domain
PPE_dom
Domain
12,585
false
false
This entry represents a domain found in proteins from actinomycetes named after a conserved N-terminal region of about 180 amino acids, the PPE motif. The C-terminal end of proteins belonging to the PPE family is variable, and on the basis of this region at least three groups can be distinguished. The MPTR subgroup is ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00823" ]
[ "PPE" ]
[ 12585 ]
1
[ "REACTOME" ]
[ "R-HSA-9636249" ]
[ "REACTOME:R-HSA-9636249" ]
1
[ "2g38", "4kxr", "4w4k", "4w4l", "5xfs", "6uuj", "6vhr", "6vj5" ]
8
[ "PUB00004280", "PUB00054031", "PUB00054032", "PUB00054033", "PUB00095123", "PUB00103913", "PUB00103914", "PUB00103929", "PUB00103930" ]
[ "9634230", "19602151", "18981138", "18267304", "31375544", "32138343", "32139546", "25155747", "25275011" ]
[ "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.", "Mycobacterial PE, PPE and ESX clusters: novel insights into the secretion of these most unusual protein families.", "The ESX-5 secretion system of Mycobacterium marinum modulates the macrophage response.", "Mycobacter...
[ 1998, 2009, 2008, 2007, 2019, 2020, 2020, 2014, 2014 ]
9
[]
[]
0
0
null
[ "Aduncisulcus paluster", "Bacteria", "Chenonavirus", "freshwater metagenome" ]
[ 1, 12580, 2, 2 ]
4
[]
[]
0
true
Domain
PPE domain
PPE domain
PPE_dom
8
IPR000031
31
PurE domain
PurE_dom
Domain
34,722
false
false
The novo purine biosynthesis proceeds by two divergent paths. In bacteria, yeasts, and plants, 5-aminoimidazole ribonucleotide (AIR) is converted to 4-carboxy-AIR (CAIR) by two enzymes: N5-carboxy-AIR (N5-CAIR) synthetase (PurK) and N5-CAIR mutase (class I PurE). In animals, the conversion of AIR to CAIR requires a sin...
[ "GO:0006189" ]
[ "'de novo' IMP biosynthetic process" ]
[ "biological_process" ]
1
[ "PFAM", "SMART", "NCBIFAM" ]
[ "PF00731", "SM01001", "TIGR01162" ]
[ "AIRC", "AIRC", "purE" ]
[ 34633, 34572, 27260 ]
3
[ "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp0110", "GenProp1406", "GenProp1730", "GenProp1757", "R-CEL-73817", "R-DME-73817", "R-GGA-419140", "R-HSA-73817", "R-MMU-73817", "R-RNO-73817" ]
[ "GP:GenProp0110", "GP:GenProp1406", "GP:GenProp1730", "GP:GenProp1757", "REACTOME:R-CEL-73817", "REACTOME:R-DME-73817", "REACTOME:R-GGA-419140", "REACTOME:R-HSA-73817", "REACTOME:R-MMU-73817", "REACTOME:R-RNO-73817" ]
10
[ "1d7a", "1o4v", "1qcz", "1u11", "1xmp", "2ate", "2fw1", "2fw6", "2fw7", "2fw8", "2fw9", "2fwa", "2fwb", "2fwi", "2fwj", "2fwp", "2h31", "2nsh", "2nsj", "2nsl", "2ywx", "3kuu", "3lp6", "3oow", "3opq", "3ors", "3rg8", "3rgg", "3trh", "4ay3", "4ay4", "4b4k"...
63
[ "PUB00056870", "PUB00068323", "PUB00068324", "PUB00080668" ]
[ "7918411", "9500840", "7918410", "8111040" ]
[ "Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms.", "Biochemical role of the Cryptococcus neoformans ADE2 protein in fungal de novo purine biosynthesis.", "Carboxylases in de novo purine biosynthesis. Characte...
[ 1994, 1998, 1994, 1994 ]
4
[]
[ "IPR033626", "IPR033747" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1469, 27332, 5127, 25, 769 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 11, 1, 3, 2, 1, 3, 1, 1, 4, 6, 1, 1, 16 ]
13
