interpro_id
string
interpro_numeric_id
int64
name
string
short_name
string
entry_type
string
protein_count
int64
is_llm
bool
is_llm_reviewed
bool
abstract
string
go_ids
list
go_terms
list
go_categories
list
go_count
int64
member_databases
list
member_accessions
list
member_names
list
member_protein_counts
list
member_count
int64
external_databases
list
external_accessions
list
external_xrefs
list
external_xref_count
int64
pdb_ids
list
structure_count
int64
publication_ids
list
pubmed_ids
list
publication_titles
list
publication_years
list
publication_count
int64
parent_ids
list
child_ids
list
parent_count
int64
child_count
int64
tree_depth
float64
taxonomy_names
list
taxonomy_protein_counts
list
taxonomy_count
int64
key_species_names
list
key_species_protein_counts
list
key_species_count
int64
in_entry_list
bool
entry_list_type
string
entry_list_name
string
names_dat_name
string
short_names_dat_name
string
split_bucket
int64
IPR001068
1,068
Adenosine A1 receptor
Adeno_A1_rcpt
Family
1,169
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" ]
[ "PR00552" ]
[ "ADENOSINEA1R" ]
[ 1169 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "18", "R-BTA-417973", "R-BTA-418594", "R-CFA-417973", "R-CFA-418594", "R-GGA-417973", "R-GGA-418594", "R-HSA-417973", "R-HSA-418594", "R-MMU-417973", "R-MMU-418594", "R-RNO-417973", "R-RNO-418594" ]
[ "IUPHAR:18", "REACTOME:R-BTA-417973", "REACTOME:R-BTA-418594", "REACTOME:R-CFA-417973", "REACTOME:R-CFA-418594", "REACTOME:R-GGA-417973", "REACTOME:R-GGA-418594", "REACTOME:R-HSA-417973", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-417973", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-417973", "REA...
13
[ "5n2s", "5uen", "6d9h", "7ld3", "7ld4" ]
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
[ "IPR001634" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 1169 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 4, 8, 3 ]
4
true
Family
Adenosine A1 receptor
Adenosine A1 receptor
Adeno_A1_rcpt
8
IPR001069
1,069
5-Hydroxytryptamine 7 receptor
5HT_7_rcpt
Family
1,680
false
false
5-hydroxytryptamine (5-HT) or serotonin, is a neurotransmitter that it is primarily found in the gastrointestinal (GI) tract, platelets, and in the central nervous system (CNS). It is implicated in a vast array of physiological and pathophysiological pathways. Receptors for 5-HT mediate both excitatory and inhibitory n...
[ "GO:0004993", "GO:0006939", "GO:0007186", "GO:0007268", "GO:0007623", "GO:0042310", "GO:0016020" ]
[ "G protein-coupled serotonin receptor activity", "smooth muscle contraction", "G protein-coupled receptor signaling pathway", "chemical synaptic transmission", "circadian rhythm", "vasoconstriction", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
7
[ "PRINTS" ]
[ "PR00652" ]
[ "5HT7RECEPTR" ]
[ 1680 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "12", "R-HSA-390666", "R-HSA-418555", "R-HSA-9706019", "R-MMU-390666", "R-MMU-418555", "R-MMU-9706019", "R-RNO-390666", "R-RNO-9706019" ]
[ "IUPHAR:12", "REACTOME:R-HSA-390666", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-9706019", "REACTOME:R-MMU-390666", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-9706019", "REACTOME:R-RNO-390666", "REACTOME:R-RNO-9706019" ]
9
[ "7xtc" ]
1
[ "PUB00064376", "PUB00064433", "PUB00064520", "PUB00064525", "PUB00064526", "PUB00064527", "PUB00064528", "PUB00064529", "PUB00064533", "PUB00064534", "PUB00064535", "PUB00064536", "PUB00064537", "PUB00064538", "PUB00066704" ]
[ "18476671", "10374714", "7908055", "8226867", "8398139", "9808674", "1166122", "7984266", "12763096", "15033384", "14654097", "12812993", "18301795", "15559250", "11989819" ]
[ "Serotonin receptors.", "Characterisation of 5-HT receptors in human coronary arteries by molecular and pharmacological techniques.", "Binding of typical and atypical antipsychotic agents to 5-hydroxytryptamine-6 and 5-hydroxytryptamine-7 receptors.", "Cloning of a novel human serotonin receptor (5-HT7) posit...
[ 2008, 1999, 1994, 1993, 1993, 1998, 1975, 1994, 2003, 2004, 2004, 2003, 2007, 2004, 2002 ]
15
[ "IPR000276" ]
[]
1
0
1
[ "Vertebrata" ]
[ 1680 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 2, 8, 4 ]
4
true
Family
5-Hydroxytryptamine 7 receptor
5-Hydroxytryptamine 7 receptor
5HT_7_rcpt
3
IPR001070
1,070
Polyomavirus coat protein VP2
Polyoma_coat_VP2
Family
636
false
false
This family includes the VP2 and VP3 internal coat proteins from Polyomaviruses, which are small dsDNA tumour viruses. Their capsids contain 360 copies of the VP1 proteins arranged in 72 pentamers. This capsid encloses the internal proteins VP2 and VP3, as well as the viral DNA. A single copy of VP2 or VP3 associates w...
[ "GO:0005198", "GO:0019028" ]
[ "structural molecule activity", "viral capsid" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PIRSF" ]
[ "PF00761", "PIRSF003377" ]
[ "Polyoma_coat2", "Polyoma_coat2" ]
[ 636, 454 ]
2
[]
[]
[]
0
[ "1cn3", "6esb" ]
2
[ "PUB00006154" ]
[ "9628860" ]
[ "Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Polyomaviridae", "bird metagenome" ]
[ 635, 1 ]
2
[]
[]
0
true
Family
Polyomavirus coat protein VP2
Polyomavirus coat protein VP2
Polyoma_coat_VP2
6
IPR001072
1,072
RNA ligase, Pab1020 family
RNA_ligase_Pab1020
Family
411
false
false
Members of this family are found, so far, in a single copy per genome and largely in thermophiles, of which only Aquifex aeolicus is bacterial rather than archaeal. PSI-BLAST converges after a single iteration to the whole of this family and reveals no convincing similarity to any other protein. The member protein Pab1...
[]
[]
[]
0
[ "PRINTS", "NCBIFAM", "CDD" ]
[ "PR01048", "TIGR01209", "cd07894" ]
[ "Y414FAMILY", "", "Adenylation_RNA_ligase" ]
[ 411, 411, 323 ]
3
[ "GP" ]
[ "GenProp0898" ]
[ "GP:GenProp0898" ]
1
[ "2vug", "3qwu", "5d1o", "5d1p", "8uce", "8ucf", "8ucg", "8uch", "8uci" ]
9
[ "PUB00049905", "PUB00086929" ]
[ "18511537", "28912583" ]
[ "The structure of an archaeal homodimeric ligase which has RNA circularization activity.", "Cleavage of 3'-terminal adenosine by archaeal ATP-dependent RNA ligase." ]
[ 2008, 2017 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "unclassified sequences" ]
[ 323, 80, 8 ]
3
[]
[]
0
true
Family
RNA ligase, Pab1020 family
RNA ligase, Pab1020 family
RNA_ligase_Pab1020
3
IPR001073
1,073
C1q domain
C1q_dom
Domain
41,268
false
false
This entry represents the C-terminal domain of C1q. C1q is a subunit of the C1 enzyme complex that activates the serum complement system. C1q comprises 6 A, 6 B and 6 C chains. These share the same topology, each possessing a small, globular N-terminal domain, a collagen-like Gly/Pro-rich central region, and a conserve...
[]
[]
[]
0
[ "PFAM", "PRINTS", "PROFILE", "SMART" ]
[ "PF00386", "PR00007", "PS50871", "SM00110" ]
[ "C1q", "COMPLEMNTC1Q", "C1Q", "C1Q" ]
[ 39751, 33154, 40016, 37173 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00857", "R-BTA-166663", "R-BTA-173623", "R-BTA-977606", "R-HSA-114608", "R-HSA-1442490", "R-HSA-163680", "R-HSA-1650814", "R-HSA-166663", "R-HSA-173623", "R-HSA-2022090", "R-HSA-2129379", "R-HSA-216083", "R-HSA-3000171", "R-HSA-381340", "R-HSA-5173105", "R-HSA-8948216", "R-HSA...
[ "PROSITEDOC:PDOC00857", "REACTOME:R-BTA-166663", "REACTOME:R-BTA-173623", "REACTOME:R-BTA-977606", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-1442490", "REACTOME:R-HSA-163680", "REACTOME:R-HSA-1650814", "REACTOME:R-HSA-166663", "REACTOME:R-HSA-173623", "REACTOME:R-HSA-2022090", "REACTOME:R-HSA-2...
35
[ "1c28", "1c3h", "1gr3", "1o91", "1pk6", "2jg8", "2jg9", "2ka3", "2oii", "2wnu", "2wnv", "4d7y", "4dou", "4f3j", "4nn0", "4oul", "4oum", "4ous", "4qpy", "4qq2", "4qqh", "4qql", "4qqo", "4qqp", "5h48", "5h49", "5h4b", "5h4c", "5hba", "5hkj", "5hzf", "5kc5"...
42
[ "PUB00000094", "PUB00000491", "PUB00001582", "PUB00002690", "PUB00003070", "PUB00075555" ]
[ "1867713", "1706597", "2591537", "2019595", "1860888", "22892318" ]
[ "The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper.", "Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q.", "Molecular cloning and chara...
[ 1991, 1991, 1989, 1991, 1991, 2012 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 4, 562, 40617, 72, 13 ]
5
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 124, 104, 87, 102 ]
4
true
Domain
C1q domain
C1q domain
C1q_dom
3
IPR001075
1,075
NIF system FeS cluster assembly, NifU, C-terminal
NIF_FeS_clus_asmbl_NifU_C
Domain
26,334
false
false
This entry represents the C-terminal of NifU and homologous proteins. NifU contains two domains: an N-terminal ( ) and a C-terminal domain [ ]. These domains exist either together or on different polypeptides, both domains being found in organisms that do not fix nitrogen (e.g. yeast), so they have a broader significan...
[ "GO:0005506", "GO:0051536", "GO:0016226" ]
[ "iron ion binding", "iron-sulfur cluster binding", "iron-sulfur cluster assembly" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF01106" ]
[ "NifU" ]
[ 26334 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-9857492", "R-HSA-9857492", "R-MMU-9857492" ]
[ "REACTOME:R-DME-9857492", "REACTOME:R-HSA-9857492", "REACTOME:R-MMU-9857492" ]
3
[ "1th5", "1veh", "1xhj", "2jnv", "2m5o", "2z51" ]
6
[ "PUB00003442", "PUB00005420", "PUB00028014", "PUB00035635", "PUB00035636", "PUB00035637", "PUB00035638", "PUB00035639", "PUB00035640", "PUB00058194", "PUB00160405", "PUB00160406" ]
[ "8875867", "8048161", "11498000", "16221578", "16211402", "16843540", "15937904", "17350000", "15278785", "17698959", "32108236", "33007329" ]
[ "A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.", "The modular structure of NifU proteins.", "Incorporation of iron-sulphur clusters in membrane-bound proteins.", "How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins.", "Mechanisms of iron-s...
[ 1996, 1994, 2001, 2005, 2005, 2006, 2005, 2007, 2004, 2007, 2020, 2021 ]
12
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 812, 17747, 7306, 4, 465 ]
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",...
[ 21, 1, 5, 3, 1, 4, 2, 1, 12, 3, 1, 1, 18 ]
13
true
Domain
NIF system FeS cluster assembly, NifU, C-terminal
NIF system FeS cluster assembly, NifU, C-terminal
NIF_FeS_clus_asmbl_NifU_C
5
IPR001077
1,077
O-methyltransferase, C-terminal domain
COMT_C
Domain
49,683
false
false
This domain includes a range of O-methyltransferases (COMT) some of which utilise S-adenosyl methionine as substrate [ ]. In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. In eukaryotes, DNA methylation has been implicated in the control of several cell...
[ "GO:0008171" ]
[ "O-methyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00891" ]
[ "Methyltransf_2" ]
[ 49683 ]
1
[ "EC", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.1.1", "GenProp1331", "GenProp1388", "GenProp1695", "R-BTA-209931", "R-DDI-209931", "R-HSA-209931", "R-MMU-209931", "R-RNO-209931" ]
[ "EC:2.1.1", "GP:GenProp1331", "GP:GenProp1388", "GP:GenProp1695", "REACTOME:R-BTA-209931", "REACTOME:R-DDI-209931", "REACTOME:R-HSA-209931", "REACTOME:R-MMU-209931", "REACTOME:R-RNO-209931" ]
9
[ "1fp1", "1fp2", "1fpq", "1kyw", "1kyz", "1qzz", "1r00", "1tw2", "1tw3", "1x19", "1x1a", "1x1b", "1x1c", "1x1d", "1xds", "1xdu", "1zg3", "1zga", "1zgj", "1zhf", "2ip2", "2qyo", "2r3s", "3dp7", "3gwz", "3gxo", "3i53", "3i58", "3i5u", "3i64", "3lst", "3mcz"...
162
[ "PUB00000141", "PUB00001090", "PUB00006319", "PUB00006400", "PUB00054125", "PUB00057957", "PUB00057958" ]
[ "8434913", "7773746", "7897657", "9484457", "12826405", "16225687", "21858014" ]
[ "Purification of a 40-kilodalton methyltransferase active in the aflatoxin biosynthetic pathway.", "DNA modification by methyltransferases.", "Universal catalytic domain structure of AdoMet-dependent methyltransferases.", "Plant O-methyltransferases: molecular analysis, common signature and classification.", ...
[ 1993, 1995, 1995, 1998, 2003, 2005, 2011 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 224, 12533, 36819, 107 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "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" ]
[ 83, 6, 9, 2, 7, 110, 3, 124 ]
8
true
Domain
O-methyltransferase, C-terminal domain
O-methyltransferase, C-terminal domain
COMT_C
5
IPR001078
1,078
2-oxoacid dehydrogenase acyltransferase, catalytic domain
2-oxoacid_DH_actylTfrase
Domain
85,524
false
false
This domain is found in the lipoamide acyltransferase component of the branched-chain alpha-keto acid dehydrogenase complex , which catalyses the overall conversion of alpha-keto acids to acyl-CoA and carbon dioxide [ ]. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxy...
[ "GO:0016746" ]
[ "acyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00198" ]
[ "2-oxoacid_dh" ]
[ 85524 ]
1
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "2.3.1", "GenProp1408", "R-BTA-204174", "R-BTA-5362517", "R-BTA-70895", "R-BTA-9013407", "R-BTA-9837999", "R-BTA-9857492", "R-BTA-9859138", "R-BTA-9861559", "R-CEL-204174", "R-CEL-5362517", "R-CEL-9013407", "R-CEL-9837999", "R-CEL-9857492", "R-CEL-9859138", "R-CEL-9861559", "R-DDI-...
[ "EC:2.3.1", "GP:GenProp1408", "REACTOME:R-BTA-204174", "REACTOME:R-BTA-5362517", "REACTOME:R-BTA-70895", "REACTOME:R-BTA-9013407", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9857492", "REACTOME:R-BTA-9859138", "REACTOME:R-BTA-9861559", "REACTOME:R-CEL-204174", "REACTOME:R-CEL-5362517", "REACT...
67
[ "1b5s", "1c4t", "1dpb", "1dpc", "1dpd", "1e2o", "1eaa", "1eab", "1eac", "1ead", "1eae", "1eaf", "1scz", "2ihw", "2ii3", "2ii4", "2ii5", "2xt6", "3b8k", "3duf", "3dv0", "3dva", "3l60", "3mae", "3rqc", "4n72", "4ofs", "6ct0", "6h05", "6h55", "6h60", "6pbr"...
68
[ "PUB00003302" ]
[ "8487300" ]
[ "Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 A resolution." ]
[ 1993 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 716, 62739, 20862, 1207 ]
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",...
[ 37, 4, 8, 18, 2, 31, 6, 3, 31, 21, 2, 2, 68 ]
13
true
Domain
2-oxoacid dehydrogenase acyltransferase, catalytic domain
2-oxoacid dehydrogenase acyltransferase, catalytic domain
2-oxoacid_DH_actylTfrase
5
IPR001079
1,079
Galectin, carbohydrate recognition domain
Galectin_CRD
Domain
22,779
false
false
Galectins (also known as galaptins or S-lectin) are a family of proteins defined by having at least one characteristic carbohydrate recognition domain (CRD) with an affinity for beta-galactosides and sharing certain sequence elements. Members of the galectins family are found in mammals, birds, amphibians, fish, nemato...
[ "GO:0030246" ]
[ "carbohydrate binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART", "SMART", "CDD" ]
[ "PF00337", "PS51304", "SM00276", "SM00908", "cd00070" ]
[ "Gal-bind_lectin", "GALECTIN", "GLECT", "Gal-bind_lectin", "GLECT" ]
[ 22260, 22619, 17348, 20944, 19521 ]
5
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-381426", "R-BTA-8957275", "R-CEL-6798695", "R-CFA-6798695", "R-GGA-381426", "R-GGA-8957275", "R-HSA-381426", "R-HSA-451927", "R-HSA-6798695", "R-HSA-879415", "R-HSA-8939246", "R-HSA-8941333", "R-HSA-8957275", "R-HSA-9725554", "R-MMU-381426", "R-MMU-6798695", "R-MMU-8957275", ...
[ "REACTOME:R-BTA-381426", "REACTOME:R-BTA-8957275", "REACTOME:R-CEL-6798695", "REACTOME:R-CFA-6798695", "REACTOME:R-GGA-381426", "REACTOME:R-GGA-8957275", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-451927", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-879415", "REACTOME:R-HSA-8939246", "REACTOME:R-H...
20
[ "1a3k", "1a78", "1bkz", "1c1f", "1c1l", "1g86", "1gan", "1gzw", "1hdk", "1hlc", "1is3", "1is4", "1is5", "1is6", "1kjl", "1kjr", "1lcl", "1qkq", "1qmj", "1sla", "1slb", "1slc", "1slt", "1ul9", "1ulc", "1uld", "1ule", "1ulf", "1ulg", "1w6m", "1w6n", "1w6o"...
459
[ "PUB00021763", "PUB00026983", "PUB00038165", "PUB00043740" ]
[ "8262940", "8747464", "16051274", "14758066" ]
[ "X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.", "Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins.", "Structural basis of a...
[ 1993, 1995, 2005, 2004 ]
4
[]
[]
0
0
null
[ "Bacteria", "Bamfordvirae", "Eukaryota", "Methanobrevibacter arboriphilus JCM 13429 = DSM 1125", "metagenomes" ]
[ 145, 5, 22623, 1, 5 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 34, 44, 55, 15, 66, 35, 34, 65, 69 ]
9
true
Domain
Galectin, carbohydrate recognition domain
Galectin, carbohydrate recognition domain
Galectin_CRD
5
IPR001082
1,082
Fimbrial protein pilin
Pilin
Family
7,569
false
false
Pilin is a component of type IV pilus (T4P), a polar flexible filament, which consists of a single polypeptide chain arranged in a helical configuration of five subunits per turn, which is involved cell adhesion, microcolony formation, twitching motility and transformation [ , ]. Gram-negative bacteria produce pilin wh...
[ "GO:0007155", "GO:0009289" ]
[ "cell adhesion", "pilus" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF00114" ]
[ "Pilin" ]
[ 7569 ]
1
[]
[]
[]
0
[ "1ay2", "1dzo", "1hpw", "1oqw", "1qve", "1rg0", "1x6p", "1x6q", "1x6r", "1x6x", "1x6y", "1x6z", "2hi2", "2hil", "2pil", "2py0", "3jc8", "3jc9", "3jyz", "3jzz", "3sok", "4v1j", "4xa2", "5cfv", "5ihj", "5jw8", "5kua", "5vaw", "5vxx", "5vxy", "6bbk", "8p2v"...
50
[ "PUB00000011", "PUB00003398", "PUB00095077", "PUB00095078" ]
[ "2898203", "3118043", "31431558", "10850981" ]
[ "The physiology and biochemistry of pili.", "An analysis of the organization and evolution of type 4 fimbrial (MePhe) subunit proteins.", "Type IV Pili Can Mediate Bacterial Motility within Epithelial Cells.", "ComP, a pilin-like protein essential for natural competence in Acinetobacter sp. Strain BD413: regu...
[ 1988, 1987, 2019, 2000 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 7459, 13, 97 ]
3
[]
[]
0
true
Family
Fimbrial protein pilin
Fimbrial protein pilin
Pilin
2
IPR001083
1,083
Copper fist DNA-binding domain
Cu_fist_DNA-bd_dom
Domain
3,411
false
false
Some fungal transcription factors contain an N-terminal domain, the copper fist, which seems to be involved in copper-dependent DNA-binding [ , ]. These proteins activate the transcription of the metallothionein gene in response to copper. Metallothionein maintains copper levels in yeast [ , ]. The copper fist domain, ...
[ "GO:0003677", "GO:0003700", "GO:0005507", "GO:0006355" ]
[ "DNA binding", "DNA-binding transcription factor activity", "copper ion binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PFAM", "PRINTS", "PROSITE", "PROFILE", "SMART", "SMART" ]
[ "PF00649", "PR00617", "PS01119", "PS50073", "SM00412", "SM01090" ]
[ "Copper-fist", "COPPERFIST", "COPPER_FIST_1", "COPPER_FIST_2", "Cu_FIST", "Copper-fist" ]
[ 3076, 2550, 728, 3397, 2979, 3087 ]
6
[ "PROSITEDOC" ]
[ "PDOC00863" ]
[ "PROSITEDOC:PDOC00863" ]
1
[ "1co4" ]
1
[ "PUB00001242", "PUB00002782", "PUB00006077", "PUB00016288" ]
[ "8262047", "8509391", "3052856", "9665167" ]
[ "MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast.", "Regulation of metallothionein genes by the ACE1 and AMT1 transcription factors.", "Copper activates metallothionein gene transcription by altering the conformatio...
[ 1993, 1993, 1988, 1998 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Hepacivirus hominis" ]
[ 14, 3394, 3 ]
3
[ "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)" ]
[ 2, 3, 2 ]
3
true
Domain
Copper fist DNA-binding domain
Copper fist DNA-binding domain
Cu_fist_DNA-bd_dom
9
IPR001084
1,084
Microtubule associated protein, tubulin-binding repeat
MAP_tubulin-bd_rpt
Repeat
9,975
false
false
Microtubules consist of tubulins as well as a group of additional proteins collectively known as the Microtubule Associated Proteins (MAP). MAP's have been classified into two classes: high molecular weight MAP's and Tau protein. The Tau proteins promote microtubule assembly and stabilise microtubules. The C-terminal r...
[ "GO:0015631" ]
[ "tubulin binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROSITE", "PROFILE" ]
[ "PF00418", "PS00229", "PS51491" ]
[ "Tubulin-binding", "TAU_MAP_1", "TAU_MAP_2" ]
[ 9967, 9410, 9879 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00201", "R-HSA-264870", "R-HSA-9619483", "R-HSA-9833482", "R-MMU-264870", "R-MMU-9833482", "R-RNO-264870", "R-RNO-9833482" ]
[ "PROSITEDOC:PDOC00201", "REACTOME:R-HSA-264870", "REACTOME:R-HSA-9619483", "REACTOME:R-HSA-9833482", "REACTOME:R-MMU-264870", "REACTOME:R-MMU-9833482", "REACTOME:R-RNO-264870", "REACTOME:R-RNO-9833482" ]
8
[ "2mz7", "5mp3", "5n5a", "5n5b", "5nvb", "5o3l", "5o3o", "5o3t", "6cvj", "6cvn", "6gx5", "6hre", "6hrf", "6nwp", "6nwq", "6qjh", "6qjm", "6qjp", "6qjq", "6tjo", "6tjx", "6vh7", "6vha", "6vhl", "6vi3", "7mkf", "7mkg", "7mkh", "7nrq", "7nrs", "7nrt", "7nrv"...
203
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Eukaryota", "Mycobacterium attenuatum" ]
[ 9974, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 154, 11, 27, 29, 47 ]
6
true
Repeat
Microtubule associated protein, tubulin-binding repeat
Microtubule associated protein, tubulin-binding repeat
MAP_tubulin-bd_rpt
4
IPR001085
1,085
Serine hydroxymethyltransferase
Ser_HO-MeTrfase
Family
44,709
false
false
This entry includes serine hydroxymethyltransferases and related uncharacterised proteins. Serine hydroxymethyltransferase catalyses the reversible interconversion of serine and glycine with tetrahydrofolate serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for th...
[ "GO:0004372", "GO:0030170", "GO:0019264", "GO:0035999" ]
[ "glycine hydroxymethyltransferase activity", "pyridoxal phosphate binding", "glycine biosynthetic process from L-serine", "tetrahydrofolate interconversion" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]
4
[ "HAMAP", "PIRSF", "CDD" ]
[ "MF_00051", "PIRSF000412", "cd00378" ]
[ "SHMT", "SHMT", "SHMT" ]
[ 42445, 42460, 44053 ]
3
[ "EC", "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "2.1.2", "2.1.2.1", "GenProp1356", "GenProp1386", "GenProp1414", "GenProp1747", "PWY-1622", "PWY-181", "PWY-2161", "PWY-2201", "PWY-3661", "PWY-3841", "PWY-5497", "PWY-8325", "PWY-8362", "PWY-8363", "PDOC00090", "R-BTA-196757", "R-BTA-9013408", "R-BTA-9837999", "R-CEL-196757"...
