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
IPR000413
413
Integrin alpha chain
Integrin_alpha
Family
27,236
false
false
null
[ "GO:0007155", "GO:0008305" ]
[ "cell adhesion", "integrin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01185" ]
[ "INTEGRINA" ]
[ 27236 ]
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-1566948", "R-BTA-1566977", "R-BTA-198933", "R-BTA-202733", "R-BTA-210991", "R-BTA-216083", "R-BTA-3000157", "R-BTA-6798695", "R-BTA-8874081", "R-BTA-9634597", "R-BTA-9860927", "R-CEL-114608", "R-CEL-1236973", "R-CEL-1566977", "R-CEL-198933", "R-CEL-202733", "R-CEL-210991", "...
[ "REACTOME:R-BTA-1566948", "REACTOME:R-BTA-1566977", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-202733", "REACTOME:R-BTA-210991", "REACTOME:R-BTA-216083", "REACTOME:R-BTA-3000157", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8874081", "REACTOME:R-BTA-9634597", "REACTOME:R-BTA-9860927", "REACTOME:R-...
129
[ "1jv2", "1l5g", "1m1x", "1tye", "1u8c", "2vc2", "2vdk", "2vdl", "2vdm", "2vdn", "2vdo", "2vdp", "2vdq", "2vdr", "3fcs", "3fcu", "3ije", "3k6s", "3k71", "3k72", "3nid", "3nif", "3nig", "3t3m", "3t3p", "3v4p", "3v4v", "3vi3", "3vi4", "3zdx", "3zdy", "3zdz"...
159
[ "PUB00000811", "PUB00001505", "PUB00005772", "PUB00006166", "PUB00009789", "PUB00011882", "PUB00015915", "PUB00015985", "PUB00035000", "PUB00035002" ]
[ "3028640", "2199285", "8990162", "3327687", "12297042", "12826403", "14689578", "2467745", "12361595", "12234368" ]
[ "Integrins: a family of cell surface receptors.", "Integrins and other cell adhesion molecules.", "Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain.", "cDNA cloning and complete primary structure of the alpha subunit of a leukocyte adhesion glycoprotein,...
[ 1987, 1990, 1997, 1987, 2002, 2003, 2004, 1989, 2002, 2002 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 54, 3216, 23937, 29 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 64, 6, 74, 84, 87 ]
6
true
Family
Integrin alpha chain
Integrin alpha chain
Integrin_alpha
1
IPR000415
415
Nitroreductase-like
Nitroreductase-like
Homologous_superfamily
117,350
false
false
This domain superfamily is characteristic of nitroreductase enzymes and related oxidoreductases. Members of this family utilise FMN as a cofactor and are often found to be homodimers. Possible characteristics include Oxygen-insensitive NAD(P)H nitroreductase (FMN-dependent nitroreductase) (Dihydropteridine reductase) (...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:3.40.109.10", "SSF55469" ]
[ "", "" ]
[ 117090, 115325 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-209968", "R-DME-209968", "R-DRE-209968", "R-HSA-209968", "R-MMU-209968", "R-RNO-209968" ]
[ "REACTOME:R-CEL-209968", "REACTOME:R-DME-209968", "REACTOME:R-DRE-209968", "REACTOME:R-HSA-209968", "REACTOME:R-MMU-209968", "REACTOME:R-RNO-209968" ]
6
[ "1bkj", "1ds7", "1f5v", "1icr", "1icu", "1icv", "1idt", "1kqb", "1kqc", "1kqd", "1nec", "1nox", "1oo5", "1oo6", "1oon", "1ooq", "1v5y", "1v5z", "1vfr", "1vkw", "1yki", "1ylr", "1ylu", "1ywq", "1zch", "2b67", "2bkj", "2fre", "2h0u", "2hay", "2i7h", "2ifa"...
163
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 2509, 106467, 3, 6095, 2276 ]
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, 1, 1, 2, 5, 6, 1, 1, 4, 2, 2, 4 ]
12
true
Homologous_superfamily
Nitroreductase-like
Nitroreductase-like
Nitroreductase-like
9
IPR000416
416
Haemagglutinin outer capsid protein VP4, concanavalin-like domain
VP4_concanavalin-like
Domain
15,407
false
false
This entry represents the N-terminal concanavalin-like domain from the VP4 protein of rotavirus. The rotavirus outer capsid consists of the coat glycoprotein VP7 and the spike protein VP4. VP4 functions in cell attachment and membrane penetration. VP4 is cleaved by the host's trypsin-like proteases to produce two fragm...
[ "GO:0019058", "GO:0019028" ]
[ "viral life cycle", "viral capsid" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF00426" ]
[ "VP4_haemagglut" ]
[ 15407 ]
1
[]
[]
[]
0
[ "1kqr", "1kri", "2aen", "2dwr", "2i2s", "2p3i", "2p3j", "2p3k", "3sis", "3sit", "3tay", "3tb0", "4drr", "4drv", "4ds0", "4v7q", "4yfw", "4yfz", "4yg0", "4yg3", "4yg6", "5ca6", "5caz", "5cb7", "5gj6", "5jdb", "5vki", "5vks", "5vx4", "5vx5", "5vx8", "5vx9"...
72
[ "PUB00010692", "PUB00033183", "PUB00033184" ]
[ "11867517", "11462006", "8131735" ]
[ "The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site.", "Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* core.", "Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map...
[ 2002, 2001, 1994 ]
3
[]
[]
0
0
null
[ "Rotavirus" ]
[ 15407 ]
1
[]
[]
0
true
Domain
Haemagglutinin outer capsid protein VP4, concanavalin-like domain
Haemagglutinin outer capsid protein VP4, concanavalin-like domain
VP4_concanavalin-like
2
IPR000417
417
Hydroxyethylthiazole kinase
Hyethyz_kinase
Family
12,661
false
false
Most microorganisms and plants can synthesise thiamin de novo [ ]. In this de novo pathway, the thiazole and pyrimidine moieties of thiamin are made separately and coupled together to form thiamin phosphate. For the thiazole moiety, 4-methyl-5-(2-hydroxyethyl)thiazole (THZ), the key salvage step is phosphorylation to g...
[ "GO:0000287", "GO:0004417", "GO:0005524", "GO:0009228" ]
[ "magnesium ion binding", "hydroxyethylthiazole kinase activity", "ATP binding", "thiamine biosynthetic process" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "HAMAP", "PFAM", "PIRSF", "PRINTS", "NCBIFAM", "CDD" ]
[ "MF_00228", "PF02110", "PIRSF000513", "PR01099", "TIGR00694", "cd01170" ]
[ "Thz_kinase", "HK", "Thz_kinase", "HYETHTZKNASE", "thiM", "THZ_kinase" ]
[ 11723, 12659, 10298, 12381, 6680, 11946 ]
6
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.1.50", "GenProp1289", "GenProp1513", "GenProp1674", "GenProp1702", "PWY-6897", "PWY-7356", "PWY-7357", "PWY-8457" ]
[ "EC:2.7.1.50", "GP:GenProp1289", "GP:GenProp1513", "GP:GenProp1674", "GP:GenProp1702", "METACYC:PWY-6897", "METACYC:PWY-7356", "METACYC:PWY-7357", "METACYC:PWY-8457" ]
9
[ "1c3q", "1ekk", "1ekq", "1esj", "1esq", "3dzv", "3hpd", "3nl2", "3nl3", "3nl5", "3nl6", "3nm1", "3nm3", "5cga", "5cge", "5cm5", "5coj", "6jyy", "6k28" ]
19
[ "PUB00002882", "PUB00017550", "PUB00058768", "PUB00073180", "PUB00073181", "PUB00101306", "PUB00101307" ]
[ "7982968", "2542220", "20968298", "23816351", "19348578", "31439375", "26960569" ]
[ "Isolation and characterization of the THI6 gene encoding a bifunctional thiamin-phosphate pyrophosphorylase/hydroxyethylthiazole kinase from Saccharomyces cerevisiae.", "The thiM locus and its relation to phosphorylation of hydroxyethylthiazole in Escherichia coli.", "Domain organization in Candida glabrata TH...
[ 1994, 1989, 2010, 2013, 2009, 2019, 2016 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 406, 9769, 2422, 64 ]
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" ]
[ 4, 1, 1, 3, 1, 1, 3 ]
7
true
Family
Hydroxyethylthiazole kinase
Hydroxyethylthiazole kinase
Hyethyz_kinase
9
IPR000418
418
Ets domain
Ets_dom
Domain
37,990
false
false
Transcription factors are protein molecules that bind to specific DNA sequences in the genome, resulting in the induction or inhibition of gene transcription [ ]. The ets oncogene is such a factor, possessing a region of 85-90 amino acids known as the ETS (erythroblast transformation specific) domain [ , , ]. This doma...
[ "GO:0003700", "GO:0043565", "GO:0006355" ]
[ "DNA-binding transcription factor activity", "sequence-specific DNA binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PRINTS", "PROSITE", "PROSITE", "PROFILE", "SMART" ]
[ "PF00178", "PR00454", "PS00345", "PS00346", "PS50061", "SM00413" ]
[ "Ets", "ETSDOMAIN", "ETS_DOMAIN_1", "ETS_DOMAIN_2", "ETS_DOMAIN_3", "ETS" ]
[ 37211, 36257, 27751, 32309, 37792, 36955 ]
6
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00374", "R-BTA-2559585", "R-BTA-8939247", "R-CEL-2559585", "R-CEL-8939245", "R-DME-2151201", "R-DME-2559585", "R-DME-5687128", "R-DME-8939245", "R-DME-8939247", "R-HSA-1912408", "R-HSA-198753", "R-HSA-2151201", "R-HSA-2559585", "R-HSA-5687128", "R-HSA-8939236", "R-HSA-8939245", ...
[ "PROSITEDOC:PDOC00374", "REACTOME:R-BTA-2559585", "REACTOME:R-BTA-8939247", "REACTOME:R-CEL-2559585", "REACTOME:R-CEL-8939245", "REACTOME:R-DME-2151201", "REACTOME:R-DME-2559585", "REACTOME:R-DME-5687128", "REACTOME:R-DME-8939245", "REACTOME:R-DME-8939247", "REACTOME:R-HSA-1912408", "REACTOME:...
32
[ "1awc", "1bc7", "1bc8", "1dux", "1fli", "1gvj", "1hbx", "1k6o", "1k78", "1k79", "1k7a", "1md0", "1mdm", "1pue", "1r36", "1wwx", "1yo5", "2dao", "2lf7", "2lf8", "2md5", "2nny", "2stt", "2stw", "2ypr", "3jtg", "3mfk", "3ri4", "3wts", "3wtt", "3wtu", "3wtv"...
125
[ "PUB00001436", "PUB00001895", "PUB00001899", "PUB00010609", "PUB00014976" ]
[ "8425553", "2253872", "2163347", "12559563", "14693367" ]
[ "The Ets family of transcription factors.", "The ETS-domain: a new DNA-binding motif that recognizes a purine-rich core DNA sequence.", "Sequence-specific DNA binding of the proto-oncoprotein ets-1 defines a transcriptional activator sequence within the long terminal repeat of the Moloney murine sarcoma virus."...
[ 1993, 1990, 1990, 2003, 2004 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteriales", "Viruses", "ecological metagenomes" ]
[ 67, 37804, 114, 2, 3 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 15, 160, 24, 106, 120, 118 ]
6
true
Domain
Ets domain
Ets domain
Ets_dom
9
IPR000421
421
Coagulation factor 5/8, C-terminal domain
FA58C
Domain
89,507
false
false
Blood coagulation factors V and VIII contain a C-terminal, twice repeated, domain of about 150 amino acids, which is called F5/8 type C, FA58C, or C1/C2- like domain. In the Dictyostelium discoideum (Slime mold) cell adhesion protein discoidin, a related domain, named discoidin I-like domain, DLD, or DS, has been found...
[]
[]
[]
0
[ "PFAM", "PROSITE", "PROSITE", "PROFILE", "SMART", "CDD" ]
[ "PF00754", "PS01285", "PS01286", "PS50022", "SM00231", "cd00057" ]
[ "F5_F8_type_C", "FA58C_1", "FA58C_2", "FA58C_3", "FA58C", "FA58C" ]
[ 79316, 28418, 24530, 79248, 38034, 33558 ]
6
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00988", "R-CEL-1257604", "R-CEL-1433557", "R-CEL-1433559", "R-CEL-186763", "R-CEL-186797", "R-CEL-216083", "R-CEL-4420097", "R-CEL-5673001", "R-CEL-6811558", "R-CEL-9607240", "R-DRE-194306", "R-DRE-399954", "R-DRE-399956", "R-HSA-114608", "R-HSA-140837", "R-HSA-140875", "R-HSA...
[ "PROSITEDOC:PDOC00988", "REACTOME:R-CEL-1257604", "REACTOME:R-CEL-1433557", "REACTOME:R-CEL-1433559", "REACTOME:R-CEL-186763", "REACTOME:R-CEL-186797", "REACTOME:R-CEL-216083", "REACTOME:R-CEL-4420097", "REACTOME:R-CEL-5673001", "REACTOME:R-CEL-6811558", "REACTOME:R-CEL-9607240", "REACTOME:R-D...
72
[ "1cfg", "1czs", "1czt", "1czv", "1d7p", "1eut", "1euu", "1fac", "1gof", "1gog", "1goh", "1iqd", "1k3i", "1kex", "1sdd", "1t2x", "1tvg", "1w8n", "1w8o", "1wcq", "1xpw", "2ber", "2bzd", "2eib", "2eic", "2eid", "2eie", "2j1a", "2j1e", "2j7m", "2jd9", "2jda"...
227
[ "PUB00000383", "PUB00000416", "PUB00000770", "PUB00000771", "PUB00001120", "PUB00001468", "PUB00002850", "PUB00004623", "PUB00004819", "PUB00005035" ]
[ "8504111", "7893714", "3125864", "2110840", "8639264", "8856064", "7515064", "3092220", "8390675", "7613471" ]
[ "Determination of the disulfide bridges in factor Va light chain.", "Membrane-binding peptide from the C2 domain of factor VIII forms an amphipathic structure as determined by NMR spectroscopy.", "Blood coagulation factors V and VIII: structural and functional similarities and their relationship to hemorrhagic ...
[ 1993, 1995, 1988, 1990, 1996, 1996, 1994, 1986, 1993, 1995 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 42, 42302, 46712, 90, 361 ]
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" ]
[ 8, 4, 128, 15, 150, 67, 2, 5, 111, 4 ]
10
true
Domain
Coagulation factor 5/8, C-terminal domain
Coagulation factor 5/8, C-terminal domain
FA58C
7
IPR000422
422
3,4-dihydroxy-2-butanone 4-phosphate synthase, RibB
DHBP_synthase_RibB
Family
31,639
false
false
3,4-dihydroxy-2-butanone 4-phosphate synthase ( ) (DHBP synthase) (RibB) catalyses the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate, the latter serving as the biosynthetic precursor for the xylene ring of riboflavin [ ]. In Photobacterium leiognathi, the riboflavin synthesis ...
[ "GO:0008686", "GO:0009231" ]
[ "3,4-dihydroxy-2-butanone-4-phosphate synthase activity", "riboflavin biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "NCBIFAM" ]
[ "MF_00180", "PF00926", "TIGR00506" ]
[ "RibB", "DHBP_synthase", "ribB" ]
[ 24712, 31637, 29769 ]
3
[ "EC", "GP", "METACYC", "METACYC" ]
[ "4.1.99.12", "GenProp1734", "PWY-6167", "PWY-6168" ]
[ "EC:4.1.99.12", "GP:GenProp1734", "METACYC:PWY-6167", "METACYC:PWY-6168" ]
4
[ "1g57", "1g58", "1iez", "1k49", "1k4i", "1k4l", "1k4o", "1k4p", "1pvw", "1pvy", "1snn", "1tks", "1tku", "2ris", "2riu", "3h07", "3lqu", "3lrj", "3ls6", "3mgz", "3mio", "3mk5", "4ffj", "4i14", "4p6c", "4p6d", "4p6p", "4p77", "4p8e", "4p8j", "6mnz", "7tye"...
39
[ "PUB00003582", "PUB00043824" ]
[ "9211332", "11396941" ]
[ "Biosynthesis of riboflavin: 3,4-dihydroxy-2-butanone-4-phosphate synthase.", "Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon of Photobacterium leiognathi." ]
[ 1997, 2001 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 852, 26006, 4175, 3, 603 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 15, 1, 1, 6, 1, 1, 34 ]
7
true
Family
3,4-dihydroxy-2-butanone 4-phosphate synthase, RibB
3,4-dihydroxy-2-butanone 4-phosphate synthase, RibB
DHBP_synthase_RibB
4
IPR000424
424
Primosome PriB/single-strand DNA-binding
Primosome_PriB/ssb
Family
63,565
false
false
The Escherichia coli single-strand binding protein [ ] (gene ssb), also known as the helix-destabilising protein, is a protein of 177 amino acids. It binds tightly, as a homotetramer, to single-stranded DNA (ss-DNA) and plays an important role in DNA replication, recombination and repair. Closely related variants of SS...
[ "GO:0003697" ]
[ "single-stranded DNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "CDD" ]
[ "PF00436", "PS50935", "cd04496" ]
[ "SSB", "SSB", "SSB_OBF" ]
[ 58482, 63301, 55566 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00602", "R-CEL-9837999", "R-CEL-9913635", "R-DME-9837999", "R-DME-9913635", "R-HSA-2151201", "R-HSA-9837999", "R-HSA-9913635", "R-MMU-9837999", "R-MMU-9913635", "R-RNO-9837999", "R-RNO-9913635", "R-SCE-9837999", "R-SPO-9837999" ]
[ "PROSITEDOC:PDOC00602", "REACTOME:R-CEL-9837999", "REACTOME:R-CEL-9913635", "REACTOME:R-DME-9837999", "REACTOME:R-DME-9913635", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9913635", "REACTOME:R-MMU-9837999", "REACTOME:R-MMU-9913635", "REACTOME:R-RNO-9837999", "REACTOME:...