true
Domain
PurE domain
PurE domain
PurE_dom
5
IPR000032
32
Phosphocarrier protein HPr-like
HPr-like
Domain
37,795
false
false
This entry represents a structural domain found in both the histidine-containing phosphocarrier protein HPr, as well as its structural homologues, which includes the catabolite repression protein Crh found in Bacillus subtilis [ , ]. This domain has a α+β structure found in two layers with an overall architecture of an...
[]
[]
[]
0
[ "PFAM", "PRINTS", "PROFILE", "NCBIFAM", "CDD" ]
[ "PF00381", "PR00107", "PS51350", "TIGR01003", "cd00367" ]
[ "PTS-HPr", "PHOSPHOCPHPR", "PTS_HPR_DOM", "PTS_HPr_family", "PTS-HPr_like" ]
[ 37493, 32928, 36689, 32165, 31957 ]
5
[ "GP", "GP" ]
[ "GenProp0119", "GenProp1324" ]
[ "GP:GenProp0119", "GP:GenProp1324" ]
2
[ "1cm2", "1cm3", "1fu0", "1ggr", "1hdn", "1j6t", "1jem", "1k1c", "1ka5", "1kkl", "1kkm", "1mo1", "1mu4", "1opd", "1pch", "1pfh", "1poh", "1ptf", "1qfr", "1qr5", "1rzr", "1sph", "1txe", "1vrc", "1y4y", "1y50", "1y51", "1zvv", "2ak7", "2fep", "2hid", "2hpr"...
64
[ "PUB00000073", "PUB00003342", "PUB00003612", "PUB00004777", "PUB00005010", "PUB00005243", "PUB00025027", "PUB00032584", "PUB00039040", "PUB00070137" ]
[ "2197982", "7853396", "8246840", "1549615", "7686067", "7704530", "11054290", "15713472", "16316990", "9237995" ]
[ "The bacterial phosphoenolpyruvate: glycose phosphotransferase system.", "High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data.", "Phosphoenolpyruvate:carbohydrate phosphotr...
[ 1990, 1995, 1993, 1992, 1993, 1994, 2000, 2005, 2006, 1997 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 253, 37178, 75, 6, 283 ]
5
[ "Escherichia coli (strain K12)" ]
[ 6 ]
1
true
Domain
Phosphocarrier protein HPr-like
Phosphocarrier protein HPr-like
HPr-like
9
IPR000033
33
LDLR class B repeat
LDLR_classB_rpt
Repeat
38,754
false
false
The low-density lipoprotein receptor (LDLR) is the major cholesterol-carrying lipoprotein of plasma, acting to regulate cholesterol homeostasis in mammalian cells. The LDL receptor binds LDL and transports it into cells by acidic endocytosis. In order to be internalized, the receptor-ligand complex must first cluster i...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00058", "PS51120", "SM00135" ]
[ "Ldl_recept_b", "LDLRB", "LY" ]
[ 31367, 32652, 38584 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC51120", "R-BTA-114608", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-8964026", "R-BTA-8964038", "R-DME-114608", "R-DME-1227986", "R-DME-1236394", "R-DME-1250196", "R-DME-1257604", "R-DME-177929", "R-DME-179812", "R-DME-180292", "R-DME-180336", "R-DME-182971", "R-DME-1963642", "R-D...
[ "PROSITEDOC:PDOC51120", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-8964026", "REACTOME:R-BTA-8964038", "REACTOME:R-DME-114608", "REACTOME:R-DME-1227986", "REACTOME:R-DME-1236394", "REACTOME:R-DME-1250196", "REACTOME:R-DME-1257604", "REACTOME:R-...
149
[ "1ijq", "1n7d", "1npe", "1rwi", "1rwl", "3m0c", "3p5b", "3p5c", "3s2k", "3s8v", "3s8z", "3s94", "3sob", "3soq", "3sov", "3v64", "3v65", "3ww8", "3ww9", "3wwa", "4a0p", "4dg6", "5b4x", "5fww", "5gje", "6f0q", "6f0s", "6f0t", "6h15", "6h16", "6i37", "6i38"...
98