[ "EC:2.1.2", "EC:2.1.2.1", "GP:GenProp1356", "GP:GenProp1386", "GP:GenProp1414", "GP:GenProp1747", "METACYC:PWY-1622", "METACYC:PWY-181", "METACYC:PWY-2161", "METACYC:PWY-2201", "METACYC:PWY-3661", "METACYC:PWY-3841", "METACYC:PWY-5497", "METACYC:PWY-8325", "METACYC:PWY-8362", "METACYC:...
36
[ "1bj4", "1cj0", "1dfo", "1eji", "1eqb", "1kkj", "1kkp", "1kl1", "1kl2", "1ls3", "1rv3", "1rv4", "1rvu", "1rvy", "1yjs", "1yjy", "1yjz", "2dkj", "2vgs", "2vgt", "2vgu", "2vgv", "2vgw", "2vi8", "2vi9", "2via", "2vib", "2vmn", "2vmo", "2vmp", "2vmq", "2vmr"...
176
[ "PUB00000663", "PUB00014432", "PUB00014439", "PUB00024584" ]
[ "8305478", "10828359", "11877399", "11063567" ]
[ "The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases.", "The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase.", "Crystal structure of binary an...
[ 1994, 2000, 2002, 2000 ]
4
[ "IPR049943" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 965, 31814, 11417, 11, 502 ]
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",...
[ 29, 1, 2, 2, 1, 14, 5, 2, 19, 8, 2, 2, 22 ]
13
true
Family
Serine hydroxymethyltransferase
Serine hydroxymethyltransferase
Ser_HO-MeTrfase
1
IPR001086
1,086
Prephenate dehydratase
Preph_deHydtase
Domain
30,285
false
false
Prephenate dehydratase ( , PDT) catalyses the decarboxylation of prephenate to phenylpyruvate. In microorganisms it is part of the terminal pathway of phenylalanine biosynthesis. In some bacteria such as Escherichia coli PDT is part of a bifunctional enzyme (P-protein) that also catalyses the transformation of chorisma...
[ "GO:0004664", "GO:0009094" ]
[ "prephenate dehydratase activity", "L-phenylalanine biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE" ]
[ "PF00800", "PS51171" ]
[ "PDT", "PREPHENATE_DEHYDR_3" ]
[ 30149, 30059 ]
2
[ "EC", "GP", "GP", "GP", "GP", "GP", "METACYC", "PROSITEDOC" ]
[ "4.2.1.51", "GenProp1234", "GenProp1251", "GenProp1309", "GenProp1538", "GenProp1708", "PWY-7432", "PDOC00671" ]
[ "EC:4.2.1.51", "GP:GenProp1234", "GP:GenProp1251", "GP:GenProp1309", "GP:GenProp1538", "GP:GenProp1708", "METACYC:PWY-7432", "PROSITEDOC:PDOC00671" ]
8
[ "2qmw", "2qmx", "3luy", "3mwb", "4lub", "6vh5", "7alz", "7am0" ]
8
[ "PUB00003018", "PUB00070219", "PUB00075398", "PUB00155064" ]
[ "9642265", "19082689", "17726025", "34112823" ]
[ "Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase.", "Characterization of a key trifunctional enzyme for aromatic amino acid biosynthesis in Archaeoglobus fulgidus.", "Phenylalanine biosynthesis in Arabidopsis thaliana. Identification and characterizati...
[ 1998, 2009, 2007, 2021 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 833, 23127, 5723, 602 ]
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" ]
[ 21, 1, 1, 36, 1, 2, 43 ]
7
true
Domain
Prephenate dehydratase
Prephenate dehydratase
Preph_deHydtase
3
IPR001087
1,087
GDSL lipase/esterase
GDSL
Family
78,421
false
false
GDSL esterases and lipases are hydrolytic enzymes with multifunctional properties [ ]. This new subclass of lipolytic enzymes possesses a distinct GDSL sequence motif different from the GxSxG motif found in many lipases [ ]. Members include; Aeromonas hydrophila lipase, Vibrio mimicus lecithinase, Vibrio parahaemolytic...
[ "GO:0016788" ]
[ "hydrolase activity, acting on ester bonds" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00657" ]
[ "Lipase_GDSL" ]
[ 78421 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "...
[ "3.1.1", "3.1.1.-", "PWY-1921", "PWY-5835", "PWY-6190", "PWY-6308", "PWY-6322", "PWY-6339", "PWY-6415", "PWY-6558", "PWY-6848", "PWY-7002", "PWY-7352", "PWY-7367", "PWY-7521", "PWY-7599", "PWY-7660", "PWY-7712", "PWY-7713", "PWY-7730", "PWY-7769", "PWY-7982", "PWY-8058", ...
[ "EC:3.1.1", "EC:3.1.1.-", "METACYC:PWY-1921", "METACYC:PWY-5835", "METACYC:PWY-6190", "METACYC:PWY-6308", "METACYC:PWY-6322", "METACYC:PWY-6339", "METACYC:PWY-6415", "METACYC:PWY-6558", "METACYC:PWY-6848", "METACYC:PWY-7002", "METACYC:PWY-7352", "METACYC:PWY-7367", "METACYC:PWY-7521", ...
35
[ "1deo", "1dex", "1k7c", "1pp4", "2wab", "2wao", "3c1u", "3kvn", "3mil", "3u37", "4dev", "5w78", "5w7a", "5w7b", "5w7c", "5w7d", "5w7e", "5w7f", "5xtu", "6jkz", "6jl0", "6jl1", "6jl2", "6uqv", "6uqw", "6uqx", "6uqy", "6uqz", "6ur0", "6ur1", "7ztn", "8a24"...
63
[ "PUB00005440", "PUB00033179", "PUB00095657" ]
[ "7610479", "15522763", "19555778" ]
[ "A new family of lipolytic enzymes?", "GDSL family of serine esterases/lipases.", "Identification and biochemical characterization of a GDSL-motif carboxylester hydrolase from Carica papaya latex." ]
[ 1995, 2004, 2009 ]
3
[]
[ "IPR035669" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 11, 11465, 66858, 15, 72 ]
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...
[ 500, 12, 9, 2, 14, 12, 2, 379, 10, 1, 1, 495 ]
12
true
Family
GDSL lipase/esterase
GDSL lipase/esterase
GDSL
3
IPR001088
1,088
Glycoside hydrolase, family 4
Glyco_hydro_4
Family
16,615
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF02056", "PR00732", "PTHR32092" ]
[ "Glyco_hydro_4", "GLHYDRLASE4", "" ]
[ 16110, 15892, 16557 ]
3
[ "CAZY", "EC", "GP", "PROSITEDOC" ]
[ "GH4", "3.2.1", "GenProp1293", "PDOC01027" ]
[ "CAZY:GH4", "EC:3.2.1", "GP:GenProp1293", "PROSITEDOC:PDOC01027" ]
4
[ "1obb", "1s6y", "1u8x", "1up4", "1up6", "1up7", "1vjt", "3fef", "3u95", "5c3m", "6dux", "6dvv", "6kcx", "6vc6", "6wbt", "7br4", "7brf", "7ctd", "7ctl", "7ctm" ]
20
[ "PUB00003025", "PUB00004870", "PUB00005266", "PUB00031705", "PUB00100086" ]
[ "9765262", "7624375", "8535779", "15341727", "31409483" ]
[ "The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-alpha-glucosidase. Assignment to family 4 of the glycosylhydrolase superfamily.", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechan...
[ 1998, 1995, 1995, 2004, 2019 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 196, 16133, 39, 247 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 1, 3 ]
2
true
Family
Glycoside hydrolase, family 4
Glycoside hydrolase, family 4
Glyco_hydro_4
3
IPR001089
1,089
CXC chemokine
Chemokine_CXC
Family
6,302
false
false
Most members of this family of low-molecular weight proteins seem to have mitogenic, chemotactic or inflammatory activities. They are released by phagocytes, mesenchymal cells and a wide variety of tissue cells, upon exposure to inflammation [ ]. These small cytokines are also called intercrines or chemokines. They are...
[ "GO:0008009", "GO:0006955", "GO:0005576" ]
[ "chemokine activity", "immune response", "extracellular region" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00437" ]
[ "SMALLCYTKCXC" ]
[ 6302 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00434", "R-BTA-375276", "R-BTA-380108", "R-BTA-418594", "R-BTA-6798695", "R-CFA-375276", "R-CFA-380108", "R-CFA-418594", "R-DRE-380108", "R-DRE-418594", "R-GGA-380108", "R-GGA-418594", "R-GGA-6798695", "R-HSA-114608", "R-HSA-140875", "R-HSA-202733", "R-HSA-2559582", "R-HSA-375...
[ "PROSITEDOC:PDOC00434", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-380108", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-6798695", "REACTOME:R-CFA-375276", "REACTOME:R-CFA-380108", "REACTOME:R-CFA-418594", "REACTOME:R-DRE-380108", "REACTOME:R-DRE-418594", "REACTOME:R-GGA-380108", "REACTOME:R-GGA-418...
42
[ "1f9p", "1f9q", "1f9r", "1f9s", "1icw", "1ikl", "1ikm", "1il8", "1ilp", "1ilq", "1lv9", "1mgs", "1mi2", "1msg", "1msh", "1nap", "1o7y", "1o7z", "1o80", "1pfm", "1pfn", "1plf", "1qe6", "1qnk", "1rhp", "1rjt", "1rod", "1tvx", "2il8", "2mgs", "2r3z", "3il8"...
75
[ "PUB00001373", "PUB00001646" ]
[ "2523801", "1639201" ]
[ "Purification of granulocyte chemotactic peptide/interleukin-8 reveals N-terminal sequence heterogeneity similar to that of beta-thromboglobulin.", "Interleukin-8, a chemotactic and inflammatory cytokine." ]
[ 1989, 1992 ]
2
[]
[]
0
0
null
[ "Bilateria", "Viruses" ]
[ 6247, 55 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 14, 23, 31, 27 ]
4
true
Family
CXC chemokine
CXC chemokine
Chemokine_CXC
1
IPR001090
1,090
Ephrin, ligand binding domain
EPH_LBD
Domain
21,481
false
false
The Eph LBD domain forms a compact globular structure which folds into a jellyroll β-sandwich composed of 11 antiparallel β-strands. It has two antiparallel β-sheets, with the usual left-handed twist, packed against each other to form a compact β-sandwich, and a short 3(10) helix [ , , ]. The Eph receptors, which bind ...
[ "GO:0005515" ]
[ "protein binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF01404", "PS51550", "SM00615" ]
[ "Ephrin_lbd", "EPH_LBD", "EPH_lbd" ]
[ 21373, 21427, 21196 ]
3
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.10.1", "R-CEL-2682334", "R-CEL-3928662", "R-CEL-3928663", "R-CEL-3928664", "R-CEL-3928665", "R-CEL-9013149", "R-CEL-9013404", "R-CEL-9013408", "R-CEL-9013420", "R-CEL-9013423", "R-CEL-9013424", "R-DRE-2682334", "R-DRE-3928662", "R-DRE-3928663", "R-DRE-3928664", "R-DRE-3928665", ...
[ "EC:2.7.10.1", "REACTOME:R-CEL-2682334", "REACTOME:R-CEL-3928662", "REACTOME:R-CEL-3928663", "REACTOME:R-CEL-3928664", "REACTOME:R-CEL-3928665", "REACTOME:R-CEL-9013149", "REACTOME:R-CEL-9013404", "REACTOME:R-CEL-9013408", "REACTOME:R-CEL-9013420", "REACTOME:R-CEL-9013423", "REACTOME:R-CEL-901...
56
[ "1kgy", "1nuk", "1shw", "2bba", "2hle", "2lw8", "2qbx", "2wo1", "2wo2", "2wo3", "2x10", "2x11", "3c8x", "3ckh", "3czu", "3etp", "3fl7", "3gxu", "3hei", "3hpn", "3mbw", "3mx0", "3nru", "3p1i", "3skj", "4bk4", "4bk5", "4bka", "4bkf", "4et7", "4l0p", "4m4p"...
53
[ "PUB00004289", "PUB00010665", "PUB00052266" ]
[ "9853759", "11780069", "19525919" ]
[ "Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2.", "Crystal structure of an Eph receptor-ephrin complex.", "Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex." ]
[ 1998, 2001, 2009 ]
3
[]
[ "IPR034231", "IPR034238", "IPR034245", "IPR034251", "IPR034263", "IPR034266", "IPR034270", "IPR034277", "IPR034280", "IPR034283", "IPR034287", "IPR034290" ]
0
12
0
[ "Metazoa" ]
[ 21481 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 91, 11, 60, 50, 57 ]
6
true
Domain
Ephrin, ligand binding domain
Ephrin, ligand binding domain
EPH_LBD
6
IPR001091
1,091
Restriction/modification DNA-methyltransferase
RM_Methyltransferase
Family
30,105
false
false
Site-specific DNA-methyltransferase, N-6 adenine-specific DNA methylase ( ) and cytosine-N4-specific ( ) are enzymes that specifically methylate the amino group at the C-4 position of cytosines and the N-6 position of adenine in DNA. In prokaryotes, the major role of DNA methylation is to protect host DNA against degra...
[ "GO:0003677", "GO:0008170" ]
[ "DNA binding", "N-methyltransferase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS" ]
[ "PR00508" ]
[ "S21N4MTFRASE" ]
[ 30105 ]
1
[ "EC", "PROSITEDOC" ]
[ "2.1.1", "PDOC00088" ]
[ "EC:2.1.1", "PROSITEDOC:PDOC00088" ]
2
[ "1boo", "1g60", "2zie", "2zif", "2zig", "5hek", "5hfj", "6pbd", "8s9m", "8s9n", "8s9o", "8urk", "9c3s", "9c3t", "9c3u" ]
15
[ "PUB00000092", "PUB00100208" ]
[ "7663118", "33624263" ]
[ "Structure and function of DNA methyltransferases.", "Prokaryotic DNA methylation and its functional roles." ]
[ 1995, 2021 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1201, 25844, 199, 1194, 1667 ]
5
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Restriction/modification DNA-methyltransferase
Restriction/modification DNA-methyltransferase
RM_Methyltransferase
2
IPR001093
1,093
IMP dehydrogenase/GMP reductase
IMP_DH_GMPRt
Domain
51,582
false
false
null
[ "GO:0003824" ]
[ "catalytic activity" ]
[ "molecular_function" ]
1
[ "PFAM", "CDD" ]
[ "PF00478", "cd00381" ]
[ "IMPDH", "IMPDH" ]
[ 51582, 48186 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "1.7.1.7", "R-BTA-6798695", "R-BTA-73817", "R-BTA-9748787", "R-CEL-6798695", "R-CEL-73817", "R-CEL-74217", "R-CEL-9748787", "R-DDI-6798695", "R-DDI-73817", "R-DDI-9748787", "R-DME-6798695", "R-DME-73817", "R-DME-9748787", "R-DRE-6798695", "R-DRE-73817", "R-DRE-9748787", "R-HSA-6798...
[ "EC:1.7.1.7", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-73817", "REACTOME:R-BTA-9748787", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-73817", "REACTOME:R-CEL-74217", "REACTOME:R-CEL-9748787", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-73817", "REACTOME:R-DDI-9748787", "REACTOME:R-DME-6798695", ...
37
[ "1ak5", "1b3o", "1eep", "1jcn", "1jr1", "1lrt", "1me7", "1me8", "1me9", "1meh", "1mei", "1mew", "1nf7", "1nfb", "1pvn", "1vrd", "1ypf", "1zfj", "2a1y", "2a7r", "2ble", "2bwg", "2bzn", "2c6q", "2cu0", "2qr6", "3ffs", "3khj", "3r2g", "3tsb", "3tsd", "3usb"...
209
[ "PUB00000471", "PUB00002466", "PUB00002609" ]
[ "2904262", "2902093", "1969416" ]
[ "Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12.", "Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs.", "Two distinct cDNAs for human IMP dehydrogenase." ]
[ 1988, 1988, 1990 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 894, 38161, 11340, 27, 1160 ]
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",...
[ 9, 5, 17, 5, 2, 45, 18, 1, 6, 22, 5, 1, 13 ]
13
true
Domain
IMP dehydrogenase/GMP reductase
IMP dehydrogenase/GMP reductase
IMP_DH_GMPRt
6
IPR001094
1,094
Flavodoxin-like
Flavdoxin-like
Domain
41,065
false
false
This entry includes flavodoxins and flavodoxin-like proteins, such as NADPH-dependent diflavin oxidoreductase NDOR1 and nitric oxide synthases.
[ "GO:0010181" ]
[ "FMN binding" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR00369" ]
[ "FLAVODOXIN" ]
[ 41065 ]
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-156581", "R-CEL-1614635", "R-CEL-9759218", "R-DDI-1222556", "R-DDI-1474151", "R-DDI-203615", "R-DDI-203754", "R-DDI-392154", "R-DDI-5218920", "R-DDI-5578775", "R-DDI-9009391", "R-DDI-9033241", "R-DDI-9856530", "R-DME-1222556", "R-DME-1474151", "R-DME-203615", "R-DME-203754", ...
[ "REACTOME:R-CEL-156581", "REACTOME:R-CEL-1614635", "REACTOME:R-CEL-9759218", "REACTOME:R-DDI-1222556", "REACTOME:R-DDI-1474151", "REACTOME:R-DDI-203615", "REACTOME:R-DDI-203754", "REACTOME:R-DDI-392154", "REACTOME:R-DDI-5218920", "REACTOME:R-DDI-5578775", "REACTOME:R-DDI-9009391", "REACTOME:R-...
93
[ "1akq", "1aku", "1akv", "1amo", "1b1c", "1bu5", "1bvy", "1c7e", "1c7f", "1czh", "1czo", "1d03", "1f4p", "1fx1", "1i1o", "1j8q", "1j9e", "1j9g", "1j9z", "1ja0", "1ja1", "1tll", "1wsb", "1wsw", "1xt6", "1xyv", "1xyy", "1ykg", "1yob", "2bf4", "2bn4", "2bpo"...
93
[ "PUB00000282", "PUB00000480", "PUB00003573" ]
[ "3085707", "2597140", "7830610" ]
[ "NADPH-cytochrome P-450 oxidoreductase: flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins.", "The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus.", "Flavodoxins." ]
[ 1986, 1989, 1994 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 30, 17317, 23667, 51 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 19, 4, 34, 9, 2, 38, 21, 3, 11, 37, 3, 4, 32 ]
13
true
Domain
Flavodoxin-like
Flavodoxin-like
Flavdoxin-like
9
IPR001095
1,095
Acetyl-CoA carboxylase, alpha subunit
Acetyl_CoA_COase_a_su
Family
21,413
false
false
This entry contains the alpha subunit (Acetyl-coenzyme A carboxylase carboxyl transferase ACCA ) of the acetyl coenzyme A carboxylase complex ( ). ACCA catalyses the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA, the first step in the sy...
[ "GO:0003989", "GO:0016743", "GO:0006633", "GO:0009317" ]
[ "acetyl-CoA carboxylase activity", "carboxyl- or carbamoyltransferase activity", "fatty acid biosynthetic process", "acetyl-CoA carboxylase complex" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "HAMAP", "NCBIFAM", "PFAM", "PRINTS", "PANTHER", "NCBIFAM" ]
[ "MF_00823", "NF041504", "PF03255", "PR01069", "PTHR42853", "TIGR00513" ]
[ "AcetylCoA_CT_alpha", "AccA_sub", "ACCA", "ACCCTRFRASEA", "", "accA" ]
[ 18097, 18949, 21313, 19260, 20918, 18279 ]
6
[ "EC", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.1.3.15", "GenProp0214", "GenProp1111", "GenProp1512", "PWY-4381", "PWY-5743", "PWY-5744", "PWY-5789", "PWY-6722" ]
[ "EC:2.1.3.15", "GP:GenProp0214", "GP:GenProp1111", "GP:GenProp1512", "METACYC:PWY-4381", "METACYC:PWY-5743", "METACYC:PWY-5744", "METACYC:PWY-5789", "METACYC:PWY-6722" ]
9
[ "2f9i", "2f9y", "5kdr", "8uxz", "8uz2", "9e4n", "9e4o" ]
7
[ "PUB00002735" ]
[ "1355089" ]
[ "The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase." ]
[ 1992 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Marine Group I thaumarchaeote", "unclassified sequences" ]
[ 19546, 1511, 1, 355 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 6, 1 ]
2
true
Family
Acetyl-CoA carboxylase, alpha subunit
Acetyl-CoA carboxylase, alpha subunit
Acetyl_CoA_COase_a_su
6
IPR001096
1,096
Peptidase C13, legumain
Peptidase_C13
Family
14,148
false
false
Asparaginyl endopeptidase, also known as legumain, is a family of cysteine proteases found in many organisms. This group of cysteine peptidases belong to the MEROPS peptidase family C13 (legumain family, clan CD). A type example is legumain from Canavalia ensiformis (Jack bean, Horse bean) [ ]. Although legumains were ...
[ "GO:0008233", "GO:0006508" ]
[ "peptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "PRINTS", "PANTHER" ]
[ "PF01650", "PIRSF019663", "PR00776", "PTHR12000" ]
[ "Peptidase_C13", "Legumain", "HEMOGLOBNASE", "" ]
[ 13835, 8933, 10713, 6817 ]
4
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.22", "R-BTA-162791", "R-HSA-162791", "R-HSA-1679131", "R-HSA-196791", "R-HSA-2132295", "R-MMU-162791", "R-MMU-1679131", "R-MMU-2132295", "R-RNO-1679131", "R-RNO-196791", "R-RNO-2132295" ]
[ "EC:3.4.22", "REACTOME:R-BTA-162791", "REACTOME:R-HSA-162791", "REACTOME:R-HSA-1679131", "REACTOME:R-HSA-196791", "REACTOME:R-HSA-2132295", "REACTOME:R-MMU-162791", "REACTOME:R-MMU-1679131", "REACTOME:R-MMU-2132295", "REACTOME:R-RNO-1679131", "REACTOME:R-RNO-196791", "REACTOME:R-RNO-2132295" ]
12
[ "4aw9", "4awa", "4awb", "4d3x", "4d3y", "4d3z", "4fgu", "4n6n", "4n6o", "4noj", "4nok", "4nol", "4nom", "5h0i", "5lu8", "5lu9", "5lua", "5lub", "5nij", "5obt", "5zbi", "6azt", "6dhi", "6idv", "6l4v", "6l4w", "6l4x", "6l4y", "6lko", "6xt5", "6ysa", "7f5j"...
47
[ "PUB00000523", "PUB00003009", "PUB00003577", "PUB00011704", "PUB00020025", "PUB00030423", "PUB00068164", "PUB00070962", "PUB00070963", "PUB00070966", "PUB00070968", "PUB00070970", "PUB00076953" ]
[ "8457210", "9065484", "7845226", "11517925", "9891971", "14725770", "8978684", "24696276", "7852272", "17028179", "15275249", "10793132", "7044372" ]
[ "Expression and partial characterization of a cathepsin B-like enzyme (Sm31) and a proposed 'haemoglobinase' (Sm32) from Schistosoma mansoni.", "Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase.", "Families of cysteine peptidases.", "Evolutionary lines of cysteine p...
[ 1993, 1997, 1994, 2001, 1998, 2004, 1996, 2014, 1994, 2006, 1996, 2000, 1982 ]
13
[]
[ "IPR028361", "IPR043577" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 25, 2135, 11957, 31 ]
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...
[ 22, 3, 10, 1, 17, 10, 1, 15, 14, 1, 1, 39 ]
12
true
Family
Peptidase C13, legumain
Peptidase C13, legumain
Peptidase_C13
9
IPR001098
1,098
DNA-directed DNA polymerase, family A, palm domain
DNA-dir_DNA_pol_A_palm_dom
Domain
50,221
false
false
null
[ "GO:0003677", "GO:0003887", "GO:0006260" ]
[ "DNA binding", "DNA-directed DNA polymerase activity", "DNA replication" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "SMART" ]
[ "PF00476", "SM00482" ]
[ "DNA_pol_A", "POLAc" ]
[ 48502, 48544 ]
2
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.7.7", "PDOC00412", "R-DME-5685939", "R-DME-9913635", "R-HSA-5685939", "R-HSA-6783310", "R-HSA-9913635", "R-MMU-5685939", "R-MMU-6783310", "R-MMU-9913635", "R-RNO-9913635" ]
[ "EC:2.7.7.7", "PROSITEDOC:PDOC00412", "REACTOME:R-DME-5685939", "REACTOME:R-DME-9913635", "REACTOME:R-HSA-5685939", "REACTOME:R-HSA-6783310", "REACTOME:R-HSA-9913635", "REACTOME:R-MMU-5685939", "REACTOME:R-MMU-6783310", "REACTOME:R-MMU-9913635", "REACTOME:R-RNO-9913635" ]
11
[ "1bgx", "1d8y", "1d9d", "1d9f", "1dpi", "1jxe", "1kfd", "1kfs", "1kln", "1krp", "1ksp", "1ktq", "1l3s", "1l3t", "1l3u", "1l3v", "1l5u", "1lv5", "1njw", "1njx", "1njy", "1njz", "1nk0", "1nk4", "1nk5", "1nk6", "1nk7", "1nk8", "1nk9", "1nkb", "1nkc", "1nke"...