14
[ "1eqq", "1eyg", "1kaw", "1qvc", "1s3o", "1se8", "1sru", "1txy", "1ue1", "1ue5", "1ue6", "1ue7", "1v1q", "1woc", "1x3e", "1x3f", "1x3g", "1z9f", "2ccz", "2cwa", "2dud", "2fxq", "2ihe", "2ihf", "2pnh", "2vw9", "3a5u", "3afp", "3afq", "3eiv", "3en2", "3fhw"...
75
[ "PUB00003606", "PUB00054930", "PUB00054931" ]
[ "2087220", "8663106", "1856227" ]
[ "The single-stranded DNA-binding protein of Escherichia coli.", "The ordered assembly of the phiX174-type primosome. III. PriB facilitates complex formation between PriA and DnaT.", "The priB and priC replication proteins of Escherichia coli. Genes, DNA sequence, overexpression, and purification." ]
[ 1990, 1996, 1991 ]
3
[]
[ "IPR011344", "IPR023646" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 40, 54766, 6631, 1152, 9, 967 ]
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",...
[ 25, 1, 1, 1, 3, 7, 3, 2, 16, 7, 1, 1, 30 ]
13
true
Family
Primosome PriB/single-strand DNA-binding
Primosome PriB/single-strand DNA-binding
Primosome_PriB/ssb
2
IPR000425
425
Major intrinsic protein
MIP
Family
84,698
false
false
The major intrinsic protein (MIP) family is large and diverse, possessing over 100 members that form transmembrane channels. These channel proteins function in water, small carbohydrate (e.g., glycerol), urea, NH3, CO2 and possibly ion transport, by an energy independent mechanism. They are found ubiquitously in bacter...
[ "GO:0015267", "GO:0055085", "GO:0016020" ]
[ "channel activity", "transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PRINTS", "NCBIFAM", "CDD" ]
[ "PF00230", "PR00783", "TIGR00861", "cd00333" ]
[ "MIP", "MINTRINSICP", "MIP", "MIP" ]
[ 84432, 81202, 41513, 40660 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00193", "R-BTA-1237044", "R-BTA-1247673", "R-BTA-432040", "R-BTA-432047", "R-CFA-1237044", "R-CFA-1247673", "R-CFA-432040", "R-CFA-432047", "R-DDI-1237044", "R-DDI-1247673", "R-DDI-432040", "R-DDI-432047", "R-DME-1237044", "R-DME-1247673", "R-DME-432040", "R-DME-432047", "R-GG...
[ "PROSITEDOC:PDOC00193", "REACTOME:R-BTA-1237044", "REACTOME:R-BTA-1247673", "REACTOME:R-BTA-432040", "REACTOME:R-BTA-432047", "REACTOME:R-CFA-1237044", "REACTOME:R-CFA-1247673", "REACTOME:R-CFA-432040", "REACTOME:R-CFA-432047", "REACTOME:R-DDI-1237044", "REACTOME:R-DDI-1247673", "REACTOME:R-DD...
47
[ "1fqy", "1fx8", "1h6i", "1ih5", "1j4n", "1lda", "1ldf", "1ldi", "1rc2", "1sor", "1ymg", "1z98", "2abm", "2b5f", "2b6o", "2b6p", "2c32", "2d57", "2evu", "2f2b", "2o9d", "2o9e", "2o9f", "2o9g", "2w1p", "2w2e", "2zz9", "3c02", "3cll", "3cn5", "3cn6", "3d9s"...
96
[ "PUB00005368", "PUB00025063", "PUB00028718", "PUB00053662" ]
[ "1715617", "11039922", "11780053", "10957645" ]
[ "Tandem sequence repeats in transmembrane channel proteins.", "Structure of a glycerol-conducting channel and the basis for its selectivity.", "Structural basis of water-specific transport through the AQP1 water channel.", "Crystallization and preliminary X-ray crystallographic analysis of water channel AQP1....
[ 1991, 2000, 2001, 2000 ]
4
[]
[ "IPR015685", "IPR016697", "IPR023275", "IPR026252", "IPR034294", "IPR044222", "IPR044226", "IPR054631" ]
0
8
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 363, 28568, 55200, 8, 559 ]
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",...
[ 143, 18, 28, 24, 2, 71, 36, 1, 96, 50, 4, 1, 248 ]
13
true
Family
Major intrinsic protein
Major intrinsic protein
MIP
8
IPR000426
426
Proteasome alpha-subunit, N-terminal domain
Proteasome_asu_N
Domain
32,944
false
false
The proteasome (or macropain) ( ) [ , , , , ] is a multicatalytic proteinase complex in eukaryotes and archaea, and in some bacteria, that is involved in an ATP/ubiquitin-dependent non-lysosomal proteolytic pathway. In eukaryotes the 20S proteasome is composed of 28 distinct subunits which form a highly ordered ring-sh...
[ "GO:0006511", "GO:0019773" ]
[ "ubiquitin-dependent protein catabolic process", "proteasome core complex, alpha-subunit complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PROSITE", "SMART" ]
[ "PF10584", "PS00388", "SM00948" ]
[ "Proteasome_A_N", "PROTEASOME_ALPHA_1", "Proteasome_A_N" ]
[ 32651, 29476, 32862 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00326", "R-BTA-1169091", "R-BTA-1234176", "R-BTA-1236974", "R-BTA-1236978", "R-BTA-174084", "R-BTA-174154", "R-BTA-174178", "R-BTA-174184", "R-BTA-187577", "R-BTA-195253", "R-BTA-202424", "R-BTA-2467813", "R-BTA-2871837", "R-BTA-349425", "R-BTA-350562", "R-BTA-382556", "R-BTA-...
[ "PROSITEDOC:PDOC00326", "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1234176", "REACTOME:R-BTA-1236974", "REACTOME:R-BTA-1236978", "REACTOME:R-BTA-174084", "REACTOME:R-BTA-174154", "REACTOME:R-BTA-174178", "REACTOME:R-BTA-174184", "REACTOME:R-BTA-187577", "REACTOME:R-BTA-195253", "REACTOME:R-BTA-...
366
[ "1fnt", "1g0u", "1g65", "1iru", "1j2p", "1j2q", "1jd2", "1pma", "1ryp", "1ya7", "1yar", "1yau", "1z7q", "2f16", "2fak", "2fnc", "2gha", "2ghb", "2gpl", "2ku1", "2ku2", "2z5c", "2zcy", "3bdm", "3c91", "3c92", "3d29", "3dy3", "3dy4", "3e47", "3gpj", "3gpt"...
589
[ "PUB00000148", "PUB00000524", "PUB00001329", "PUB00004123", "PUB00005460", "PUB00030848", "PUB00080992" ]
[ "2643381", "7682410", "7697118", "1317508", "8882582", "9087403", "2535672" ]
[ "The multicatalytic proteinase of mammalian cells.", "Proteasomes: multicatalytic proteinase complexes.", "Proteasomes. Multicatalytic proteinase complexes.", "Proteolysis, proteasomes and antigen presentation.", "Proteasomes: destruction as a programme.", "Structure of 20S proteasome from yeast at 2.4 A ...
[ 1989, 1993, 1993, 1992, 1996, 1997, 1989 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1263, 40, 31584, 57 ]
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...
[ 40, 7, 10, 16, 39, 33, 7, 29, 34, 7, 7, 71 ]
12
true
Domain
Proteasome alpha-subunit, N-terminal domain
Proteasome alpha-subunit, N-terminal domain
Proteasome_asu_N
7
IPR000429
429
Proteinase inhibitor I14, hirudin
Prot_inh_hirudin
Family
37
false
false
The hirudin family are proteinase inhibitors that belong to MEROPS inhibitor family I14, clan IM. Hirudin is a potent thrombin inhibitor secreted by the salivary glands of the Hirudinaria manillensis (Buffalo leech) and Hirudo medicinalis (Medicinal leech) [ ]. It forms a stable non-covalent complex with alpha-thrombin...
[ "GO:0004867" ]
[ "serine-type endopeptidase inhibitor activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PIRSF", "PRINTS" ]
[ "PF00713", "PIRSF001640", "PR00777" ]
[ "Hirudin", "Hirudin", "HIRUDIN" ]
[ 36, 33, 34 ]
3
[]
[]
[]
0
[ "1hic", "1hrt", "1ihs", "2hir", "2joo", "2pw8", "3htc", "4hir", "4htc", "4mlf", "5hir", "6hir", "7a0d", "7a0e", "7a0f" ]
15
[ "PUB00004614" ]
[ "3513162" ]
[ "Cloning and expression of a cDNA coding for the anticoagulant hirudin from the bloodsucking leech, Hirudo medicinalis." ]
[ 1986 ]
1
[]
[]
0
0
null
[ "Opisthokonta" ]
[ 37 ]
1
[]
[]
0
true
Family
Proteinase inhibitor I14, hirudin
Proteinase inhibitor I14, hirudin
Prot_inh_hirudin
4
IPR000431
431
5-Hydroxytryptamine 5B receptor
5HT5B_rcpt
Family
144
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:0007186", "GO:0016020" ]
[ "G protein-coupled serotonin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00519" ]
[ "5HT5BRECEPTR" ]
[ 144 ]
1
[]
[]
[]
0
[]
0
[ "PUB00064376", "PUB00064499", "PUB00064501", "PUB00064503", "PUB00064508", "PUB00064509", "PUB00064586", "PUB00066704" ]
[ "18476671", "16846620", "8450829", "7682702", "11343685", "11295248", "15921820", "11989819" ]
[ "Serotonin receptors.", "SB-699551-A (3-cyclopentyl-N-[2-(dimethylamino)ethyl]-N-[(4'-{[(2-phenylethyl)amino]methyl}-4-biphenylyl)methyl]propanamide dihydrochloride), a novel 5-ht5A receptor-selective antagonist, enhances 5-HT neuronal function: Evidence for an autoreceptor role for the 5-ht5A receptor in guinea ...
[ 2008, 2006, 1993, 1993, 2001, 2001, 2005, 2002 ]
8
[ "IPR002231" ]
[]
1
0
1
[ "Amniota" ]
[ 144 ]
1
[ "Mus musculus", "Rattus norvegicus" ]
[ 2, 2 ]
2
true
Family
5-Hydroxytryptamine 5B receptor
5-Hydroxytryptamine 5B receptor
5HT5B_rcpt
8
IPR000433
433
Zinc finger, ZZ-type
Znf_ZZ
Domain
55,405
false
false
This entry represents ZZ-type zinc finger domains, named because of their ability to bind two zinc ions [ ]. These domains contain 4-6 Cys residues that participate in zinc binding (plus additional Ser/His residues), including a Cys-X2-Cys motif found in other zinc finger domains. These zinc fingers are thought to be i...
[ "GO:0008270" ]
[ "zinc ion binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PFAM", "PROSITE", "PROFILE", "SMART" ]
[ "PF00569", "PF25299", "PS01357", "PS50135", "SM00291" ]
[ "ZZ", "ZZ_ADA2", "ZF_ZZ_1", "ZF_ZZ_2", "ZnF_ZZ" ]
[ 46165, 5794, 42474, 51141, 48808 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50135", "R-BTA-9772755", "R-CEL-112382", "R-CEL-113418", "R-CEL-1234158", "R-CEL-201722", "R-CEL-3899300", "R-CEL-5250924", "R-CEL-5689901", "R-CEL-5696395", "R-CEL-5696400", "R-CEL-674695", "R-CEL-6781823", "R-CEL-6782135", "R-CEL-6782210", "R-CEL-6796648", "R-CEL-6798695", "...
[ "PROSITEDOC:PDOC50135", "REACTOME:R-BTA-9772755", "REACTOME:R-CEL-112382", "REACTOME:R-CEL-113418", "REACTOME:R-CEL-1234158", "REACTOME:R-CEL-201722", "REACTOME:R-CEL-3899300", "REACTOME:R-CEL-5250924", "REACTOME:R-CEL-5689901", "REACTOME:R-CEL-5696395", "REACTOME:R-CEL-5696400", "REACTOME:R-C...
234
[ "1tot", "2dip", "2e5r", "2fc7", "2n1a", "4xi6", "4xi7", "4xib", "5u7g", "5yp7", "5yp8", "5ypa", "5ypb", "5ypc", "5ype", "5ypf", "5ypg", "5yph", "6cw2", "6cw3", "6ds6", "6e83", "6e86", "6k15", "6khz", "6kw3", "6kw4", "6kw5", "6miu", "6mj7", "6tda", "6v8o"...
70
[ "PUB00005449", "PUB00014077", "PUB00031525", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812", "PUB00035845", "PUB00042936", "PUB00042937", "PUB00073506", "PUB00073507" ]
[ "8848831", "12665246", "15476823", "17210253", "15963892", "15718139", "10529348", "11179890", "16522193", "15705950", "17009962", "11777910", "19279142" ]
[ "ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins.", "Zinc fingers--folds for many occasions.", "ZZ domain of CBP: an unusual zinc finger fold in a protein interaction module.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc fi...
[ 1996, 2002, 2004, 2007, 2005, 2005, 1999, 2001, 2006, 2005, 2007, 2002, 2009 ]
13
[]
[ "IPR041981", "IPR041983", "IPR041984", "IPR041986", "IPR041987", "IPR042056" ]
0
6
0
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 4, 55388, 6, 7 ]
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...
[ 77, 21, 161, 48, 107, 77, 3, 28, 100, 2, 4, 125 ]
12
true
Domain
Zinc finger, ZZ-type
Zinc finger, ZZ-type
Znf_ZZ
6
IPR000434
434
Polycystic kidney disease type 1 protein
PC1
Family
1,621
false
false
Polycystin-1 (PC1) plays a critical role in renal tubule diameter control. Mutations in the polycystin-1 gene cause cyst formation in human autosomal dominant polycystic kidney disease [ , ]. It may serve as a cell surface signaling receptor at cell-cell/cell-matrix junctions and as a mechano-sensor in renal primary ci...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR00500" ]
[ "POLYCYSTIN1" ]
[ 1621 ]
1
[ "REACTOME", "REACTOME" ]
[ "R-HSA-5620916", "R-MMU-5620916" ]
[ "REACTOME:R-HSA-5620916", "REACTOME:R-MMU-5620916" ]
2
[ "6a70", "8z6b", "8z6f", "8z6h", "8zkh", "8zkr", "8zks", "8zkt", "8zku" ]
9
[ "PUB00033611", "PUB00071542", "PUB00071543", "PUB00071544" ]
[ "12482949", "17525154", "8554072", "22508176" ]
[ "Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations.", "Characterization of cis-autoproteolysis of polycystin-1, the product of human polycystic kidney disease 1 gene.", "Screening the 3' region of the...
[ 2002, 2007, 1996, 2012 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 17, 1604 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 11, 6, 4 ]
4
true
Family
Polycystic kidney disease type 1 protein
Polycystic kidney disease type 1 protein
PC1
1
IPR000435
435
Tektins
Tektins
Family
7,999
false
false
This entry represents the tektins family. Its members include tektin 1-5, tektin-B1.
[ "GO:0060294" ]
[ "cilium movement involved in cell motility" ]
[ "biological_process" ]
1
[ "PRINTS", "PANTHER" ]
[ "PR00511", "PTHR19960" ]
[ "TEKTIN", "" ]
[ 5631, 7956 ]
2
[]
[]
[]
0
[ "7rro", "7ung", "8i7o", "8i7r", "8iyj", "8j07", "8otz", "8snb", "8to0", "9cpb", "9cpc", "9fqr" ]
12
[ "PUB00070939", "PUB00070940", "PUB00070942" ]
[ "18671835", "3282233", "24521320" ]
[ "The tektin family of microtubule-stabilizing proteins.", "Evidence for tektins in centrioles and axonemal microtubules.", "Localization of Tektin 1 at both acrosome and flagella of mouse and bull spermatozoa." ]
[ 2008, 1988, 2014 ]
3
[ "IPR048256" ]
[]
1
0
1
[ "Bacteria", "Eukaryota" ]
[ 2, 7997 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 7, 7, 25, 15, 13 ]
6
true
Family
Tektins
Tektins
Tektins
5
IPR000436
436
Sushi/SCR/CCP domain
Sushi_SCR_CCP_dom
Domain
85,490
false
false
The extracellular sushi domain is characterised by a consensus sequence spanning ~60 residues containing four invariant cysteine residues forming two disulfide-bridges (I-III and II-IV), a highly conserved tryptophan, and conserved glycine, proline, and hydrophobic residues [ ]. Sushi domains are known to be involved i...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART", "CDD" ]
[ "PF00084", "PS50923", "SM00032", "cd00033" ]
[ "Sushi", "SUSHI", "CCP", "CCP" ]
[ 78104, 83272, 79931, 81798 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50923", "R-BTA-166663", "R-BTA-173736", "R-BTA-174577", "R-BTA-1971475", "R-BTA-2022870", "R-BTA-2022923", "R-BTA-2024101", "R-BTA-202733", "R-BTA-3000178", "R-BTA-381426", "R-BTA-8957275", "R-BTA-977606", "R-CFA-114608", "R-DME-114608", "R-DME-202733", "R-DME-373080", "R-DME-...
[ "PROSITEDOC:PDOC50923", "REACTOME:R-BTA-166663", "REACTOME:R-BTA-173736", "REACTOME:R-BTA-174577", "REACTOME:R-BTA-1971475", "REACTOME:R-BTA-2022870", "REACTOME:R-BTA-2022923", "REACTOME:R-BTA-2024101", "REACTOME:R-BTA-202733", "REACTOME:R-BTA-3000178", "REACTOME:R-BTA-381426", "REACTOME:R-BTA...
148
[ "1c1z", "1ckl", "1e5g", "1elv", "1ghq", "1gkg", "1gkn", "1gpz", "1h03", "1h04", "1h2p", "1h2q", "1haq", "1hcc", "1hfh", "1hfi", "1ly2", "1m11", "1md7", "1md8", "1ntj", "1ntl", "1nwv", "1ojv", "1ojw", "1ojy", "1ok1", "1ok2", "1ok3", "1ok9", "1ppq", "1q3x"...