[ "PUB00000798", "PUB00003391", "PUB00004868", "PUB00017008", "PUB00017009", "PUB00017010", "PUB00042617" ]
[ "6091915", "9790844", "7603991", "3513311", "3494949", "11373616", "17457719" ]
[ "The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its mRNA.", "An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components.", "Three-dimensional structure of a cyst...
[ 1984, 1998, 1995, 1986, 1987, 2001, 2007 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 55, 1176, 37473, 50 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 6, 13, 96, 35, 90, 66, 2, 2, 69, 3 ]
10
true
Repeat
LDLR class B repeat
LDLR class B repeat
LDLR_classB_rpt
6
IPR000034
34
Laminin IV
Laminin_IV
Domain
13,238
false
false
Laminin is a large molecular weight glycoprotein present only in basement membranes in almost every animal tissue. Each laminin is a heterotrimer assembled from alpha, beta and gamma chain subunits, secreted and incorporated into cell-associated extracellular matrices. The laminins can self-assemble, bind to other matr...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00052", "PS51115", "SM00281" ]
[ "Laminin_B", "LAMININ_IVA", "LamB" ]
[ 13156, 12809, 12513 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC51115", "R-HSA-1474228", "R-HSA-1971475", "R-HSA-2022090", "R-HSA-2022928", "R-HSA-2024096", "R-HSA-216083", "R-HSA-2214320", "R-HSA-3000157", "R-HSA-3000171", "R-HSA-3000178", "R-HSA-3560783", "R-HSA-3560801", "R-HSA-3656237", "R-HSA-3656253", "R-HSA-373760", "R-HSA-381426", ...
[ "PROSITEDOC:PDOC51115", "REACTOME:R-HSA-1474228", "REACTOME:R-HSA-1971475", "REACTOME:R-HSA-2022090", "REACTOME:R-HSA-2022928", "REACTOME:R-HSA-2024096", "REACTOME:R-HSA-216083", "REACTOME:R-HSA-2214320", "REACTOME:R-HSA-3000157", "REACTOME:R-HSA-3000171", "REACTOME:R-HSA-3000178", "REACTOME:R...
32
[ "4yep", "4yeq", "9i5a", "9i5b" ]
4
[ "PUB00012222", "PUB00017000", "PUB00017032" ]
[ "3182802", "10842354", "15363809" ]
[ "Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains.", "Form and function: the laminin family of heterotrimers.", "Assembly and tissue functions of early embryonic laminins and netrins." ]
[ 1988, 2000, 2004 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "hydrothermal vent metagenome" ]
[ 87, 13125, 24, 2 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 18, 67, 36, 17, 20, 28 ]
6
true
Domain
Laminin IV
Laminin IV
Laminin_IV
6
IPR000035
35
Alkylbase DNA glycosidase, conserved site
Alkylbase_DNA_glycsylse_CS
Conserved_site
2,672
false
false
Alkylbase DNA glycosidases [ ] are DNA repair enzymes that hydrolyse the deoxyribose N-glycosidic bond to excise various alkylated bases from a damaged DNA polymer. In Escherichia coli there are two alkylbase DNA glycosidases: one (gene tag) which is constitutively expressed and which is specific for the removal of 3-m...
[ "GO:0003905", "GO:0006281" ]
[ "alkylbase DNA N-glycosylase activity", "DNA repair" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00516" ]
[ "ALKYLBASE_DNA_GLYCOS" ]
[ 2672 ]
1
[ "EC", "PROSITEDOC" ]
[ "3.2.2.21", "PDOC00447" ]
[ "EC:3.2.2.21", "PROSITEDOC:PDOC00447" ]
2