333
[ "PUB00004393", "PUB00004443", "PUB00004955", "PUB00092104" ]
[ "1870963", "8451181", "2196557", "10364165" ]
[ "Compilation and alignment of DNA polymerase sequences.", "Compilation, alignment, and phylogenetic relationships of DNA polymerases.", "An attempt to unify the structure of polymerases.", "DNA polymerases: structural diversity and common mechanisms." ]
[ 1991, 1993, 1990, 1999 ]
4
[]
[ "IPR047580" ]
0
1
0
[ "Bacteria", "Eukaryota", "Methanobacteriati", "Viruses", "unclassified sequences" ]
[ 32331, 9569, 18, 6793, 1510 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 17, 2, 9, 2, 1, 19, 15, 1, 12, 11, 1, 1, 36 ]
13
true
Domain
DNA-directed DNA polymerase, family A, palm domain
DNA-directed DNA polymerase, family A, palm domain
DNA-dir_DNA_pol_A_palm_dom
5
IPR001099
1,099
Chalcone/stilbene synthase, N-terminal
Chalcone/stilbene_synt_N
Domain
19,414
false
false
This entry represents the N-terminal domain of chalcone and stilbene synthases and related proteins. Chalcone synthases (CHS) ( ) and stilbene synthases (STS) (formerly known as resveratrol synthases) are related plant enzymes, members of the plant polyketide synthase superfamily. CHS is an important enzyme in flavonoi...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00195" ]
[ "Chal_sti_synt_N" ]
[ 19414 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME" ]
[ "2.3.1", "2.3.1.74", "PWY-5135", "PWY-6316", "PWY-6515", "PWY-6787", "PWY-7397", "PWY-7897", "PDOC00403", "R-DDI-199220", "R-DDI-75105" ]
[ "EC:2.3.1", "EC:2.3.1.74", "METACYC:PWY-5135", "METACYC:PWY-6316", "METACYC:PWY-6515", "METACYC:PWY-6787", "METACYC:PWY-7397", "METACYC:PWY-7897", "PROSITEDOC:PDOC00403", "REACTOME:R-DDI-199220", "REACTOME:R-DDI-75105" ]
11
[ "1bi5", "1bq6", "1cgk", "1cgz", "1chw", "1cml", "1d6f", "1d6h", "1d6i", "1ee0", "1i86", "1i88", "1i89", "1i8b", "1jwx", "1qlv", "1ted", "1tee", "1u0m", "1u0u", "1u0v", "1u0w", "1xes", "1xet", "1z1e", "1z1f", "2d3m", "2d51", "2d52", "2h84", "2p0u", "3a5q"...
128
[ "PUB00002705", "PUB00072442", "PUB00095149" ]
[ "2033084", "2184816", "21909286" ]
[ "The role of cysteines in polyketide synthases. Site-directed mutagenesis of resveratrol and chalcone synthases, two key enzymes in different plant-specific pathways.", "Stilbene and chalcone synthases: related enzymes with key functions in plant-specific pathways.", "Chalcone synthase and its functions in plan...
[ 1991, 1990, 2011 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Streptomyces phage ZL12", "unclassified sequences" ]
[ 7822, 11558, 1, 33 ]
4
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 56, 1, 87, 75 ]
4
true
Domain
Chalcone/stilbene synthase, N-terminal
Chalcone/stilbene synthase, N-terminal
Chalcone/stilbene_synt_N
5
IPR001100
1,100
Pyridine nucleotide-disulphide oxidoreductase, class I
Pyr_nuc-diS_OxRdtase
Family
94,776
false
false
The pyridine nucleotide-disulphide reductases (PNDR) use the isoalloxazine ring of FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate. On the basis of sequence and structural similar...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PIRSF" ]
[ "PIRSF000350" ]
[ "Mercury_reductase_MerA" ]
[ 94776 ]
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-204174", "R-BTA-3299685", "R-BTA-499943", "R-BTA-5263617", "R-BTA-5362517", "R-BTA-5628897", "R-BTA-6783984", "R-BTA-70895", "R-BTA-9837999", "R-BTA-9853506", "R-BTA-9858328", "R-BTA-9859138", "R-BTA-9861559", "R-CEL-204174", "R-CEL-3299685", "R-CEL-499943", "R-CEL-5362517", ...
[ "REACTOME:R-BTA-204174", "REACTOME:R-BTA-3299685", "REACTOME:R-BTA-499943", "REACTOME:R-BTA-5263617", "REACTOME:R-BTA-5362517", "REACTOME:R-BTA-5628897", "REACTOME:R-BTA-6783984", "REACTOME:R-BTA-70895", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9853506", "REACTOME:R-BTA-9858328", "REACTOME:R-...
96
[ "1aog", "1bhy", "1bwc", "1bzl", "1dnc", "1dxl", "1ebd", "1fea", "1feb", "1fec", "1ger", "1ges", "1get", "1geu", "1gra", "1grb", "1gre", "1grf", "1grg", "1grh", "1grt", "1gsn", "1gxf", "1h6v", "1jeh", "1k4q", "1lpf", "1lvl", "1nda", "1ojt", "1onf", "1typ"...
262
[ "PUB00000149", "PUB00000154", "PUB00000284", "PUB00004100", "PUB00004586" ]
[ "2643922", "2241146", "3718941", "2067578", "1311113" ]
[ "Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases.", "Variations in the activity of glutathione reductase and the cellular glutathione content in relation to sensitivity to methylviologen in Escherichia coli.", "Purification and...
[ 1989, 1990, 1986, 1991, 1992 ]
5
[]
[ "IPR006258", "IPR017817", "IPR021179", "IPR022962", "IPR046952" ]
0
5
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. cti6f5", "plasmids", "unclassified sequences" ]
[ 1326, 78925, 13663, 1, 3, 858 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 16, 3, 8, 4, 4, 19, 15, 2, 10, 15, 3, 2, 23 ]
13
true
Family
Pyridine nucleotide-disulphide oxidoreductase, class I
Pyridine nucleotide-disulphide oxidoreductase, class I
Pyr_nuc-diS_OxRdtase
8
IPR001102
1,102
Transglutaminase, N-terminal
Transglutaminase_N
Domain
10,971
false
false
Synonym(s): Protein-glutamine gamma-glutamyltransferase, Fibrinoligase, TGase.
[ "GO:0018149" ]
[ "peptide cross-linking" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF00868" ]
[ "Transglut_N" ]
[ 10971 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.3.2.13", "R-HSA-114608", "R-HSA-140875", "R-HSA-6785807", "R-HSA-6809371", "R-MMU-114608", "R-MMU-140875", "R-MMU-6809371", "R-RNO-114608", "R-RNO-140875", "R-RNO-6809371" ]
[ "EC:2.3.2.13", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-140875", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-6809371", "REACTOME:R-MMU-114608", "REACTOME:R-MMU-140875", "REACTOME:R-MMU-6809371", "REACTOME:R-RNO-114608", "REACTOME:R-RNO-140875", "REACTOME:R-RNO-6809371" ]
11
[ "1evu", "1ex0", "1f13", "1fie", "1g0d", "1ggt", "1ggu", "1ggy", "1kv3", "1l9m", "1l9n", "1nud", "1nuf", "1nug", "1qrk", "2q3z", "3ly6", "3s3j", "3s3p", "3s3s", "4kty", "4pyg", "5mhl", "5mhm", "5mhn", "5mho", "6a8p", "6kzb", "7tvz", "7tw0", "7tw1", "7tw3"...
53
[ "PUB00001513", "PUB00002570", "PUB00095164", "PUB00095165" ]
[ "1683845", "1974250", "15692067", "19269200" ]
[ "Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues.", "Structure of transglutaminases.", "Protein-4.2 association with band 3 (AE1, SLCA4) in Xenopus oocytes: effects of three natural protein-4.2 mutations associated with hemolytic anemia.", "Protein 4.2: a complex linker." ]
[ 1991, 1990, 2005, 2009 ]
4
[]
[]
0
0
null
[ "Eukaryota" ]
[ 10971 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 49, 3, 37, 30, 22 ]
5
true
Domain
Transglutaminase, N-terminal
Transglutaminase, N-terminal
Transglutaminase_N
1
IPR001103
1,103
Androgen receptor
Andrgn_rcpt
Family
794
false
false
Steroid or nuclear hormone receptors (NRs) constitute an important super-family of transcription regulators that are involved in diverse physiological functions, including control of embryonic development, cell differentiation and homeostasis. Members include the steroid hormone receptors and receptors for thyroid horm...
[ "GO:0003677", "GO:0004879", "GO:0005496", "GO:0006355", "GO:0030521", "GO:0005634" ]
[ "DNA binding", "nuclear receptor activity", "steroid binding", "regulation of DNA-templated transcription", "androgen receptor signaling pathway", "nucleus" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]
6
[ "PFAM", "PRINTS" ]
[ "PF02166", "PR00521" ]
[ "Androgen_recep", "ANDROGENR" ]
[ 794, 613 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-HSA-3371497", "R-HSA-383280", "R-HSA-4090294", "R-HSA-5625886", "R-HSA-5689880", "R-HSA-8940973", "R-MMU-3371497", "R-MMU-383280", "R-MMU-4090294", "R-MMU-5625886", "R-MMU-5689880", "R-MMU-8940973", "R-RNO-3371497", "R-RNO-383280", "R-RNO-4090294", "R-RNO-5625886", "R-RNO-5689880"...
[ "REACTOME:R-HSA-3371497", "REACTOME:R-HSA-383280", "REACTOME:R-HSA-4090294", "REACTOME:R-HSA-5625886", "REACTOME:R-HSA-5689880", "REACTOME:R-HSA-8940973", "REACTOME:R-MMU-3371497", "REACTOME:R-MMU-383280", "REACTOME:R-MMU-4090294", "REACTOME:R-MMU-5625886", "REACTOME:R-MMU-5689880", "REACTOME:...
23
[]
0
[ "PUB00001993", "PUB00003098", "PUB00004464", "PUB00006168", "PUB00007120" ]
[ "1307250", "1569163", "7899080", "8165128", "12089231" ]
[ "Androgen receptor gene mutations identified by SSCP in fourteen subjects with androgen insensitivity syndrome.", "A single amino acid substitution (Met786----Val) in the steroid-binding domain of human androgen receptor leads to complete androgen insensitivity syndrome.", "Vitamin D receptor contains multiple ...
[ 1992, 1992, 1995, 1994, 2002 ]
5
[]
[]
0
0
null
[ "Eukaryota" ]
[ 794 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 28, 1, 2 ]
3
true
Family
Androgen receptor
Androgen receptor
Andrgn_rcpt
9
IPR001104
1,104
3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal
3-oxo-5_a-steroid_4-DH_C
Domain
16,924
false
false
3-oxo-5-alpha-steroid 4-dehydrogenases, catalyse the conversion of 3-oxo-5-alpha-steroid + acceptor to 3-oxo-delta(4)-steroid + reduced acceptor. The steroid 5-alpha-reductase enzyme is responsible for the formation of dihydrotestosterone, this hormone promotes the differentiation of male external genitalia and the pro...
[ "GO:0016627", "GO:0006629" ]
[ "oxidoreductase activity, acting on the CH-CH group of donors", "lipid metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02544" ]
[ "Steroid_dh" ]
[ 16924 ]
1
[ "EC", "GP", "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "1.3.1", "GenProp1376", "GenProp1552", "GenProp1569", "GenProp1742", "PDOC50244", "R-BTA-193048", "R-BTA-75876", "R-CEL-193048", "R-CEL-446199", "R-CEL-75876", "R-DDI-75876", "R-DME-193048", "R-DME-446199", "R-DRE-193048", "R-DRE-446199", "R-HSA-193048", "R-HSA-446199", "R-HSA-47...
[ "EC:1.3.1", "GP:GenProp1376", "GP:GenProp1552", "GP:GenProp1569", "GP:GenProp1742", "PROSITEDOC:PDOC50244", "REACTOME:R-BTA-193048", "REACTOME:R-BTA-75876", "REACTOME:R-CEL-193048", "REACTOME:R-CEL-446199", "REACTOME:R-CEL-75876", "REACTOME:R-DDI-75876", "REACTOME:R-DME-193048", "REACTOME:...
35
[ "7bw1", "7c83" ]
2
[ "PUB00007121", "PUB00007122", "PUB00020382", "PUB00089495", "PUB00089496" ]
[ "1686016", "8602526", "1944596", "20637498", "12482854" ]
[ "Characterization and chromosomal mapping of a human steroid 5 alpha-reductase gene and pseudogene and mapping of the mouse homologue.", "A role for brassinosteroids in light-dependent development of Arabidopsis.", "Deletion of steroid 5 alpha-reductase 2 gene in male pseudohermaphroditism.", "SRD5A3 is requi...
[ 1991, 1996, 1991, 2010, 2003 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Promethearchaeati", "Yasminevirus sp. GU-2018", "unclassified sequences" ]
[ 695, 16188, 6, 1, 34 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 22, 5, 24, 4, 16, 20, 3, 18, 18, 2, 3, 36 ]
12
true
Domain
3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal
3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal
3-oxo-5_a-steroid_4-DH_C
8
IPR001105
1,105
Thromboxane receptor
Thbox_rcpt
Family
1,726
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:0004960", "GO:0007186", "GO:0016020" ]
[ "thromboxane receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00429" ]
[ "THROMBOXANER" ]
[ 1726 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "346", "R-BTA-391908", "R-BTA-416476", "R-BTA-416482", "R-BTA-428930", "R-HSA-391908", "R-HSA-416476", "R-HSA-416482", "R-HSA-428930", "R-MMU-391908", "R-MMU-416476", "R-MMU-416482", "R-MMU-428930", "R-RNO-391908", "R-RNO-416476", "R-RNO-416482", "R-RNO-428930" ]
[ "IUPHAR:346", "REACTOME:R-BTA-391908", "REACTOME:R-BTA-416476", "REACTOME:R-BTA-416482", "REACTOME:R-BTA-428930", "REACTOME:R-HSA-391908", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-416482", "REACTOME:R-HSA-428930", "REACTOME:R-MMU-391908", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-416482", "RE...
17
[ "6iiu", "6iiv", "8xjn", "8xjo", "9gg5", "9ggg" ]
6
[ "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
[ "IPR008365" ]
[]
1
0
1
[ "Eukaryota", "Halocatena pleomorpha", "Pseudomonadati" ]
[ 1723, 1, 2 ]
3
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 14, 5, 3, 2 ]
4
true
Family
Thromboxane receptor
Thromboxane receptor
Thbox_rcpt
5
IPR001106
1,106
Aromatic amino acid lyase
Aromatic_Lyase
Family
32,459
false
false
This family includes phenylalanine ammonia-lyase, (PAL; ), histidine ammonia-lyase, (HAL; ), and tyrosine aminomutase, ( ) [ , , ]. PAL and HAL are members of the Lyase class I_like superfamily of enzymes that, catalyze similar beta-elimination reactions and are active as homotetramers. Both PAL and HAL contain a catal...
[]
[]
[]
0
[ "PFAM", "PANTHER", "CDD" ]
[ "PF00221", "PTHR10362", "cd00332" ]
[ "Lyase_aromatic", "", "PAL-HAL" ]
[ 32158, 31750, 28449 ]
3
[ "EC", "EC", "GP", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.3.1", "4.3.1.3", "GenProp1619", "PWY-5028", "PWY-5030", "PDOC00424", "R-BTA-70921", "R-CEL-70921", "R-DDI-70921", "R-HSA-70921", "R-MMU-70921", "R-RNO-70921" ]
[ "EC:4.3.1", "EC:4.3.1.3", "GP:GenProp1619", "METACYC:PWY-5028", "METACYC:PWY-5030", "PROSITEDOC:PDOC00424", "REACTOME:R-BTA-70921", "REACTOME:R-CEL-70921", "REACTOME:R-DDI-70921", "REACTOME:R-HSA-70921", "REACTOME:R-MMU-70921", "REACTOME:R-RNO-70921" ]
12
[ "1b8f", "1eb4", "1gk2", "1gk3", "1gkj", "1gkm", "1t6j", "1t6p", "1w27", "1y2m", "2nyf", "2nyn", "2o6y", "2o78", "2o7b", "2o7d", "2o7e", "2o7f", "2ohy", "2qve", "2rjr", "2rjs", "2yii", "3czo", "3kdy", "3kdz", "3nz4", "3unv", "4baa", "4bab", "4c5r", "4c5s"...
48
[ "PUB00014374", "PUB00023551", "PUB00025286", "PUB00031359", "PUB00035855", "PUB00057431", "PUB00057432", "PUB00057433", "PUB00079866", "PUB00079867" ]
[ "12502351", "10220322", "11895450", "15350127", "16478474", "7925471", "16793524", "19222035", "11578924", "12667480" ]
[ "Plant-like biosynthetic pathways in bacteria: from benzoic acid to chalcone.", "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.", "Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism.", "Cr...
[ 2002, 1999, 2002, 2004, 2006, 1994, 2006, 2009, 2001, 2003 ]
10
[]
[ "IPR005921", "IPR005922", "IPR022314", "IPR031007" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "Mimiviridae", "unclassified sequences" ]
[ 249, 22263, 9621, 2, 324 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "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" ]
[ 18, 1, 7, 12, 4, 1, 36, 3, 82 ]
9
true
Family
Aromatic amino acid lyase
Aromatic amino acid lyase
Aromatic_Lyase
5
IPR001107
1,107
Band 7 domain
Band_7
Domain
124,553
false
false
The band-7 protein family comprises a diverse set of membrane-bound proteins characterised by the presence of a conserved domain, the band-7 domain, also known as SPFH or PHB domain [ ]. The exact function of the band-7 domain is not known, but examples from animal and bacterial stomatin-type proteins demonstrate bindi...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF01145", "SM00244" ]
[ "Band_7", "PHB" ]
[ 124408, 106709 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-382556", "R-BTA-5213460", "R-BTA-5673000", "R-BTA-5675482", "R-BTA-8849932", "R-BTA-8949664", "R-BTA-8980692", "R-BTA-9013106", "R-BTA-9696264", "R-BTA-9696273", "R-BTA-9840373", "R-CEL-2672351", "R-CEL-373753", "R-CEL-382556", "R-CEL-5673000", "R-CEL-6798695", "R-CEL-8949664"...
[ "REACTOME:R-BTA-382556", "REACTOME:R-BTA-5213460", "REACTOME:R-BTA-5673000", "REACTOME:R-BTA-5675482", "REACTOME:R-BTA-8849932", "REACTOME:R-BTA-8949664", "REACTOME:R-BTA-8980692", "REACTOME:R-BTA-9013106", "REACTOME:R-BTA-9696264", "REACTOME:R-BTA-9696273", "REACTOME:R-BTA-9840373", "REACTOME...
98
[ "1win", "2rpb", "3bk6", "4fvf", "4fvg", "4fvj", "7vhp", "7vhq", "7wh3", "7wi3", "8gn9", "8j4i", "8rrh", "8z5g", "9bq2", "9cz1", "9cz2", "9o6s", "9o6t", "9o9u", "9o9z", "9oa0", "9oh9", "9unl" ]
24
[ "PUB00019208", "PUB00055449", "PUB00076124" ]
[ "10542406", "4326772", "24782879" ]
[ "The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins.", "Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.", "Mitochondrial Band-7 family proteins: scaffolds for respiratory chain assembly?" ]
[ 1999, 1971, 2014 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1539, 75659, 45258, 824, 1273 ]
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",...
[ 54, 36, 36, 33, 4, 69, 49, 5, 51, 47, 2, 3, 59 ]
13
true
Domain
Band 7 domain
Band 7 domain
Band_7
1
IPR001108
1,108
Peptidase A22A, presenilin
Peptidase_A22A
Family
5,626
false
false
This group of aspartic peptidases belong to MEROPS peptidase family A22 (presenilin family), 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 Alzheimer's dis...
[ "GO:0042500", "GO:0016485", "GO:0016020" ]
[ "aspartic endopeptidase activity, intramembrane cleaving", "protein processing", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF01080", "PR01072", "PTHR10202" ]
[ "Presenilin", "PRESENILIN", "" ]
[ 5603, 4484, 5550 ]
3
[ "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-6798695", "R-BTA-9839383", "R-CEL-1251985", "R-CEL-3928665", "R-DDI-6798695", "R-DME-1251985", "R-DME-3928665", "R-DRE-1251985", "R-DRE-193692", "R-DRE-3928665", "R-DRE-6798695", "R-DRE-9839383", "...
[ "EC:3.4.23.-", "REACTOME:R-BTA-1251985", "REACTOME:R-BTA-193692", "REACTOME:R-BTA-205043", "REACTOME:R-BTA-3928665", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-9839383", "REACTOME:R-CEL-1251985", "REACTOME:R-CEL-3928665", "REACTOME:R-DDI-6798695", "REACTOME:R-DME-1251985", "REACTOME:R-DME-39286...
59
[ "2kr6", "4uis", "5a63", "5fn2", "5fn3", "5fn4", "5fn5", "6idf", "6iyc", "6lqg", "6lr4", "7c9i", "7d8x", "7y5t", "7y5x", "7y5z", "8im7", "8k8e", "8kco", "8kcp", "8kcs", "8kct", "8kcu", "8oqy", "8oqz", "8x52", "8x53", "8x54", "9k95" ]
29
[ "PUB00000093", "PUB00000349", "PUB00000522", "PUB00000974", "PUB00001330", "PUB00002010", "PUB00011023", "PUB00011707", "PUB00021296", "PUB00042504", "PUB00065205", "PUB00066803", "PUB00076784", "PUB00076785", "PUB00076786", "PUB00076827", "PUB00076828", "PUB00076829", "PUB000768...
[ "2194475", "1851433", "8439290", "9791530", "6795036", "9521418", "10331925", "11566868", "10864493", "2682266", "23254940", "21765428", "4912600", "10497172", "21751400", "9450754", "26280335", "8755489", "10206644", "11518718", "14504279" ]
[ "The structure and function of the aspartic proteinases.", "Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.", "Evolutionary families of peptidases.", "Introduction: genetic determinants of mid- and late-life dementias.", "Gastric proteinases--structure, func...
[ 1990, 1991, 1993, 1998, 1981, 1998, 1999, 2001, 2000, 1989, 2013, 2011, 1970, 1999, 2011, 1998, 2015, 1996, 1999, 2001, 2003 ]
21
[ "IPR006639" ]
[ "IPR001493", "IPR001686", "IPR002031" ]
1
3
0
[ "Archaea", "Eukaryota", "marine sediment metagenome" ]
[ 8, 5610, 8 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 8, 3, 5, 4, 52, 7, 9, 5, 9 ]
9
true
Family
Peptidase A22A, presenilin
Peptidase A22A, presenilin
Peptidase_A22A
6
IPR001109
1,109
Hydrogenase expression/formation protein, HupF/HypC
Hydrogenase_HupF/HypC
Family
9,542
false
false
The large subunit of [NiFe]-hydrogenase, as well as other nickel metalloenzymes, is synthesised as a precursor devoid of the metalloenzyme active site. This precursor then undergoes a complex post-translational maturation process that requires a number of accessory proteins. The hydrogenase expression/formation and mat...
[]
[]
[]
0
[ "PFAM", "PRINTS", "PANTHER", "NCBIFAM" ]
[ "PF01455", "PR00445", "PTHR35177", "TIGR00074" ]
[ "HupF_HypC", "HUPFHYPC", "", "hypC_hupF" ]
[ 9541, 8694, 8765, 8791 ]
4
[ "PROSITEDOC" ]
[ "PDOC00841" ]
[ "PROSITEDOC:PDOC00841" ]
1
[ "2ot2", "2z1c", "3d3r", "3vyr", "3vys", "3vyt", "3vyu" ]
7
[ "PUB00003839", "PUB00011027", "PUB00014218" ]
[ "8497190", "9485446", "10783387" ]
[ "Organization of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of two hyp regulatory mutants.", "Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation.", "Anal...
[ 1993, 1998, 2000 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 436, 8940, 11, 155 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Hydrogenase expression/formation protein, HupF/HypC
Hydrogenase expression/formation protein, HupF/HypC
Hydrogenase_HupF/HypC
5
IPR001110
1,110
Uncharacterised protein family UPF0012, conserved site
UPF0012_CS
Conserved_site
26,058
false
false
A group of uncharacterised proteins share this well-conserved region centred on a cysteine residue. These proteins are a subset of the carbon-nitrogen hydrolase family indicating that these as yet uncharacterised proteins may be related to members of this family [ ].
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01227" ]
[ "UPF0012" ]
[ 26058 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.5.1", "PDOC00943", "R-DDI-6798695", "R-SCE-6798695", "R-SPO-6798695" ]
[ "EC:3.5.1", "PROSITEDOC:PDOC00943", "REACTOME:R-DDI-6798695", "REACTOME:R-SCE-6798695", "REACTOME:R-SPO-6798695" ]
5
[ "1ems", "1f89", "3p8k", "4h5u", "4hg3", "4hg5", "7elf" ]
7
[ "PUB00005733" ]
[ "7987228" ]
[ "A new family of carbon-nitrogen hydrolases." ]
[ 1994 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 571, 21633, 3654, 200 ]
4
[ "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)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe ...
[ 1, 5, 2, 2, 2, 1, 4, 2, 1 ]
9
true
Conserved_site
Uncharacterised protein family UPF0012, conserved site
Uncharacterised protein family UPF0012, conserved site
UPF0012_CS
2
IPR001111
1,111
TGF-beta, propeptide
TGF-b_propeptide
Domain
25,467
false
false
This entry represents the propeptide region of TGF-beta that forms LAP. TGF-beta is secreted as a latent complex, consisting of the TGF-beta dimer non-covalently bound to LAP (latency associated peptide) plus a latent TGF-beta binding protein (LTBP). After post-translational processing, TGF-beta binds non-covalently to...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00688" ]
[ "TGFb_propeptide" ]
[ 25467 ]
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-114608", "R-BTA-1502540", "R-BTA-201451", "R-BTA-209822", "R-BTA-2129379", "R-BTA-2173789", "R-BTA-2473224", "R-BTA-381426", "R-BTA-8957275", "R-BTA-9839389", "R-BTA-9839406", "R-DME-114608", "R-DME-1502540", "R-DME-201451", "R-DME-2129379", "R-DME-2173788", "R-DME-2173789", ...