241
[ "PUB00006163", "PUB00018393", "PUB00018395" ]
[ "1829116", "2751824", "10775260" ]
[ "Three-dimensional structure of a complement control protein module in solution.", "Structure-function relationships of the complement components.", "Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle." ]
[ 1991, 1989, 2000 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "viral metagenome" ]
[ 19, 85165, 305, 1 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 20, 273, 123, 391, 180, 277 ]
6
true
Domain
Sushi/SCR/CCP domain
Sushi/SCR/CCP domain
Sushi_SCR_CCP_dom
8
IPR000438
438
Acetyl-CoA carboxylase carboxyl transferase, beta subunit
Acetyl_CoA_COase_Trfase_b_su
Family
42,336
false
false
Fatty acid synthesis involves a set of reactions, starting with carboxylation of acetyl-CoA to malonyl-CoA. This is an irreversible reaction, catalysed by the acetyl-CoA carboxylase complex ( ); a heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and two non-identical carboxyl transferase subunits (a...
[ "GO:0003989", "GO:0006633", "GO:0009317" ]
[ "acetyl-CoA carboxylase activity", "fatty acid biosynthetic process", "acetyl-CoA carboxylase complex" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PRINTS", "NCBIFAM" ]
[ "MF_01395", "PR01070", "TIGR00515" ]
[ "AcetylCoA_CT_beta", "ACCCTRFRASEB", "accD" ]
[ 29880, 41244, 27940 ]
3
[ "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
[ "1on3", "1on9", "1x0u", "1xnv", "1xnw", "1xny", "1xo6", "2f9i", "2f9y", "3iav", "3ib9", "3ibb", "3mfm", "5inf", "5ing", "5ini", "5kdr", "8uxz", "8uz2", "9e4n", "9e4o", "9j0c" ]
22
[ "PUB00002735" ]
[ "1355089" ]
[ "The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase." ]
[ 1992 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 296, 26094, 15471, 475 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus" ]
[ 9, 1, 2, 1 ]
4
true
Family
Acetyl-CoA carboxylase carboxyl transferase, beta subunit
Acetyl-CoA carboxylase carboxyl transferase, beta subunit
Acetyl_CoA_COase_Trfase_b_su
1
IPR000439
439
Large ribosomal subunit protein eL15
Ribosomal_eL15
Family
7,022
false
false
A number of eukaryotic and archaebacterial ribosomal proteins can be grouped on the basis of sequence similarities [ ]. One of these families consists of: Mammalian eL15. Insect eL15. Plant eL15. Yeast YL10 (L13) (Rp15r). Archaebacterial eL15 (known as L15e). These proteins have about 200 amino acid residues. Ribosomes...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER", "SMART" ]
[ "PF00827", "PTHR11847", "SM01384" ]
[ "Ribosomal_L15e", "", "Ribosomal_L15e" ]
[ 7010, 6882, 6925 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00919", "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:PDOC00919", "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...
65
[ "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"...
679
[ "PUB00000245", "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "7733938", "11297922", "11290319", "11114498" ]
[ "The Thermoplasma acidophilum rpl15 gene encodes a homologue of eukaryotic ribosomal proteins L15/YL10.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]
[ 1995, 2001, 2001, 2000 ]
4
[]
[ "IPR020926" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 920, 5, 6043, 54 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 7, 1, 1, 2, 12, 4, 1, 10, 7, 2, 2, 24 ]
12
true
Family
Large ribosomal subunit protein eL15
Large ribosomal subunit protein eL15
Ribosomal_eL15
3
IPR000440
440
NADH:ubiquinone/plastoquinone oxidoreductase, chain 3
NADH_UbQ/plastoQ_OxRdtase_su3
Family
65,714
false
false
This family contains chain 3 of the NADH-ubiquinone / plastoquinone oxidoreductase.
[ "GO:0008137" ]
[ "NADH dehydrogenase (ubiquinone) activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PANTHER" ]
[ "PF00507", "PTHR11058" ]
[ "Oxidored_q4", "" ]
[ 65672, 64485 ]
2
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "7.1.1.-", "GenProp0135", "GenProp1198", "GenProp1254", "GenProp1341", "GenProp1537", "GenProp1583", "GenProp1608", "GenProp1751", "R-BTA-5419276", "R-BTA-611105", "R-BTA-6799198", "R-CEL-5419276", "R-DME-5419276", "R-DME-611105", "R-DME-6799198", "R-DRE-611105", "R-GGA-5419276", ...
[ "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-BTA-611105", "REACTOME:R-BTA-6799198", "REACTOME:R-CEL-5419276", "REACTOME:R-DME-5419276", "...
32
[ "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"...
326
[ "PUB00005074", "PUB00043561", "PUB00045437" ]
[ "1470679", "10940377", "18394423" ]
[ "The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.", "The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.", "Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)." ]
[ 1992, 2000, 2008 ]
3
[]
[ "IPR023043" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 663, 18057, 46419, 575 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 8, 2, 1, 3, 1, 431, 5, 1, 8, 4, 4 ]
11
true
Family
NADH:ubiquinone/plastoquinone oxidoreductase, chain 3
NADH:ubiquinone/plastoquinone oxidoreductase, chain 3
NADH_UbQ/plastoQ_OxRdtase_su3
3
IPR000443
443
Islet amyloid polypeptide
IAPP
Family
709
false
false
Islet amyloid polypeptide (IAPP) (also known as diabetes-associated peptide or amylin) is a pancreatic islet hormone that is stored with insulin in beta cell granules [ ]. IAPP has a propensity to form islet cell-disrupting amyloid deposits, and opposes the action of insulin in peripheral tissues; the peptide may there...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR00818" ]
[ "ISLETAMYLOID" ]
[ 709 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-419812", "R-HSA-210745", "R-HSA-418555", "R-HSA-419812", "R-HSA-977225", "R-MMU-418555", "R-MMU-419812", "R-RNO-419812" ]
[ "REACTOME:R-CFA-419812", "REACTOME:R-HSA-210745", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-419812", "REACTOME:R-HSA-977225", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-419812", "REACTOME:R-RNO-419812" ]
8
[ "2g48", "2kb8", "2kj7", "2l86", "3hgz", "5k5g", "5mgq", "6ucj", "6uck", "6vw2", "6y1a", "6zrf", "6zrq", "6zrr", "7m61", "7m62", "7m64", "7m65", "7tyf", "7tyi", "7tyl", "7tyx", "7tzf", "7ykw", "7yl0", "7yl3", "7yl7", "8awt", "8az0", "8az1", "8az2", "8az3"...
67
[ "PUB00000189", "PUB00000497", "PUB00004696" ]
[ "2192709", "2039456", "2690069" ]
[ "Canine IAPP cDNA sequence provides important clues regarding diabetogenesis and amyloidogenesis in type 2 diabetes.", "Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin.", "Molecular and functional characterization of amylin, a peptide associated wit...
[ 1990, 1991, 1989 ]
3
[ "IPR021117" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 709 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 3, 1, 2 ]
4
true
Family
Islet amyloid polypeptide
Islet amyloid polypeptide
IAPP
2
IPR000445
445
Helix-hairpin-helix motif
HhH_motif
Conserved_site
50,208
false
false
The HhH motif is a stretch of approximately 20 amino acids that is present in prokaryotic and eukaryotic non-sequence-specific DNA binding proteins [ , , ]. The HhH motif is similar to, but distinct from, the HtH motif. Both of these motifs have two helices connected by a short turn. In the HtH motif the second helix b...
[ "GO:0003677" ]
[ "DNA binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00633" ]
[ "HHH" ]
[ 50208 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-110329", "R-BTA-110357", "R-CEL-110329", "R-CEL-110357", "R-GGA-110329", "R-HSA-110328", "R-HSA-110329", "R-HSA-110330", "R-HSA-110331", "R-HSA-110357", "R-HSA-9608287", "R-HSA-9608290", "R-HSA-9630221", "R-HSA-9630222", "R-MMU-110329", "R-MMU-110331", "R-MMU-110357", "R-RNO...
[ "REACTOME:R-BTA-110329", "REACTOME:R-BTA-110357", "REACTOME:R-CEL-110329", "REACTOME:R-CEL-110357", "REACTOME:R-GGA-110329", "REACTOME:R-HSA-110328", "REACTOME:R-HSA-110329", "REACTOME:R-HSA-110330", "REACTOME:R-HSA-110331", "REACTOME:R-HSA-110357", "REACTOME:R-HSA-9608287", "REACTOME:R-HSA-96...
21
[ "1kg2", "1kg3", "1kg4", "1kg5", "1kg6", "1kg7", "1kqj", "1mud", "1mun", "1muy", "1orn", "1orp", "1p59", "1rrq", "1rrs", "1vrl", "1wef", "1weg", "1wei", "2abk", "3c1y", "3c1z", "3c21", "3c23", "3g0q", "3n5n", "4yoq", "4yph", "4ypr", "4yvz", "4yxj", "4yxm"...
51
[ "PUB00004467", "PUB00006160", "PUB00006161", "PUB00006162" ]
[ "8692686", "9973609", "7664751", "9987128" ]
[ "The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA.", "Conserved domains in DNA repair proteins and evolution of repair systems.", "Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure.", "ComEA is a DNA receptor for tran...
[ 1996, 1999, 1995, 1999 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1360, 41664, 6428, 756 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 6, 1, 1, 2, 2, 25, 6, 2, 2, 8, 1, 2, 8 ]
13
true
Conserved_site
Helix-hairpin-helix motif
Helix-hairpin-helix motif
HhH_motif
2
IPR000448
448
Rhabdovirus nucleocapsid
Rhabdo_ncapsid
Domain
13,632
false
false
The Nucleocapsid (N) Protein is said to have a 'tight' structure. The carboxyl end of the N-terminal domain possesses an RNA binding domain. Sequence alignments show 2 regions of reasonable conservation, approx. 64-103 and 201-329 [ ]. A whole functional protein is required for encapsidation to take place [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF00945" ]
[ "Rhabdo_ncap" ]
[ 13632 ]
1
[]
[]
[]
0
[ "2gic", "2gtt", "2qvj", "2wyy", "3hhw", "3hhz", "3pmk", "3pto", "3ptx", "3pu0", "3pu1", "3pu4", "5uk4", "5ukb", "6bjy", "7umk", "7uml", "7uws", "7xpn", "7yg7", "8b8v", "8ffr", "8fwl", "8u0a", "8u0b" ]
25
[ "PUB00003173", "PUB00005627" ]
[ "9603315", "9501055" ]
[ "Identification of a region of the rabies virus N protein involved in direct binding to the viral RNA.", "The specificity of rabies virus RNA encapsidation by nucleoprotein." ]
[ 1998, 1998 ]
2
[]
[]
0
0
null
[ "Protostomia", "Riboviria" ]
[ 190, 13442 ]
2
[]
[]
0
true
Domain
Rhabdovirus nucleocapsid
Rhabdovirus nucleocapsid
Rhabdo_ncapsid
7
IPR000450
450
5-Hydroxytryptamine 1F receptor
5HT1F_rcpt
Family
589
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...
[]
[]
[]
0
[ "CDD" ]
[ "cd15334" ]
[ "7tmA_5-HT1F" ]
[ 589 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "5", "R-HSA-390666", "R-HSA-418594", "R-MMU-390666", "R-MMU-418594", "R-RNO-390666", "R-RNO-418594" ]
[ "IUPHAR:5", "REACTOME:R-HSA-390666", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-390666", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-390666", "REACTOME:R-RNO-418594" ]
7
[ "7exd" ]
1
[ "PUB00064376", "PUB00064431", "PUB00064433", "PUB00064434", "PUB00064435", "PUB00066704" ]
[ "18476671", "8380639", "10374714", "8384716", "11072640", "11989819" ]
[ "Serotonin receptors.", "Cloning of another human serotonin receptor (5-HT1F): a fifth 5-HT1 receptor subtype coupled to the inhibition of adenylate cyclase.", "Characterisation of 5-HT receptors in human coronary arteries by molecular and pharmacological techniques.", "Molecular cloning and functional expres...
[ 2008, 1993, 1999, 1993, 2000, 2002 ]
6
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 589 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 4 ]
3
true
Family
5-Hydroxytryptamine 1F receptor
5-Hydroxytryptamine 1F receptor
5HT1F_rcpt
8
IPR000451
451
NF-kappa-B/Dorsal
NFkB/Dor
Family
7,773
false
false
The transcription factor NF-kB (Nuclear Factor-kappaB) was first identified as a DNA-binding protein specific for the 10-base pair kB site in the immunoglobulin k light-chain enhancer of B lymphocytes [ ], but has subsequently been found in many different cell types. NF-kB represents a group of structurally related pro...
[ "GO:0003700", "GO:0006355", "GO:0005737" ]
[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription", "cytoplasm" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS", "PANTHER" ]
[ "PR00057", "PTHR24169" ]
[ "NFKBTNSCPFCT", "" ]
[ 7111, 7706 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00924", "R-CFA-1169091", "R-CFA-1810476", "R-CFA-193692", "R-CFA-202424", "R-CFA-209560", "R-CFA-2871837", "R-CFA-3134963", "R-CFA-3214841", "R-CFA-445989", "R-CFA-448706", "R-CFA-5607764", "R-CFA-5621575", "R-CFA-5684264", "R-CFA-6798695", "R-CFA-9020702", "R-CFA-933542", "R-...
[ "PROSITEDOC:PDOC00924", "REACTOME:R-CFA-1169091", "REACTOME:R-CFA-1810476", "REACTOME:R-CFA-193692", "REACTOME:R-CFA-202424", "REACTOME:R-CFA-209560", "REACTOME:R-CFA-2871837", "REACTOME:R-CFA-3134963", "REACTOME:R-CFA-3214841", "REACTOME:R-CFA-445989", "REACTOME:R-CFA-448706", "REACTOME:R-CFA...
112
[ "1a3q", "1bfs", "1bft", "1bvo", "1gji", "1ikn", "1k3z", "1le5", "1le9", "1lei", "1my5", "1my7", "1nfi", "1nfk", "1ooa", "1oy3", "1ram", "1svc", "1u36", "1u3j", "1u3y", "1u3z", "1u41", "1u42", "1vkx", "1zk9", "1zka", "2i9t", "2o61", "2ram", "2v2t", "3do7"...
61
[ "PUB00000613", "PUB00004200", "PUB00063589", "PUB00073034", "PUB00073035" ]
[ "2018779", "7530332", "17114415", "15371334", "22302935" ]
[ "The inducible transcription activator NF-kappa B: regulation by distinct protein subunits.", "Structure of NF-kappa B p50 homodimer bound to a kappa B site.", "Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 1986. 46: 705-716.", "Signaling to NF-kappaB.", "NF-κB, the firs...
[ 1991, 1995, 2006, 2004, 2012 ]
5
[]
[ "IPR011363" ]
0
1
0
[ "Avian reticuloendotheliosis virus", "Opisthokonta" ]
[ 1, 7772 ]
2
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 16, 8, 33, 30, 25 ]
5
true
Family
NF-kappa-B/Dorsal
NF-kappa-B/Dorsal
NFkB/Dor
4
IPR000452
452
Kappa opioid receptor
Kappa_opi_rcpt
Family
706
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:0038048", "GO:0007186", "GO:0016020" ]
[ "dynorphin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00532" ]
[ "KAPPAOPIOIDR" ]
[ 706 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "318", "R-BTA-375276", "R-BTA-418594", "R-HSA-375276", "R-HSA-418594", "R-HSA-9022699", "R-MMU-375276", "R-MMU-418594", "R-RNO-375276", "R-RNO-418594" ]
[ "IUPHAR:318", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-418594", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-9022699", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594" ]
10
[ "6b73", "6vi4", "7y1f", "7yit", "8dzp", "8dzq", "8dzr", "8dzs", "8f7w", "8feg", "8vve", "8vvf", "8vvg", "9d61", "9mqk", "9mql" ]
16
[ "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
[ "IPR001418" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 706 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 3, 2 ]
3
true
Family
Kappa opioid receptor
Kappa opioid receptor
Kappa_opi_rcpt
5
IPR000453
453
Chorismate synthase
Chorismate_synth
Family
29,488
false
false
Chorismate synthase (CS; 5-enolpyruvylshikimate-3-phosphate phospholyase; 1-carboxyvinyl-3-phosphoshikimate phosphate-lyase; E.C. 4.2.3.5) catalyzes the seventh and final step in the shikimate pathway which is used in prokaryotes, fungi and plants for the biosynthesis of aromatic amino acids. It catalyzes the 1,4-trans...
[ "GO:0004107", "GO:0009073" ]
[ "chorismate synthase activity", "aromatic amino acid family biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00300", "PF01264", "PIRSF001456", "PTHR21085", "TIGR00033", "cd07304" ]
[ "Chorismate_synth", "Chorismate_synt", "Chorismate_synth", "", "aroC", "Chorismate_synthase" ]
[ 27649, 29481, 27013, 29390, 27936, 28050 ]
6
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "METACYC", "PROSITEDOC", "REACTOME" ]
[ "4.2.3.5", "GenProp0001", "GenProp1234", "GenProp1291", "GenProp1309", "GenProp1478", "GenProp1538", "GenProp1550", "PWY-6163", "PDOC00628", "R-MTU-964903" ]
[ "EC:4.2.3.5", "GP:GenProp0001", "GP:GenProp1234", "GP:GenProp1291", "GP:GenProp1309", "GP:GenProp1478", "GP:GenProp1538", "GP:GenProp1550", "METACYC:PWY-6163", "PROSITEDOC:PDOC00628", "REACTOME:R-MTU-964903" ]
11
[ "1q1l", "1qxo", "1r52", "1r53", "1sq1", "1um0", "1umf", "1ztb", "2g85", "2o11", "2o12", "2qhf", "4bai", "4baj", "4ecd", "4lj2", "4o90", "4ob9", "5wuy", "5z9a", "7rca" ]
21
[ "PUB00002667", "PUB00003811", "PUB00030073", "PUB00030439", "PUB00030526", "PUB00031826", "PUB00039012", "PUB00079715", "PUB00079716", "PUB00079717", "PUB00079718", "PUB00079719" ]
[ "1718979", "1837329", "14705034", "14656434", "14573601", "15095868", "16459102", "17348836", "17662045", "8674765", "18279385", "17326665" ]
[ "Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers.", "Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae.", "Crystal structure of chorismate syntha...