[ "1diz", "1mpg", "1pvs", "3cvs", "3cvt", "3cw7", "3cwa", "3cws", "3cwt", "3cwu", "3d4v", "3ogd", "3oh6", "3oh9", "3s6i", "4b21", "4b22", "4b23", "4b24", "4hsb" ]
20
[ "PUB00000053", "PUB00001200", "PUB00001201" ]
[ "3052269", "2265619", "2265620" ]
[ "Regulation and expression of the adaptive response to alkylating agents.", "Cloning and expression in Escherichia coli of a gene for an alkylbase DNA glycosylase from Saccharomyces cerevisiae; a homologue to the bacterial alkA gene.", "Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to th...
[ 1988, 1990, 1990 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Dikarya", "unclassified sequences" ]
[ 60, 2495, 106, 11 ]
4
[ "Escherichia coli (strain K12)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1, 1, 2 ]
3
true
Conserved_site
Alkylbase DNA glycosidase, conserved site
Alkylbase DNA glycosidase, conserved site
Alkylbase_DNA_glycsylse_CS
1
IPR000036
36
Peptidase A26, omptin
Peptidase_A26_omptin
Family
1,686
false
false
This group of aspartic peptidases belongs to the MEROPS family A26 (clan AF). Members of the family are transmembrane proteins. The type example for the family is omptin (also known as protease VII) from Escherichia coli, the product of the ompT gene. Omptin preferentially cleaves polypeptides between two basically-cha...
[ "GO:0004175", "GO:0006508", "GO:0009279" ]
[ "endopeptidase activity", "proteolysis", "cell outer membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PIRSF", "PRINTS" ]
[ "PF01278", "PIRSF001522", "PR00482" ]
[ "Omptin", "Peptidase_A26", "OMPTIN" ]
[ 1686, 1234, 1423 ]
3
[ "PROSITEDOC" ]
[ "PDOC00657" ]
[ "PROSITEDOC:PDOC00657" ]
1
[ "1i78", "2x4m", "2x55", "2x56", "4dcb", "7xw0" ]
6
[ "PUB00000093", "PUB00000349", "PUB00000522", "PUB00001330", "PUB00002071", "PUB00003795", "PUB00011023", "PUB00011707", "PUB00021296", "PUB00042504", "PUB00065205", "PUB00066803", "PUB00076784", "PUB00076785", "PUB00076786", "PUB00076883" ]
[ "2194475", "1851433", "8439290", "6795036", "3056908", "2526282", "10331925", "11566868", "10864493", "2682266", "23254940", "21765428", "4912600", "10497172", "21751400", "11401715" ]
[ "The structure and function of the aspartic proteinases.", "Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.", "Evolutionary families of peptidases.", "Gastric proteinases--structure, function, evolution and mechanism of action.", "Purification, characterizat...
[ 1990, 1991, 1993, 1981, 1988, 1989, 1999, 2001, 2000, 1989, 2013, 2011, 1970, 1999, 2011, 2001 ]
16
[]
[]
0
0
null
[ "Bacteria", "Beauveria bassiana D1-5", "Nesevirus", "ecological metagenomes" ]
[ 1681, 1, 2, 2 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Peptidase A26, omptin
Peptidase A26, omptin
Peptidase_A26_omptin
4
IPR000037
37
SsrA-binding protein
SsrA-bd_prot
Family
25,307
false
false
This entry represents SsrA-binding protein (aka small protein B or SmpB), which is a unique RNA-binding protein that is conserved throughout the bacterial kingdom and is an essential component of the SsrA quality-control system. Tight recognition of codon-anticodon pairings by the ribosome ensures the accuracy and fide...
[ "GO:0003723" ]
[ "RNA binding" ]
[ "molecular_function" ]
1