[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-1502540", "REACTOME:R-BTA-201451", "REACTOME:R-BTA-209822", "REACTOME:R-BTA-2129379", "REACTOME:R-BTA-2173789", "REACTOME:R-BTA-2473224", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-8957275", "REACTOME:R-BTA-9839389", "REACTOME:R-BTA-9839406", "REACTOME:R-...
120
[ "4ycg", "4yci", "5ffo", "5hly", "5hlz", "5ntu", "5nxs", "5vqf", "5vqp", "6gff", "6p7j", "6sf2", "6uja", "6umx", "7poi", "7poj", "7y1r", "7y1t", "8c7h", "8fxs", "8fxv", "8rew", "8rex", "8udz", "8vs6", "8vsb", "8vsc", "8vsd" ]
28
[ "PUB00003550", "PUB00083453" ]
[ "9150447", "15611103" ]
[ "Latent transforming growth factor-beta: structural features and mechanisms of activation.", "Latent transforming growth factor-beta (TGF-beta) binding proteins: orchestrators of TGF-beta availability." ]
[ 1997, 2005 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 63, 25402, 2 ]
3
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 86, 8, 92, 61, 58 ]
5
true
Domain
TGF-beta, propeptide
TGF-beta, propeptide
TGF-b_propeptide
9
IPR001114
1,114
Adenylosuccinate synthetase
Adenylosuccinate_synthetase
Family
36,537
false
false
Adenylosuccinate synthetase ( ) plays an important role in purine biosynthesis, by catalysing the GTP-dependent conversion of IMP and aspartic acid to AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate gr...
[ "GO:0000166", "GO:0004019", "GO:0006164" ]
[ "nucleotide binding", "adenylosuccinate synthase activity", "purine nucleotide biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PFAM", "PANTHER", "SMART", "NCBIFAM", "CDD" ]
[ "MF_00011", "PF00709", "PTHR11846", "SM00788", "TIGR00184", "cd03108" ]
[ "Adenylosucc_synth", "Adenylsucc_synt", "", "Adenylsucc_synt", "purA", "AdSS" ]
[ 35956, 36516, 36354, 35965, 30688, 32428 ]
6
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.3.4.4", "GenProp0747", "GenProp1372", "GenProp1406", "GenProp1592", "PWY-7219", "PDOC00444", "R-BTA-73817", "R-CEL-73817", "R-DDI-73817", "R-DME-73817", "R-DRE-73817", "R-GGA-421203", "R-HSA-73817", "R-MMU-73817", "R-PFA-73817", "R-SCE-73817", "R-SPO-73817", "R-SSC-73817", "...
[ "EC:6.3.4.4", "GP:GenProp0747", "GP:GenProp1372", "GP:GenProp1406", "GP:GenProp1592", "METACYC:PWY-7219", "PROSITEDOC:PDOC00444", "REACTOME:R-BTA-73817", "REACTOME:R-CEL-73817", "REACTOME:R-DDI-73817", "REACTOME:R-DME-73817", "REACTOME:R-DRE-73817", "REACTOME:R-GGA-421203", "REACTOME:R-HSA...
20
[ "1ade", "1adi", "1cg0", "1cg1", "1cg3", "1cg4", "1ch8", "1cib", "1dj2", "1dj3", "1gim", "1gin", "1hon", "1hoo", "1hop", "1iwe", "1j4b", "1juy", "1kjx", "1kkb", "1kkf", "1ksz", "1lny", "1lon", "1loo", "1mez", "1mf0", "1mf1", "1nht", "1p9b", "1qf4", "1qf5"...
62
[ "PUB00006296", "PUB00006475" ]
[ "8244965", "10669609" ]
[ "Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains.", "Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana." ]
[ 1993, 2000 ]
2
[]
[ "IPR027509", "IPR027529", "IPR046383" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 905, 26416, 8208, 175, 833 ]
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",...
[ 7, 1, 4, 2, 1, 8, 6, 1, 4, 8, 1, 1, 7 ]
13
true
Family
Adenylosuccinate synthetase
Adenylosuccinate synthetase
Adenylosuccinate_synthetase
7
IPR001115
1,115
Alpha 1B adrenoceptor
ADRA1B_rcpt
Family
687
false
false
This entry represents the alpha 1B adrenoceptor. It is widely distributed, with high levels occurring in the CNS, mainly in the cerebral cortex and brainstem [ , ], and in peripheral tissues such as the kidney and lung [ , ]. Alpha 1B adrenoceptor has been shown to couple to phospholipase A2 and cause the activation of...
[ "GO:0004937", "GO:0006937", "GO:0007186", "GO:0019229", "GO:0055117", "GO:0016020" ]
[ "alpha1-adrenergic receptor activity", "regulation of muscle contraction", "G protein-coupled receptor signaling pathway", "regulation of vasoconstriction", "regulation of cardiac muscle contraction", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
6
[ "PRINTS", "CDD" ]
[ "PR00556", "cd15326" ]
[ "ADRENRGCA1BR", "7tmA_alpha1B_AR" ]
[ 571, 628 ]
2
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "23", "R-HSA-390696", "R-HSA-416476", "R-HSA-416482", "R-MMU-390696", "R-MMU-416476", "R-MMU-416482", "R-RNO-390696", "R-RNO-416476", "R-RNO-416482" ]
[ "IUPHAR:23", "REACTOME:R-HSA-390696", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-416482", "REACTOME:R-MMU-390696", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-416482", "REACTOME:R-RNO-390696", "REACTOME:R-RNO-416476", "REACTOME:R-RNO-416482" ]
10
[]
0
[ "PUB00066376", "PUB00066377", "PUB00066392", "PUB00066393", "PUB00066395", "PUB00066396", "PUB00066399", "PUB00066410", "PUB00066991" ]
[ "18882199", "2855960", "9285356", "8114668", "2887122", "9280371", "11337028", "10517699", "8232229" ]
[ "A study of the adrenotropic receptors.", "Subtypes of alpha 2-adrenoceptors: pharmacological and molecular biological evidence converge.", "Distribution of alpha 1a-, alpha 1b- and alpha 1d-adrenergic receptor mRNA in the rat brain and spinal cord.", "Localization of mRNA for three distinct alpha 1-adrenergi...
[ 1948, 1988, 1997, 1994, 1987, 1997, 2000, 1999, 1993 ]
9
[ "IPR002233" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 687 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 5, 3 ]
3
true
Family
Alpha 1B adrenoceptor
Alpha 1B adrenoceptor
ADRA1B_rcpt
6
IPR001116
1,116
Somatostatin receptor 1
Somatstn_rcpt_1
Family
738
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" ]
[ "PR00587" ]
[ "SOMATOSTTN1R" ]
[ 738 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "355", "R-CFA-375276", "R-CFA-418594", "R-HSA-375276", "R-HSA-418594", "R-MMU-375276", "R-MMU-418594", "R-RNO-375276", "R-RNO-418594" ]
[ "IUPHAR:355", "REACTOME:R-CFA-375276", "REACTOME:R-CFA-418594", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594" ]
9
[ "8xio", "8xip", "9ik8", "9ik9" ]
4
[ "PUB00013316", "PUB00063572", "PUB00063590", "PUB00063595", "PUB00063596", "PUB00063597", "PUB00063598", "PUB00063599", "PUB00063600", "PUB00063601", "PUB00063602", "PUB00063603", "PUB00063604", "PUB00063605", "PUB00063618", "PUB00063619" ]
[ "14507421", "10433861", "7792934", "8243278", "8078491", "7907795", "1346068", "8483934", "15361490", "10598790", "1328199", "7538774", "9426226", "8684611", "18406829", "8034040" ]
[ "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, 1997, 1994 ]
16
[ "IPR000586" ]
[]
1
0
1
[ "Vertebrata" ]
[ 738 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 1, 2, 3 ]
4
true
Family
Somatostatin receptor 1
Somatostatin receptor 1
Somatstn_rcpt_1
2
IPR001117
1,117
Multicopper oxidase, second cupredoxin domain
Cu-oxidase_2nd
Domain
67,950
false
false
This entry represents the second cupredoxin domain of multicopper oxidases. This domain is also present in proteins that have lost the ability to bind copper. Copper is one of the most prevalent transition metals in living organisms and its biological function is intimately related to its redox properties. Since free c...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00394" ]
[ "Cu-oxidase" ]
[ 67950 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.10.3", "R-HSA-381426", "R-HSA-425410", "R-HSA-5619049", "R-HSA-5619060", "R-HSA-8957275", "R-HSA-917937", "R-MMU-381426", "R-MMU-425410", "R-MMU-8957275", "R-MMU-917937", "R-RNO-381426", "R-RNO-425410", "R-RNO-8957275", "R-RNO-917937" ]
[ "EC:1.10.3", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-425410", "REACTOME:R-HSA-5619049", "REACTOME:R-HSA-5619060", "REACTOME:R-HSA-8957275", "REACTOME:R-HSA-917937", "REACTOME:R-MMU-381426", "REACTOME:R-MMU-425410", "REACTOME:R-MMU-8957275", "REACTOME:R-MMU-917937", "REACTOME:R-RNO-381426", ...
15
[ "1a65", "1aoz", "1aq8", "1as6", "1as7", "1as8", "1aso", "1asp", "1asq", "1bq5", "1et5", "1et7", "1et8", "1gs6", "1gs7", "1gs8", "1gsk", "1gw0", "1gyc", "1hau", "1haw", "1hfu", "1j9q", "1j9r", "1j9s", "1j9t", "1kbv", "1kbw", "1kcb", "1kcw", "1kv7", "1kya"...
455
[ "PUB00000062", "PUB00000901", "PUB00001382", "PUB00001602", "PUB00011817", "PUB00035911", "PUB00035912", "PUB00035913", "PUB00101322", "PUB00101323", "PUB00101324" ]
[ "3052293", "8293473", "2404764", "1995346", "11867755", "14572631", "11041837", "16234932", "35079912", "9413439", "35175277" ]
[ "Cofactor proteins in the assembly and expression of blood clotting enzyme complexes.", "The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.", "The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships.", "A structure-der...
[ 1988, 1994, 1990, 1991, 2002, 2003, 2000, 2005, 2022, 1997, 2022 ]
11
[]
[ "IPR034258", "IPR034271", "IPR034282", "IPR034285", "IPR044130" ]
0
5
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 105, 16562, 50310, 972, 1 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "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...
[ 190, 1, 14, 1, 16, 7, 10, 105, 7, 3, 1, 170 ]
12
true
Domain
Multicopper oxidase, second cupredoxin domain
Multicopper oxidase, second cupredoxin domain
Cu-oxidase_2nd
2
IPR001119
1,119
S-layer homology domain
SLH_dom
Domain
43,372
false
false
S-layers are paracrystalline mono-layered assemblies of (glyco)proteins which coat the surface of bacteria [ , ]. Several S-layer proteins and some other cell wall proteins contain one or more copies of a domain of about 50-60 residues, which has been called SLH (for S-layer homology). Although it was originally propos...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF00395", "PS51272" ]
[ "SLH", "SLH" ]
[ 41308, 42991 ]
2
[ "GP" ]
[ "GenProp0811" ]
[ "GP:GenProp0811" ]
1
[ "3pyw", "4aq1", "6bt4", "6cwc", "6cwf", "6cwh", "6cwi", "6cwl", "6cwm", "6cwn", "6cwr", "7sv3", "7sv4", "7sv5", "7sv6", "7zgx", "7zgy", "8acq", "8ae1", "8agd", "8bym", "8bys", "8byt", "8bz2", "9g93" ]
25
[ "PUB00043754", "PUB00043755", "PUB00043756", "PUB00043757", "PUB00043758" ]
[ "10366863", "10648507", "10049812", "15758211", "16487313" ]
[ "Bacterial S-layers.", "S-Layer proteins.", "Structural research on surface layers: a focus on stability, surface layer homology domains, and surface layer-cell wall interactions.", "The structure of secondary cell wall polymers: how Gram-positive bacteria stick their cell walls together.", "Protein cell su...
[ 1999, 2000, 1998, 2005, 2006 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 2, 42205, 737, 28, 400 ]
5
[ "Arabidopsis thaliana" ]
[ 21 ]
1
true
Domain
S-layer homology domain
S-layer homology domain
SLH_dom
2
IPR001122
1,122
Capsid protein C, flavivirus
Flavi_capsidC
Domain
16,272
false
false
Flaviruses are small, enveloped RNA viruses that use arthropods such as mosquitoes for transmission to their vertebrate hosts, and include Yellow fever virus, West Nile virus, Tick-borne encephalitis virus, Japanese encephalitis virus, and Dengue virus 2 [ ]. Flaviviruses consist of three structural proteins: the core ...
[ "GO:0005198", "GO:0019028" ]
[ "structural molecule activity", "viral capsid" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF01003" ]
[ "Flavi_capsid" ]
[ 16272 ]
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
[ "1r6r", "1sfk", "5ow2", "5ygh", "5z0r", "5z0v", "6c44", "6lnt", "6vg5", "6vso", "7ywq", "8cxg", "8cxh", "8cxi" ]
14
[ "PUB00015617", "PUB00020600" ]
[ "15378043", "12768036" ]
[ "Transmission cycles, host range, evolution and emergence of arboviral disease.", "Flavivirus capsid is a dimeric alpha-helical protein." ]
[ 2004, 2003 ]
2
[]
[]
0
0
null
[ "Orthornavirae" ]
[ 16272 ]
1
[]
[]
0
true
Domain
Capsid protein C, flavivirus
Capsid protein C, flavivirus
Flavi_capsidC
7
IPR001123
1,123
Amino acid exporter protein, LeuE-type
LeuE-type
Family
97,605
false
false
A number of amino acid exporter proteins belong to this family. LeuE encodes an exporter of leucine and some other structurally unrelated amino acids [ ]. This family also includes threonine efflux protein RhtC [ ], arginine exporter protein ArgO/YggA [ ], as well as a number of uncharacterised proteins from a variety ...
[ "GO:0006865", "GO:0016020" ]
[ "amino acid transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF01810", "PIRSF006324", "PTHR30086" ]
[ "LysE", "LeuE", "" ]
[ 97300, 46652, 94460 ]
3
[]
[]
[]
0
[]
0
[ "PUB00042858", "PUB00085012", "PUB00085015" ]
[ "15150242", "10386596", "16098526" ]
[ "Evidence for an arginine exporter encoded by yggA (argO) that is regulated by the LysR-type transcriptional regulator ArgP in Escherichia coli.", "The novel transmembrane Escherichia coli proteins involved in the amino acid efflux.", "The yeaS (leuE) gene of Escherichia coli encodes an exporter of leucine, and...
[ 2004, 1999, 2005 ]
3
[]
[ "IPR004777", "IPR004778" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 1043, 95631, 128, 1, 802 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 1, 6 ]
2
true
Family
Amino acid exporter protein, LeuE-type
Amino acid exporter protein, LeuE-type
LeuE-type
6
IPR001124
1,124
Lipid-binding serum glycoprotein, C-terminal
Lipid-bd_serum_glycop_C
Domain
9,924
false
false
This entry represents the C-terminal domain found in several lipid-binding serum glycoproteins. The N- and C-terminal domains share a similar two-layer α/β structure, but they show little sequence identity. Proteins containing this C-terminal domain include: Bactericidal permeability-increasing protein (BPI) Lipopolysa...
[ "GO:0008289" ]
[ "lipid binding" ]
[ "molecular_function" ]
1
[ "PFAM", "SMART" ]
[ "PF02886", "SM00329" ]
[ "LBP_BPI_CETP_C", "BPI2" ]
[ 9629, 8795 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00367", "R-BTA-166016", "R-BTA-6798695", "R-BTA-6803157", "R-CEL-166016", "R-CEL-5686938", "R-DDI-166016", "R-DDI-5686938", "R-DDI-6798695", "R-DDI-6803157", "R-HSA-166016", "R-HSA-166020", "R-HSA-381426", "R-HSA-5686938", "R-HSA-6785807", "R-HSA-6798695", "R-HSA-6803157", "R-...
[ "PROSITEDOC:PDOC00367", "REACTOME:R-BTA-166016", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6803157", "REACTOME:R-CEL-166016", "REACTOME:R-CEL-5686938", "REACTOME:R-DDI-166016", "REACTOME:R-DDI-5686938", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-6803157", "REACTOME:R-HSA-166016", "REACTOME:R-HS...
34
[ "1bp1", "1ewf", "2obd", "4ews", "4f2a", "4m4d" ]
6
[ "PUB00005225", "PUB00021529", "PUB00043816", "PUB00043817", "PUB00043818", "PUB00043819", "PUB00043820" ]
[ "9188532", "10843855", "12887306", "17277799", "18245229", "16364440", "12693940" ]
[ "Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.", "The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold.", "Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): structure...
[ 1997, 2000, 2003, 2007, 2008, 2006, 2003 ]
7
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati" ]
[ 9919, 5 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 13, 12, 5, 29, 19, 5, 33, 7 ]
8
true
Domain
Lipid-binding serum glycoprotein, C-terminal
Lipid-binding serum glycoprotein, C-terminal
Lipid-bd_serum_glycop_C
2
IPR001126
1,126
UmuC domain
UmuC
Domain
74,485
false
false
In Escherichia coli, UV and many chemicals appear to cause mutagenesis by a process of translesion synthesis that requires DNA polymerase III and the SOS-regulated proteins UmuD, UmuC and RecA. This machinery allows the replication to continue through DNA lesion, and therefore avoid lethal interruption of DNA replicati...
[ "GO:0006281" ]
[ "DNA repair" ]
[ "biological_process" ]
1
[ "PFAM", "PROFILE" ]
[ "PF00817", "PS50173" ]
[ "IMS", "UMUC" ]
[ 73409, 67718 ]
2
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.7.7", "PDOC50173", "R-CEL-5655862", "R-CEL-5696397", "R-CEL-5696400", "R-CEL-6782135", "R-CEL-6782210", "R-DME-110312", "R-DME-110320", "R-DME-5655862", "R-DME-5656121", "R-GGA-353503", "R-HSA-110312", "R-HSA-110320", "R-HSA-5655862", "R-HSA-5656121", "R-HSA-5656169", "R-HSA-5...
[ "EC:2.7.7.7", "PROSITEDOC:PDOC50173", "REACTOME:R-CEL-5655862", "REACTOME:R-CEL-5696397", "REACTOME:R-CEL-5696400", "REACTOME:R-CEL-6782135", "REACTOME:R-CEL-6782210", "REACTOME:R-DME-110312", "REACTOME:R-DME-110320", "REACTOME:R-DME-5655862", "REACTOME:R-DME-5656121", "REACTOME:R-GGA-353503",...
46
[ "1im4", "1jih", "1jx4", "1jxl", "1k1q", "1k1s", "1n48", "1n56", "1ryr", "1rys", "1s0m", "1s0n", "1s0o", "1s10", "1s97", "1s9f", "1t3n", "1t94", "1zet", "2ago", "2agp", "2agq", "2alz", "2aq4", "2asd", "2asj", "2asl", "2atl", "2au0", "2bq3", "2bqr", "2bqu"...
517
[ "PUB00010596" ]
[ "9560379" ]
[ "Mutagenesis and more: umuDC and the Escherichia coli SOS response." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 690, 55711, 17235, 15, 6, 828 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 24, 3, 19, 3, 2, 24, 30, 4, 17, 20, 2, 3, 74 ]
13
true
Domain
UmuC domain
UmuC domain
UmuC
1
IPR001127
1,127
Phosphotransferase system, sugar-specific permease EIIA type 1
PTS_EIIA_1_perm
Domain
26,985
false
false
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [ , ] is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of incoming sugar substrates and coupled with translocation across the cell membrane, makes the PTS a link between the uptake and metabolism of sugars...
[ "GO:0009401" ]
[ "phosphoenolpyruvate-dependent sugar phosphotransferase system" ]
[ "biological_process" ]
1
[ "PFAM", "PROSITE", "PROFILE", "NCBIFAM" ]
[ "PF00358", "PS00371", "PS51093", "TIGR00830" ]
[ "PTS_EIIA_1", "PTS_EIIA_TYPE_1_HIS", "PTS_EIIA_TYPE_1", "PTBA" ]
[ 26951, 22965, 26714, 25313 ]
4
[ "EC", "GP", "GP", "PROSITEDOC" ]
[ "2.7.1", "GenProp0119", "GenProp1159", "PDOC00528" ]
[ "EC:2.7.1", "GP:GenProp0119", "GP:GenProp1159", "PROSITEDOC:PDOC00528" ]
4
[ "1ax3", "1f3g", "1f3z", "1ggr", "1gla", "1glb", "1glc", "1gld", "1gle", "1gpr", "1o2f", "2f3g", "2gpr", "2mp0", "3our", "4jbw" ]
16
[ "PUB00000073", "PUB00002162", "PUB00003612", "PUB00017027", "PUB00017028" ]
[ "2197982", "1537788", "8246840", "7815935", "11361063" ]
[ "The bacterial phosphoenolpyruvate: glycose phosphotransferase system.", "Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.", "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.", "The bacterial phosp...
[ 1990, 1992, 1993, 1994, 2001 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 26866, 55, 64 ]
3
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Domain
Phosphotransferase system, sugar-specific permease EIIA type 1
Phosphotransferase system, sugar-specific permease EIIA type 1
PTS_EIIA_1_perm
5
IPR001128
1,128
Cytochrome P450
Cyt_P450
Family
579,284
false
false
This entry represents Cytochrome P450 and closely related proteins. This family also includes germacrene A hydroxylase (GAO1; ) from plants such as lettuce (Lactuca sativa). GAO1 is required for the biosynthesis of germacrene-derived sesquiterpene lactones, which are characteristic natural products in members of the As...
[ "GO:0004497", "GO:0005506", "GO:0016705", "GO:0020037" ]
[ "monooxygenase activity", "iron ion binding", "oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen", "heme binding" ]
[ "molecular_function", "molecular_function", "molecular_function", "molecular_function" ]
4
[ "PFAM", "PRINTS" ]
[ "PF00067", "PR00385" ]
[ "p450", "P450" ]
[ 579154, 393170 ]
2
[ "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "GenProp1217", "GenProp1246", "GenProp1338", "GenProp1417", "GenProp1437", "GenProp1594", "GenProp1603", "GenProp1609", "GenProp1622", "GenProp1638", "GenProp1644", "GenProp1666", "GenProp1740", "GenProp1742", "GenProp1745", "GenProp1759", "GenProp1760", "PDOC00081", "R-BTA-19127...
[ "GP:GenProp1217", "GP:GenProp1246", "GP:GenProp1338", "GP:GenProp1417", "GP:GenProp1437", "GP:GenProp1594", "GP:GenProp1603", "GP:GenProp1609", "GP:GenProp1622", "GP:GenProp1638", "GP:GenProp1644", "GP:GenProp1666", "GP:GenProp1740", "GP:GenProp1742", "GP:GenProp1745", "GP:GenProp1759"...
243
[ "1akd", "1bu7", "1bvy", "1c8j", "1cl6", "1cmj", "1cmn", "1cp4", "1cpt", "1dt6", "1dz4", "1dz6", "1dz8", "1dz9", "1e9x", "1ea1", "1egy", "1ehe", "1ehf", "1ehg", "1eup", "1f24", "1f25", "1f26", "1f4t", "1f4u", "1fag", "1fah", "1geb", "1ged", "1gei", "1gej"...
1,517
[ "PUB00033965", "PUB00033966", "PUB00033967", "PUB00033969", "PUB00090178" ]
[ "16042601", "17023115", "15128046", "8637843", "20351109" ]
[ "Biodiversity of cytochrome P450 redox systems.", "Cytochrome P450--redox partner fusion enzymes.", "Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.", "Structural domains of P450-containi...
[ 2005, 2007, 2004, 1995, 2010 ]
5
[]
[ "IPR002397", "IPR002399", "IPR002401", "IPR002402", "IPR002403", "IPR002949", "IPR047146", "IPR050121", "IPR050182", "IPR050364", "IPR050479" ]
0
11
0
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Viruses", "unclassified sequences" ]
[ 862, 100946, 476053, 2, 87, 1334 ]
6
[ "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...
[ 1297, 87, 231, 195, 439, 264, 41, 1161, 358, 3, 2, 1138 ]
12
true
Family
Cytochrome P450
Cytochrome P450
Cyt_P450
7
IPR001129
1,129
Membrane-associated, eicosanoid/glutathione metabolism (MAPEG) protein
Membr-assoc_MAPEG
Family
28,449
false
false
This entry represents a widespread protein family known as MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) [ ]. This group of membrane associated proteins with highly divergent functions, such as the metabolism of eicosanoids [ , ]. Included are: 5-lipoxygenase activating protein (gene FLA...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF01124" ]
[ "MAPEG" ]
[ 28449 ]
1
[ "EC", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.5.1", "GenProp1603", "GenProp1653", "R-BTA-156590", "R-BTA-2142688", "R-BTA-2142691", "R-BTA-2142700", "R-BTA-2162123", "R-BTA-5423646", "R-BTA-9026762", "R-BTA-9026766", "R-CFA-2162123", "R-DDI-156590", "R-DDI-2142688", "R-DDI-2142691", "R-DDI-2142700", "R-DDI-5423646", "R-DDI-...