[ 1991, 1991, 2004, 2003, 2004, 2004, 2006, 2007, 2007, 1996, 2008, 2007 ]
12
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Pandoravirus", "unclassified sequences" ]
[ 833, 24687, 3277, 6, 685 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 6, 1, 1, 3, 1, 1, 21 ]
7
true
Family
Chorismate synthase
Chorismate synthase
Chorismate_synth
2
IPR000454
454
ATP synthase, F0 complex, subunit C
ATP_synth_F0_csu
Family
46,957
false
false
This entry represents subunit C (also called subunit 9, or proteolipid) found in the F0 complex of F-ATPases. Ten C subunits form an oligomeric ring that makes up the F0 rotor. The flux of protons through the ATPase channel drives the rotation of the C subunit ring, which in turn is coupled to the rotation of the F1 co...
[ "GO:0015078", "GO:0015986", "GO:0045259" ]
[ "proton transmembrane transporter activity", "proton motive force-driven ATP synthesis", "proton-transporting ATP synthase complex" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PRINTS", "PANTHER" ]
[ "MF_01396", "PR00124", "PTHR10031" ]
[ "ATP_synth_c_bact", "ATPASEC", "" ]
[ 43936, 45905, 31932 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00526", "R-BTA-1268020", "R-BTA-163210", "R-BTA-8949613", "R-CEL-1268020", "R-CEL-163210", "R-CEL-8949613", "R-DDI-1268020", "R-HSA-1268020", "R-HSA-163210", "R-HSA-8949613", "R-MMU-1268020", "R-MMU-163210", "R-MMU-8949613", "R-RNO-1268020", "R-RNO-163210", "R-RNO-8949613" ]
[ "PROSITEDOC:PDOC00526", "REACTOME:R-BTA-1268020", "REACTOME:R-BTA-163210", "REACTOME:R-BTA-8949613", "REACTOME:R-CEL-1268020", "REACTOME:R-CEL-163210", "REACTOME:R-CEL-8949613", "REACTOME:R-DDI-1268020", "REACTOME:R-HSA-1268020", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "REACTOME:R-M...
17
[ "1a91", "1aty", "1c0v", "1c17", "1c99", "1ijp", "1l6t", "1qo1", "1wu0", "1yce", "2w5j", "2wgm", "2wie", "2wpd", "2x2v", "2xnd", "2xok", "2xqs", "2xqt", "2xqu", "3u2f", "3u2y", "3u32", "3ud0", "3v3c", "3zk1", "3zk2", "3zo6", "3zry", "4b2q", "4bem", "4cbj"...
319
[ "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020632", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]
[ "11309608", "15473999", "15078220", "14630314", "20450191", "18937357", "1385979", "9741106" ]
[ "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disciplinary approach.", "Mechanics of coupling proto...
[ 2001, 2004, 2004, 2003, 2010, 2008, 1992, 1998 ]
8
[]
[ "IPR005953" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 197, 23935, 22346, 479 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 10, 1, 3, 3, 1, 10, 5, 2, 9, 14, 1, 1, 5 ]
13
true
Family
ATP synthase, F0 complex, subunit C
ATP synthase, F0 complex, subunit C
ATP_synth_F0_csu
4
IPR000455
455
5-Hydroxytryptamine 2A receptor
5HT2A_rcpt
Family
747
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:0007186", "GO:0005886" ]
[ "G protein-coupled serotonin receptor activity", "G protein-coupled receptor signaling pathway", "plasma membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00516" ]
[ "5HT2ARECEPTR" ]
[ 747 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "6", "R-CFA-390666", "R-CFA-416476", "R-HSA-390666", "R-HSA-416476", "R-MMU-390666", "R-MMU-416476", "R-RNO-390666", "R-RNO-416476" ]
[ "IUPHAR:6", "REACTOME:R-CFA-390666", "REACTOME:R-CFA-416476", "REACTOME:R-HSA-390666", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-390666", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-390666", "REACTOME:R-RNO-416476" ]
9
[ "6wha", "7ran", "8uwl", "8v6u", "9arx", "9ary", "9arz", "9as0", "9as1", "9as2", "9as3", "9as4", "9as5", "9as6", "9as7", "9as8", "9as9", "9asa" ]
18
[ "PUB00064376", "PUB00064385", "PUB00064437", "PUB00064440", "PUB00064441", "PUB00064442", "PUB00064443", "PUB00064444", "PUB00064445", "PUB00064446", "PUB00064447", "PUB00064448", "PUB00064449", "PUB00064450", "PUB00064451", "PUB00064464", "PUB00064465", "PUB00064466", "PUB000667...
[ "18476671", "7796165", "16803859", "9555012", "10216183", "11672605", "16277612", "14754868", "11517239", "19324062", "17728034", "11027922", "18621097", "2779889", "12417689", "1580230", "11960784", "9491270", "11989819" ]
[ "Serotonin receptors.", "The distribution of 5-HT1A and 5-HT2A receptor mRNA in human brain.", "Functional selectivity and classical concepts of quantitative pharmacology.", "Localization of 5-HT2A receptor in rat cerebral cortex and olfactory system revealed by immunohistochemistry using two antibodies raise...
[ 2008, 1995, 2007, 1998, 1999, 2001, 2005, 2004, 2001, 2009, 2008, 2000, 2008, 1989, 2002, 1992, 2002, 1997, 2002 ]
19
[ "IPR002231" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 747 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 7, 2, 2 ]
4
true
Family
5-Hydroxytryptamine 2A receptor
5-Hydroxytryptamine 2A receptor
5HT2A_rcpt
3
IPR000456
456
Large ribosomal subunit protein bL17
Ribosomal_bL17
Family
29,578
false
false
This entry represents ribosomal subunit protein bL17 family from bacteria and eukaryotes. Large ribosomal subunit protein bL17 (also known as L17) is one of the proteins from the large ribosomal subunit. Bacterial L17 is a protein of 120 to 130 amino-acid residues while yeast YmL8 is twice as large (238 residues). The ...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]
[ "MF_01368", "PF01196", "PTHR14413", "TIGR00059" ]
[ "Ribosomal_bL17", "Ribosomal_L17", "", "L17" ]
[ 24610, 29558, 29409, 27454 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00897", "R-BTA-5389840", "R-BTA-5419276", "R-BTA-9937383", "R-HSA-5368286", "R-HSA-5389840", "R-HSA-5419276", "R-HSA-9937383", "R-MMU-5389840", "R-MMU-5419276", "R-MMU-9937383", "R-RNO-5389840", "R-RNO-5419276", "R-RNO-9937383" ]
[ "PROSITEDOC:PDOC00897", "REACTOME:R-BTA-5389840", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-9937383", "REACTOME:R-HSA-5368286", "REACTOME:R-HSA-5389840", "REACTOME:R-HSA-5419276", "REACTOME:R-HSA-9937383", "REACTOME:R-MMU-5389840", "REACTOME:R-MMU-5419276", "REACTOME:R-MMU-9937383", "REACTOME:...
14
[ "1gd8", "1nkw", "1nwx", "1nwy", "1sm1", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xbp", "2cqm", "2ftc", "2j28", "2rdo", "2zjp", "2zjq", "2zjr", "3bbx", "3cf5", "3dll", "3iy9", "3j3v", "3j3w", "3j5l", "3j6b", "3j7y", "3j7z", "3j8g", "3j9m", "3j9w", "3j9y"...
1,267
[ "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "11297922", "11290319", "11114498" ]
[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]
[ 2001, 2001, 2000 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "candidate division MSBL1 archaeon SCGC-AAA382N08", "unclassified sequences" ]
[ 23836, 5215, 1, 526 ]
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",...
[ 14, 1, 1, 1, 1, 2, 4, 1, 8, 6, 1, 1, 10 ]
13
true
Family
Large ribosomal subunit protein bL17
Large ribosomal subunit protein bL17
Ribosomal_bL17
1
IPR000458
458
Mucin-like glycoprotein
Tryp_mucin
Family
2,348
false
false
This family of trypanosomal proteins resemble vertebrate mucins. The protein consists of three regions. The N and C terminii are conserved between all members of the family, whereas the central region is not well conserved and contains a large number of threonine residues which can be glycosylated [ ]. Indirect evidenc...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01456" ]
[ "Mucin" ]
[ 2348 ]
1
[]
[]
[]
0
[]
0
[ "PUB00002922" ]
[ "7592617" ]
[ "The protozoan Trypanosoma cruzi has a family of genes resembling the mucin genes of mammalian cells." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2348 ]
1
[]
[]
0
true
Family
Mucin-like glycoprotein
Mucin-like glycoprotein
Tryp_mucin
3
IPR000460
460
Neuroligin
Nlgn
Family
6,103
false
false
Neuroligins (NLGNs) interact with the neurexin family members and are involved in the modulation of synaptic transmission [ ]. Mammals have four Nlgn proteins, with the Nlgn3 and Nlgn4 gene in humans localised to the X-chromosome. In humans, the Nlgn4 gene is complemented on the Y-chromosome by a similar Nlgn5 gene [ ]...
[ "GO:0042043", "GO:0016020" ]
[ "neurexin family protein binding", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01090" ]
[ "NEUROLIGIN" ]
[ 6103 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-6794361", "R-MMU-6794361", "R-RNO-6794361" ]
[ "REACTOME:R-HSA-6794361", "REACTOME:R-MMU-6794361", "REACTOME:R-RNO-6794361" ]
3
[ "2wqz", "2xb6", "3b3q", "3be8", "3biw", "3bix", "3bl8", "3vkf", "5oj6", "5ojk", "5v5v", "5xeq", "7cee", "7ceg", "8g7d", "8g7y", "8g7z", "8g80", "8g81", "8gs3", "8gs4" ]
21
[ "PUB00071363", "PUB00071472" ]
[ "18923512", "17275284" ]
[ "Neuroligins and neurexins link synaptic function to cognitive disease.", "Neurexin-neuroligin signaling in synapse development." ]
[ 2008, 2007 ]
2
[]
[]
0
0
null
[ "Bilateria" ]
[ 6103 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 56, 21, 13, 14 ]
4
true
Family
Neuroligin
Neuroligin
Nlgn
8
IPR000462
462
CDP-alcohol phosphatidyltransferase
CDP-OH_P_trans
Family
95,650
false
false
A number of phosphatidyltransferases, which are all involved in phospholipid biosynthesis and that share the property of catalysing the displacement of CMP from a CDP-alcohol by a second alcohol with formation of a phosphodiester bond and concomitant breaking of a phosphoride anhydride bond share a conserved sequence r...
[ "GO:0016780", "GO:0008654", "GO:0016020" ]
[ "phosphotransferase activity, for other substituted phosphate groups", "phospholipid biosynthetic process", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF01066" ]
[ "CDP-OH_P_transf" ]
[ 95650 ]
1
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.8", "GenProp0724", "GenProp1252", "GenProp1351", "GenProp1352", "GenProp1548", "GenProp1627", "GenProp1758", "PDOC00321", "R-BTA-1483191", "R-BTA-1483213", "R-CEL-1482925", "R-CEL-1483076", "R-DDI-1483191", "R-DDI-1483213", "R-DME-1482925", "R-DME-1483076", "R-DME-1483226", ...
[ "EC:2.7.8", "GP:GenProp0724", "GP:GenProp1252", "GP:GenProp1351", "GP:GenProp1352", "GP:GenProp1548", "GP:GenProp1627", "GP:GenProp1758", "PROSITEDOC:PDOC00321", "REACTOME:R-BTA-1483191", "REACTOME:R-BTA-1483213", "REACTOME:R-CEL-1482925", "REACTOME:R-CEL-1483076", "REACTOME:R-DDI-1483191"...
47
[ "4mnd", "4o6m", "4o6n", "4q7c", "5d91", "5d92", "6h53", "6h59", "6h5a", "6wm5", "6wmv", "7b1k", "7b1l", "7b1n", "7drj", "7drk", "7pow", "8ero", "8erp", "8gyw", "8gyx", "8ul9", "8urp", "8urt", "9uet" ]
25
[ "PUB00002448", "PUB00002684", "PUB00151491" ]
[ "3031032", "1848238", "29958934" ]
[ "Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae.", "sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPT1 and EPT1 gene products.", "Schizosaccharomyc...
[ 1987, 1991, 2018 ]
3
[]
[ "IPR004533", "IPR004570", "IPR014387", "IPR014472", "IPR026027", "IPR044268", "IPR044270" ]
0
7
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 2048, 67870, 23704, 24, 2004 ]
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",...
[ 27, 5, 13, 17, 3, 20, 22, 6, 15, 20, 5, 4, 62 ]
13
true
Family
CDP-alcohol phosphatidyltransferase
CDP-alcohol phosphatidyltransferase
CDP-OH_P_trans
8
IPR000463
463
Cytosolic fatty-acid binding
Fatty_acid-bd
Domain
17,642
false
false
The Fatty Acid-Binding Proteins (FABPs) are a family of proteins that are principally located in the cytosol and are characterised by the ability to bind to hydrophobic ligands, such as fatty acids, retinol, retinoic acid, bile salts and pigments [ , ]. Recently, a number of family members have been identified that are...
[ "GO:0008289" ]
[ "lipid binding" ]
[ "molecular_function" ]
1
[ "PRINTS", "PROSITE" ]
[ "PR00178", "PS00214" ]
[ "FATTYACIDBP", "FABP" ]
[ 17257, 12508 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00188", "R-BTA-163560", "R-BTA-189483", "R-BTA-400206", "R-BTA-5362517", "R-BTA-5365859", "R-BTA-6798695", "R-BTA-9707564", "R-CEL-159418", "R-CEL-163560", "R-CEL-189483", "R-CEL-2453902", "R-CEL-5362517", "R-CEL-5365859", "R-CEL-6798695", "R-CEL-975634", "R-DRE-163560", "R-DR...
[ "PROSITEDOC:PDOC00188", "REACTOME:R-BTA-163560", "REACTOME:R-BTA-189483", "REACTOME:R-BTA-400206", "REACTOME:R-BTA-5362517", "REACTOME:R-BTA-5365859", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-9707564", "REACTOME:R-CEL-159418", "REACTOME:R-CEL-163560", "REACTOME:R-CEL-189483", "REACTOME:R-CEL-...
60
[ "1a18", "1a2d", "1a57", "1ab0", "1acd", "1adl", "1ael", "1alb", "1b4m", "1b56", "1blr", "1bm5", "1bwy", "1cbi", "1cbq", "1cbr", "1cbs", "1crb", "1dc9", "1eal", "1eii", "1eio", "1fdq", "1fe3", "1ftp", "1g5w", "1g74", "1g7n", "1ggl", "1hmr", "1hms", "1hmt"...
750
[ "PUB00000681", "PUB00003643", "PUB00003644", "PUB00027738" ]
[ "3129018", "2266965", "2266967", "8422392" ]
[ "A survey on cytosolic non-enzymic proteins involved in the metabolism of lipophilic compounds: from organic anion binders to new protein families.", "Cellular fatty acid-binding proteins: current concepts and future directions.", "Historic overview of studies on fatty acid-binding proteins.", "Ligand-protein...
[ 1987, 1990, 1990, 1993 ]
4
[ "IPR000566" ]
[]
1
0
1
[ "Bacteria", "Eukaryota" ]
[ 18, 17624 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 12, 28, 4, 40, 30, 51 ]
6
true
Domain
Cytosolic fatty-acid binding
Cytosolic fatty-acid binding
Fatty_acid-bd
1
IPR000466
466
Adenosine A3 receptor
Adeno_A3_rcpt
Family
1,229
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" ]
[ "PR00555" ]
[ "ADENOSINEA3R" ]
[ 1229 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "21", "R-BTA-417973", "R-BTA-418594", "R-CFA-417973", "R-CFA-418594", "R-HSA-417973", "R-HSA-418594", "R-MMU-417973", "R-MMU-418594", "R-RNO-417973", "R-RNO-418594" ]
[ "IUPHAR:21", "REACTOME:R-BTA-417973", "REACTOME:R-BTA-418594", "REACTOME:R-CFA-417973", "REACTOME:R-CFA-418594", "REACTOME:R-HSA-417973", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-417973", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-417973", "REACTOME:R-RNO-418594" ]
11
[ "8x16", "8x17", "9ebh", "9ebi", "9ehs" ]
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
[ "Euteleostomi" ]
[ 1229 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 5, 5 ]
3
true
Family
Adenosine A3 receptor
Adenosine A3 receptor
Adeno_A3_rcpt
4
IPR000467
467
G-patch domain
G_patch_dom
Domain
56,953
false
false
The G-patch domain is an approximately 48 amino acid domain, which is found in a single copy in several RNA-associated proteins and in type D retroviral polyproteins. It is widespread among eukaryotes but is absent in archaea and bacteria. The G-patch domain has been called after its most notable feature, the presence ...