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00023", "PF01668", "PTHR30308", "TIGR00086", "cd09294" ]
[ "SmpB", "SmpB", "", "smpB", "SmpB" ]
[ 25037, 25306, 25250, 24888, 23281 ]
5
[ "PROSITEDOC" ]
[ "PDOC01021" ]
[ "PROSITEDOC:PDOC01021" ]
1
[ "1j1h", "1k8h", "1p6v", "1wjx", "1zc8", "2czj", "2ob7", "3iyq", "3iyr", "3iz4", "4v6t", "4v8q", "5zey", "6q95", "6q97", "6q98", "6q9a", "7abz", "7ac7", "7acj", "7acr", "7ljp", "8vs9", "8vsa" ]
24
[ "PUB00006449", "PUB00045920" ]
[ "10393194", "19132006" ]
[ "SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA).", "Ribosome hijacking: a role for small protein B during trans-translation." ]
[ 1999, 2009 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "candidate division MSBL1 archaeon SCGC-AAA382A20", "unclassified sequences" ]
[ 24543, 206, 15, 1, 542 ]
5
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
SsrA-binding protein
SsrA-binding protein
SsrA-bd_prot
7
IPR000039
39
Large ribosomal subunit protein eL18
Ribosomal_eL18
Family
6,950
false
false
Members of this family are large subunit ribosomal proteins which are found in eukaryotes and archaea [ , , ]. These proteins have 115 to 187 amino-acid residues. The family consists of: Vertebrate eL18 (known as L14 in Xenopus) [ , ] Plant eL18 Yeast eL18 (Rp28) Haloarcula marismortui (Halobacterium marismortui) HL29 ...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PANTHER" ]
[ "PTHR10934" ]
[ "" ]
[ 6950 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00850", "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-CFA-156827", "R-CFA-1799339", "R-CFA-6791226", "R-CFA-72689...
[ "PROSITEDOC:PDOC00850", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-7270...
79
[ "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"...
671
[ "PUB00000657", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00059102", "PUB00101554" ]
[ "8218404", "11297922", "11290319", "11114498", "22096102", "32669547" ]
[ "Nucleotide and deduced amino acid sequence of human ribosomal protein L18.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "The structure of the eukaryotic ribosome at 3.0 A resolution.", "Structural sn...
[ 1993, 2001, 2001, 2000, 2011, 2020 ]
6
[]
[ "IPR022947" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 728, 6, 6198, 18 ]
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...
[ 14, 1, 1, 2, 10, 10, 1, 6, 12, 2, 2, 15 ]
12
true
Family
Large ribosomal subunit protein eL18
Large ribosomal subunit protein eL18
Ribosomal_eL18
6
IPR000040
40
Acute myeloid leukemia 1 protein (AML1)/Runt
AML1_Runt
Family
6,664
false
false
null
[ "GO:0003677", "GO:0005524", "GO:0006355", "GO:0005634" ]
[ "DNA binding", "ATP binding", "regulation of DNA-templated transcription", "nucleus" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PRINTS", "PANTHER" ]
[ "PR00967", "PTHR11950" ]
[ "ONCOGENEAML1", "" ]
[ 6254, 6650 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-CEL-549127", "R-CEL-8877330", "R-CEL-8878166", "R-CEL-8934593", "R-CEL-8936459", "R-CEL-8939236", "R-CEL-8939243", "R-CEL-8939245", "R-CEL-8939246", "R-CEL-8939247", "R-CEL-8939902", "R-CEL-8941326", "R-CEL-8941855", "R-CEL-8941858", "R-CEL-8951430", "R-CEL-8951671", "R-CEL-895193...