[ "EC:2.5.1", "GP:GenProp1603", "GP:GenProp1653", "REACTOME:R-BTA-156590", "REACTOME:R-BTA-2142688", "REACTOME:R-BTA-2142691", "REACTOME:R-BTA-2142700", "REACTOME:R-BTA-2162123", "REACTOME:R-BTA-5423646", "REACTOME:R-BTA-9026762", "REACTOME:R-BTA-9026766", "REACTOME:R-CFA-2162123", "REACTOME:R...
49
[ "2h8a", "2pno", "2q7m", "2q7r", "2uuh", "2uui", "3b29", "3dww", "3hkk", "3leo", "3pcv", "4al0", "4al1", "4bpm", "4j7t", "4j7y", "4jc7", "4jcz", "4jrz", "4nta", "4ntb", "4ntf", "4wab", "4yk5", "4yl0", "4yl1", "4yl3", "5bqg", "5bqh", "5bqi", "5hv9", "5i9k"...
50
[ "PUB00005060", "PUB00044025", "PUB00099804", "PUB00099806", "PUB00099807" ]
[ "10091672", "17632548", "31681188", "32745470", "31456794" ]
[ "Common structural features of MAPEG -- a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism.", "Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis.", "From Cyanobacteria to Human, MAPEG-Type G...
[ 1999, 2007, 2019, 2020, 2019 ]
5
[]
[ "IPR001446", "IPR040162" ]
0
2
0
[ "Bacteria", "Eukaryota", "metagenomes", "uncultured Caudovirales phage", "uncultured Poseidoniia archaeon" ]
[ 13400, 14891, 156, 1, 1 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 8, 13, 15, 1, 15, 13, 3, 3, 23, 7 ]
10
true
Family
Membrane-associated, eicosanoid/glutathione metabolism (MAPEG) protein
Membrane-associated, eicosanoid/glutathione metabolism (MAPEG) protein
Membr-assoc_MAPEG
5
IPR001130
1,130
3'-5' ssDNA/RNA exonuclease TatD-like
TatD-like
Family
59,829
false
false
This protein family includes 3'-5' ssDNA/RNA exonuclease TatD and many uncharacterised deoxyribonucleases and metal-dependent hydrolases. The family is related to a large superfamily of metalloenzymes [ ]. TatD has been shown to be a 3'-5' exonuclease that processes single-stranded DNA in DNA repair [ , ]. In E. coli T...
[ "GO:0016788" ]
[ "hydrolase activity, acting on ester bonds" ]
[ "molecular_function" ]
1
[ "PFAM", "PIRSF", "CDD" ]
[ "PF01026", "PIRSF005902", "cd01310" ]
[ "TatD_DNase", "DNase_TatD", "TatD_DNAse" ]
[ 59829, 47312, 49683 ]
3
[ "PROSITEDOC", "REACTOME" ]
[ "PDOC00836", "R-HSA-381038" ]
[ "PROSITEDOC:PDOC00836", "REACTOME:R-HSA-381038" ]
2
[ "1j6o", "1xwy", "1yix", "1zzm", "2gzx", "2xio", "2y1h", "3e2v", "3gg7", "3guw", "3ipw", "3rcm", "4p5u", "4pe8", "6l25", "8efg" ]
16
[ "PUB00004994", "PUB00007123", "PUB00077112", "PUB00100209", "PUB00100210", "PUB00100211", "PUB00100212" ]
[ "9144792", "10747959", "25114049", "31298381", "23187801", "33412752", "33192097" ]
[ "An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.", "TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export.", "Structure and function of TatD exonuclease in DNA repair.", "TATDN1 promotes the devel...
[ 1997, 2000, 2014, 2019, 2012, 2020, 2020 ]
7
[]
[ "IPR011589", "IPR012022", "IPR015991", "IPR024918", "IPR049677" ]
0
5
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1571, 43312, 14075, 7, 864 ]
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",...
[ 22, 6, 21, 4, 3, 21, 14, 2, 8, 17, 2, 2, 73 ]
13
true
Family
3'-5' ssDNA/RNA exonuclease TatD-like
3'-5' ssDNA/RNA exonuclease TatD-like
TatD-like
7
IPR001131
1,131
Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site
Peptidase_M24B_aminopep-P_CS
Conserved_site
32,989
false
false
Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00491" ]
[ "PROLINE_PEPTIDASE" ]
[ 32989 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00417", "R-DDI-163125", "R-HSA-163125", "R-MMU-163125", "R-RNO-163125", "R-SCE-163125", "R-SSC-163125" ]
[ "PROSITEDOC:PDOC00417", "REACTOME:R-DDI-163125", "REACTOME:R-HSA-163125", "REACTOME:R-MMU-163125", "REACTOME:R-RNO-163125", "REACTOME:R-SCE-163125", "REACTOME:R-SSC-163125" ]
7
[ "1a16", "1jaw", "1m35", "1n51", "1pv9", "1w2m", "1w7v", "1wbq", "1wl6", "1wl9", "1wlr", "1wn1", "1wy2", "2bh3", "2bha", "2bhb", "2bhc", "2bhd", "2bn7", "2bws", "2bwt", "2bwu", "2bww", "2bwy", "2how", "2iw2", "2okn", "2v3x", "2v3z", "2zsg", "3ctz", "3l24"...
77
[ "PUB00003579" ]
[ "7674922" ]
[ "Evolutionary families of metallopeptidases." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1274, 23967, 7270, 478 ]
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",...
[ 4, 2, 2, 1, 2, 16, 14, 3, 5, 15, 3, 3, 7 ]
13
true
Conserved_site
Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site
Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site
Peptidase_M24B_aminopep-P_CS
9
IPR001132
1,132
SMAD domain
SMAD_dom
Domain
15,997
false
false
This entry represents the SMAD (Mothers against decapentaplegic (MAD) homologue) (also called MH2 for MAD homology 2) domain found at the C-terminal of MAD related proteins such as Smads. This domain is separated from the MH1 domain by a non-conserved linker region. The MH2 domain mediates interaction with a wide varie...
[ "GO:0006355" ]
[ "regulation of DNA-templated transcription" ]
[ "biological_process" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF03166", "PS51076", "SM00524" ]
[ "MH2", "MH2", "DWB" ]
[ 15874, 15947, 15463 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC51075", "R-BTA-201451", "R-BTA-5689880", "R-BTA-8941326", "R-CEL-1181150", "R-CEL-1502540", "R-CEL-201451", "R-CEL-2173788", "R-CEL-2173789", "R-CEL-2173795", "R-CEL-2173796", "R-CEL-5689880", "R-CEL-8941326", "R-CEL-8941855", "R-CEL-9617828", "R-DME-1181150", "R-DME-1502540", ...
[ "PROSITEDOC:PDOC51075", "REACTOME:R-BTA-201451", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-8941326", "REACTOME:R-CEL-1181150", "REACTOME:R-CEL-1502540", "REACTOME:R-CEL-201451", "REACTOME:R-CEL-2173788", "REACTOME:R-CEL-2173789", "REACTOME:R-CEL-2173795", "REACTOME:R-CEL-2173796", "REACTOME:R-...
99
[ "1dd1", "1dev", "1g88", "1khu", "1khx", "1mjs", "1mk2", "1mr1", "1u7f", "1u7v", "1ygs", "3dit", "3gmj", "4r9p", "5c4v", "5xoc", "5xod", "5zoj", "5zok", "6m64", "6zvq", "7cd1", "7co1" ]
23
[ "PUB00004255", "PUB00004902", "PUB00017916", "PUB00019858", "PUB00097244", "PUB00097273" ]
[ "9230443", "8799132", "14631647", "11532220", "19218245", "17507407" ]
[ "Drosophila Mad binds to DNA and directly mediates activation of vestigial by Decapentaplegic.", "Mammalian dwarfins are phosphorylated in response to transforming growth factor beta and are implicated in control of cell growth.", "Relationship between the DNA binding domains of SMAD and NFI/CTF transcription f...
[ 1997, 1996, 2003, 2001, 2009, 2007 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Human immunodeficiency virus type 1", "bird metagenome" ]
[ 12, 15983, 1, 1 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 16, 27, 15, 43, 26, 43 ]
6
true
Domain
SMAD domain
SMAD domain
SMAD_dom
2
IPR001133
1,133
NADH-ubiquinone oxidoreductase chain 4L/K
NADH_UbQ_OxRdtase_chain4L/K
Family
50,921
false
false
This entry represents NADH:ubiquinone oxidoreductase, chain 4L, as well as NADH-quinone oxidoreductase ( ). In eukaryotes, these enzymes are usually found in either mitochondria or chloroplasts as part of the respiratory-chain NADH dehydrogenase (also known as complex I or NADH-ubiquinone oxidoreductase), an oligomeric...
[ "GO:0016651", "GO:0042773" ]
[ "oxidoreductase activity, acting on NAD(P)H", "ATP synthesis coupled electron transport" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PANTHER" ]
[ "MF_01456", "PTHR11434" ]
[ "NDH1_NuoK", "" ]
[ 33026, 50177 ]
2
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "7.1.1.-", "GenProp0135", "GenProp1198", "GenProp1254", "GenProp1341", "GenProp1537", "GenProp1583", "GenProp1608", "GenProp1751", "R-BTA-5419276", "R-DME-5419276", "R-GGA-5419276", "R-HSA-5419276", "R-MMU-5419276", "R-RNO-5419276", "R-SSC-5419276" ]
[ "EC:7.1.1.-", "GP:GenProp0135", "GP:GenProp1198", "GP:GenProp1254", "GP:GenProp1341", "GP:GenProp1537", "GP:GenProp1583", "GP:GenProp1608", "GP:GenProp1751", "REACTOME:R-BTA-5419276", "REACTOME:R-DME-5419276", "REACTOME:R-GGA-5419276", "REACTOME:R-HSA-5419276", "REACTOME:R-MMU-5419276", ...
16
[ "3rko", "4he8", "4hea", "4wz7", "5gpn", "5gup", "5lc5", "5ldw", "5ldx", "5lnk", "5o31", "5xtc", "5xtd", "5xth", "5xti", "6g2j", "6g72", "6gcs", "6h8k", "6hum", "6i0d", "6i1p", "6khi", "6khj", "6l7o", "6l7p", "6nbq", "6nbx", "6nby", "6q8o", "6q8w", "6q8x"...
300
[ "PUB00005074", "PUB00043559", "PUB00043560", "PUB00043561", "PUB00045437" ]
[ "1470679", "15843018", "18307315", "10940377", "18394423" ]
[ "The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.", "Tracing the evolution of a large protein complex in the eukaryotes, NADH:ubiquinone oxidoreductase (Complex I).", "Production of reactive oxygen species by complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli and comparison to...
[ 1992, 2005, 2008, 2000, 2008 ]
5
[ "IPR039428" ]
[ "IPR053568" ]
1
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 549, 17694, 32161, 517 ]
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" ]
[ 7, 2, 13, 1, 296, 5, 2, 4, 3, 3 ]
10
true
Family
NADH-ubiquinone oxidoreductase chain 4L/K
NADH-ubiquinone oxidoreductase chain 4L/K
NADH_UbQ_OxRdtase_chain4L/K
7
IPR001135
1,135
NADH-quinone oxidoreductase, subunit D
NADH_Q_OxRdtase_suD
Domain
45,225
false
false
This entry represents the subunit D (NuoD) of NADH-quinone oxidoreductase ( ) and the subunit H (NdhH) of NAD(P)H-quinone oxidoreductase ([ec:1.6.5.-]). NADH-quinone (Q) oxidoreductase is a large and complex redox proton pump, which utilises the free energy derived from oxidation of NADH with lipophilic electron/proton...
[ "GO:0016651", "GO:0048038", "GO:0051287" ]
[ "oxidoreductase activity, acting on NAD(P)H", "quinone binding", "NAD binding" ]
[ "molecular_function", "molecular_function", "molecular_function" ]
3
[ "PFAM" ]
[ "PF00346" ]
[ "Complex1_49kDa" ]
[ 45225 ]
1
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "7.1.1.-", "GenProp0135", "R-BTA-611105", "R-BTA-6799198", "R-CEL-6799198", "R-DDI-6799198", "R-HSA-611105", "R-HSA-6799198", "R-MMU-611105", "R-MMU-6799198", "R-RNO-611105", "R-RNO-6799198" ]
[ "EC:7.1.1.-", "GP:GenProp0135", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-6799198", "REACTOME:R-CEL-6799198", "REACTOME:R-DDI-6799198", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-6799198", "REACTOME:R-MMU-611105", "REACTOME:R-MMU-6799198", "REACTOME:R-RNO-611105", "REACTOME:R-RNO-6799198" ]
12
[ "2fug", "2ybb", "3i9v", "3iam", "3ias", "3m9s", "4hea", "4wz7", "5gpn", "5gup", "5lc5", "5ldw", "5ldx", "5lnk", "5o31", "5xtb", "5xtd", "5xth", "5xti", "6cfw", "6g2j", "6g72", "6gcs", "6h8k", "6hum", "6i0d", "6i1p", "6khi", "6khj", "6l7o", "6l7p", "6nbq"...
344
[ "PUB00045442" ]
[ "11695831" ]
[ "The origin of cluster N2 of the energy-transducing NADH-quinone oxidoreductase: comparisons of phylogenetically related enzymes." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1635, 23233, 19509, 848 ]
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",...
[ 9, 2, 2, 3, 3, 19, 4, 1, 9, 5, 5 ]
11
true
Domain
NADH-quinone oxidoreductase, subunit D
NADH-quinone oxidoreductase, subunit D
NADH_Q_OxRdtase_suD
7
IPR001136
1,136
Merozoite surface protein 2
MSA2
Family
1,145
false
false
This entry represents a protein family specific to the genus Plasmodium. The merozoite surface antigen 2 (MSA-2) may play a role in the merozoite attachment to the erythrocyte. This protein was proposed to be a candidate for a protective vaccine against malaria [ , ].
[ "GO:0007155", "GO:0016020" ]
[ "cell adhesion", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PIRSF" ]
[ "PF00985", "PIRSF003575" ]
[ "MSA_2", "MSA_2" ]
[ 1145, 356 ]
2
[]
[]
[]
0
[]
0
[ "PUB00099710", "PUB00099712" ]
[ "23836419", "15661043" ]
[ "Redefining an epitope of a malaria vaccine candidate, with antibodies against the N-terminal MSA-2 antigen of Plasmodium harboring non-natural peptide bonds.", "Herpesvirus saimiri immortalization of Aotus T lymphocytes specific for an immunogenically modified peptide of Plasmodium falciparum merozoite surface a...
[ 2013, 2005 ]
2
[]
[]
0
0
null
[ "Plasmodium" ]
[ 1145 ]
1
[]
[]
0
true
Family
Merozoite surface protein 2
Merozoite surface protein 2
MSA2
3
IPR001137
1,137
Glycoside hydrolase family 11
Glyco_hydro_11
Family
5,963
false
false
Glycoside hydrolase family 11 comprises enzymes with only one known activity, xylanase ( ), involved in the hydrolysis of xylan [ ]. These enzymes were formerly known as cellulase family G. O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, ...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS", "PANTHER" ]
[ "PR00911", "PTHR46828" ]
[ "GLHYDRLASE11", "" ]
[ 5666, 5942 ]
2
[ "CAZY", "EC", "PROSITEDOC" ]
[ "GH11", "3.2.1.8", "PDOC00622" ]
[ "CAZY:GH11", "EC:3.2.1.8", "PROSITEDOC:PDOC00622" ]
3
[ "1axk", "1bcx", "1bk1", "1bvv", "1c5h", "1c5i", "1enx", "1f5j", "1h1a", "1h4g", "1h4h", "1hix", "1hv0", "1hv1", "1igo", "1m4w", "1pvx", "1qh6", "1qh7", "1red", "1ree", "1ref", "1t6g", "1te1", "1ukr", "1xnb", "1xnc", "1xnd", "1xnk", "1xxn", "1xyn", "1xyo"...
194
[ "PUB00004870", "PUB00005266", "PUB00079200" ]
[ "7624375", "8535779", "16844780" ]
[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls." ]
[ 1995, 1995, 2006 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteriales", "unclassified sequences" ]
[ 2120, 3692, 30, 121 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 2 ]
1
true
Family
Glycoside hydrolase family 11
Glycoside hydrolase family 11
Glyco_hydro_11
4
IPR001138
1,138
Zn(2)Cys(6) fungal-type DNA-binding domain
Zn2Cys6_DnaBD
Domain
280,723
false
false
The N-terminal region of a number of fungal transcriptional regulatory proteins contains a Cys-rich motif that is involved in zinc-dependent binding of DNA. The region forms a binuclear Zn cluster, in which two Zn atoms are bound by six Cys residues [ , ]. A wide range of proteins are known to contain this domain. Thes...
[ "GO:0000981", "GO:0008270", "GO:0006355" ]
[ "DNA-binding transcription factor activity, RNA polymerase II-specific", "zinc ion binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PROSITE", "PROFILE", "SMART", "CDD" ]
[ "PF00172", "PS00463", "PS50048", "SM00066", "cd00067" ]
[ "Zn_clus", "ZN2_CY6_FUNGAL_1", "ZN2_CY6_FUNGAL_2", "GAL4", "GAL4" ]
[ 240034, 218494, 252045, 242366, 273837 ]
5
[ "PROSITEDOC" ]
[ "PDOC00378" ]
[ "PROSITEDOC:PDOC00378" ]
1
[ "1ajy", "1aw6", "1cld", "1d66", "1f4s", "1f5e", "1hwt", "1pyc", "1pyi", "1qp9", "1zme", "2alc", "2er8", "2ere", "2erg", "2hap", "3alc", "3coq", "6e33", "6f07", "6gyp", "6gys", "6gyu", "6k15", "6kw3", "6kw4", "6kw5", "6o19", "6p7v", "6p7w", "6p7x", "6v8o"...
38
[ "PUB00004117", "PUB00004702", "PUB00022897", "PUB00030043", "PUB00036683" ]
[ "1557122", "2107541", "9303004", "7958913", "11566132" ]
[ "DNA recognition by GAL4: structure of a protein-DNA complex.", "GAL4 transcription factor is not a \"zinc finger\" but forms a Zn(II)2Cys6 binuclear cluster.", "Crystal structure of a PUT3-DNA complex reveals a novel mechanism for DNA recognition by a protein containing a Zn2Cys6 binuclear cluster.", "Crysta...
[ 1992, 1990, 1997, 1994, 2001 ]
5
[]
[ "IPR020448" ]
0
1
0
[ "Bacteria", "Eukaryota", "Natrinema zhouii", "marine sediment metagenome" ]
[ 5, 280716, 1, 1 ]
4
[ "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)" ]
[ 133, 55, 32 ]
3
true
Domain
Zn(2)Cys(6) fungal-type DNA-binding domain
Zn(2)Cys(6) fungal-type DNA-binding domain
Zn2Cys6_DnaBD
4
IPR001139
1,139
Glycoside hydrolase family 30
Glyco_hydro_30
Family
15,273
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:0004348", "GO:0006665" ]
[ "glucosylceramidase activity", "sphingolipid metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS", "PANTHER" ]
[ "PR00843", "PTHR11069" ]
[ "GLHYDRLASE30", "" ]
[ 9107, 15253 ]
2
[ "CAZY", "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GH30", "3.2.1", "3.2.1.45", "R-CEL-9840310", "R-HSA-390471", "R-HSA-9840310", "R-MMU-9840310" ]
[ "CAZY:GH30", "EC:3.2.1", "EC:3.2.1.45", "REACTOME:R-CEL-9840310", "REACTOME:R-HSA-390471", "REACTOME:R-HSA-9840310", "REACTOME:R-MMU-9840310" ]
7
[ "1nof", "1ogs", "1y7v", "2f61", "2j25", "2nsx", "2nt0", "2nt1", "2v3d", "2v3e", "2v3f", "2vt0", "2wcg", "2wkl", "2wnw", "2xwd", "2xwe", "2y24", "3gtn", "3gxd", "3gxf", "3gxi", "3gxm", "3ke0", "3keh", "3kl0", "3kl3", "3kl5", "3rik", "3ril", "4ckq", "4fmv"...
91
[ "PUB00000001", "PUB00004615", "PUB00004870", "PUB00005266" ]
[ "9316290", "3456607", "7624375", "8535779" ]
[ "Differences in origin of the 1448C mutation in patients with Gaucher disease.", "Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site.", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Stru...
[ 1997, 1986, 1995, 1995 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 7377, 7838, 58 ]
3
[ "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" ]
[ 4, 2, 5, 20, 2, 1, 3 ]
7
true
Family
Glycoside hydrolase family 30
Glycoside hydrolase family 30
Glyco_hydro_30
5
IPR001141
1,141
Large ribosomal subunit protein eL27
Ribosomal_eL27
Family
5,872
false
false
Large ribosomal subunit protein eL27 is found in fungi, plants, algae and vertebrates [ , ]. The family has a specific signature at the C terminus. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This l...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER" ]
[ "PF01777", "PTHR10497" ]
[ "Ribosomal_L27e", "" ]
[ 5792, 5674 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00851", "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72706",...
[ "PROSITEDOC:PDOC00851", "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...
76
[ "3j6x", "3j6y", "3j77", "3j78", "3j79", "3j7o", "3j7p", "3j7q", "3j7r", "3j92", "3jag", "3jah", "3jai", "3jaj", "3jan", "3jbn", "3jbo", "3jbp", "3jcs", "3jct", "4d5y", "4d67", "4u3m", "4u3n", "4u3u", "4u4n", "4u4o", "4u4q", "4u4r", "4u4u", "4u4y", "4u4z"...
550
[ "PUB00000666", "PUB00004579", "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "8148381", "8058833", "11297922", "11290319", "11114498" ]
[ "Cloning and nucleotide sequence of a full length cDNA encoding ribosomal protein L27 from human fetal kidney.", "Nucleotide sequence of a cDNA clone for a 60S ribosomal protein L27 gene from potato (Solanum tuberosum L.).", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The ...
[ 1994, 1994, 2001, 2001, 2000 ]
5
[]
[]
0
0
null
[ "Eukaryota", "Gammaproteobacteria", "Picornavirales sp." ]
[ 5869, 2, 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...
[ 11, 1, 2, 1, 5, 4, 1, 4, 11, 2, 2, 10 ]
12
true
Family
Large ribosomal subunit protein eL27
Large ribosomal subunit protein eL27
Ribosomal_eL27
8
IPR001142
1,142
Yeast membrane protein DUP/COS
DUP/COS
Family
543
false
false
A number of uncharacterised integral membrane proteins from yeast contain an internal duplication due to duplicated genes. Duplicated copies of genes may be classified in two types of cluster organisation. The first type includes genes sharing a significant level of identity in the amino acid sequences of their predict...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00674" ]
[ "DUP" ]
[ 543 ]
1
[]
[]
[]
0
[]
0
[ "PUB00006379" ]
[ "9234674" ]
[ "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Marinifilum caeruleilacunae", "Saccharomycetaceae" ]
[ 1, 542 ]
2
[ "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 25 ]
1
true
Family
Yeast membrane protein DUP/COS
Yeast membrane protein DUP/COS
DUP/COS
7
IPR001144
1,144
Heat-labile enterotoxin, A chain
Enterotoxin_A
Family
1,016
false
false
Escherichia coli heat-labile enterotoxin is a bacterial protein toxin with an AB5 multimer structure, in which the B pentamer ( ) has a membrane-binding function and the A chain is needed for enzymatic activity [ ]. The B subunits are arranged as a donut-shaped pentamer, each subunit participating in ~30 hydrogen bonds...
[ "GO:0090729", "GO:0005615" ]
[ "toxin activity", "extracellular space" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PRINTS" ]
[ "PF01375", "PR00771" ]
[ "Enterotoxin_a", "ENTEROTOXINA" ]
[ 1014, 466 ]
2
[ "REACTOME" ]
[ "R-HSA-9760173" ]
[ "REACTOME:R-HSA-9760173" ]
1
[ "1htl", "1lt3", "1lt4", "1lta", "1ltb", "1ltg", "1lti", "1lts", "1ltt", "1s5b", "1s5c", "1s5d", "1s5e", "1s5f", "1tii", "1xtc", "2a5d", "2a5f", "2a5g", "8oxs", "8q6i", "8qre" ]
22
[ "PUB00003304" ]
[ "8478941" ]
[ "Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin." ]
[ 1993 ]
1
[]
[]
0
0
null
[ "Affertcholeramvirus", "Bacteria", "Eukaryota" ]
[ 7, 249, 760 ]
3
[]
[]
0
true
Family
Heat-labile enterotoxin, A chain
Heat-labile enterotoxin, A chain
Enterotoxin_A
1
IPR001146
1,146
Geminivirus AL1 replication-associated protein, MSV type
Gemini_AL1_MSV
Family
1,184
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:0042025" ]
[ "host cell nucleus" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR00229" ]
[ "GEMCOATMSVL1" ]
[ 1184 ]
1
[ "EC" ]
[ "3.1.21.-" ]
[ "EC:3.1.21.-" ]
1
[]
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
[ "IPR001191" ]
[]
1
0
1
[ "Mastrevirus", "Ziziphus jujuba var. spinosa" ]
[ 1182, 2 ]
2
[]
[]
0
true
Family
Geminivirus AL1 replication-associated protein, MSV type
Geminivirus AL1 replication-associated protein, MSV type
Gemini_AL1_MSV
2
IPR001147
1,147
Large ribosomal subunit protein eL21
Ribosomal_eL21
Family
8,206
false
false
The eL21 family contains proteins from a number of eukaryotic and archaebacterial organisms which include mammalian eL21, Entamoeba histolytica eL21, Caenorhabditis elegans eL21 (C14B9.7), Saccharomyces cerevisiae (Baker's yeast) eL21 (URP1) and Haloarcula marismortui eL21 (HL31). Ribosomes are the particles that catal...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER" ]
[ "PF01157", "PTHR20981" ]
[ "Ribosomal_L21e", "" ]
[ 8069, 7753 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00901", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72706", "R-DDI-975956", "R-DDI-975957", "R-HSA-156827", "R-HSA-156902", "R-HSA-1799339", "R-HSA-192823", "R-HSA-2408557...