[ "GO:0003676" ]
[ "nucleic acid binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF01585", "PS50174", "SM00443" ]
[ "G-patch", "G_PATCH", "G_patch" ]
[ 52006, 56445, 48691 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50174", "R-CEL-72163", "R-DME-72163", "R-HSA-6802952", "R-HSA-72163", "R-HSA-72203", "R-MMU-72163", "R-MMU-72203", "R-RNO-72163", "R-RNO-72203", "R-SPO-72163", "R-SPO-72203" ]
[ "PROSITEDOC:PDOC50174", "REACTOME:R-CEL-72163", "REACTOME:R-DME-72163", "REACTOME:R-HSA-6802952", "REACTOME:R-HSA-72163", "REACTOME:R-HSA-72203", "REACTOME:R-MMU-72163", "REACTOME:R-MMU-72203", "REACTOME:R-RNO-72163", "REACTOME:R-RNO-72203", "REACTOME:R-SPO-72163", "REACTOME:R-SPO-72203" ]
12
[ "5y88", "6sh6", "6sh7", "7dco", "7dcp", "7dcr", "7dd3", "7dvq", "7qtt", "8ch6", "8ejm", "8gxl", "8gxm", "8p4e", "8p4f", "8rdy", "8ro0", "8ro1", "8ro2", "8w8f", "9esh", "9esi", "9l5r", "9l5s", "9l5t" ]
25
[]
[]
[]
[]
0
[]
[ "IPR026822" ]
0
1
0
[ "Bacteria", "Eukaryota", "Methanobacterium veterum", "Riboviria", "unclassified sequences" ]
[ 27, 56863, 1, 56, 6 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 88, 16, 40, 38, 100, 56, 9, 39, 84, 5, 7, 81 ]
12
true
Domain
G-patch domain
G-patch domain
G_patch_dom
5
IPR000468
468
Barstar (barnase inhibitor)
Barstar
Domain
8,766
false
false
Barstar is a small single chain protein. Barnase is the extracellular ribonuclease of Bacillus amyloliquefaciens, and barstar its specific intracellular inhibitor [ , ]. Expression of barstar is necessary to counter the lethal effect of expressed active barnase. The structure of the barstar consists of two layers of pa...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01337" ]
[ "Barstar" ]
[ 8766 ]
1
[]
[]
[]
0
[ "1a19", "1ab7", "1ay7", "1b27", "1b2s", "1b2u", "1b3s", "1bgs", "1brs", "1bta", "1btb", "1x1u", "1x1w", "1x1x", "1x1y", "2cx6", "2hxx", "2za4", "3da7", "5f4c", "6pqk", "7mrx" ]
22
[ "PUB00000403", "PUB00003231", "PUB00005346" ]
[ "8043575", "3050134", "2696173" ]
[ "Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution.", "Barnase and barstar. Expression of its cloned inhibitor permits expression of a cloned ribonuclease.", "Barnase and barstar: two small proteins to fold and fit together." ]
[ 1994, 1988, 1989 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "metagenomes" ]
[ 8686, 25, 19, 36 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Barstar (barnase inhibitor)
Barstar (barnase inhibitor)
Barstar
4
IPR000469
469
G-protein alpha subunit, group 12/13
Gprotein_alpha_12/13
Family
2,742
false
false
Guanine nucleotide binding proteins (G-proteins) are membrane-associated, heterotrimeric proteins composed of three subunits: alpha ( ), beta ( ) and gamma ( ) [ ]. G proteins and their receptors (GPCRs) form one of the most prevalent signalling systems in mammalian cells, regulating systems as diverse as sensory perce...
[ "GO:0001664", "GO:0003924", "GO:0007186", "GO:0007266" ]
[ "G protein-coupled receptor binding", "GTPase activity", "G protein-coupled receptor signaling pathway", "Rho protein signal transduction" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]
4
[ "PRINTS" ]
[ "PR00440" ]
[ "GPROTEINA12" ]
[ 2742 ]
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-193648", "R-CEL-416482", "R-CEL-428930", "R-CEL-456926", "R-CEL-9013148", "R-CEL-9013149", "R-DME-193648", "R-DME-416482", "R-DME-428930", "R-DME-9013148", "R-DME-9013149", "R-HSA-193648", "R-HSA-416482", "R-HSA-428930", "R-HSA-456926", "R-HSA-9013148", "R-HSA-9013149", "R-M...
[ "REACTOME:R-CEL-193648", "REACTOME:R-CEL-416482", "REACTOME:R-CEL-428930", "REACTOME:R-CEL-456926", "REACTOME:R-CEL-9013148", "REACTOME:R-CEL-9013149", "REACTOME:R-DME-193648", "REACTOME:R-DME-416482", "REACTOME:R-DME-428930", "REACTOME:R-DME-9013148", "REACTOME:R-DME-9013149", "REACTOME:R-HSA...
28
[ "1zca", "1zcb", "3ab3", "3cx6", "3cx7", "3cx8", "7sf7", "7sf8", "7t6b", "7wy0", "7wz7", "7x10", "7ydh", "7ydj", "8h8j", "8ikl", "8kgg", "8zme", "8zx4", "8zx5", "9e51", "9ge2", "9ge3", "9ite", "9iy8", "9izh", "9jhp", "9v0u" ]
28
[ "PUB00005142", "PUB00015166", "PUB00015168", "PUB00015169", "PUB00015170", "PUB00015171", "PUB00015172", "PUB00015174" ]
[ "1902986", "15294442", "15119945", "14762218", "11313912", "9278091", "11882385", "14607242" ]
[ "Diversity of G proteins in signal transduction.", "G protein activation by G protein coupled receptors: ternary complex formation or catalyzed reaction?", "Biochemistry of transmembrane signaling mediated by trimeric G proteins.", "G protein signaling: insights from new structures.", "Regulation of G prote...
[ 1991, 2004, 2004, 2004, 2001, 1997, 2002, 2003 ]
8
[ "IPR001019" ]
[]
1
0
1
[ "Eukaryota" ]
[ 2742 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 7, 2, 3, 7, 7 ]
6
true
Family
G-protein alpha subunit, group 12/13
G-protein alpha subunit, group 12/13
Gprotein_alpha_12/13
2
IPR000471
471
Interferon alpha/beta/delta
Interferon_alpha/beta/delta
Family
6,166
false
false
null
[ "GO:0005126", "GO:0006952", "GO:0005576" ]
[ "cytokine receptor binding", "defense response", "extracellular region" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PRINTS", "PROSITE", "PANTHER", "SMART", "CDD" ]
[ "PF00143", "PR00266", "PS00252", "PTHR11691", "SM00076", "cd00095" ]
[ "Interferon", "INTERFERONAB", "INTERFERON_A_B_D", "", "IFabd", "IFab" ]
[ 6155, 3976, 3426, 5967, 5244, 2264 ]
6
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00225", "R-CFA-909733", "R-CFA-912694", "R-GGA-909733", "R-GGA-912694", "R-HSA-2559580", "R-HSA-909733", "R-HSA-912694", "R-HSA-918233", "R-HSA-933541", "R-HSA-9705671", "R-HSA-983231", "R-HSA-9833109", "R-MMU-909733", "R-MMU-912694", "R-RNO-909733", "R-RNO-912694" ]
[ "PROSITEDOC:PDOC00225", "REACTOME:R-CFA-909733", "REACTOME:R-CFA-912694", "REACTOME:R-GGA-909733", "REACTOME:R-GGA-912694", "REACTOME:R-HSA-2559580", "REACTOME:R-HSA-909733", "REACTOME:R-HSA-912694", "REACTOME:R-HSA-918233", "REACTOME:R-HSA-933541", "REACTOME:R-HSA-9705671", "REACTOME:R-HSA-98...
17
[ "1au1", "1b5l", "1ifa", "1itf", "1rh2", "1wu3", "2hym", "2kz1", "2lag", "2lms", "3oq3", "3piv", "3piw", "3s9d", "3se3", "3se4", "3ux9", "3wcy", "4ypg", "4z5r", "6jhd", "7e0e", "7wkh", "7wz5", "8irq", "9gvl", "9gvo", "9gw5" ]
28
[ "PUB00001107", "PUB00004593", "PUB00081575" ]
[ "3022999", "6170983", "10547147" ]
[ "Molecular cloning and expression in Escherichia coli of equine type I interferons.", "DNA sequence of a major human leukocyte interferon gene.", "The type I interferon receptor: structure, function, and evolution of a family business." ]
[ 1986, 1981, 1999 ]
3
[]
[]
0
0
null
[ "Bacteria", "Metazoa" ]
[ 2, 6164 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 8, 51, 51, 32 ]
4
true
Family
Interferon alpha/beta/delta
Interferon alpha/beta/delta
Interferon_alpha/beta/delta
1
IPR000472
472
Activin types I and II receptor domain
Activin_recp
Domain
14,218
false
false
This is a hydrophilic cysteine-rich ligand-binding domain found in both TGF-beta receptor types (type I and II). In both types, this domain posses a 9 amino acid cysteine box, with the the consensus CCX{4-5}CN. The type I receptors also possess 7 extracellular residues preceding the cysteine box [ , , ]. The Transformi...
[ "GO:0004675", "GO:0016020" ]
[ "transmembrane receptor protein serine/threonine kinase activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF01064" ]
[ "Activin_recp" ]
[ 14218 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.11.30", "R-BTA-2173788", "R-BTA-2173789", "R-BTA-2173791", "R-BTA-5689880", "R-BTA-9839389", "R-DME-1502540", "R-DME-201451", "R-DME-2173788", "R-DME-2173789", "R-DME-2173791", "R-DME-5689880", "R-DME-9839389", "R-HSA-1181150", "R-HSA-1433617", "R-HSA-1502540", "R-HSA-201451", ...
[ "EC:2.7.11.30", "REACTOME:R-BTA-2173788", "REACTOME:R-BTA-2173789", "REACTOME:R-BTA-2173791", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-9839389", "REACTOME:R-DME-1502540", "REACTOME:R-DME-201451", "REACTOME:R-DME-2173788", "REACTOME:R-DME-2173789", "REACTOME:R-DME-2173791", "REACTOME:R-DME-568...
41
[ "1bte", "1es7", "1lx5", "1nys", "1nyu", "1rew", "1s4y", "2goo", "2h62", "2h64", "2hlq", "2hlr", "2k3g", "2l5s", "2pjy", "2qj9", "2qja", "2qjb", "3evs", "3kfd", "3nh7", "3qb4", "4fao", "5ngv", "5nh3", "5nhr", "6mac", "7l0j", "7mrz", "7oly", "7ppa", "7ppb"...
41
[ "PUB00001067", "PUB00001915", "PUB00004493", "PUB00005725", "PUB00005768", "PUB00005778", "PUB00073004" ]
[ "9309176", "8299934", "8397373", "8047140", "8909794", "9023056", "9759503" ]
[ "From receptor to nucleus: the Smad pathway.", "The TGF-beta superfamily: new members, new receptors, and new genetic tests of function in different organisms.", "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity.", "Mechanism of activati...
[ 1997, 1994, 1993, 1994, 1996, 1996, 1998 ]
7
[]
[]
0
0
null
[ "Metazoa" ]
[ 14218 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 40, 25, 41, 30, 52 ]
6
true
Domain
Activin types I and II receptor domain
Activin types I and II receptor domain
Activin_recp
2
IPR000473
473
Large ribosomal subunit protein bL36
Ribosomal_bL36
Family
37,500
false
false
Ribosomal protein bL36 (also known as L36) is the smallest protein from the large subunit of the prokaryotic ribosome. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities can be grouped into: bacterial L36; algal and plant chloroplast L36; Cyanelle L36; fungal and animal L36. L36 i...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PFAM", "PROSITE", "PANTHER", "NCBIFAM" ]
[ "MF_00251", "PF00444", "PS00828", "PTHR42888", "TIGR01022" ]
[ "Ribosomal_bL36", "Ribosomal_L36", "RIBOSOMAL_L36", "", "rpmJ_bact" ]
[ 36540, 37429, 32008, 26534, 35899 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00650", "R-DRE-5389840", "R-DRE-5419276", "R-HSA-5368286", "R-HSA-5389840", "R-HSA-5419276", "R-HSA-9937383", "R-MMU-5389840", "R-MMU-5419276", "R-MMU-9937383", "R-RNO-5389840", "R-RNO-5419276", "R-RNO-9937383" ]
[ "PROSITEDOC:PDOC00650", "REACTOME:R-DRE-5389840", "REACTOME:R-DRE-5419276", "REACTOME:R-HSA-5368286", "REACTOME:R-HSA-5389840", "REACTOME:R-HSA-5419276", "REACTOME:R-HSA-9937383", "REACTOME:R-MMU-5389840", "REACTOME:R-MMU-5419276", "REACTOME:R-MMU-9937383", "REACTOME:R-RNO-5389840", "REACTOME:...
13
[ "1dfe", "1dgz", "1nkw", "1nwx", "1nwy", "1sm1", "1vy4", "1vy5", "1vy6", "1vy7", "1xbp", "2j28", "2rdo", "2zjp", "2zjq", "2zjr", "3bbx", "3cf5", "3dll", "3j5l", "3j6b", "3j7y", "3j7z", "3j8g", "3j9m", "3j9w", "3j9y", "3j9z", "3ja1", "3jbu", "3jbv", "3jcd"...
1,106
[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00104109" ]
[ "11297922", "11290319", "11114498", "32559334" ]
[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "YkgM and YkgO maintain translation by replacing their paralogs, zinc-binding ribosomal proteins L31 and L36, with identical activities." ]
[ 2001, 2001, 2000, 2020 ]
4
[]
[ "IPR047621" ]
0
1
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 20999, 16322, 179 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 4, 1, 1, 1, 3, 1, 1, 1, 5, 1, 1, 1, 11 ]
13
true
Family
Large ribosomal subunit protein bL36
Large ribosomal subunit protein bL36
Ribosomal_bL36
7
IPR000475
475
Retroviral Vif (Viral infectivity) protein
Vif
Family
21,799
false
false
The virion infectivity factor (vif) is an accessory protein, which is essential for HIV replication in host cells. Vif of Human immunodeficiency virus 1 (HIV-1) affects the infectivity of virus particles [ ] to T lymphocytes and macrophages (in some cases increasing the infectivity of HIV-1 particles by 100- to 1000-fo...
[ "GO:0019058" ]
[ "viral life cycle" ]
[ "biological_process" ]
1
[ "HAMAP", "PFAM", "PRINTS" ]
[ "MF_04081", "PF00559", "PR00349" ]
[ "HIV_VIF", "Vif", "VIRIONINFFCT" ]
[ 17385, 21799, 21024 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-162585", "R-HSA-162588", "R-HSA-162592", "R-HSA-162594", "R-HSA-164516", "R-HSA-164525", "R-HSA-164843", "R-HSA-173107", "R-HSA-175474", "R-HSA-175567", "R-HSA-177539", "R-HSA-180585", "R-HSA-180689", "R-HSA-180910" ]
[ "REACTOME:R-HSA-162585", "REACTOME:R-HSA-162588", "REACTOME:R-HSA-162592", "REACTOME:R-HSA-162594", "REACTOME:R-HSA-164516", "REACTOME:R-HSA-164525", "REACTOME:R-HSA-164843", "REACTOME:R-HSA-173107", "REACTOME:R-HSA-175474", "REACTOME:R-HSA-175567", "REACTOME:R-HSA-177539", "REACTOME:R-HSA-180...
14
[ "2ma9", "3dcg", "4n9f", "6nil", "6p59", "8cx0", "8cx1", "8cx2", "8e40", "8fvi", "8fvj", "8h0i", "8j62", "8szk" ]
14
[ "PUB00003492", "PUB00003498", "PUB00005104", "PUB00014092", "PUB00093483", "PUB00093484", "PUB00093485", "PUB00093486" ]
[ "1995946", "1357189", "3497453", "14618252", "24586532", "30961890", "25408426", "30941116" ]
[ "A specific inhibitor of cysteine proteases impairs a Vif-dependent modification of human immunodeficiency virus type 1 Env protein.", "Role of vif in replication of human immunodeficiency virus type 1 in CD4+ T lymphocytes.", "The sor gene of HIV-1 is required for efficient virus transmission in vitro.", "Th...
[ 1991, 1992, 1987, 2003, 2014, 2019, 2015, 2019 ]
8
[]
[]
0
0
null
[ "Actinomycetes", "Lentivirus" ]
[ 2, 21797 ]
2
[]
[]
0
true
Family
Retroviral Vif (Viral infectivity) protein
Retroviral Vif (Viral infectivity) protein
Vif
3
IPR000476
476
Glycoprotein hormone alpha chain
Glyco_hormone
Family
1,532
false
false
Glycoprotein hormones [ , ] (or gonadotropins) are a family of proteins, which include the mammalian hormones follitropin (FSH), lutropin (LSH), thyrotropin(TSH) placental chorionic gonadotropins hCG and eCG [ ] and chorionic gonadotropin (CG), as well as at least two forms of fish gonadotropins. These hormones are cen...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PRINTS", "PROSITE", "PROSITE", "PROFILE", "PANTHER", "SMART" ]
[ "PF00236", "PR00274", "PS00779", "PS00780", "PS50277", "PTHR11509", "SM00067" ]
[ "Hormone_6", "GLYCOHORMONE", "GLYCO_HORMONE_ALPHA_1", "GLYCO_HORMONE_ALPHA_2", "GLYCO_HORMONE_ALPHA_3", "", "GHA" ]
[ 1257, 1092, 1041, 980, 1528, 1092, 1092 ]
7
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00623", "R-BTA-193048", "R-BTA-193993", "R-BTA-209822", "R-BTA-209968", "R-BTA-375281", "R-BTA-418555", "R-BTA-8866910", "R-BTA-975578", "R-HSA-193048", "R-HSA-193993", "R-HSA-209822", "R-HSA-209968", "R-HSA-375281", "R-HSA-418555", "R-HSA-8866910", "R-HSA-975578", "R-MMU-1930...
[ "PROSITEDOC:PDOC00623", "REACTOME:R-BTA-193048", "REACTOME:R-BTA-193993", "REACTOME:R-BTA-209822", "REACTOME:R-BTA-209968", "REACTOME:R-BTA-375281", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-8866910", "REACTOME:R-BTA-975578", "REACTOME:R-HSA-193048", "REACTOME:R-HSA-193993", "REACTOME:R-HSA-209...
39
[ "1dz7", "1e9j", "1fl7", "1hcn", "1hd4", "1hrp", "1qfw", "1xwd", "4ay9", "4mqw", "7fig", "7fih", "7fii", "7t9i", "7utz", "7xw5", "8i2g" ]
17
[ "PUB00000033", "PUB00000517", "PUB00001110", "PUB00002390", "PUB00004177", "PUB00004333" ]
[ "6267989", "1445230", "1713773", "6177696", "8202136", "6314263" ]
[ "Glycoprotein hormones: structure and function.", "Molecular structures of glycoprotein hormones and functions of their carbohydrate components.", "Molecular cloning of the rhesus glycoprotein hormone alpha-subunit gene.", "alpha Subunit of rat pituitary glycoprotein hormones. Primary structure of the precurs...