[ "REACTOME:R-CEL-549127", "REACTOME:R-CEL-8877330", "REACTOME:R-CEL-8878166", "REACTOME:R-CEL-8934593", "REACTOME:R-CEL-8936459", "REACTOME:R-CEL-8939236", "REACTOME:R-CEL-8939243", "REACTOME:R-CEL-8939245", "REACTOME:R-CEL-8939246", "REACTOME:R-CEL-8939247", "REACTOME:R-CEL-8939902", "REACTOME...
103
[ "1cmo", "1co1", "1e50", "1ean", "1eao", "1eaq", "1h9d", "1hjb", "1hjc", "1io4", "1ljm", "2j6w", "3wts", "3wtt", "3wtu", "3wtv", "3wtw", "3wtx", "3wty", "3wu1", "4l0y", "4l0z", "4l18", "6vg8", "6vgd", "6vge", "6vgg" ]
27
[ "PUB00004459" ]
[ "7651838" ]
[ "Alternative splicing and genomic structure of the AML1 gene involved in acute myeloid leukemia." ]
[ 1995 ]
1
[]
[ "IPR016554" ]
0
1
0
[ "Opisthokonta" ]
[ 6664 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 62, 23, 24, 19, 21 ]
6
true
Family
Acute myeloid leukemia 1 protein (AML1)/Runt
Acute myeloid leukemia 1 protein (AML1)/Runt
AML1_Runt
2
IPR000043
43
Adenosylhomocysteinase-like
Adenosylhomocysteinase-like
Family
32,325
false
false
Adenosylhomocysteinase (S-adenosyl-L-homocysteine hydrolase, ) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. This enzyme is ubiquitous, highly conserved, and may play a key role in the regulation of the intr...
[]
[]
[]
0
[ "HAMAP", "PFAM", "PIRSF", "PANTHER", "SMART", "NCBIFAM", "CDD" ]
[ "MF_00563", "PF05221", "PIRSF001109", "PTHR23420", "SM00996", "TIGR00936", "cd00401" ]
[ "AdoHcyase", "AdoHcyase", "Ad_hcy_hydrolase", "", "AdoHcyase", "ahcY", "SAHH" ]
[ 21082, 30992, 25259, 32094, 30320, 25484, 27797 ]
7
[ "EC", "GP", "GP", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME",...
[ "3.13.2.1", "GenProp0789", "GenProp1399", "PWY-5041", "PDOC00603", "R-BTA-156581", "R-BTA-1614635", "R-BTA-425381", "R-CEL-156581", "R-CEL-1614635", "R-DDI-156581", "R-DDI-1614635", "R-DME-156581", "R-DME-1614635", "R-DME-425381", "R-DME-5578775", "R-HSA-112043", "R-HSA-1489509", ...
[ "EC:3.13.2.1", "GP:GenProp0789", "GP:GenProp1399", "METACYC:PWY-5041", "PROSITEDOC:PDOC00603", "REACTOME:R-BTA-156581", "REACTOME:R-BTA-1614635", "REACTOME:R-BTA-425381", "REACTOME:R-CEL-156581", "REACTOME:R-CEL-1614635", "REACTOME:R-DDI-156581", "REACTOME:R-DDI-1614635", "REACTOME:R-DME-156...
42
[ "1a7a", "1b3r", "1d4f", "1k0u", "1ky4", "1ky5", "1li4", "1v8b", "1xwf", "2h5l", "2ziz", "2zj0", "2zj1", "3ce6", "3d64", "3dhy", "3g1u", "3glq", "3gvp", "3h9u", "3mtg", "3n58", "3nj4", "3ond", "3one", "3onf", "3x2e", "3x2f", "4lvc", "4pfj", "4pgf", "4yvf"...
121
[ "PUB00021119", "PUB00038377", "PUB00079516", "PUB00079517", "PUB00083397", "PUB00083401", "PUB00083402", "PUB00083418", "PUB00083432", "PUB00083433", "PUB00083434" ]
[ "9586999", "16061414", "11325033", "15165742", "12525476", "16793548", "16527252", "19220705", "24518248", "21152975", "27382360" ]
[ "Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength.", "Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His 54, Asp130, Glu155, Lys185, and Aspl89.", "Structure and function of S-adenosylhomocysteine hydrolase.", "S-Adenosylhomocyste...
[ 1998, 2005, 2000, 2004, 2003, 2006, 2006, 2009, 2014, 2011, 2016 ]
11
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 975, 17748, 12842, 8, 752 ]