[ "PROSITEDOC:PDOC00901", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-975956", "REACTOME:R-CEL-975957", "REACTOME:R-DDI-156827", "REACTOME:R-DDI-1799339", "REACTOME:R-DDI-72689", "REACTOME:R-DDI-72706", "REACTOME:R-DDI-975956...
52
[ "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"...
661
[ "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "11297922", "11290319", "11114498" ]
[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]
[ 2001, 2001, 2000 ]
3
[]
[ "IPR022856" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 907, 3, 7262, 34 ]
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...
[ 12, 1, 1, 1, 7, 2, 1, 7, 24, 2, 2, 19 ]
12
true
Family
Large ribosomal subunit protein eL21
Large ribosomal subunit protein eL21
Ribosomal_eL21
9
IPR001148
1,148
Alpha carbonic anhydrase domain
CA_dom
Domain
41,398
false
false
This entry represents a domain characteristic of alpha class carbonic anhydrases. The dominating secondary structure is a 10-stranded, twisted β-sheet, which divides the molecules into two halves [ ]. Alpha-CAs contain a single zinc atom bound to three conserved histidine residues. The catalytically active group is the...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00194", "PS51144", "SM01057" ]
[ "Carb_anhydrase", "ALPHA_CA_2", "Carb_anhydrase" ]
[ 40984, 41094, 38840 ]
3
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REAC...
[ "4.2.1.1", "PWY-241", "PWY-5743", "PWY-5744", "PWY-5789", "PWY-6142", "PWY-7115", "PWY-7117", "PDOC00146", "R-BTA-1237044", "R-BTA-1247673", "R-BTA-1475029", "R-CEL-1237044", "R-CEL-1247673", "R-CEL-1475029", "R-DRE-1237044", "R-DRE-1247673", "R-DRE-1475029", "R-GGA-1237044", "...
[ "EC:4.2.1.1", "METACYC:PWY-241", "METACYC:PWY-5743", "METACYC:PWY-5744", "METACYC:PWY-5789", "METACYC:PWY-6142", "METACYC:PWY-7115", "METACYC:PWY-7117", "PROSITEDOC:PDOC00146", "REACTOME:R-BTA-1237044", "REACTOME:R-BTA-1247673", "REACTOME:R-BTA-1475029", "REACTOME:R-CEL-1237044", "REACTOME...
40
[ "12ca", "1a42", "1am6", "1avn", "1azm", "1bcd", "1bic", "1bn1", "1bn3", "1bn4", "1bnm", "1bnn", "1bnq", "1bnt", "1bnu", "1bnv", "1bnw", "1bv3", "1bzm", "1ca2", "1ca3", "1cah", "1cai", "1caj", "1cak", "1cal", "1cam", "1can", "1cao", "1cay", "1caz", "1ccs"...
1,443
[ "PUB00017888", "PUB00017891", "PUB00017892", "PUB00044806", "PUB00044807", "PUB00088695" ]
[ "8673298", "9336012", "11493685", "18336305", "10978542", "8382771" ]
[ "Functional diversity, conservation, and convergence in the evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene families.", "Structure and mechanism of carbonic anhydrase.", "Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpre...
[ 1996, 1997, 2001, 2008, 2000, 1993 ]
6
[]
[ "IPR041887" ]
0
1
0
[ "Bacteria", "Eukaryota", "Viruses", "candidate division MSBL1 archaeon SCGC-AAA385M02", "metagenomes" ]
[ 4205, 36970, 121, 1, 101 ]
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", "Zea mays" ]
[ 36, 8, 69, 26, 74, 58, 1, 38, 79, 42 ]
10
true
Domain
Alpha carbonic anhydrase domain
Alpha carbonic anhydrase domain
CA_dom
8
IPR001150
1,150
Glycine radical domain
Gly_radical
Domain
23,524
false
false
Glycyl radical enzymes are involved in a great variety of functions, including nucleotide, pyruvate and toluene metabolism [ ]. A glycyl radical is formed by the removal of a hydrogen from a glycine and the resulting radical is located on the protein main chain. Escherichia coli formate C-acetyltransferase ( ) is a key...
[ "GO:0003824" ]
[ "catalytic activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF01228", "PS51149" ]
[ "Gly_radical", "GLY_RADICAL_2" ]
[ 18210, 23421 ]
2
[ "PROSITEDOC" ]
[ "PDOC00665" ]
[ "PROSITEDOC:PDOC00665" ]
1
[ "1cm5", "1h16", "1h17", "1h18", "1h78", "1h79", "1h7a", "1h7b", "1hk8", "1mzo", "1r8w", "1r9d", "2f3o", "2pfl", "2y8n", "2yaj", "3pfl", "4mtj", "4pkc", "4pkf", "5a0u", "5a0z", "5bwd", "5bwe", "5fau", "5fav", "5faw", "5fay", "5i2a", "5i2g", "5kdp", "5ymr"...
58
[ "PUB00004806", "PUB00004820", "PUB00014425", "PUB00033790", "PUB00057234" ]
[ "1310545", "8421692", "11444864", "10574800", "8702830" ]
[ "The free radical in pyruvate formate-lyase is located on glycine-734.", "A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene.", "YfiD of Escherichia coli and Y06I of bacteriophage T4 as autonomous glycyl radical cofactors reconstit...
[ 1992, 1993, 2001, 1999, 1996 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 39, 21918, 295, 1022, 250 ]
5
[ "Escherichia coli (strain K12)" ]
[ 6 ]
1
true
Domain
Glycine radical domain
Glycine radical domain
Gly_radical
9
IPR001151
1,151
G protein-coupled receptor 6
GPR6
Family
584
false
false
G protein-coupled receptor 12 (GPR12) was initially isolated from a rat pituitary library, and is found in discrete regions of the brain, pituitary and testis, but is absent in other tissues [ , ]. Three human homologues (GPR12, GPR6 and GPR3) have also been isolated [ ]. The 3 genes have been localised to human chromo...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR00649" ]
[ "GPR6ORPHANR" ]
[ 584 ]
1
[]
[]
[]
0
[ "8t1v", "8t1w", "8tf5", "8tyw" ]
4
[ "PUB00001626", "PUB00001967" ]
[ "1840531", "8530049" ]
[ "Cloning, sequencing and tissue distribution of a candidate G protein-coupled receptor from rat pituitary gland.", "Molecular cloning and chromosomal localization of human genes encoding three closely related G protein-coupled receptors." ]
[ 1991, 1995 ]
2
[ "IPR000723" ]
[]
1
0
1
[ "Bacteria", "Eukaryota" ]
[ 3, 581 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 4, 2, 2 ]
4
true
Family
G protein-coupled receptor 6
G protein-coupled receptor 6
GPR6
4
IPR001152
1,152
Beta-thymosin
Beta-thymosin
Family
3,353
false
false
This entry represents beta-thymosin family. Its members include thymosin beta-4, -10, -15 from humans and their homologues (such as thymosin beta 11/12) from fish. Thymosin beta-4 (Tbeta) is a small protein that sequesters actin monomers to help maintain the high concentrations of unpolymerised actin in higher eukaryot...
[ "GO:0003785", "GO:0007015" ]
[ "actin monomer binding", "actin filament organization" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "PROSITE", "PANTHER", "SMART" ]
[ "PF01290", "PIRSF001828", "PS00500", "PTHR12021", "SM00152" ]
[ "Thymosin", "Thymosin_beta", "THYMOSIN_B4", "", "THY" ]
[ 3345, 1290, 1901, 2296, 3193 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00433", "R-HSA-114608", "R-MMU-114608", "R-SSC-114608" ]
[ "PROSITEDOC:PDOC00433", "REACTOME:R-HSA-114608", "REACTOME:R-MMU-114608", "REACTOME:R-SSC-114608" ]
4
[ "1hj0", "1t44", "3m3n", "3sjh", "3tu5", "3u8x", "3u9d", "3u9z", "4pl7", "4pl8" ]
10
[ "PUB00072891", "PUB00072893", "PUB00072894", "PUB00072895", "PUB00072896", "PUB00072897", "PUB00072898", "PUB00072899", "PUB00072900", "PUB00072901", "PUB00072902" ]
[ "25313062", "15037574", "18306930", "20637781", "18272284", "22328534", "12761500", "24732964", "24993983", "17567946", "24053380" ]
[ "Structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization.", "Thymosin-beta4 inhibits corneal epithelial cell apoptosis after ethanol exposure in vitro.", "Actin-sequestering protein, thymosin-beta-4 (TB4), inhibits caspase-3 activation in paclitaxel-induced tumor cell death.",...
[ 2014, 2004, 2007, 2010, 2008, 2012, 2003, 2014, 2014, 2007, 2013 ]
11
[]
[]
0
0
null
[ "Bacillati", "Eukaryota" ]
[ 2, 3351 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 5, 3, 14, 10, 15 ]
6
true
Family
Beta-thymosin
Beta-thymosin
Beta-thymosin
6
IPR001153
1,153
Barwin domain
Barwin_dom
Domain
2,189
false
false
Barwin is a basic protein isolated from aqueous extracts of barley seeds. It is 125 amino acids in length, and contains six cysteine residues that combine to form three disulphide bridges [ , ]. Comparative analysis shows the sequence to be highly similar to a 122 amino acid stretch in the C-terminal of the products of...
[ "GO:0042742", "GO:0050832" ]
[ "defense response to bacterium", "defense response to fungus" ]
[ "biological_process", "biological_process" ]
2
[ "PFAM", "PRINTS", "PROFILE" ]
[ "PF00967", "PR00602", "PS51174" ]
[ "Barwin", "BARWIN", "BARWIN_3" ]
[ 2133, 1626, 1791 ]
3
[ "PROSITEDOC" ]
[ "PDOC00619" ]
[ "PROSITEDOC:PDOC00619" ]
1
[ "1bw3", "1bw4", "4jp6", "4jp7", "7ksn" ]
5
[ "PUB00000371", "PUB00000372" ]
[ "1390663", "1390664" ]
[ "Primary structure of barwin: a barley seed protein closely related to the C-terminal domain of proteins encoded by wound-induced plant genes.", "Secondary structure in solution of barwin from barley seed using 1H nuclear magnetic resonance spectroscopy." ]
[ 1992, 1992 ]
2
[]
[]
0
0
null
[ "Bacteria", "Chlorovirus", "Eukaryota" ]
[ 51, 6, 2132 ]
3
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 14, 15 ]
3
true
Domain
Barwin domain
Barwin domain
Barwin_dom
6
IPR001154
1,154
DNA topoisomerase II, eukaryotic-type
TopoII_euk
Family
9,850
false
false
This entry represents DNA topoisomerase II enzymes from eukaryotes and viruses. Topoisomerase II primarily functions in introducing negative supercoils into DNA, and is of particular importance during the segregation of chromosomes during mitosis [ , ]. In eukaryotes and viruses, this enzyme occurs as a single polypept...
[ "GO:0003677", "GO:0003918", "GO:0005524", "GO:0006265" ]
[ "DNA binding", "DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity", "ATP binding", "DNA topological change" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PRINTS" ]
[ "PR01158" ]
[ "TOPISMRASEII" ]
[ 9850 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "5.6.2.2", "R-CEL-4615885", "R-DDI-4615885", "R-DME-4615885", "R-HSA-1362277", "R-HSA-4615885", "R-MMU-4615885", "R-RNO-4615885", "R-SCE-4615885", "R-SPO-4615885", "R-SSC-4615885" ]
[ "EC:5.6.2.2", "REACTOME:R-CEL-4615885", "REACTOME:R-DDI-4615885", "REACTOME:R-DME-4615885", "REACTOME:R-HSA-1362277", "REACTOME:R-HSA-4615885", "REACTOME:R-MMU-4615885", "REACTOME:R-RNO-4615885", "REACTOME:R-SCE-4615885", "REACTOME:R-SPO-4615885", "REACTOME:R-SSC-4615885" ]
11
[ "1bgw", "1bjt", "2rgr", "3l4j", "3l4k", "3qx3", "4fm9", "4g0u", "4g0v", "4g0w", "4gfh", "4j3n", "5gwi", "5gwj", "5gwk", "5zad", "5zen", "5zqf", "5zrf", "6ca8", "6zy5", "6zy6", "6zy7", "6zy8", "7yq8", "8gcc", "8j87", "8j88", "8j89", "8j8a", "8j8b", "8j8c"...
61
[ "PUB00004227", "PUB00005437", "PUB00016842", "PUB00020793", "PUB00020794", "PUB00020795", "PUB00020806", "PUB00020807", "PUB00020808" ]
[ "8538787", "7770916", "11395412", "12596227", "12042765", "7980433", "15289664", "9631649", "14996935" ]
[ "Structure and mechanism of DNA topoisomerase II.", "The mechanisms of DNA topoisomerases.", "DNA topoisomerases: structure, function, and mechanism.", "Phylogenomics of type II DNA topoisomerases.", "Cellular roles of DNA topoisomerases: a molecular perspective.", "Structure and function of type II DNA t...
[ 1996, 1995, 2001, 2003, 2002, 1994, 2004, 1998, 2004 ]
9
[ "IPR001241" ]
[]
1
0
1
[ "Escherichia coli", "Eukaryota", "Viruses", "metagenomes" ]
[ 1, 9070, 508, 271 ]
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...
[ 5, 4, 5, 1, 10, 6, 2, 5, 8, 1, 1, 61 ]
12
true
Family
DNA topoisomerase II, eukaryotic-type
DNA topoisomerase II, eukaryotic-type
TopoII_euk
7
IPR001155
1,155
NADH:flavin oxidoreductase/NADH oxidase, N-terminal
OxRdtase_FMN_N
Domain
97,389
false
false
The TIM-barrel fold is a closed barrel structure composed of an eight-fold repeat of β-α units, where the eight parallel β strands on the inside are covered by the eight α helices on the outside [ ]. It is a widely distributed fold which has been found in many enzyme families that catalyse completely unrelated reaction...
[ "GO:0010181", "GO:0016491" ]
[ "FMN binding", "oxidoreductase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF00724" ]
[ "Oxidored_FMN" ]
[ 97389 ]
1
[]
[]
[]
0
[ "1bwk", "1bwl", "1djn", "1djq", "1gvo", "1gvq", "1gvr", "1gvs", "1gwj", "1h50", "1h51", "1h60", "1h61", "1h62", "1h63", "1icp", "1icq", "1ics", "1k02", "1k03", "1o94", "1o95", "1oya", "1oyb", "1oyc", "1ps9", "1q45", "1vji", "1vyp", "1vyr", "1vys", "1z41"...
247
[ "PUB00027645", "PUB00027646" ]
[ "11257493", "12206759" ]
[ "The TIM-barrel fold: a versatile framework for efficient enzymes.", "One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions." ]
[ 2001, 2002 ]
2
[]
[ "IPR037348", "IPR054629" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 955, 72181, 23239, 1014 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "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 / AT...
[ 24, 8, 2, 3, 27, 2, 3, 38 ]
8
true
Domain
NADH:flavin oxidoreductase/NADH oxidase, N-terminal
NADH:flavin oxidoreductase/NADH oxidase, N-terminal
OxRdtase_FMN_N
5
IPR001157
1,157
Non-structural protein NS1, flavivirus
Flavi_NS1
Domain
14,362
false
false
The Flavivirus genome polypepetide contains the capsid protein C (core protein), the matrix protein (envelope protein M), the major envelope protein E, a number of small non structural proteins (NS1, NS2A, NS2B, NS4A and NS4B), helicase and RNA-directed polymerase (NS5) [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF00948" ]
[ "Flavi_NS1" ]
[ 14362 ]
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
[ "4o6b", "4o6c", "4o6d", "4oie", "4oig", "4oii", "4tpl", "5gs6", "5iy3", "5k6k", "5o19", "5o36", "5x8y", "5yxa", "6weq", "6wer", "7bsc", "7bsd", "7k93", "7wur", "7wus", "7wut", "7wuu", "7wuv", "8cxg", "8cxh", "8cxi", "8jkf", "8jkh", "8jqm", "8jqn", "8jqs"...
46
[ "PUB00003540" ]
[ "9371625" ]
[ "trans-Complementation of yellow fever virus NS1 reveals a role in early RNA replication." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Bacteria", "Orthornavirae", "Pancrustacea" ]
[ 2, 14355, 5 ]
3
[]
[]
0
true
Domain
Non-structural protein NS1, flavivirus
Non-structural protein NS1, flavivirus
Flavi_NS1
4
IPR001158
1,158
DIX domain
DIX
Domain
10,020
false
false
Proteins of the dishevelled family (Dsh and Dvl) play a key role in the transduction of the Wg/Wnt signal from the cell surface to the nucleus: in response to Wnt signal, they block the degradation of beta- catenin by interacting with the scaffolding protein axin. The N terminus of proteins of the dishevelled family an...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00778", "PS50841", "SM00021" ]
[ "DIX", "DIX", "DAX" ]
[ 9688, 9737, 8649 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50841", "R-CEL-195253", "R-CEL-196299", "R-CEL-201688", "R-CEL-2028269", "R-CEL-4086400", "R-CEL-4641258", "R-CEL-4641262", "R-CEL-5099900", "R-CEL-5663220", "R-CEL-8856825", "R-CEL-8856828", "R-DME-195253", "R-DME-196299", "R-DME-201688", "R-DME-209155", "R-DME-209190", "R-DM...
[ "PROSITEDOC:PDOC50841", "REACTOME:R-CEL-195253", "REACTOME:R-CEL-196299", "REACTOME:R-CEL-201688", "REACTOME:R-CEL-2028269", "REACTOME:R-CEL-4086400", "REACTOME:R-CEL-4641258", "REACTOME:R-CEL-4641262", "REACTOME:R-CEL-5099900", "REACTOME:R-CEL-5663220", "REACTOME:R-CEL-8856825", "REACTOME:R-C...
100
[ "1wsp", "2d5g", "3pz7", "3pz8", "4wip", "5y3b", "5y3c", "6iw3", "6jck", "6vcc", "8wm9", "8wma" ]
12
[ "PUB00001930", "PUB00003043", "PUB00003709", "PUB00018315", "PUB00018316", "PUB00018317", "PUB00060611" ]
[ "9407023", "10318824", "10330181", "11041490", "11027605", "12384700", "15857680" ]
[ "Wnt signaling: a common theme in animal development.", "Functional domains of axin. Importance of the C terminus as an oligomerization domain.", "DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability.", "Effects of rat Axin domains on axis for...
[ 1997, 1999, 1999, 2000, 2000, 2002, 2005 ]
7
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "ecological metagenomes" ]
[ 26, 9981, 11, 2 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 39, 10, 27, 16, 25 ]
6
true
Domain
DIX domain
DIX domain
DIX
1
IPR001160
1,160
Peptidase M20C, Xaa-His dipeptidase
Peptidase_M20C
Family
9,158
false
false
This majority of this group of proteins are aminoacyl-histidine dipeptidases (Xaa-His dipeptidases, cytosol non-specific dipeptidases, peptidase D), which are zinc-containing metallopeptidases that belong to MEROPS peptidase family M20 (clan MH), subfamily M20C [ ]. Proteins of this clan have two catalytic zinc ions at...
[ "GO:0006508" ]
[ "proteolysis" ]
[ "biological_process" ]
1
[ "PIRSF", "PRINTS", "PANTHER", "NCBIFAM", "CDD" ]
[ "PIRSF016599", "PR00934", "PTHR43501", "TIGR01893", "cd03890" ]
[ "Xaa-His_dipept", "XHISDIPTASE", "", "aa-his-dipept", "M20_pepD" ]
[ 7990, 8919, 9018, 8058, 7319 ]
5
[ "GP" ]
[ "GenProp1242" ]
[ "GP:GenProp1242" ]
1
[ "2qyv", "3mru" ]
2
[ "PUB00002117", "PUB00003579" ]
[ "1695895", "7674922" ]
[ "Peptidase D gene (pepD) of Escherichia coli K-12: nucleotide sequence, transcript mapping, and comparison with other peptidase genes.", "Evolutionary families of metallopeptidases." ]
[ 1990, 1995 ]
2
[ "IPR002933" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Myoviridae sp. ctTrm2", "unclassified sequences" ]
[ 79, 8570, 295, 1, 213 ]
5
[ "Escherichia coli (strain K12)", "Zea mays" ]
[ 1, 1 ]
2
true
Family
Peptidase M20C, Xaa-His dipeptidase
Peptidase M20C, Xaa-His dipeptidase
Peptidase_M20C
2
IPR001161
1,161
Helicase XPB/Ssl2
XPB/Ssl2
Family
4,883
false
false
XPB, also known as Ssl2, Ercc3, RepB, Rad25 or haywire, is a core subunit of the eukaryotic basal transcription factor complex TFIIH, which plays a dual role in transcription and DNA repair [ ]. It is involved in nucleotide excision repair of DNA and in RNA transcription by RNA polymerase II [ ]. TFIIH is a multiprotei...
[ "GO:0003678", "GO:0006289", "GO:0006367" ]
[ "DNA helicase activity", "nucleotide-excision repair", "transcription initiation at RNA polymerase II promoter" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "NCBIFAM" ]
[ "TIGR00603" ]
[ "rad25" ]
[ 4883 ]
1
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "5.6.2.4", "GenProp2048", "R-BTA-113418", "R-BTA-5696395", "R-BTA-5696400", "R-BTA-674695", "R-BTA-6781823", "R-BTA-6782135", "R-BTA-6782210", "R-BTA-6796648", "R-BTA-72086", "R-BTA-73762", "R-BTA-73772", "R-BTA-73776", "R-BTA-73779", "R-BTA-73863", "R-BTA-75953", "R-BTA-75955", ...
[ "EC:5.6.2.4", "GP:GenProp2048", "REACTOME:R-BTA-113418", "REACTOME:R-BTA-5696395", "REACTOME:R-BTA-5696400", "REACTOME:R-BTA-674695", "REACTOME:R-BTA-6781823", "REACTOME:R-BTA-6782135", "REACTOME:R-BTA-6782210", "REACTOME:R-BTA-6796648", "REACTOME:R-BTA-72086", "REACTOME:R-BTA-73762", "REACT...
154
[ "4ern", "5fmf", "5ivw", "5iy6", "5iy7", "5iy8", "5iy9", "5of4", "5oqj", "5oqm", "5sva", "6gym", "6nmi", "6o9l", "6o9m", "6ro4", "7ad8", "7egb", "7egc", "7ena", "7enc", "7k01", "7k04", "7lbm", "7m2u", "7ml0", "7ml1", "7ml2", "7ml3", "7ml4", "7nvr", "7nvv"...
72
[ "PUB00000019", "PUB00057247", "PUB00062805", "PUB00062808", "PUB00062809", "PUB00062813", "PUB00076972", "PUB00160831" ]
[ "8304337", "14534314", "10024882", "16947863", "9012405", "21592869", "25641424", "17259543" ]
[ "Clinical heterogeneity within xeroderma pigmentosum associated with mutations in the DNA repair and transcription gene ERCC3.", "Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent transcription in vitro.", "Reconstitution of the transcription factor TFIIH: assignment of functions for the...
[ 1994, 2003, 1999, 2006, 1997, 2011, 2015, 2007 ]
8
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 4, 4879 ]
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...
[ 9, 1, 2, 2, 9, 4, 1, 4, 4, 1, 1, 10 ]
12
true
Family
Helicase XPB/Ssl2
Helicase XPB/Ssl2
XPB/Ssl2
2
IPR001162
1,162
UvrC, RNAse H endonuclease domain
UvrC_RNase_H_dom
Domain
28,669
false
false
This entry represents the RNAse H endonuclease domain, located at the C-terminal, between the UvrBC and the (HhH)2 domains, nearby the N-terminal of the HhH. Despite the lack of sequence homology, the endonuclease domain has an RNase H-like fold, which is characteristic of enzymes with nuclease or polynucleotide transf...
[ "GO:0009381" ]
[ "excinuclease ABC activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PFAM", "PROFILE" ]
[ "PF08459", "PF22920", "PS50165" ]
[ "UvrC_RNaseH_dom", "UvrC_RNaseH", "UVRC" ]
[ 27873, 26382, 28410 ]
3
[ "PROSITEDOC" ]
[ "PDOC50164" ]
[ "PROSITEDOC:PDOC50164" ]
1
[ "2nrr", "2nrt", "2nrv", "2nrw", "2nrx", "2nrz", "3c65", "8b0q" ]
8
[ "PUB00042023" ]
[ "17245438" ]
[ "Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad." ]
[ 2007 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 617, 26976, 326, 750 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
UvrC, RNAse H endonuclease domain
UvrC, RNAse H endonuclease domain
UvrC_RNase_H_dom
7
IPR001163
1,163
Sm domain, eukaryotic/archaea-type
Sm_dom_euk/arc
Domain
74,250
false
false
This domain is found in Lsm (like-Sm) proteins, which have a core structure consisting of an open β-barrel with an SH3-like topology. Lsm (like-Sm) proteins have diverse functions, and are thought to be important modulators of RNA biogenesis and function [ , ]. The Sm proteins form part of specific small nuclear ribonu...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF01423", "SM00651" ]
[ "LSM", "Sm" ]
[ 73324, 70941 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-111367", "R-BTA-191859", "R-BTA-430039", "R-BTA-72163", "R-BTA-72165", "R-BTA-73856", "R-BTA-77588", "R-CEL-111367", "R-CEL-191859", "R-CEL-430039", "R-CEL-72163", "R-CEL-72165", "R-CEL-73856", "R-CEL-77588", "R-DDI-111367", "R-DDI-430039", "R-DDI-72163", "R-DDI-73856", "R...