[ 1981, 1992, 1991, 1982, 1994, 1983 ]
6
[]
[]
0
0
null
[ "Eumetazoa" ]
[ 1532 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 10, 5, 6 ]
4
true
Family
Glycoprotein hormone alpha chain
Glycoprotein hormone alpha chain
Glyco_hormone
2
IPR000477
477
Reverse transcriptase domain
RT_dom
Domain
818,713
false
false
The use of an RNA template to produce DNA, for integration into the host genome and exploitation of a host cell, is a strategy employed in the replication of retroid elements, such as the retroviruses and bacterial retrons. The enzyme catalysing polymerisation is an RNA-directed DNA-polymerase, or reverse trancriptase ...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF00078", "PS50878" ]
[ "RVT_1", "RT_POL" ]
[ 794049, 712318 ]
2
[ "EC", "EC", "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "2.7.7.49", "2.7.7.7", "3.1.26", "PDOC50878", "R-HSA-162585", "R-HSA-162588", "R-HSA-162592", "R-HSA-162594", "R-HSA-164516", "R-HSA-164525", "R-HSA-164843", "R-HSA-171319", "R-HSA-173107", "R-HSA-175474", "R-HSA-175567", "R-HSA-177539", "R-HSA-180689", "R-HSA-180910", "R-HSA-201...
[ "EC:2.7.7.49", "EC:2.7.7.7", "EC:3.1.26", "PROSITEDOC:PDOC50878", "REACTOME:R-HSA-162585", "REACTOME:R-HSA-162588", "REACTOME:R-HSA-162592", "REACTOME:R-HSA-162594", "REACTOME:R-HSA-164516", "REACTOME:R-HSA-164525", "REACTOME:R-HSA-164843", "REACTOME:R-HSA-171319", "REACTOME:R-HSA-173107", ...
24
[ "1bqm", "1bqn", "1c0t", "1c0u", "1c1b", "1c1c", "1d0e", "1d1u", "1dlo", "1dtq", "1dtt", "1eet", "1ep4", "1fk9", "1fko", "1fkp", "1har", "1hmv", "1hni", "1hnv", "1hpz", "1hqe", "1hqu", "1hvu", "1hys", "1i6j", "1ikv", "1ikw", "1ikx", "1iky", "1j5o", "1jkh"...
636
[ "PUB00006358", "PUB00012846", "PUB00070025" ]
[ "8828137", "1377403", "12758069" ]
[ "Structure, function, and evolution of bacterial reverse transcriptase.", "Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor.", "Reverse transcriptase and reverse splicing activities encoded by the mobile group II intron cobI1 of fission yeast mitochondrial DNA." ]
[ 1995, 1992, 2003 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "IncL/M plasmid R471a", "Viruses", "unclassified sequences" ]
[ 306, 30317, 357094, 1, 430320, 675 ]
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",...
[ 199, 7, 242, 68, 1, 54, 29, 1, 2054, 42, 5, 15, 220 ]
13
true
Domain
Reverse transcriptase domain
Reverse transcriptase domain
RT_dom
6
IPR000479
479
Cation-independent mannose-6-phosphate receptor repeat
CIMR_rpt
Repeat
2,280
false
false
The cation-independent mannose-6-phosphate receptor is a multi-functional transmembrane glycoprotein whose major function is to bind and transport M6P-bearing glycoproteins from the trans-Golgi network or the cell surface to lysosomes. It appears to mediate the uptake and processing of M6P-containing cytokines and pept...
[ "GO:0005537", "GO:0038023", "GO:0007041" ]
[ "D-mannose binding", "signaling receptor activity", "lysosomal transport" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF00878" ]
[ "CIMR" ]
[ 2280 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-432722", "R-HSA-6798695", "R-HSA-6811440", "R-HSA-8856825", "R-HSA-8856828", "R-MMU-432722", "R-MMU-6798695", "R-MMU-6811440", "R-MMU-8856825", "R-MMU-8856828" ]
[ "REACTOME:R-HSA-432722", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-6811440", "REACTOME:R-HSA-8856825", "REACTOME:R-HSA-8856828", "REACTOME:R-MMU-432722", "REACTOME:R-MMU-6798695", "REACTOME:R-MMU-6811440", "REACTOME:R-MMU-8856825", "REACTOME:R-MMU-8856828" ]
10
[ "1e6f", "1gp0", "1gp3", "1gqb", "1q25", "1syo", "1sz0", "2cnj", "2kva", "2kvb", "2l21", "2l29", "2l2a", "2l2g", "2lla", "2m68", "2m6t", "2v5n", "2v5o", "2v5p", "5iei", "6p8i", "6um1", "6um2", "6v02", "6z30", "6z31", "6z32" ]
28
[ "PUB00004007", "PUB00087233", "PUB00087234" ]
[ "2957598", "16779663", "19251055" ]
[ "Insulin-like growth factor II receptor as a multifunctional binding protein.", "Mannose-6-phosphate/insulin-like growth factor II receptor expression and tumor development.", "Insulin-like growth factor-2/mannose-6 phosphate receptors." ]
[ 1987, 2006, 2009 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2280 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 5, 6, 8, 9 ]
5
true
Repeat
Cation-independent mannose-6-phosphate receptor repeat
Cation-independent mannose-6-phosphate receptor repeat
CIMR_rpt
4
IPR000480
480
Glutelin
Glutelin
Family
60
false
false
Glutelins are major storage proteins that aggregate in protein bodies in the endosperm of Zea mays (Maize) [ , ]. They comprise the second largest protein fraction in Maize endosperm [ ] (zeins being the largest), and show sequence similarities to other cereal storage proteins, such as gliadins, glutenins, hordeins, et...
[ "GO:0045735" ]
[ "nutrient reservoir activity" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR00211" ]
[ "GLUTELIN" ]
[ 60 ]
1
[]
[]
[]
0
[]
0
[ "PUB00004334", "PUB00004575" ]
[ "3839076", "16668595" ]
[ "Nucleic acid (cDNA) and amino acid sequences of the maize endosperm protein glutelin-2.", "Nucleotide Sequence of a cDNA Clone Encoding gamma-Coixin from Coix lacryma-jobi Seeds." ]
[ 1985, 1991 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 15, 45 ]
2
[ "Zea mays" ]
[ 17 ]
1
true
Family
Glutelin
Glutelin
Glutelin
6
IPR000481
481
GPCR fungal pheromone B alpha receptor
GPCR_Pheromne_B_alpha_rcpt
Family
1,033
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:0004934", "GO:0007186", "GO:0016020" ]
[ "mating-type alpha-factor pheromone receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00901" ]
[ "PHEROMONEBAR" ]
[ 1033 ]
1
[]
[]
[]
0
[]
0
[ "PUB00001139", "PUB00001274", "PUB00001736", "PUB00004338", "PUB00004657", "PUB00004961", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "16453635", "7489716", "8978100", "3001640", "2836861", "8170923", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Nucleotide sequences of STE2 and STE3, cell type-specific sterile genes from Saccharomyces cerevisiae.", "The mating-type locus B alpha 1 of Schizophyllum commune contains a pheromone receptor gene and putative pheromone genes.", "Allelic divergence at B alpha 1 pheromone receptor genes of Schizophyllum commun...
[ 1985, 1995, 1996, 1985, 1988, 1994, 2003, 1994, 2005, 2009, 2006, 2013 ]
12
[ "IPR001499" ]
[]
1
0
1
[ "Agaricomycetes" ]
[ 1033 ]
1
[]
[]
0
true
Family
GPCR fungal pheromone B alpha receptor
GPCR fungal pheromone B alpha receptor
GPCR_Pheromne_B_alpha_rcpt
3
IPR000482
482
5-Hydroxytryptamine 2B receptor
5HT2B_rcpt
Family
790
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:0007507", "GO:0042310", "GO:0050795", "GO:0016020" ]
[ "G protein-coupled serotonin receptor activity", "smooth muscle contraction", "G protein-coupled receptor signaling pathway", "heart development", "vasoconstriction", "regulation of behavior", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
7
[ "PRINTS" ]
[ "PR00651" ]
[ "5HT2BRECEPTR" ]
[ 790 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "7", "R-HSA-390666", "R-HSA-416476", "R-MMU-390666", "R-MMU-416476", "R-RNO-390666", "R-RNO-416476" ]
[ "IUPHAR:7", "REACTOME:R-HSA-390666", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-390666", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-390666", "REACTOME:R-RNO-416476" ]
7
[ "5tud", "7srr", "9jgk" ]
3
[ "PUB00064376", "PUB00064437", "PUB00064468", "PUB00064469", "PUB00064470", "PUB00064471", "PUB00064472", "PUB00064476", "PUB00064477", "PUB00064478", "PUB00064479", "PUB00064480", "PUB00066704" ]
[ "18476671", "16803859", "1331748", "8706927", "8078486", "11413089", "18511249", "12244304", "19118279", "19307114", "18337424", "16461587", "11989819" ]
[ "Serotonin receptors.", "Functional selectivity and classical concepts of quantitative pharmacology.", "Molecular cloning, functional expression, and pharmacological characterization of a novel serotonin receptor (5-hydroxytryptamine2F) from rat stomach fundus.", "Immunohistochemical localisation of the serot...
[ 2008, 2007, 1992, 1996, 1994, 2001, 2008, 2002, 2009, 2009, 2008, 2006, 2002 ]
13
[ "IPR002231" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 790 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 2, 1, 3 ]
4
true
Family
5-Hydroxytryptamine 2B receptor
5-Hydroxytryptamine 2B receptor
5HT2B_rcpt
7
IPR000483
483
Cysteine-rich flanking region, C-terminal
Cys-rich_flank_reg_C
Domain
81,792
false
false
Leucine-rich repeats (LRR, see ) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape [ ]. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [ ]. Proteins containi...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF01463", "SM00082" ]
[ "LRRCT", "LRRCT" ]
[ 14037, 81481 ]
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-114608", "R-BTA-168142", "R-BTA-5682910", "R-BTA-8849932", "R-CEL-209968", "R-CEL-376176", "R-CEL-6798695", "R-CEL-8941413", "R-CEL-9010553", "R-DME-168142", "R-DME-209442", "R-DME-214842", "R-DME-214844", "R-DME-214862", "R-DME-214863", "R-DME-214869", "R-DME-214874", "R-DM...
[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-168142", "REACTOME:R-BTA-5682910", "REACTOME:R-BTA-8849932", "REACTOME:R-CEL-209968", "REACTOME:R-CEL-376176", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-8941413", "REACTOME:R-CEL-9010553", "REACTOME:R-DME-168142", "REACTOME:R-DME-209442", "REACTOME:R-DM...
213
[ "1gwb", "1m0z", "1m10", "1ook", "1ozn", "1p8t", "1p8v", "1p9a", "1qyy", "1sq0", "1u0n", "1w8a", "1ziw", "2a0z", "2ifg", "2v70", "2v9s", "2v9t", "2wfh", "2xot", "2z66", "3b2d", "3cig", "3ciy", "3fxi", "3j0a", "3kj4", "3p72", "3pmh", "3rez", "3rfe", "3rg1"...
179
[ "PUB00007147", "PUB00017058" ]
[ "11751054", "14747988" ]
[ "The leucine-rich repeat as a protein recognition motif.", "Structural principles of leucine-rich repeat (LRR) proteins." ]
[ 2001, 2004 ]
2
[]
[ "IPR031635" ]
0
1
0
[ "Cotesia sesamiae Mombasa bracovirus", "Eukaryota", "Pseudomonadati" ]
[ 1, 81789, 2 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 12, 269, 64, 250, 170, 235 ]
6
true
Domain
Cysteine-rich flanking region, C-terminal
Cysteine-rich flanking region, C-terminal
Cys-rich_flank_reg_C
2
IPR000484
484
Photosynthetic reaction centre, L/M
Photo_RC_L/M
Family
46,829
false
false
This entry describes the photosynthetic reaction centre L and M subunits, and the homologous D1 (PsbA) and D2 (PsbD) photosystem II (PSII) reaction centre proteins from cyanobacteria, algae and plants. The D1 and D2 proteins only show approximately 15% sequence homology with the L and M subunits, however the conserved ...
[ "GO:0009772", "GO:0019684" ]
[ "photosynthetic electron transport in photosystem II", "photosynthesis, light reaction" ]
[ "biological_process", "biological_process" ]
2
[ "PFAM", "PRINTS" ]
[ "PF00124", "PR00256" ]
[ "Photo_RC", "REACTNCENTRE" ]
[ 46828, 42280 ]
2
[ "EC", "METACYC", "PROSITEDOC" ]
[ "1.10.3.9", "PWY-101", "PDOC00217" ]
[ "EC:1.10.3.9", "METACYC:PWY-101", "PROSITEDOC:PDOC00217" ]
3
[ "1aig", "1aij", "1ds8", "1dv3", "1dv6", "1dxr", "1e14", "1e6d", "1eys", "1f6n", "1fnp", "1fnq", "1izl", "1jgw", "1jgx", "1jgy", "1jgz", "1jh0", "1k6l", "1k6n", "1kby", "1l9b", "1l9j", "1m3x", "1mps", "1ogv", "1pcr", "1prc", "1pss", "1pst", "1qov", "1r2c"...
395
[ "PUB00014111", "PUB00014116", "PUB00015279", "PUB00015357", "PUB00015359", "PUB00015395", "PUB00034760", "PUB00034761", "PUB00034762", "PUB00082625" ]
[ "11095707", "11005826", "2676514", "12518057", "14871485", "12872158", "15329728", "16931113", "8027023", "27386923" ]
[ "Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer.", "Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described...
[ 2000, 2000, 1989, 2003, 2004, 2003, 2004, 2006, 1994, 2016 ]
10
[]
[ "IPR005781", "IPR005871", "IPR055266" ]
0
3
0
[ "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 4111, 39553, 1555, 1610 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 11, 18, 12 ]
3
true
Family
Photosynthetic reaction centre, L/M
Photosynthetic reaction centre, L/M
Photo_RC_L/M
8
IPR000487
487
Non-structural protein NS2B, flavivirus
Flavi_NS2B
Domain
11,454
false
false
Pathogenic members of the flavivirus family [E1], including West Nile Virus (WNV) and Dengue Virus (DV), are growing global threats for which there are no specific treatments. The genome encodes three structural proteins found in the mature virion (C, prM, and E) and seven "non-structural" (i.e., not part of the virion...
[ "GO:0004252", "GO:0044423" ]
[ "serine-type endopeptidase activity", "virion component" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PROFILE" ]
[ "PF01002", "PS51527" ]
[ "Flavi_NS2B", "FLAVIVIRUS_NS2B" ]
[ 11074, 11424 ]
2
[ "EC", "EC", "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.1.1.56", "2.1.1.57", "2.7.7.48", "3.4.21.91", "3.6.1.15", "3.6.4.13", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210", "PWY-7375", "PWY-7379" ]
[ "EC:2.1.1.56", "EC:2.1.1.57", "EC:2.7.7.48", "EC:3.4.21.91", "EC:3.6.1.15", "EC:3.6.4.13", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7185", "METACYC:PWY-7198", "METACYC:PWY-7210", "METACYC:PWY-7375", "METACYC:PWY-7379" ]
13
[ "2fom", "2fp7", "2ggv", "2ijo", "2m9p", "2m9q", "2wv9", "2yol", "3e90", "3l6p", "3lkw", "3u1i", "3u1j", "4m9f", "4m9i", "4m9k", "4m9m", "4m9t", "4r8t", "5gj4", "5gpi", "5gxj", "5h4i", "5h6v", "5idk", "5lc0", "5t1v", "5tfn", "5yod", "5yof", "5yvj", "5yvu"...
264
[ "PUB00041729", "PUB00057952", "PUB00057953", "PUB00103480" ]
[ "17400917", "19693793", "20042502", "30951555" ]
[ "Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold.", "Homology modeling and molecular dynamics simulations of Dengue virus NS2B/NS3 protease: insight into molecular interaction.", "Serotype-specific structural differences in the protease-cofactor ...
[ 2007, 2010, 2010, 2019 ]
4
[]
[]
0
0
null
[ "Bacteria", "Orthornavirae" ]
[ 5, 11449 ]
2
[]
[]
0
true
Domain
Non-structural protein NS2B, flavivirus
Non-structural protein NS2B, flavivirus
Flavi_NS2B
9
IPR000488
488
Death domain
Death_dom
Domain
56,908
false
false
The death domain (DD) is a homotypic protein interaction module composed of a bundle of six α-helices. DD is related in sequence and structure to the death effector domain (DED, see ) and the caspase recruitment domain (CARD, see ), which work in similar pathways and show similar interaction properties [ ]. DD bind eac...
[ "GO:0005515", "GO:0007165" ]
[ "protein binding", "signal transduction" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00531", "PS50017", "SM00005" ]
[ "Death", "DEATH_DOMAIN", "DEATH" ]
[ 50881, 45461, 39680 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50017", "R-BTA-1257604", "R-BTA-140534", "R-BTA-209543", "R-BTA-209560", "R-BTA-2562578", "R-BTA-3371378", "R-BTA-450302", "R-BTA-450321", "R-BTA-5218900", "R-BTA-5357786", "R-BTA-5357905", "R-BTA-5357956", "R-BTA-5669034", "R-BTA-5675482", "R-BTA-6811558", "R-BTA-69416", "R-B...
[ "PROSITEDOC:PDOC50017", "REACTOME:R-BTA-1257604", "REACTOME:R-BTA-140534", "REACTOME:R-BTA-209543", "REACTOME:R-BTA-209560", "REACTOME:R-BTA-2562578", "REACTOME:R-BTA-3371378", "REACTOME:R-BTA-450302", "REACTOME:R-BTA-450321", "REACTOME:R-BTA-5218900", "REACTOME:R-BTA-5357786", "REACTOME:R-BTA...
301
[ "1d2z", "1ddf", "1e3y", "1e41", "1fad", "1ich", "1ik7", "1ngr", "1wh4", "1wmg", "1wxp", "1ygo", "2d96", "2dbf", "2gf5", "2ib1", "2n80", "2n83", "2n97", "2o71", "2of5", "2yqf", "2yvi", "3ezq", "3g5b", "3mop", "3oq9", "4d8o", "4f42", "4f44", "4o6x", "5uke"...
69
[ "PUB00005444", "PUB00015011", "PUB00015012", "PUB00015013", "PUB00015014", "PUB00015057" ]
[ "7482697", "14585074", "14601641", "11504623", "12691620", "15226512" ]
[ "The death domain: a module shared by proteins with diverse cellular functions.", "Death receptors.", "Receptor-mediated choreography of life and death.", "The death domain superfamily: a tale of two interfaces?", "Mal and MyD88: adapter proteins involved in signal transduction by Toll-like receptors.", "...