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, 1, 10, 6, 14, 22, 1, 7, 20, 1, 1, 11 ]
12
true
Family
Adenosylhomocysteinase-like
Adenosylhomocysteinase-like
Adenosylhomocysteinase-like
3
IPR000044
44
Uncharacterised lipoprotein MG045
Uncharacterised_lipoprot_MG045
Family
79
false
false
Mycoplasma genitalium has the smallest known genome of any free-living organism. Its complete genome sequence has been determined by whole-genome random sequencing and assembly [ ]. Only 470 putative coding regions were identified, including genes for DNA replication, transcription and translation, DNA repair, cellular...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR00905" ]
[ "MG045FAMILY" ]
[ 79 ]
1
[]
[]
[]
0
[]
0
[ "PUB00002233", "PUB00005212" ]
[ "8253680", "7569993" ]
[ "A survey of the Mycoplasma genitalium genome by using random sequencing.", "The minimal gene complement of Mycoplasma genitalium." ]
[ 1993, 1995 ]
2
[]
[]
0
0
null
[ "Mycoplasmatota", "Plasmodium vivax North Korean" ]
[ 78, 1 ]
2
[]
[]
0
true
Family
Uncharacterised lipoprotein MG045
Uncharacterised lipoprotein MG045
Uncharacterised_lipoprot_MG045
7
IPR000045
45
Prepilin type IV endopeptidase, peptidase domain
Prepilin_IV_endopep_pep
Domain
31,058
false
false
This entry represents the peptidase domain from the prepilin type IV endopeptidases [ ]. It can be found on its own such as peptidase HopD in Salmonella typhimurium , or in the case of the bifunctional enzymes such as Prepilin leader peptidase/N-methyltransferase in Vibrio cholerae , next to a methylation domain . This...
[ "GO:0004190", "GO:0016020" ]
[ "aspartic-type endopeptidase activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF01478" ]
[ "Peptidase_A24" ]
[ 31058 ]
1
[ "EC", "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METAC...
[ "2.1.1.-", "3.4.23.43", "GenProp0295", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-...
[ "EC:2.1.1.-", "EC:3.4.23.43", "GP:GenProp0295", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", ...
148
[ "3s0x" ]
1
[ "PUB00000093", "PUB00000349", "PUB00000522", "PUB00001330", "PUB00011023", "PUB00011707", "PUB00014343", "PUB00014532", "PUB00020023", "PUB00021296", "PUB00042504", "PUB00065205", "PUB00066803", "PUB00076784", "PUB00076785", "PUB00076786" ]
[ "2194475", "1851433", "8439290", "6795036", "10331925", "11566868", "14622420", "9224881", "10625704", "10864493", "2682266", "23254940", "21765428", "4912600", "10497172", "21751400" ]
[ "The structure and function of the aspartic proteinases.", "Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.", "Evolutionary families of peptidases.", "Gastric proteinases--structure, function, evolution and mechanism of action.", "Crystal structure of the hy...
[ 1990, 1991, 1993, 1981, 1999, 2001, 2003, 1997, 2000, 2000, 1989, 2013, 2011, 1970, 1999, 2011 ]
16
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Plasmid R64", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 845, 29656, 19, 1, 536, 1 ]
6
[ "Escherichia coli (strain K12)", "Mus musculus" ]
[ 2, 1 ]
2
true
Domain
Prepilin type IV endopeptidase, peptidase domain
Prepilin type IV endopeptidase, peptidase domain
Prepilin_IV_endopep_pep
9
End of preview. Expand in Data Studio