[ "REACTOME:R-BTA-111367", "REACTOME:R-BTA-191859", "REACTOME:R-BTA-430039", "REACTOME:R-BTA-72163", "REACTOME:R-BTA-72165", "REACTOME:R-BTA-73856", "REACTOME:R-BTA-77588", "REACTOME:R-CEL-111367", "REACTOME:R-CEL-191859", "REACTOME:R-CEL-430039", "REACTOME:R-CEL-72163", "REACTOME:R-CEL-72165", ...
57
[ "1b34", "1d3b", "1h64", "1i4k", "1i5l", "1i81", "1i8f", "1jbm", "1jri", "1ljo", "1lnx", "1loj", "1m5q", "1m8v", "1mgq", "1n9r", "1n9s", "1th7", "3bw1", "3cw1", "3jb9", "3jcm", "3jcr", "3pgg", "3pgw", "3swn", "4c8q", "4c92", "4emg", "4emh", "4emk", "4f7u"...
176
[ "PUB00001270", "PUB00016606", "PUB00016607", "PUB00016608", "PUB00016613", "PUB00058144" ]
[ "7744013", "10801455", "12438310", "15130578", "11399068", "20826804" ]
[ "snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions.", "Functions of Lsm proteins in mRNA degradation and splicing.", "Lsm Proteins are required for normal processing and stability of ribosomal RNAs.", "Why do cells need an assembly machi...
[ 1995, 2000, 2003, 2004, 2001, 2010 ]
6
[ "IPR047575" ]
[ "IPR033871", "IPR034101", "IPR034102", "IPR034103", "IPR034104", "IPR034105", "IPR034109", "IPR034110" ]
1
8
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1436, 21, 72717, 76 ]
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...
[ 90, 19, 22, 37, 59, 49, 18, 59, 80, 16, 16, 126 ]
12
true
Domain
Sm domain, eukaryotic/archaea-type
Sm domain, eukaryotic/archaea-type
Sm_dom_euk/arc
4
IPR001164
1,164
Arf GTPase activating protein
ArfGAP_dom
Domain
68,703
false
false
Proteins containing this domain include ARF1-directed GTPase-activating protein, the cycle control GTPase activating protein (GAP) GCS1 which is important for the regulation of the ADP ribosylation factor ARF, a member of the Ras superfamily of GTP-binding proteins [ ]. The GTP-bound form of ARF is essential for the ma...
[ "GO:0005096" ]
[ "GTPase activator activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROFILE", "SMART" ]
[ "PF01412", "PR00405", "PS50115", "SM00105" ]
[ "ArfGap", "REVINTRACTNG", "ARFGAP", "ArfGap" ]
[ 68595, 63057, 67141, 67741 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50115", "R-BTA-6807878", "R-BTA-6811434", "R-BTA-9013408", "R-CEL-6811434", "R-CEL-9013408", "R-DME-3928664", "R-DME-5620916", "R-DME-9013149", "R-DME-9013404", "R-DME-9013406", "R-DME-9013420", "R-DME-9013423", "R-DME-9013424", "R-HSA-1251985", "R-HSA-373752", "R-HSA-381038", ...
[ "PROSITEDOC:PDOC50115", "REACTOME:R-BTA-6807878", "REACTOME:R-BTA-6811434", "REACTOME:R-BTA-9013408", "REACTOME:R-CEL-6811434", "REACTOME:R-CEL-9013408", "REACTOME:R-DME-3928664", "REACTOME:R-DME-5620916", "REACTOME:R-DME-9013149", "REACTOME:R-DME-9013404", "REACTOME:R-DME-9013406", "REACTOME:...
66
[ "1dcq", "2b0o", "2crr", "2crw", "2d9l", "2iqj", "2olm", "2owa", "2p57", "3dwd", "3feh", "3fm8", "3jue", "3lju", "3lvq", "3lvr", "3mdb", "3o47", "3sub", "3t9k", "4f1p", "5nzs", "6jmt", "7jtz" ]
24
[ "PUB00003022", "PUB00014900", "PUB00014901" ]
[ "9446556", "10601011", "10102276" ]
[ "Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1).", "Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta.", "Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydr...
[ 1998, 1999, 1999 ]
3
[]
[ "IPR044732", "IPR047006" ]
0
2
0
[ "Eukaryota", "metagenomes" ]
[ 68701, 2 ]
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...
[ 84, 10, 165, 25, 123, 84, 5, 53, 122, 6, 6, 187 ]
12
true
Domain
Arf GTPase activating protein
Arf GTPase activating protein
ArfGAP_dom
6
IPR001165
1,165
T4-type lysozyme
T4-type_lysozyme
Family
871
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0003796", "GO:0016998" ]
[ "lysozyme activity", "cell wall macromolecule catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00684" ]
[ "T4LYSOZYME" ]
[ 871 ]
1
[ "CAZY", "EC" ]
[ "GH24", "3.2.1.17" ]
[ "CAZY:GH24", "EC:3.2.1.17" ]
2
[ "102l", "103l", "104l", "107l", "108l", "109l", "110l", "111l", "112l", "113l", "114l", "115l", "118l", "119l", "120l", "122l", "123l", "125l", "126l", "127l", "128l", "129l", "130l", "131l", "137l", "138l", "139l", "140l", "141l", "142l", "143l", "144l"...
873
[ "PUB00004082", "PUB00004870", "PUB00005266" ]
[ "2234094", "7624375", "8535779" ]
[ "A mutant T4 lysozyme displays five different crystal conformations.", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases." ]
[ 1990, 1995, 1995 ]
3
[ "IPR002196" ]
[ "IPR046397" ]
1
1
0
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 215, 27, 621, 8 ]
4
[]
[]
0
true
Family
T4-type lysozyme
T4-type lysozyme
T4-type_lysozyme
9
IPR001166
1,166
Hyperglycemic hormone
Hyperglycemic
Family
1,010
false
false
Hyperglycemic hormone, which controls blood sugar levels, is an abundant peptide in the sinus glands of isopods and decapods [ , ]. The peptide is a potent secretagogue, releasing digestive enzymes from the hepatopancreas. It may act as a stress hormone. The peptide contains around 70 amino acid residues, and includes ...
[ "GO:0005184", "GO:0005576" ]
[ "neuropeptide hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR00550" ]
[ "HYPRGLYCEMIC" ]
[ 1010 ]
1
[ "PROSITEDOC" ]
[ "PDOC00963" ]
[ "PROSITEDOC:PDOC00963" ]
1
[ "1j0t", "5b5i", "5xs1" ]
3
[ "PUB00000190", "PUB00001435", "PUB00001577" ]
[ "2169734", "8436119", "2792364" ]
[ "Amino acid sequence of a peptide with both molt-inhibiting and hyperglycemic activities in the lobster, Homarus americanus.", "Isolation and molecular characterization of a hyperglycemic neuropeptide from the sinus gland of the terrestrial isopod Armadillidium vulgare (Crustacea).", "Amino acid sequence of the...
[ 1990, 1993, 1989 ]
3
[ "IPR031098" ]
[ "IPR000346", "IPR001262" ]
1
2
0
[ "Ecdysozoa" ]
[ 1010 ]
1
[ "Drosophila melanogaster" ]
[ 6 ]
1
true
Family
Hyperglycemic hormone
Hyperglycemic hormone
Hyperglycemic
4
IPR001168
1,168
Adrenocorticotrophin (ACTH) receptor
ACTH_rcpt
Family
576
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:0004978", "GO:0007186", "GO:0016020" ]
[ "corticotropin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00520" ]
[ "ACTROPHINR" ]
[ 576 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "283", "R-BTA-375276", "R-BTA-418555", "R-HSA-375276", "R-HSA-418555", "R-HSA-5579031", "R-MMU-375276", "R-MMU-418555", "R-SSC-375276", "R-SSC-418555" ]
[ "IUPHAR:283", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-418555", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-5579031", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418555", "REACTOME:R-SSC-375276", "REACTOME:R-SSC-418555" ]
10
[ "8gy7", "9k3l" ]
2
[ "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
[ "IPR001671" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 576 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 3 ]
3
true
Family
Adrenocorticotrophin (ACTH) receptor
Adrenocorticotrophin (ACTH) receptor
ACTH_rcpt
6
IPR001170
1,170
Adenylyl cyclase class-4/guanylyl cyclase
ANPR/GUC
Family
6,345
false
false
This entry includes the natriuretic peptide receptors (ANP-A, ANP-B and ANP-C) from animals [ , ] and guanylate cyclases 2G (GUC2G) from rodents. GUC2G is closely related to the natriuretic peptide receptors, but all ligands known to activate other receptors failed to stimulate its enzymic activity [ ]. Natriuretic pep...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PRINTS", "PROSITE" ]
[ "PR00255", "PS00458" ]
[ "NATPEPTIDER", "ANF_RECEPTORS" ]
[ 6194, 1822 ]
2
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.6.1.2", "PDOC00430", "R-BTA-5578768", "R-CEL-2514859", "R-HSA-5578768", "R-MMU-5578768", "R-RNO-5578768" ]
[ "EC:4.6.1.2", "PROSITEDOC:PDOC00430", "REACTOME:R-BTA-5578768", "REACTOME:R-CEL-2514859", "REACTOME:R-HSA-5578768", "REACTOME:R-MMU-5578768", "REACTOME:R-RNO-5578768" ]
7
[ "1dp4", "1jdn", "1jdp", "1t34", "1yk0", "1yk1", "3a3k", "7brg", "7brh", "7bri", "7brj", "7brk", "7brl", "8tg9", "8tga", "9bcl", "9bcn", "9bco", "9bcp", "9bcq", "9bcs", "9bcv" ]
22
[ "PUB00001497", "PUB00002592", "PUB00077555", "PUB00077556", "PUB00077557" ]
[ "2568301", "1978722", "14713286", "15146390", "10377427" ]
[ "The guanylate cyclase/receptor family of proteins.", "The primary structure of the rat guanylyl cyclase A/atrial natriuretic peptide receptor gene.", "Identification of an orphan guanylate cyclase receptor selectively expressed in mouse testis.", "Mutations in the transmembrane natriuretic peptide receptor N...
[ 1989, 1990, 2004, 2004, 1999 ]
5
[]
[]
0
0
null
[ "Eukaryota", "bird metagenome" ]
[ 6344, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 21, 3, 19, 11, 17 ]
6
true
Family
Adenylyl cyclase class-4/guanylyl cyclase
Adenylyl cyclase class-4/guanylyl cyclase
ANPR/GUC
2
IPR001171
1,171
Sterol biosynthesis ERG24/DHCR-like
ERG24_DHCR-like
Family
11,960
false
false
This entry represents a group of enzymes involved in the steroid biosynthetic pathway, including 7-dehydrocholesterol reductase and Delta(14)-sterol reductase LBR (lamin B receptor) from animals [ , , ], Delta(14)-sterol reductase from fungi and plants [ , , ] and Delta(24(24(1)))-sterol reductase from yeast [ ]. These...
[ "GO:0016628", "GO:0016126", "GO:0016020" ]
[ "oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor", "sterol biosynthetic process", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF01222" ]
[ "ERG4_ERG24" ]
[ 11960 ]
1
[ "EC", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "1.3.1", "GenProp1246", "GenProp1609", "PDOC00780", "R-BTA-6807047", "R-BTA-6807062", "R-DDI-191273", "R-DDI-6807062", "R-DME-191273", "R-DME-6807062", "R-DRE-6807047", "R-DRE-6807062", "R-HSA-191273", "R-HSA-2426168", "R-HSA-2995383", "R-HSA-6807047", "R-HSA-6807062", "R-HSA-89806...
[ "EC:1.3.1", "GP:GenProp1246", "GP:GenProp1609", "PROSITEDOC:PDOC00780", "REACTOME:R-BTA-6807047", "REACTOME:R-BTA-6807062", "REACTOME:R-DDI-191273", "REACTOME:R-DDI-6807062", "REACTOME:R-DME-191273", "REACTOME:R-DME-6807062", "REACTOME:R-DRE-6807047", "REACTOME:R-DRE-6807062", "REACTOME:R-HS...
52
[ "4quv", "9l5r", "9l5s", "9l5t" ]
4
[ "PUB00001844", "PUB00100216", "PUB00100217", "PUB00100218", "PUB00100219", "PUB00100220", "PUB00100221" ]
[ "8125337", "21436218", "27336722", "11897574", "10859167", "15054108", "25637936" ]
[ "The identification of a gene family in the Saccharomyces cerevisiae ergosterol biosynthesis pathway.", "A sterol C-14 reductase encoded by FgERG24B is responsible for the intrinsic resistance of Fusarium graminearum to amine fungicides.", "The Lamin B receptor is essential for cholesterol synthesis and perturb...
[ 1994, 2011, 2016, 2002, 2000, 2004, 2015 ]
7
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Mimiviridae", "candidate division MSBL1 archaeon SCGC-AAA259I07", "ecological metagenomes" ]
[ 115, 11826, 13, 1, 5 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 9, 1, 6, 1, 31, 17, 2, 10, 13, 2, 2, 22 ]
12
true
Family
Sterol biosynthesis ERG24/DHCR-like
Sterol biosynthesis ERG24/DHCR-like
ERG24_DHCR-like
5
IPR001172
1,172
Flagellar motor switch FliN/Type III secretion HrcQb
FliN_T3SS_HrcQb
Family
16,332
false
false
The flagellar motor switch in Escherichia coli and Salmonella typhimurium regulates the direction of flagellar rotation and hence controls swimming behaviour. The switch is a complex apparatus that responds to signals transduced by the chemotaxis sensory signalling system during chemotactic behaviour [ ]. The switch co...
[ "GO:0003774", "GO:0006935", "GO:0071973", "GO:0009425" ]
[ "cytoskeletal motor activity", "chemotaxis", "bacterial-type flagellum-dependent cell motility", "bacterial-type flagellum basal body" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR00956" ]
[ "FLGMOTORFLIN" ]
[ 16332 ]
1
[]
[]
[]
0
[ "1o6a", "1o9y", "1yab", "4yxb", "4yxc", "5xrw", "8umd", "8umx", "8uox", "8upl", "8vib", "8vid", "8vkq", "8vkr", "8wiw", "8wo5", "8woe", "8xp0", "8xp1", "8yjt", "9n49", "9n4z" ]
22
[ "PUB00001834", "PUB00002083", "PUB00002290", "PUB00004790" ]
[ "8224881", "2656645", "8631704", "1631122" ]
[ "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 ]
4
[]
[ "IPR012826" ]
0
1
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 16106, 18, 208 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Flagellar motor switch FliN/Type III secretion HrcQb
Flagellar motor switch FliN/Type III secretion HrcQb
FliN_T3SS_HrcQb
9
IPR001173
1,173
Glycosyltransferase 2-like
Glyco_trans_2-like
Domain
427,627
false
false
This domain is found in a diverse family of glycosyl transferases that transfer the sugar from UDP-glucose, UDP-N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids [ ]. The biosynthesis of disaccharides, oligosaccharides and polysaccha...
[]
[]
[]
0
[ "PFAM", "PFAM" ]
[ "PF00535", "PF13632" ]
[ "Glycos_transf_2", "Glyco_trans_2_3" ]
[ 398184, 31973 ]
2
[ "CAZY", "EC", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "GT2", "2.4.1", "GenProp1517", "GenProp1712", "GenProp1756", "R-BTA-6811436", "R-BTA-913709", "R-CEL-6811436", "R-CEL-913709", "R-DDI-480985", "R-DME-190372", "R-DME-480985", "R-DME-6811436", "R-DME-913709", "R-DRE-913709", "R-HSA-162699", "R-HSA-190372", "R-HSA-446203", "R-HSA-4...
[ "CAZY:GT2", "EC:2.4.1", "GP:GenProp1517", "GP:GenProp1712", "GP:GenProp1756", "REACTOME:R-BTA-6811436", "REACTOME:R-BTA-913709", "REACTOME:R-CEL-6811436", "REACTOME:R-CEL-913709", "REACTOME:R-DDI-480985", "REACTOME:R-DME-190372", "REACTOME:R-DME-480985", "REACTOME:R-DME-6811436", "REACTOME...
47
[ "1h7l", "1h7q", "1qg8", "1qgq", "1qgs", "1xhb", "2d7i", "2d7r", "2ffu", "2ffv", "2z86", "2z87", "3bcv", "3ckj", "3ckn", "3cko", "3ckq", "3ckv", "3e25", "3e26", "3f1y", "3kia", "3l7i", "3l7j", "3l7k", "3l7l", "3l7m", "3o3p", "4d0t", "4d0z", "4d11", "4ddz"...
142
[ "PUB00009409", "PUB00091409" ]
[ "9334165", "27973583" ]
[ "A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities.", "Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance." ]
[ 1997, 2016 ]
2
[]
[ "IPR035518", "IPR045885" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Plasmid pWQ799", "Viruses", "unclassified sequences" ]
[ 9741, 351558, 58313, 1, 518, 7496 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 93, 15, 93, 26, 11, 97, 50, 7, 49, 101, 2, 2, 110 ]
13
true
Domain
Glycosyltransferase 2-like
Glycosyltransferase 2-like
Glyco_trans_2-like
2
IPR001174
1,174
HddA/FKP
HddA/FKP
Family
3,650
false
false
This entry includes D-glycero-alpha-D-manno-heptose 7-phosphate kinase (HddA) from Mycobacterium tuberculosis and its orthologue L-fucokinase/L-fucose-1-P guanylyltransferase (FKP) from Bacteroides fragilis [ ]. HddA catalyses the phosphorylation of D-glycero-alpha-D-manno-heptose 7-phosphate at the C-1 position to for...
[ "GO:0005524", "GO:0016301" ]
[ "ATP binding", "kinase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS" ]
[ "PR00960" ]
[ "LMBPPROTEIN" ]
[ 3650 ]
1
[ "EC", "METACYC" ]
[ "2.7.1.168", "PWY-6478" ]
[ "EC:2.7.1.168", "METACYC:PWY-6478" ]
2
[ "3k85", "4n3o", "4usk", "4usm", "4ut4", "4utg", "5yys", "9iip", "9iit" ]
9
[ "PUB00003676", "PUB00003870", "PUB00004888", "PUB00155378", "PUB00158917" ]
[ "1846667", "8577249", "8610181", "30242642", "33412198" ]
[ "Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase.", "Molecular characterization of the lincomycin-production gene cluster of Streptomyces lincolnensis 78-11.", "An integrated map of the genome of the tubercle bacillus, Mycobacterium tuber...
[ 1991, 1995, 1996, 2019, 2021 ]
5
[]
[ "IPR014606" ]
0
1
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "metagenomes" ]
[ 95, 3037, 7, 299, 212 ]
5
[ "Caenorhabditis elegans", "Rattus norvegicus" ]
[ 1, 1 ]
2
true
Family
HddA/FKP
HddA/FKP
HddA/FKP
1
IPR001177
1,177
DNA helicase E1, C-terminal, Papillomavirus
PPV_DNA_helicase_E1_C
Domain
3,379
false
false
Papillomaviruses (PPV) are a large family of DNA tumour viruses which give rise to warts in their host species. The helicase E1 protein is an ATP-dependent DNA helicase required for initiation of viral DNA replication [ , ]. It forms a complex with the viral E2 protein, which is a site-specific DNA-binding transcriptio...
[ "GO:0003677", "GO:0003678", "GO:0005524", "GO:0006260" ]
[ "DNA binding", "DNA helicase activity", "ATP binding", "DNA replication" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PFAM" ]
[ "PF00519" ]
[ "PPV_E1_C" ]
[ 3379 ]
1
[ "EC" ]
[ "5.6.2.4" ]
[ "EC:5.6.2.4" ]
1
[ "1tue", "2gxa", "2v9p", "5a9k", "7apd" ]
5
[ "PUB00024726", "PUB00028030", "PUB00028031", "PUB00028032", "PUB00028033", "PUB00031575" ]
[ "10949036", "8389467", "2176744", "9060646", "9658141", "15289463" ]
[ "Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus.", "The E1 protein of bovine papilloma virus 1 is an ATP-dependent DNA helicase.", "Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transact...
[ 2000, 1993, 1990, 1997, 1998, 2004 ]
6
[]
[]
0
0
null
[ "Eukaryota", "Viruses" ]
[ 33, 3346 ]
2
[]
[]
0
true
Domain
DNA helicase E1, C-terminal, Papillomavirus
DNA helicase E1, C-terminal, Papillomavirus
PPV_DNA_helicase_E1_C
1
IPR001178
1,178
Pesticidal crystal protein, domain II
Pest_cryst_dom_II
Domain
832
false
false
This entry represents the conserved second domain of the toxic core. The crystal proteins of Bacillus thuringiensis have been extensively studied because of their pesticidal properties and their high natural levels of production [ ]. When an insect ingests these proteins, they are activated by proteolytic cleavage. The...
[ "GO:0005102" ]
[ "signaling receptor binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00555" ]
[ "Endotoxin_M" ]
[ 832 ]
1
[]
[]
[]
0
[ "1ciy", "1dlc", "1ji6", "1w99", "2c9k", "3eb7", "4arx", "4ary", "4moa", "4qx0", "4qx1", "4qx2", "4qx3", "4w8j", "5zi1", "6dj4", "6lfp", "6ovb", "6owk", "6wpc", "7ear", "8w7n", "8yqh", "9buv", "9h99" ]
25
[ "PUB00015089", "PUB00015090", "PUB00025909", "PUB00083810" ]
[ "7490762", "11468393", "11377201", "9729610" ]
[ "Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation.", "Structure of the insecticidal bacterial delta-endotoxin Cry3Bb1 of Bacillus thuringiensis.", "Structure of Cry2Aa suggests an unexpected receptor binding epitope.", "Revision of the nomenclature for the Bacillus t...
[ 1995, 2001, 2001, 1998 ]
4
[]
[]
0
0
null
[ "Bacillota", "Mesangiospermae" ]
[ 829, 3 ]
2
[ "Zea mays" ]
[ 1 ]
1
true
Domain
Pesticidal crystal protein, domain II
Pesticidal crystal protein, domain II
Pest_cryst_dom_II
7
IPR001181
1,181
Interleukin-7
IL-7
Family
868
false
false
This entry represents interleukin-7 (IL7), it is a hematopoietic growth factor produced by bone marrow stromal cells. It promotes growth of B- and T-cell precursors and functions with IL2 in the activation of mature T-cells [ , ]. IL-7 and IL-7Ralpha bind the gamma-c receptor forming a complex required for the developm...
[ "GO:0005139", "GO:0008083", "GO:0006955", "GO:0005576" ]
[ "interleukin-7 receptor binding", "growth factor activity", "immune response", "extracellular region" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PIRSF", "PRINTS", "PANTHER", "SMART" ]
[ "PF01415", "PIRSF001942", "PR00435", "PTHR48492", "SM00127" ]
[ "IL7", "IL-7", "INTERLEUKIN7", "", "IL7" ]
[ 839, 223, 693, 865, 438 ]
5
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-1266695", "R-HSA-1266695", "R-MMU-1266695", "R-RNO-1266695", "R-SSC-1266695" ]
[ "REACTOME:R-BTA-1266695", "REACTOME:R-HSA-1266695", "REACTOME:R-MMU-1266695", "REACTOME:R-RNO-1266695", "REACTOME:R-SSC-1266695" ]
5
[ "3di2", "3di3" ]
2
[ "PUB00004024", "PUB00004679", "PUB00051389" ]
[ "3259677", "2643102", "19141282" ]
[ "Stimulation of B-cell progenitors by cloned murine interleukin-7.", "Human interleukin 7: molecular cloning and growth factor activity on human and murine B-lineage cells.", "Structural and biophysical studies of the human IL-7/IL-7Ralpha complex." ]
[ 1988, 1989, 2009 ]
3
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 868 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 8, 4, 5 ]
3
true
Family
Interleukin-7
Interleukin-7
IL-7
7
IPR001182
1,182
Probable peptidoglycan glycosyltransferase FtsW/RodA
FtsW/RodA
Family
59,762
false
false
A number of prokaryotic integral membrane proteins involved in cell cycle processes have been found to be structurally related [ , ]. These proteins include, the Escherichia coli and related bacteria cell division protein ftsW and the rod shape-determining protein rodA (or mrdB), the Bacillus subtilis stage V sporulati...
[ "GO:0051301", "GO:0016020" ]
[ "cell division", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PANTHER" ]
[ "PF01098", "PTHR30474" ]
[ "FTSW_RODA_SPOVE", "" ]
[ 59746, 59288 ]
2
[ "EC", "PROSITEDOC" ]
[ "2.4.99.28", "PDOC00352" ]
[ "EC:2.4.99.28", "PROSITEDOC:PDOC00352" ]
2
[ "6bar", "6bas", "6pl5", "6pl6", "8bh1", "8p1u", "8tj3" ]
7
[ "PUB00002092", "PUB00003802", "PUB00083894" ]
[ "2509435", "2113157", "27525505" ]
[ "Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively.", "The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures.", ...
[ 1989, 1990, 2016 ]
3
[]
[ "IPR011923", "IPR013437" ]
0
2
0
[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 58234, 118, 1, 1409 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Probable peptidoglycan glycosyltransferase FtsW/RodA
Probable peptidoglycan glycosyltransferase FtsW/RodA
FtsW/RodA
2
IPR001183
1,183
Muscarinic acetylcholine receptor M3
Musac_Ach_M3_rcpt
Family
757
false
false
Muscarinic acetylcholine receptors are members of rhodopsin-like G-protein coupled receptor family. They play several important roles; they mediate many of the effects of acetylcholine in the central and peripheral nervous system and modulate a variety of physiological functions, such as airway, eye and intestinal smoo...