[ 1995, 2003, 2003, 2001, 2003, 2004 ]
6
[]
[ "IPR033994", "IPR033998", "IPR034029", "IPR034037", "IPR034249", "IPR035533", "IPR037924", "IPR037926", "IPR037934", "IPR037971", "IPR042058", "IPR042151", "IPR042154", "IPR042155", "IPR042156", "IPR042747", "IPR047096" ]
0
17
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 11, 531, 56345, 5, 16 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 22, 382, 31, 199, 134, 160 ]
6
true
Domain
Death domain
Death domain
Death_dom
8
IPR000489
489
Pterin-binding domain
Pterin-binding_dom
Domain
61,372
false
false
The ~250-residue pterin-binding domain has been shown to adopt a (β/α)8 barrel fold, which has the overall shape of a distorted cylinder. It has eight α-helices stacked around the outside of an inner cylinder of parallel β-strands. The pterin ring binds at the bottom of the (β/α)8 barrel in a polar cup-like region that...
[ "GO:0042558" ]
[ "pteridine-containing compound metabolic process" ]
[ "biological_process" ]
1
[ "PFAM", "PROSITE", "PROSITE", "PROFILE" ]
[ "PF00809", "PS00792", "PS00793", "PS50972" ]
[ "Pterin_bind", "DHPS_1", "DHPS_2", "PTERIN_BINDING" ]
[ 59453, 25194, 27827, 61177 ]
4
[ "EC", "GP", "GP", "METACYC", "PROSITEDOC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME...
[ "2.5.1.15", "GenProp1332", "GenProp1616", "PWY-6614", "PDOC00630", "PDOC50972", "R-CEL-156581", "R-CEL-1614635", "R-CEL-9013407", "R-CEL-9759218", "R-DDI-156581", "R-DDI-1614635", "R-DDI-9013407", "R-DDI-9759218", "R-HSA-156581", "R-HSA-1614635", "R-HSA-3359467", "R-HSA-3359469", ...
[ "EC:2.5.1.15", "GP:GenProp1332", "GP:GenProp1616", "METACYC:PWY-6614", "PROSITEDOC:PDOC00630", "PROSITEDOC:PDOC50972", "REACTOME:R-CEL-156581", "REACTOME:R-CEL-1614635", "REACTOME:R-CEL-9013407", "REACTOME:R-CEL-9759218", "REACTOME:R-DDI-156581", "REACTOME:R-DDI-1614635", "REACTOME:R-DDI-901...
28
[ "1ad1", "1ad4", "1aj0", "1aj2", "1ajz", "1eye", "1f6y", "1q7m", "1q7q", "1q7z", "1q85", "1q8a", "1q8j", "1tws", "1tww", "1twz", "1tx0", "1tx2", "2bmb", "2dqw", "2dza", "2dzb", "2e7f", "2ogy", "2q14", "2vef", "2veg", "2vp8", "2y5j", "2y5s", "2yci", "2ycj"...
149
[ "PUB00003947", "PUB00014006", "PUB00018443" ]
[ "9187658", "10997901", "14752199" ]
[ "Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase.", "Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.", "Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase." ]
[ 1997, 2000, 2004 ]
3
[]
[ "IPR006390" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 1512, 52078, 6370, 28, 4, 1380 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae ...
[ 9, 1, 1, 2, 9, 1, 1, 6, 6, 1, 1, 3 ]
12
true
Domain
Pterin-binding domain
Pterin-binding domain
Pterin-binding_dom
1
IPR000491
491
Inhibin, beta A subunit
Inhibin_betaA
Family
752
false
false
Inhibins and activins are glycoproteins, secreted by the gonads, that belong to the transforming growth factor beta family [ ]. They participate in differentiation and growth of diverse cell types. Inhibin inhibits secretion of follicle-stimulating hormone by the pituitary [ ]. Inhibin has two isoforms, A and B, with t...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR00670" ]
[ "INHIBINBA" ]
[ 752 ]
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-1502540", "R-BTA-201451", "R-BTA-209822", "R-BTA-2473224", "R-BTA-9839406", "R-HSA-1502540", "R-HSA-201451", "R-HSA-209822", "R-HSA-2473224", "R-HSA-9839406", "R-MMU-1502540", "R-MMU-201451", "R-MMU-209822", "R-MMU-2473224", "R-MMU-9839406", "R-RNO-1502540", "R-RNO-201451", ...
[ "REACTOME:R-BTA-1502540", "REACTOME:R-BTA-201451", "REACTOME:R-BTA-209822", "REACTOME:R-BTA-2473224", "REACTOME:R-BTA-9839406", "REACTOME:R-HSA-1502540", "REACTOME:R-HSA-201451", "REACTOME:R-HSA-209822", "REACTOME:R-HSA-2473224", "REACTOME:R-HSA-9839406", "REACTOME:R-MMU-1502540", "REACTOME:R-...
25
[ "5hly", "5hlz" ]
2
[ "PUB00001456", "PUB00003992", "PUB00006558", "PUB00006578" ]
[ "7813465", "2417121", "9207855", "9989858" ]
[ "Genomic cloning and sequence analyses of the bovine alpha-, beta A- and beta B-inhibin/activin genes. Identification of transcription factor AP-2-binding sites in the 5'-flanking regions by DNase I footprinting.", "Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homol...
[ 1994, 1985, 1997, 1998 ]
4
[ "IPR015615" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 752 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 4, 5, 2 ]
4
true
Family
Inhibin, beta A subunit
Inhibin, beta A subunit
Inhibin_betaA
5
IPR000492
492
Protamine-2
PRM2
Family
156
false
false
The protamines are a diverse family of small arginine-rich proteins that are synthesized in the late-stage spermatids of many animals and plants. They bind to DNA, condensing the spermatid genome into a genetically inactive state. The two protamines found in mammals, P1 and P2, are the most widely studied. Both P1 and ...
[ "GO:0003677", "GO:0007286", "GO:0051276" ]
[ "DNA binding", "spermatid development", "chromosome organization" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM", "PANTHER" ]
[ "PF00841", "PTHR21341" ]
[ "Protamine_P2", "" ]
[ 156, 151 ]
2
[ "REACTOME" ]
[ "R-HSA-9821993" ]
[ "REACTOME:R-HSA-9821993" ]
1
[]
0
[ "PUB00006287", "PUB00075474" ]
[ "8513810", "17903313" ]
[ "Evolution of pro-protamine P2 genes in primates.", "The protamine family of sperm nuclear proteins." ]
[ 1993, 2007 ]
2
[]
[]
0
0
null
[ "Bilateria" ]
[ 156 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 2 ]
3
true
Family
Protamine-2
Protamine-2
PRM2
5
IPR000493
493
Inositol 1,4,5-trisphosphate receptor
InsP3_rcpt
Family
7,217
false
false
The inositol 1,4,5-trisphosphate (IP3)3 receptors (IP3R) are tetrameric intracellular Ca2 release channels on the endoplasmic membrane that are activated by the ligand IP3 [ ]. The mammalian IP3R family consists of three isoforms (IP3R1, IP3R2, and IP3R3). They form homotetrameric or heterotetrameric channels [ ]. They...
[ "GO:0005220", "GO:0070679", "GO:0006816", "GO:0005783" ]
[ "inositol 1,4,5-trisphosphate-gated calcium channel activity", "inositol 1,4,5 trisphosphate binding", "calcium ion transport", "endoplasmic reticulum" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR00779" ]
[ "INSP3RECEPTR" ]
[ 7217 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "GenProp2098", "R-CEL-114508", "R-CEL-139853", "R-CEL-381676", "R-CEL-5578775", "R-CEL-9717207", "R-CEL-983695", "R-DDI-114508", "R-DDI-139853", "R-DDI-5578775", "R-DDI-9717207", "R-DME-114508", "R-DME-139853", "R-DME-381676", "R-DME-5578775", "R-DME-9717207", "R-DME-983695", "R-HS...
[ "GP:GenProp2098", "REACTOME:R-CEL-114508", "REACTOME:R-CEL-139853", "REACTOME:R-CEL-381676", "REACTOME:R-CEL-5578775", "REACTOME:R-CEL-9717207", "REACTOME:R-CEL-983695", "REACTOME:R-DDI-114508", "REACTOME:R-DDI-139853", "REACTOME:R-DDI-5578775", "REACTOME:R-DDI-9717207", "REACTOME:R-DME-114508...
47
[ "1n4k", "1xzz", "3jav", "3jrr", "3t8s", "3uj0", "3uj4", "5gug", "5x9z", "5xa0", "5xa1", "6dqj", "6dqn", "6dqs", "6dqv", "6dqz", "6dr0", "6dr2", "6dra", "6drc", "6mu1", "6mu2", "6uqk", "7lhe", "7lhf", "7t3p", "7t3q", "7t3r", "7t3t", "7t3u", "8eaq", "8ear"...
41
[ "PUB00087175", "PUB00087176", "PUB00153736" ]
[ "20813840", "20843799", "15760480" ]
[ "Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening.", "Structural studies of inositol 1,4,5-trisphosphate receptor: coupling ligand binding to channel gating.", "Ca2+ regulation in the absence of the iplA gene product in Dic...
[ 2010, 2010, 2005 ]
3
[ "IPR015925" ]
[]
1
0
1
[ "Eukaryota" ]
[ 7217 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 56, 2, 13, 8, 25 ]
6
true
Family
Inositol 1,4,5-trisphosphate receptor
Inositol 1,4,5-trisphosphate receptor
InsP3_rcpt
9
IPR000494
494
Receptor L-domain
Rcpt_L-dom
Domain
17,612
false
false
The structure for the first three domains of the extracellular portion of IGF-1R (type-1 insulin-like growth-factor receptor) has been solved and consists of two L-domains and a cysteine rich region (L1-Cys-rich-L2). The L-domains each consist of a single-stranded right-handed β-helix. The Cys-rich region is composed o...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01030" ]
[ "Recep_L_domain" ]
[ 17612 ]
1
[ "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-1227986", "R-CEL-1250196", "R-CEL-1251985", "R-CEL-1253288", "R-CEL-1257604", "R-CEL-177929", "R-CEL-179812", "R-CEL-180292", "R-CEL-180336", "R-CEL-182971", "R-CEL-1963642", "R-CEL-2179392", "R-CEL-416572", "R-CEL-445144", "R-CEL-5673001", "R-CEL-6785631", "R-CE...
[ "EC:2.7.10.1", "REACTOME:R-CEL-1227986", "REACTOME:R-CEL-1250196", "REACTOME:R-CEL-1251985", "REACTOME:R-CEL-1253288", "REACTOME:R-CEL-1257604", "REACTOME:R-CEL-177929", "REACTOME:R-CEL-179812", "REACTOME:R-CEL-180292", "REACTOME:R-CEL-180336", "REACTOME:R-CEL-182971", "REACTOME:R-CEL-1963642"...
191
[ "1igr", "1ivo", "1m6b", "1mox", "1n8y", "1n8z", "1nql", "1s78", "1yy9", "2a91", "2ahx", "2hr7", "3b2u", "3b2v", "3be1", "3c09", "3h3b", "3i2t", "3ltf", "3ltg", "3mzw", "3n85", "3njp", "3p0y", "3p11", "3qwq", "3u2p", "3u7u", "3u9u", "3w11", "3w12", "3w13"...
206
[ "PUB00004283", "PUB00072883" ]
[ "9690478", "15583168" ]
[ "Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor.", "PST1 and ECM33 encode two yeast cell surface GPI proteins important for cell wall integrity." ]
[ 1998, 2004 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 288, 17316, 2, 6 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 73, 55, 251, 45, 20, 55 ]
6
true
Domain
Receptor L-domain
Receptor L-domain
Rcpt_L-dom
4
IPR000496
496
Bradykinin receptor family
Brdyknn_rcpt
Family
1,852
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:0007186", "GO:0016020" ]
[ "bradykinin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00425" ]
[ "BRADYKININR" ]
[ 1852 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "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" ]
[ "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", "REACTOME:R-RNO-418...
12
[ "7eib", "7f2o" ]
2
[ "PUB00063406", "PUB00063407", "PUB00063408", "PUB00063409", "PUB00063410" ]
[ "10812256", "12755382", "9112069", "9650825", "8075864" ]
[ "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 ]
5
[ "IPR050119" ]
[ "IPR001186", "IPR001504" ]
1
2
0
[ "Chordata" ]
[ 1852 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 6, 5, 7 ]
4
true
Family
Bradykinin receptor family
Bradykinin receptor family
Brdyknn_rcpt
7
IPR000497
497
Dopamine D5 receptor
Dopamine_D5_rcpt
Family
736
false
false
Dopamine receptors are members of the rhodopsin-like G-protein coupled receptor family and are prominent in the vertebrate central nervous system (CNS). Dysfunction of dopaminergic neurotransmission in the CNS has been implicated in a variety of neuropsychiatric disorders [ ], including social phobia [ ], Tourette's sy...
[ "GO:0004952", "GO:0007189", "GO:0005886" ]
[ "dopamine neurotransmitter receptor activity", "adenylate cyclase-activating G protein-coupled receptor signaling pathway", "plasma membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00566" ]
[ "DOPAMINED1BR" ]
[ 736 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "218", "R-HSA-390651", "R-HSA-418555", "R-MMU-390651", "R-MMU-418555", "R-RNO-390651" ]
[ "IUPHAR:218", "REACTOME:R-HSA-390651", "REACTOME:R-HSA-418555", "REACTOME:R-MMU-390651", "REACTOME:R-MMU-418555", "REACTOME:R-RNO-390651" ]
6
[ "8irv" ]
1
[ "PUB00064281", "PUB00064282", "PUB00064283", "PUB00064284", "PUB00064285", "PUB00064286", "PUB00064287", "PUB00064288", "PUB00064289", "PUB00064290", "PUB00064291", "PUB00064292", "PUB00064293", "PUB00064296", "PUB00064301", "PUB00067001", "PUB00067012", "PUB00067013" ]
[ "15148138", "10698826", "16613557", "17017512", "12555236", "16961425", "11920678", "9633679", "16433053", "14060771", "1060115", "12836695", "9457173", "12563019", "16968475", "16458973", "12486173", "11584926" ]
[ "The neurobiology of dopamine signaling.", "Low dopamine D(2) receptor binding potential in social phobia.", "Dopamine and the diseased brain.", "The nigrostriatal DA pathway and Parkinson's disease.", "Relationship between functional dopamine D2 and D3 receptors gene polymorphisms and neuroleptic malignant...
[ 2004, 2000, 2006, 2006, 2003, 2006, 2002, 1998, 2005, 1963, 1975, 2003, 1998, 2003, 2006, 2006, 2002, 2001 ]
18
[ "IPR000929" ]
[]
1
0
1
[ "Vertebrata" ]
[ 736 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 2, 3 ]
4
true
Family
Dopamine D5 receptor
Dopamine D5 receptor
Dopamine_D5_rcpt
2
IPR000498
498
Outer membrane protein OmpA-like, transmembrane domain
OmpA-like_TM_dom
Domain
4,395
false
false
The ompA-like transmembrane domain is present in a number of different outer membrane proteins of several Gram-negative bacteria. Many of the proteins having this domain in the N-terminal also have the conserved bacterial outer membrane protein domain at the C terminus. The outer membrane protein A of Escherichia coli ...
[ "GO:0009279", "GO:0016020" ]
[ "cell outer membrane", "membrane" ]
[ "cellular_component", "cellular_component" ]
2
[ "PFAM" ]
[ "PF01389" ]
[ "OmpA_membrane" ]
[ 4395 ]
1
[]
[]
[]
0
[ "1bxw", "1g90", "1qjp", "2ge4", "2jmm", "2k0l", "3nb3", "9fdg", "9fzc", "9fzd" ]
10
[ "PUB00003957", "PUB00006249", "PUB00006571" ]
[ "9808047", "1974149", "10554771" ]
[ "Structure of the outer membrane protein A transmembrane domain.", "The role of the mature part of secretory proteins in translocation across the plasma membrane and in regulation of their synthesis in Escherichia coli.", "Expression and secretion of proteins in E. coli." ]
[ 1998, 1990, 1999 ]
3
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta", "metagenomes" ]
[ 4364, 7, 24 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Outer membrane protein OmpA-like, transmembrane domain
Outer membrane protein OmpA-like, transmembrane domain
OmpA-like_TM_dom
8
IPR000499
499
Endothelin receptor family
Endthln_rcpt
Family
3,130
false
false
Endothelins are able to activate a number of signal transduction processes including phospholipase A2, phospholipase C and phospholipase D, as well as cytosolic protein kinase activation. The play an important role in the regulation of the cardiovascular system [ , , ] and are the most potent vasoconstrictors identifie...
[ "GO:0004962", "GO:0007186", "GO:0008217", "GO:0042310", "GO:0048484", "GO:0016020" ]
[ "endothelin receptor activity", "G protein-coupled receptor signaling pathway", "regulation of blood pressure", "vasoconstriction", "enteric nervous system development", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
6
[ "PRINTS" ]
[ "PR00366" ]
[ "ENDOTHELINR" ]
[ 3130 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-375276", "R-BTA-416476", "R-HSA-375276", "R-HSA-416476", "R-HSA-9856649", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476", "R-SSC-375276", "R-SSC-416476" ]
[ "REACTOME:R-BTA-375276", "REACTOME:R-BTA-416476", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476", "REACTOME:R-SSC-375276", "REACTOME:R-SSC-416476" ]
11
[ "8hbd", "8hcq", "8hcx", "8iy5", "8iy6", "8xgr", "8xve", "8xvh", "8xvi", "8xvj", "8xvk", "8xvl", "8xwp", "8xwq", "8zrt" ]
15
[ "PUB00001510", "PUB00063437", "PUB00063438", "PUB00063439", "PUB00063440", "PUB00063441", "PUB00063442", "PUB00063443", "PUB00063444", "PUB00063445", "PUB00063446", "PUB00063447", "PUB00063448", "PUB00063449", "PUB00063450", "PUB00063451", "PUB00063463", "PUB00063464", "PUB000634...