InterPro Entries

This dataset contains a viewer-friendly Parquet table derived from the InterPro current release files in this repository. Each row is one InterPro entry from current_release/interpro.xml.gz.

The original source release files remain in the repository. The default datasets configuration uses the normalized Parquet files under data/ so that the Hugging Face Dataset Viewer and load_dataset() can read the entries directly.

Large release artifacts such as current_release/match_complete.xml.gz, current_release/protein2ipr.dat.gz, and current_release/sites.xml.gz are preserved as source files but are not loaded by the default table.

Splits

The split is deterministic by InterPro identifier: sha256(interpro_id) % 10. Bucket 0 is test; buckets 1 through 9 are train.

Split Rows
train 46,440
test 5,049
total 51,489

Dataset Statistics

Field Value
InterPro release 108.0
Release date 29th January 2026
Entries 51,489
Member database rows 18
Entries with GO mappings 14,799
InterPro-to-GO mapping rows 30,200
Entries with structures 30,172
Entries with publications 38,194
Entry type Rows
Family 27,308
Domain 19,276
Homologous_superfamily 3,510
Conserved_site 768
Repeat 395
Active_site 133
Binding_site 82
PTM 17
GO category Mappings
molecular_function 13,802
biological_process 11,059
cellular_component 5,339

Usage

Install the Hugging Face Datasets library:

pip install datasets

Load all splits:

from datasets import load_dataset

ds = load_dataset("LiteFold/InterPro")
print(ds)

row = ds["train"][0]
print(row["interpro_id"], row["name"], row["entry_type"])

Load one split:

from datasets import load_dataset

train = load_dataset("LiteFold/InterPro", split="train")
test = load_dataset("LiteFold/InterPro", split="test")

Stream rows without downloading the full table first:

from datasets import load_dataset

stream = load_dataset("LiteFold/InterPro", split="train", streaming=True)
for row in stream.take(5):
    print(row["interpro_id"], row["short_name"], row["protein_count"])

Filter entries with GO mappings:

from datasets import load_dataset

ds = load_dataset("LiteFold/InterPro", split="train")
with_go = ds.filter(lambda row: row["go_count"] > 0)
print(with_go[0]["interpro_id"], with_go[0]["go_ids"])

Filter protein domains with PDB structures:

from datasets import load_dataset

ds = load_dataset("LiteFold/InterPro", split="train")
domains_with_structures = ds.filter(
    lambda row: row["entry_type"] == "Domain" and row["structure_count"] > 0
)
print(domains_with_structures[0]["interpro_id"], domains_with_structures[0]["pdb_ids"][:5])

Load release database metadata directly:

import pandas as pd
from huggingface_hub import hf_hub_download

path = hf_hub_download(
    repo_id="LiteFold/InterPro",
    repo_type="dataset",
    filename="metadata/database_info.parquet",
)
database_info = pd.read_parquet(path)
print(database_info)

Columns

Column Description
interpro_id InterPro accession, such as IPR000001.
interpro_numeric_id Numeric portion of interpro_id.
name Full InterPro entry name.
short_name Short InterPro entry name from the XML attribute.
entry_type Entry class, such as Family, Domain, or Homologous_superfamily.
protein_count Number of proteins matched by the entry in the release XML.
is_llm Whether the entry is marked as LLM-generated in the source XML.
is_llm_reviewed Whether the LLM marker is reviewed in the source XML.
abstract Normalized text from the entry abstract.
go_ids GO identifiers mapped to the InterPro entry.
go_terms GO term names corresponding to go_ids.
go_categories GO namespaces corresponding to go_ids.
go_count Number of mapped GO terms.
member_databases Member databases contributing signatures.
member_accessions Signature accessions from member databases.
member_names Signature names from member databases.
member_protein_counts Protein counts for member signatures.
member_count Number of member signatures.
external_databases External resource database names.
external_accessions External resource accessions.
external_xrefs Combined external cross-references as DB:ACCESSION.
external_xref_count Number of external cross-references.
pdb_ids PDB structure identifiers.
structure_count Number of PDB structure links.
publication_ids InterPro publication identifiers.
pubmed_ids PubMed identifiers, when available.
publication_titles Publication titles.
publication_years Publication years, with 0 used when missing.
publication_count Number of publications attached to the entry.
parent_ids Parent InterPro entries from the XML hierarchy.
child_ids Child InterPro entries from the XML hierarchy.
parent_count Number of parents.
child_count Number of children.
tree_depth Minimum hierarchy depth from ParentChildTreeFile.txt, when present.
taxonomy_names Taxa listed in the taxonomy distribution.
taxonomy_protein_counts Protein counts for taxonomy_names.
taxonomy_count Number of taxonomy distribution rows.
key_species_names Key species names listed for the entry.
key_species_protein_counts Protein counts for key_species_names.
key_species_count Number of key species rows.
in_entry_list Whether the entry appears in entry.list.
entry_list_type Entry type from entry.list.
entry_list_name Entry name from entry.list.
names_dat_name Entry name from names.dat.
short_names_dat_name Short name from short_names.dat.
split_bucket Deterministic split bucket from sha256(interpro_id) % 10.

Preparation

The normalization script used to create the Parquet files is included at scripts/prepare_interpro_dataset.py.

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