[ "GO:0016907", "GO:0007186", "GO:0045987", "GO:0046541", "GO:0005886" ]
[ "G protein-coupled acetylcholine receptor activity", "G protein-coupled receptor signaling pathway", "positive regulation of smooth muscle contraction", "saliva secretion", "plasma membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "cellular_component" ]
5
[ "PRINTS" ]
[ "PR00540" ]
[ "MUSCRINICM3R" ]
[ 757 ]
1
[ "GP", "GP", "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp2096", "GenProp2098", "15", "R-HSA-390648", "R-HSA-399997", "R-HSA-416476", "R-MMU-390648", "R-MMU-416476", "R-RNO-390648", "R-RNO-416476", "R-SSC-390648", "R-SSC-416476" ]
[ "GP:GenProp2096", "GP:GenProp2098", "IUPHAR:15", "REACTOME:R-HSA-390648", "REACTOME:R-HSA-399997", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-390648", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-390648", "REACTOME:R-RNO-416476", "REACTOME:R-SSC-390648", "REACTOME:R-SSC-416476" ]
12
[ "8e9w", "8e9y", "8e9z", "8ea0" ]
4
[ "PUB00064316", "PUB00064317", "PUB00064318", "PUB00064319", "PUB00064320", "PUB00064321", "PUB00064322", "PUB00064323", "PUB00064324", "PUB00064325", "PUB00064326", "PUB00064332", "PUB00064336", "PUB00064337", "PUB00064339", "PUB00064340", "PUB00064342", "PUB00064343", "PUB000643...
[ "3443095", "3272174", "3037705", "9647869", "2470172", "8853955", "10841527", "14641022", "12725869", "17762886", "15850824", "11082420", "14744253", "15474550", "15266016", "7504306", "8981565", "11714883", "9149041", "8164520", "1723953", "16733808", "22358844", "1675...
[ "Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors.", "Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes.", "Identification of a family of muscarinic acetylcholine receptor genes.", "Inter...
[ 1987, 1988, 1987, 1998, 1989, 1996, 2000, 2003, 2003, 2007, 2005, 2000, 2004, 2004, 2004, 1993, 1996, 2001, 1997, 1994, 1991, 2006, 2012, 2006, 2012, 2000 ]
26
[ "IPR000995" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 757 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 2, 2 ]
4
true
Family
Muscarinic acetylcholine receptor M3
Muscarinic acetylcholine receptor M3
Musac_Ach_M3_rcpt
4
IPR001184
1,184
Somatostatin receptor 5
Somatstn_rcpt_5
Family
886
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" ]
[ "PR00591" ]
[ "SOMATOSTTN5R" ]
[ 886 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "359", "R-BTA-375276", "R-BTA-418594", "R-HSA-375276", "R-HSA-418594", "R-MMU-375276", "R-MMU-418594", "R-RNO-375276", "R-RNO-418594" ]
[ "IUPHAR:359", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-418594", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594" ]
9
[ "8x8l", "8x8n", "8zbe", "8zbj", "8zcj" ]
5
[ "PUB00013316", "PUB00063572", "PUB00063590", "PUB00063595", "PUB00063596", "PUB00063597", "PUB00063598", "PUB00063599", "PUB00063600", "PUB00063601", "PUB00063602", "PUB00063603", "PUB00063604", "PUB00063605", "PUB00063619", "PUB00063629" ]
[ "14507421", "10433861", "7792934", "8243278", "8078491", "7907795", "1346068", "8483934", "15361490", "10598790", "1328199", "7538774", "9426226", "8684611", "8034040", "9892225" ]
[ "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, 1999 ]
16
[ "IPR000586" ]
[]
1
0
1
[ "Vertebrata" ]
[ 886 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 4, 6, 6 ]
4
true
Family
Somatostatin receptor 5
Somatostatin receptor 5
Somatstn_rcpt_5
4
IPR001185
1,185
Large-conductance mechanosensitive channel
MS_channel
Family
19,848
false
false
Mechanosensitive ion channels (MscL) play a critical role in transducing physical stresses at the cell membrane into an electrochemical response. MscL is a protein which forms a channel organised as a homopentamer, with each subunit containing two transmembrane regions [ , , ]. Prokaryotes harbor a large-conductance me...
[ "GO:0008381", "GO:0034220", "GO:0016020" ]
[ "mechanosensitive monoatomic ion channel activity", "monoatomic ion transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PRINTS", "NCBIFAM" ]
[ "MF_00115", "PR01264", "TIGR00220" ]
[ "MscL", "MECHCHANNEL", "mscL" ]
[ 18846, 18170, 19687 ]
3
[ "PROSITEDOC" ]
[ "PDOC01030" ]
[ "PROSITEDOC:PDOC01030" ]
1
[ "2oar", "3hzq", "6ctd" ]
3
[ "PUB00003881", "PUB00005232", "PUB00053088", "PUB00097422" ]
[ "9632260", "9856938", "19701184", "22685280" ]
[ "Functional and structural conservation in the mechanosensitive channel MscL implicates elements crucial for mechanosensation.", "Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel.", "Structure of a tetrameric MscL in an expanded intermediate state.", "The Msc...
[ 1998, 1998, 2009, 2012 ]
4
[ "IPR037673" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Phage sp. ctWVj20", "metagenomes" ]
[ 15, 19380, 291, 1, 161 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Large-conductance mechanosensitive channel
Large-conductance mechanosensitive channel
MS_channel
3
IPR001186
1,186
Bradykinin receptor B1
Brdyknn_1_rcpt
Family
593
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:0006954", "GO:0007186", "GO:0009612", "GO:0016020" ]
[ "bradykinin receptor activity", "inflammatory response", "G protein-coupled receptor signaling pathway", "response to mechanical stimulus", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "cellular_component" ]
5
[ "PRINTS" ]
[ "PR00993" ]
[ "BRADYKINNB1R" ]
[ 593 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "41", "R-CFA-375276", "R-CFA-416476", "R-CFA-418594", "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:41", "REACTOME:R-CFA-375276", "REACTOME:R-CFA-416476", "REACTOME:R-CFA-418594", "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", "REA...
13
[ "7eib" ]
1
[ "PUB00063406", "PUB00063407", "PUB00063408", "PUB00063409", "PUB00063410", "PUB00063413", "PUB00063414", "PUB00063415", "PUB00063416", "PUB00063417", "PUB00063421", "PUB00063428", "PUB00063429" ]
[ "10812256", "12755382", "9112069", "9650825", "8075864", "7700250", "18725957", "1695472", "10614988", "20152050", "8846417", "8832074", "17327486" ]
[ "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, 1995, 2008, 1990, 1999, 2010, 1995, 1996, 2007 ]
13
[ "IPR000496" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 593 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 2 ]
3
true
Family
Bradykinin receptor B1
Bradykinin receptor B1
Brdyknn_1_rcpt
3
IPR001187
1,187
Tissue factor
Tissue_factor
Family
1,396
false
false
Tissue factor (TF, also known as thromboplastin) is an integral membrane glycoprotein that initiates blood coagulation by forming a complex with circulating factor VII (FVII) or VIIa (FVIIa), which it comes in contact with following damage to blood vessel walls. Calcium forms the bridge between TF and FVII, the resulta...
[ "GO:0007596", "GO:0016020" ]
[ "blood coagulation", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PIRSF", "PRINTS" ]
[ "PIRSF002498", "PR00346" ]
[ "Tissue_factor_3", "TISSUEFACTOR" ]
[ 208, 1396 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00541", "R-BTA-140834", "R-HSA-140834", "R-HSA-9031628", "R-MMU-140834", "R-RNO-140834" ]
[ "PROSITEDOC:PDOC00541", "REACTOME:R-BTA-140834", "REACTOME:R-HSA-140834", "REACTOME:R-HSA-9031628", "REACTOME:R-MMU-140834", "REACTOME:R-RNO-140834" ]
6
[ "1a21", "1ahw", "1boy", "1dan", "1fak", "1j9c", "1jps", "1o5d", "1tfh", "1uj3", "1w0y", "1w2k", "1wqv", "1wss", "1wtg", "1wun", "1wv7", "1z6j", "2a2q", "2aei", "2aer", "2b7d", "2b8o", "2c4f", "2ec9", "2f9b", "2fir", "2flb", "2flr", "2hft", "2puq", "2zp0"...
50
[ "PUB00033196", "PUB00033197", "PUB00033198", "PUB00033199", "PUB00033200" ]
[ "15569823", "16261634", "16479459", "16036212", "14872439" ]
[ "Tissue factor-factor VIIa signaling.", "Tissue factor pathway inhibitor: structure, biology and involvement in disease.", "Emerging insights in tissue factor-dependent signaling events.", "Tissue factor mediates inflammation.", "Tissue factor as an evolutionary conserved cytokine receptor: Implications for...
[ 2005, 2006, 2006, 2005, 2004 ]
5
[]
[]
0
0
null
[ "Opisthokonta", "Poriferisphaera corsica" ]
[ 1395, 1 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 4, 5, 11 ]
4
true
Family
Tissue factor
Tissue factor
Tissue_factor
6
IPR001188
1,188
Spermidine/putrescine-binding periplasmic protein
Sperm_putr-bd
Family
32,802
false
false
Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. The protein components of these traffic systems include one or two transmembrane protein components, one or two membrane-associated ATP-binding proteins and a high affinity periplasmic solute-binding p...
[ "GO:0019808", "GO:0015846", "GO:0042597" ]
[ "polyamine binding", "polyamine transport", "periplasmic space" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PIRSF", "PRINTS" ]
[ "PIRSF019574", "PR00909" ]
[ "Periplasmic_polyamine_BP", "SPERMDNBNDNG" ]
[ 19914, 32686 ]
2
[]
[]
[]
0
[ "1a99", "1pot", "1poy", "2v84", "3ttk", "3ttl", "3ttm", "3ttn", "4edp", "4eqb", "4gl0", "6hly", "6hlz", "6hm2", "6ikm", "6nlp", "6ye0", "6ye6", "6ye7", "6ye8", "6yeb", "6yec", "6yed", "7oys", "7oyt", "7oyu", "7oyv", "7oyw", "7oyx", "7oyy", "7oyz", "7xjm"...
37
[ "PUB00002665", "PUB00002787", "PUB00020309", "PUB00028071", "PUB00058383", "PUB00100223", "PUB00100224", "PUB00100225" ]
[ "1939142", "8416922", "9651355", "8897598", "22300763", "31627455", "23719730", "33406388" ]
[ "Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome.", "Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome.", "Crystal structure and mutational analysis of the...
[ 1991, 1993, 1998, 1996, 2012, 2019, 2014, 2021 ]
8
[ "IPR006059" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctLeG9", "unclassified sequences" ]
[ 181, 31578, 592, 1, 450 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 7, 3, 1, 2 ]
4
true
Family
Spermidine/putrescine-binding periplasmic protein
Spermidine/putrescine-binding periplasmic protein
Sperm_putr-bd
7
IPR001189
1,189
Manganese/iron superoxide dismutase
Mn/Fe_SOD
Family
41,408
false
false
Superoxide dismutases (SODs) ( ) catalyse the conversion of superoxide radicals to molecular oxygen. Their function is to destroy the radicals that are normally produced within cells and are toxic to biological systems. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one [...
[ "GO:0004784", "GO:0046872", "GO:0006801" ]
[ "superoxide dismutase activity", "metal ion binding", "superoxide metabolic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PIRSF", "PRINTS" ]
[ "PIRSF000349", "PR01703" ]
[ "SODismutase", "MNSODISMTASE" ]
[ 35644, 40358 ]
2
[ "EC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.15.1.1", "PWY-6854", "PDOC00083", "R-CEL-3299685", "R-DDI-2151201", "R-DDI-3299685", "R-DME-3299685", "R-HSA-1222387", "R-HSA-2151201", "R-HSA-3299685", "R-HSA-8862803", "R-HSA-8950505", "R-HSA-9615017", "R-HSA-9841251", "R-MMU-2151201", "R-MMU-3299685", "R-RNO-2151201", "R-RNO-...
[ "EC:1.15.1.1", "METACYC:PWY-6854", "PROSITEDOC:PDOC00083", "REACTOME:R-CEL-3299685", "REACTOME:R-DDI-2151201", "REACTOME:R-DDI-3299685", "REACTOME:R-DME-3299685", "REACTOME:R-HSA-1222387", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-3299685", "REACTOME:R-HSA-8862803", "REACTOME:R-HSA-8950505", ...
22
[ "1ap5", "1ap6", "1ar4", "1ar5", "1avm", "1b06", "1bs3", "1bsm", "1bt8", "1coj", "1d5n", "1dt0", "1em1", "1en4", "1en5", "1en6", "1gn2", "1gn3", "1gn4", "1gn6", "1gv3", "1i08", "1i0h", "1ids", "1isa", "1isb", "1isc", "1ix9", "1ixb", "1ja8", "1jr9", "1kkc"...
204
[ "PUB00001002", "PUB00001553", "PUB00003417", "PUB00013976", "PUB00013977" ]
[ "3315461", "3345848", "1556751", "9537987", "9931259" ]
[ "Aspects of the structure, function, and applications of superoxide dismutase.", "Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures.", "A comparison of evolutionary rates of the two major kinds of superoxide dismutase.", "Crystal structure of Y34...
[ 1987, 1988, 1992, 1998, 1999 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 820, 30177, 10139, 9, 263 ]
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",...
[ 25, 2, 1, 2, 2, 20, 5, 3, 5, 3, 1, 1, 36 ]
13
true
Family
Manganese/iron superoxide dismutase
Manganese/iron superoxide dismutase
Mn/Fe_SOD
7
IPR001190
1,190
SRCR domain
SRCR
Domain
48,487
false
false
The scavenger receptor cysteine-rich (SRCR) domain is an ancient and highly conserved domain of about 110 residues which is found in diverse secreted and cell-surface proteins, like the type I scavenger receptor, the speract receptor, CD5/Ly-1, CD6, or complement factor I [ ]. Tandem repeats of SRCR domains are common ...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM", "PFAM", "PRINTS", "PROSITE", "PROFILE", "SMART" ]
[ "PF00530", "PF15494", "PR00258", "PS00420", "PS50287", "SM00202" ]
[ "SRCR", "SRCR_2", "SPERACTRCPTR", "SRCR_1", "SRCR_2", "SR" ]
[ 37926, 6459, 33992, 24020, 46892, 42300 ]
6
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00348", "R-BTA-114608", "R-BTA-1566948", "R-BTA-2168880", "R-BTA-2243919", "R-DRE-114608", "R-DRE-2243919", "R-DRE-5683826", "R-HSA-114608", "R-HSA-1566948", "R-HSA-2168880", "R-HSA-2243919", "R-HSA-3000471", "R-HSA-3000480", "R-HSA-5578768", "R-HSA-5683826", "R-HSA-6806942", ...
[ "PROSITEDOC:PDOC00348", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-1566948", "REACTOME:R-BTA-2168880", "REACTOME:R-BTA-2243919", "REACTOME:R-DRE-114608", "REACTOME:R-DRE-2243919", "REACTOME:R-DRE-5683826", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-1566948", "REACTOME:R-HSA-2168880", "REACTOME:R-H...
40
[ "1by2", "1o5e", "1o5f", "1p57", "1z8g", "2ja4", "2jop", "2jp0", "2ott", "2oy3", "2oya", "2xrc", "3t2n", "4uq8", "5a2e", "5ce1", "5hrj", "5j4z", "5j7y", "5j8k", "5jfb", "5luf", "5o32", "5ze3", "6h8m", "6j02", "6k0l", "6k0o", "6kd5", "6q0b", "6sa4", "6sa5"...
102
[ "PUB00003964", "PUB00004717", "PUB00005429", "PUB00152485" ]
[ "10074941", "1978939", "8140623", "11741986" ]
[ "Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily.", "An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors.", "The SRCR superfamily: a family reminiscent of the Ig sup...
[ 1999, 1990, 1994, 2002 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Salinigranum rubrum", "Viruses", "metagenomes" ]
[ 219, 48253, 1, 7, 7 ]
5
[ "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", "Zea mays" ]
[ 2, 147, 17, 148, 92, 1, 126, 3 ]
8
true
Domain
SRCR domain
SRCR domain
SRCR
7
IPR001191
1,191
Geminivirus AL1, replication-associated protein
Gemini_AL1_REP
Family
8,920
false
false
Geminiviruses are characterised by a genome of circular single-stranded DNA encapsidated in twinned (geminate) quasi-isometric particles, from which the group derives its name [ ]. Most geminiviruses can be divided into two subgroups on the basis of host range and/or insect vector: i.e. those that infect dicotyledenous...
[ "GO:0005198" ]
[ "structural molecule activity" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR00227" ]
[ "GEMCOATAL1" ]
[ 8920 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.7.-", "3.1.21.-", "PWY-6322", "PWY-6626", "PWY-6749", "PWY-6955", "PWY-6998", "PWY-7127", "PWY-7419", "PWY-7529", "PWY-7706", "PWY-7719", "PWY-7735", "PWY-7737", "PWY-7769", "PWY-7888", "PWY-7904", "PWY-8117", "PWY-8179" ]
[ "EC:2.7.7.-", "EC:3.1.21.-", "METACYC:PWY-6322", "METACYC:PWY-6626", "METACYC:PWY-6749", "METACYC:PWY-6955", "METACYC:PWY-6998", "METACYC:PWY-7127", "METACYC:PWY-7419", "METACYC:PWY-7529", "METACYC:PWY-7706", "METACYC:PWY-7719", "METACYC:PWY-7735", "METACYC:PWY-7737", "METACYC:PWY-7769",...
19
[ "1l2m", "1l5i", "6q1m", "6we0", "6we1", "7kik", "7vg8" ]
7
[ "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
[]
[ "IPR001146", "IPR001301" ]
0
2
0
[ "Bacteria", "Eukaryota", "Viruses" ]
[ 10, 150, 8760 ]
3
[]
[]
0
true
Family
Geminivirus AL1, replication-associated protein
Geminivirus AL1, replication-associated protein
Gemini_AL1_REP
9
IPR001192
1,192
Phosphoinositide phospholipase C family
PI-PLC_fam
Family
40,447
false
false
This entry represents phosphoinositol-specific phospholipase C (PLC) from eukaryotes. Proteins in this entry include PLC-beta, gamma, delta, epsilon, eta, zeta and inactive phospholipase C-like protein 2 (PLC-L2). Phosphoinositol-specific phospholipase C (PLC; ( ) plays an important role in signal transduction processe...
[ "GO:0035556" ]
[ "intracellular signal transduction" ]
[ "biological_process" ]
1
[ "PRINTS", "PANTHER" ]
[ "PR00390", "PTHR10336" ]
[ "PHPHLIPASEC", "" ]
[ 37831, 40396 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...
[ "3.1.4.11", "PWY-6351", "PWY-6367", "PWY-7039", "PWY-8052", "R-BTA-112043", "R-BTA-1855204", "R-BTA-399997", "R-BTA-4086398", "R-BTA-416476", "R-BTA-418217", "R-BTA-434316", "R-BTA-500657", "R-CEL-112043", "R-CEL-1855204", "R-CEL-416476", "R-DDI-112043", "R-DDI-114604", "R-DDI-11...
[ "EC:3.1.4.11", "METACYC:PWY-6351", "METACYC:PWY-6367", "METACYC:PWY-7039", "METACYC:PWY-8052", "REACTOME:R-BTA-112043", "REACTOME:R-BTA-1855204", "REACTOME:R-BTA-399997", "REACTOME:R-BTA-4086398", "REACTOME:R-BTA-416476", "REACTOME:R-BTA-418217", "REACTOME:R-BTA-434316", "REACTOME:R-BTA-5006...
164
[ "1djg", "1djh", "1dji", "1djw", "1djx", "1djy", "1djz", "1mai", "1qas", "1qat", "2fju", "2isd", "2zkm", "3qr0", "3qr1", "4gnk", "4qj3", "4qj4", "4qj5", "6pbc", "6pmp", "7sq2", "7t8t", "7z3j", "8emv", "8emw", "8emx", "8jqg", "8jqh", "8jqi", "8qju", "8t7c"...
38
[ "PUB00002715", "PUB00005394", "PUB00024211", "PUB00024218", "PUB00072646" ]
[ "1319994", "1335185", "9062102", "9048554", "23140367" ]
[ "Regulation of inositol phospholipid-specific phospholipase C isozymes.", "Regulation of phospholipase C by G proteins.", "A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-delta1.", "Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specif...
[ 1992, 1992, 1997, 1997, 2013 ]
5
[]
[ "IPR016279", "IPR016280" ]
0
2
0
[ "Eukaryota", "Viruses", "viral metagenome" ]
[ 40387, 3, 57 ]
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...
[ 39, 36, 107, 7, 103, 57, 4, 13, 82, 1, 1, 42 ]
12
true
Family
Phosphoinositide phospholipase C family
Phosphoinositide phospholipase C family
PI-PLC_fam
8
IPR001193
1,193
Membrane-bound transcription factor site-2 protease
MBTPS2
Family
6,019
false
false
This entry represents the membrane-bound transcription factor site-2 protease (MBTPS2, also known as S2P) [ ]. MBTPS2 is a membrane-embedded zinc metalloprotease that activates signaling proteins involved in sterol control of transcription and ER stress response [ ]. It cleaves several transcription factors that are ty...
[ "GO:0004222", "GO:0006508", "GO:0016020" ]
[ "metalloendopeptidase activity", "proteolysis", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS", "PANTHER" ]
[ "PR01000", "PTHR13325" ]
[ "SREBPS2PTASE", "" ]
[ 3015, 5993 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.24.85", "R-BTA-1655829", "R-BTA-381033", "R-BTA-8874177", "R-BTA-8874211", "R-HSA-1655829", "R-HSA-381033", "R-HSA-8874177", "R-HSA-8874211", "R-HSA-8963889", "R-MMU-1655829", "R-MMU-381033", "R-MMU-8874177", "R-MMU-8874211" ]
[ "EC:3.4.24.85", "REACTOME:R-BTA-1655829", "REACTOME:R-BTA-381033", "REACTOME:R-BTA-8874177", "REACTOME:R-BTA-8874211", "REACTOME:R-HSA-1655829", "REACTOME:R-HSA-381033", "REACTOME:R-HSA-8874177", "REACTOME:R-HSA-8874211", "REACTOME:R-HSA-8963889", "REACTOME:R-MMU-1655829", "REACTOME:R-MMU-3810...
14
[]
0
[ "PUB00003639", "PUB00067929", "PUB00067930", "PUB00067931", "PUB00092660" ]
[ "9659902", "19361614", "20672378", "10419520", "24099002" ]
[ "Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs.", "IFAP syndrome is caused by deficiency in MBTPS2, an intramembrane zinc metalloprotease essential for cholesterol homeostasis and ER stress response.", "Keratosis Follicularis Spinulosa D...
[ 1997, 2009, 2010, 1999, 2013 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 987, 1950, 3028, 54 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 11, 1, 2, 1, 3, 4, 3, 5, 17 ]
9
true
Family
Membrane-bound transcription factor site-2 protease
Membrane-bound transcription factor site-2 protease
MBTPS2
4
IPR001194
1,194
cDENN domain
cDENN_dom
Domain
41,456
false
false
This entry represents the core or cDENN domain. The tripartite DENN (Differentially Expressed in Normal and Neoplastic Cells) domain is an evolutionarily conserved protein module found in several proteins involved in Rab-mediated processes and, in some cases, regulation of MAPK (Mitogen-Activated Protein Kinase) signal...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF02141", "SM00799" ]
[ "DENN", "DENN" ]
[ 41357, 39353 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50211", "R-CEL-1483248", "R-CEL-8876198", "R-DME-8876198", "R-HSA-1483248", "R-HSA-1660499", "R-HSA-5357905", "R-HSA-8876198", "R-MMU-1483248", "R-MMU-5357905", "R-MMU-8876198", "R-RNO-5357905", "R-RNO-8876198", "R-SPO-8876198" ]
[ "PROSITEDOC:PDOC50211", "REACTOME:R-CEL-1483248", "REACTOME:R-CEL-8876198", "REACTOME:R-DME-8876198", "REACTOME:R-HSA-1483248", "REACTOME:R-HSA-1660499", "REACTOME:R-HSA-5357905", "REACTOME:R-HSA-8876198", "REACTOME:R-MMU-1483248", "REACTOME:R-MMU-5357905", "REACTOME:R-MMU-8876198", "REACTOME:...
14
[ "3tw8", "6ekk" ]
2
[ "PUB00007739", "PUB00018213", "PUB00065679", "PUB00160349", "PUB00160351", "PUB00160352", "PUB00160390", "PUB00160391" ]
[ "11563850", "12906859", "22065758", "35196081", "37454296", "38296963", "20472560", "28970336" ]
[ "uDENN, DENN, and dDENN: indissociable domains in Rab and MAP kinases signaling pathways.", "Molecular cloning, structural analysis, and expression of a human IRLB, MYC promoter-binding protein: new DENN domain-containing protein family emerges small star, filled.", "Insights regarding guanine nucleotide exchan...
[ 2001, 2003, 2011, 2022, 2023, 2024, 2010, 2017 ]
8
[ "IPR037516" ]
[]
1
0
1
[ "Eukaryota" ]
[ 41456 ]
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", "Schizosaccharomyces pombe (stra...
[ 18, 13, 121, 25, 102, 56, 4, 10, 90, 1, 36 ]
11
true
Domain
cDENN domain
cDENN domain
cDENN_dom
7