[ "1916094", "2451132", "11264479", "11984741", "16529555", "1331845", "16340664", "8480469", "8466176", "1847708", "2156267", "12037137", "11067800", "9239759", "1351106", "18758495", "1719979", "1849646", "1710450", "7882989", "7647976", "9413859" ]
[ "Endothelins.", "A novel potent vasoconstrictor peptide produced by vascular endothelial cells.", "Endothelin system: the double-edged sword in health and disease.", "Role of endothelin in cardiovascular disease.", "Pharmacology and physiopathology of the brain endothelin system: an overview.", "Intravent...
[ 1991, 1988, 2001, 2002, 2006, 1992, 2006, 1993, 1993, 1991, 1990, 2002, 2000, 1997, 1992, 2008, 1991, 1991, 1991, 1995, 1995, 1997 ]
22
[ "IPR000276" ]
[ "IPR001112", "IPR002175" ]
1
2
0
[ "Chordata" ]
[ 3130 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 16, 4, 5, 11 ]
4
true
Family
Endothelin receptor family
Endothelin receptor family
Endthln_rcpt
2
IPR000501
501
Tripartite terminase subunit 1
UL28/UL56
Family
638
false
false
In herpesviruses the terminase complex is a genome-packaging motor formed by a small (S-terminase) and a large terminase subunit (L-terminase), plus a third terminase subunit known as T-terminase. The S-terminase subunit, pUL28 in HSV-1 [ ] and pUL56 in HCMV [ ], binds packaging initiation sites on viral genome [ ]. Th...
[ "GO:0019073" ]
[ "viral DNA genome packaging" ]
[ "biological_process" ]
1
[ "HAMAP", "PFAM" ]
[ "MF_04014", "PF01366" ]
[ "HSV_TRM1", "PRTP" ]
[ 560, 638 ]
2
[ "REACTOME" ]
[ "R-HSA-9610379" ]
[ "REACTOME:R-HSA-9610379" ]
1
[ "6m5r", "6m5s", "6m5u", "6m5v" ]
4
[ "PUB00003546", "PUB00070917", "PUB00079196", "PUB00079197", "PUB00079204" ]
[ "9696839", "16920825", "27033706", "23175377", "23259714" ]
[ "Herpes simplex virus type 1 cleavage and packaging proteins UL15 and UL28 are associated with B but not C capsids during packaging.", "Herpes simplex virus 1 DNA packaging proteins encoded by UL6, UL15, UL17, UL28, and UL33 are located on the external surface of the viral capsid.", "Divergent Evolution of Nucl...
[ 1998, 2006, 2016, 2013, 2012 ]
5
[]
[]
0
0
null
[ "Herpesvirales", "Homo sapiens" ]
[ 637, 1 ]
2
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Tripartite terminase subunit 1
Tripartite terminase subunit 1
UL28/UL56
8
IPR000503
503
Histamine H2 receptor
Histamine_H2_rcpt
Family
498
false
false
Histamine plays an important role in a variety of pathophysiological conditions. In allergic conditions, histamine is released from basophils and mast cells and is responsible for symptoms of allergic conditions of the skin and airways. In the gastric mucosa, gastric induced histamine release stimulates parietal cells ...
[ "GO:0004969", "GO:0001696", "GO:0007186", "GO:0045907", "GO:0016020" ]
[ "histamine receptor activity", "gastric acid secretion", "G protein-coupled receptor signaling pathway", "positive regulation of vasoconstriction", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "cellular_component" ]
5
[ "PRINTS" ]
[ "PR00531" ]
[ "HISTAMINEH2R" ]
[ 498 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "263", "R-CFA-390650", "R-HSA-390650", "R-HSA-418555", "R-MMU-390650", "R-MMU-418555", "R-RNO-390650" ]
[ "IUPHAR:263", "REACTOME:R-CFA-390650", "REACTOME:R-HSA-390650", "REACTOME:R-HSA-418555", "REACTOME:R-MMU-390650", "REACTOME:R-MMU-418555", "REACTOME:R-RNO-390650" ]
7
[ "7ul3", "8pok", "8yn3", "8yn4", "8yut", "9ixj" ]
6
[ "PUB00010558", "PUB00063500", "PUB00063501", "PUB00063502", "PUB00063503", "PUB00063504", "PUB00063506", "PUB00063507", "PUB00063514", "PUB00063515", "PUB00063540", "PUB00063541", "PUB00063542", "PUB00063543", "PUB00063544", "PUB00063545" ]
[ "11179434", "16402096", "19772756", "12113221", "17490952", "19843401", "9311023", "12626656", "21618887", "7644667", "9374694", "10511481", "7299000", "2861221", "7067399", "2567579" ]
[ "Cloning and pharmacological characterization of a fourth histamine receptor (H(4)) expressed in bone marrow.", "Histamine and its receptors.", "Intranasal antihistamines for allergic rhinitis: mechanism of action.", "Histamine and antihistamines in anaphylaxis.", "Histamine and histamine intolerance.", "...
[ 2001, 2006, 2009, 2002, 2007, 2009, 1997, 2003, 2010, 1995, 1997, 1999, 1981, 1985, 1982, 1989 ]
16
[ "IPR000276" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 498 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 6, 6 ]
3
true
Family
Histamine H2 receptor
Histamine H2 receptor
Histamine_H2_rcpt
1
IPR000504
504
RNA recognition motif domain
RRM_dom
Domain
702,435
false
false
Many eukaryotic proteins containing one or more copies of a putative RNA-binding domain of about 90 amino acids are known to bind single-stranded RNAs [ , , ]. The largest group of single strand RNA-binding proteins is the eukaryotic RNA recognition motif (RRM) family that contains an eight amino acid RNP-1 consensus s...
[ "GO:0003723" ]
[ "RNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PFAM", "PFAM", "PROFILE", "SMART" ]
[ "PF00076", "PF16367", "PF28441", "PS50102", "SM00360" ]
[ "RRM_1", "RRM_7", "RRM_11", "RRM", "RRM" ]
[ 627375, 9281, 15996, 680258, 630699 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00030", "R-BTA-111367", "R-BTA-112382", "R-BTA-113418", "R-BTA-156827", "R-BTA-159227", "R-BTA-159230", "R-BTA-159231", "R-BTA-159236", "R-BTA-429947", "R-BTA-450408", "R-BTA-674695", "R-BTA-6796648", "R-BTA-6803529", "R-BTA-6807505", "R-BTA-72086", "R-BTA-72163", "R-BTA-72165...
[ "PROSITEDOC:PDOC00030", "REACTOME:R-BTA-111367", "REACTOME:R-BTA-112382", "REACTOME:R-BTA-113418", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-159227", "REACTOME:R-BTA-159230", "REACTOME:R-BTA-159231", "REACTOME:R-BTA-159236", "REACTOME:R-BTA-429947", "REACTOME:R-BTA-450408", "REACTOME:R-BTA-6746...
470
[ "1a9n", "1aud", "1b7f", "1cvj", "1d8z", "1d9a", "1drz", "1dz5", "1fht", "1fj7", "1fjc", "1fje", "1fnx", "1fxl", "1g2e", "1h2t", "1h2u", "1h2v", "1h6k", "1ha1", "1hd0", "1hd1", "1hl6", "1iqt", "1jmt", "1l3k", "1m5k", "1m5o", "1m5p", "1m5v", "1n52", "1n54"...
1,042
[ "PUB00001891", "PUB00004440", "PUB00005341", "PUB00016352", "PUB00034493", "PUB00034494", "PUB00034495", "PUB00034496", "PUB00034497", "PUB00034498" ]
[ "2470643", "8290338", "3072706", "15231733", "3192525", "3313012", "2467746", "1716386", "15853797", "16387655" ]
[ "RNA-binding proteins as developmental regulators.", "Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors.", "Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation.", "U2AF homology motifs: protein recognition in the RR...
[ 1989, 1993, 1988, 2004, 1988, 1987, 1989, 1991, 2005, 2006 ]
10
[]
[ "IPR003954", "IPR007846", "IPR014886", "IPR015047", "IPR021790", "IPR031766", "IPR033096", "IPR033107", "IPR033110", "IPR033744", "IPR034123", "IPR034125", "IPR034126", "IPR034131", "IPR034134", "IPR034138", "IPR034140", "IPR034143", "IPR034146", "IPR034147", "IPR034148", "...
0
262
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 86, 10374, 691548, 71, 356 ]
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...
[ 1370, 176, 1455, 492, 1228, 847, 72, 841, 1018, 54, 74, 2282 ]
12
true
Domain
RNA recognition motif domain
RNA recognition motif domain
RRM_dom
3
IPR000505
505
5-Hydroxytryptamine 1D receptor
5HT1D_rcpt
Family
754
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:0040012", "GO:0042310", "GO:0050795", "GO:0005886" ]
[ "G protein-coupled serotonin receptor activity", "smooth muscle contraction", "G protein-coupled receptor signaling pathway", "chemical synaptic transmission", "regulation of locomotion", "vasoconstriction", "regulation of behavior", "plasma membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
8
[ "PRINTS" ]
[ "PR00514" ]
[ "5HT1DRECEPTR" ]
[ 754 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3", "R-HSA-390666", "R-HSA-418594", "R-MMU-390666", "R-MMU-418594", "R-RNO-390666", "R-RNO-418594" ]
[ "IUPHAR:3", "REACTOME:R-HSA-390666", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-390666", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-390666", "REACTOME:R-RNO-418594" ]
7
[ "7e32" ]
1
[ "PUB00064376", "PUB00064412", "PUB00064421", "PUB00064422", "PUB00066696", "PUB00066697", "PUB00066700", "PUB00066701", "PUB00066702", "PUB00066704", "PUB00066996", "PUB00066997" ]
[ "18476671", "10193663", "7775648", "10463324", "9559931", "9453271", "8815958", "8750741", "23325368", "11989819", "8736648", "15820416" ]
[ "Serotonin receptors.", "Characterisation of the 5-HT receptor binding profile of eletriptan and kinetics of [3H]eletriptan binding at human 5-HT1B and 5-HT1D receptors.", "Role of the serotonin receptor subtype 5-HT1D on basal and stimulated growth hormone secretion.", "Zolmitriptan-induced growth hormone re...
[ 2008, 1999, 1995, 1999, 1998, 1997, 1996, 1995, 2013, 2002, 1996, 2005 ]
12
[ "IPR002231" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 754 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 1, 1, 2 ]
4
true
Family
5-Hydroxytryptamine 1D receptor
5-Hydroxytryptamine 1D receptor
5HT1D_rcpt
4
IPR000507
507
Beta 1 adrenoceptor
ADRB1_rcpt
Family
922
false
false
The adrenoceptors (or adrenergic receptors) are rhodopsin-like G protein-coupled receptors that are targets of the catecholamines, especially norepinephrine (noradrenaline) and epinephrine (adrenaline). Many cells possess these receptors, and the binding of a catecholamine to the receptor will generally stimulate the s...
[ "GO:0004940", "GO:0007189", "GO:0045823", "GO:0016020" ]
[ "beta1-adrenergic receptor activity", "adenylate cyclase-activating G protein-coupled receptor signaling pathway", "positive regulation of heart contraction", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR00561" ]
[ "ADRENRGCB1AR" ]
[ 922 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "28", "R-HSA-390696", "R-HSA-418555", "R-MMU-390696", "R-MMU-418555", "R-RNO-390696" ]
[ "IUPHAR:28", "REACTOME:R-HSA-390696", "REACTOME:R-HSA-418555", "REACTOME:R-MMU-390696", "REACTOME:R-MMU-418555", "REACTOME:R-RNO-390696" ]
6
[ "2y00", "2y01", "2y02", "2y03", "2y04", "3zpq", "3zpr", "4ami", "4amj", "4bvn", "5a8e", "6h7j", "6h7l", "6h7m", "6h7n", "6h7o", "6ibl", "6tko", "8s2t" ]
19
[ "PUB00066376", "PUB00066377", "PUB00066533", "PUB00066535", "PUB00066548", "PUB00066549", "PUB00066550", "PUB00066551", "PUB00066552", "PUB00066553", "PUB00066557" ]
[ "18882199", "2855960", "11053129", "15655528", "1695899", "8693001", "6107894", "8917438", "14711933", "25100", "12063255" ]
[ "A study of the adrenotropic receptors.", "Subtypes of alpha 2-adrenoceptors: pharmacological and molecular biological evidence converge.", "G(i)-dependent localization of beta(2)-adrenergic receptor signaling to L-type Ca(2+) channels.", "The selectivity of beta-adrenoceptor antagonists at the human beta1, b...
[ 1948, 1988, 2000, 2005, 1990, 1996, 1980, 1996, 2004, 1978, 2002 ]
11
[ "IPR002233" ]
[]
1
0
1
[ "Gnathostomata", "uncultured Mycobacteriales bacterium" ]
[ 921, 1 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 2, 3 ]
3
true
Family
Beta 1 adrenoceptor
Beta 1 adrenoceptor
ADRB1_rcpt
4
IPR000509
509
Large ribosomal subunit protein eL36
Ribosomal_eL36
Family
5,955
false
false
A number of eukaryotic ribosomal proteins can be grouped on the basis of sequence similarities. The eL36 (also known as L36e) ribosomal family consists of mammalian [ ], Caenorhabditis elegans and Drosophila L36, Candida albicans L39, and yeast YL39 ribosomal proteins [ ]. Ribosomes are the particles that catalyse mRNA...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PROSITE", "PANTHER" ]
[ "PF01158", "PS01190", "PTHR10114" ]
[ "Ribosomal_L36e", "RIBOSOMAL_L36E", "" ]
[ 5932, 4905, 5700 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00916", "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:PDOC00916", "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...
75
[ "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"...
583
[ "PUB00000224", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00101554" ]
[ "8484789", "11297922", "11290319", "11114498", "32669547" ]
[ "The primary structure of rat ribosomal protein L36.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Structural snapshots of human pre-60S ribosomal particles before and after nuclear export." ]
[ 1993, 2001, 2001, 2000, 2020 ]
5
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5955 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 10, 1, 1, 2, 4, 2, 1, 4, 11, 2, 2, 11 ]
12
true
Family
Large ribosomal subunit protein eL36
Large ribosomal subunit protein eL36
Ribosomal_eL36
4
IPR000510
510
Nitrogenase/oxidoreductase, component 1
Nase/OxRdtase_comp1
Domain
21,506
false
false
Enzymes belonging to this family include cofactor-requiring nitrogenases and protochlorophyllide reductase. The key enzymatic reactions in nitrogen fixation are catalysed by the nitrogenase complex, which has two components, the iron protein (component 2), and a component (component 1) which is either a molybdenum-iron...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00148" ]
[ "Oxidored_nitro" ]
[ 21506 ]
1
[ "EC", "METACYC", "METACYC" ]
[ "1.3.7.7", "PWY-5531", "PWY-7159" ]
[ "EC:1.3.7.7", "METACYC:PWY-5531", "METACYC:PWY-7159" ]
3
[ "1fp4", "1g20", "1g21", "1h1l", "1l5h", "1m1n", "1m1y", "1m34", "1mio", "1n2c", "1qgu", "1qh1", "1qh8", "2afh", "2afi", "2min", "2xdq", "2ynm", "3aek", "3aeq", "3aer", "3aes", "3aet", "3aeu", "3k1a", "3min", "3pdi", "3u7q", "4nd8", "4tku", "4tkv", "4wes"...
123
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1037, 16979, 2976, 514 ]
4
[]
[]
0
true
Domain
Nitrogenase/oxidoreductase, component 1
Nitrogenase/oxidoreductase, component 1
Nase/OxRdtase_comp1
6
IPR000511
511
Holocytochrome c/c1 synthase
Holocyt_c/c1_synthase
Family
6,721
false
false
Holocytochrome c-type synthase (HCCS, also known as cytochrome c-type heme lyase) ( ) and holocytochrome-c1 synthase (CC1HL, also known as cytochrome c1 heme lyase) [ ] are mitochondrial enzymes that catalyse the covalent attachment of a haem group on two cysteine residues of cytochrome c and c1. These two enzymes are ...
[ "GO:0004408", "GO:0005739" ]
[ "holocytochrome-c synthase activity", "mitochondrion" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PROSITE", "PROSITE", "PANTHER" ]
[ "PF01265", "PS00821", "PS00822", "PTHR12743" ]
[ "Cyto_heme_lyase", "CYTO_HEME_LYASE_1", "CYTO_HEME_LYASE_2", "" ]
[ 6694, 3443, 5603, 6606 ]
4
[ "EC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.4.1.17", "PWY-8145", "PWY-8146", "PDOC00647", "R-BTA-611105", "R-CEL-611105", "R-DDI-611105", "R-HSA-611105", "R-MMU-611105", "R-SCE-611105", "R-SPO-611105" ]
[ "EC:4.4.1.17", "METACYC:PWY-8145", "METACYC:PWY-8146", "PROSITEDOC:PDOC00647", "REACTOME:R-BTA-611105", "REACTOME:R-CEL-611105", "REACTOME:R-DDI-611105", "REACTOME:R-HSA-611105", "REACTOME:R-MMU-611105", "REACTOME:R-SCE-611105", "REACTOME:R-SPO-611105" ]
11
[]
0
[ "PUB00001421", "PUB00096610" ]
[ "1499554", "23150584" ]
[ "Molecular cloning and characterization of the Saccharomyces cerevisiae CYT2 gene encoding cytochrome-c1-heme lyase.", "Human mitochondrial holocytochrome c synthase's heme binding, maturation determinants, and complex formation with cytochrome c." ]
[ 1992, 2013 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 3, 6718 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 1, 9, 1, 2, 2, 2, 4, 2, 2 ]
9
true
Family
Holocytochrome c/c1 synthase
Holocytochrome c/c1 synthase
Holocyt_c/c1_synthase
6
IPR000512
512
Diphtheria toxin (NAD+-dipthamide ADP-ribosyltransferase)
Diphtheria_toxin
Family
41
false
false
Diphtheria toxin ( ) is a 58kDa protein secreted by lysogenic strains of Corynebacterium diphtheriae. The toxin causes the disease diphtheria in humans by gaining entry into the cell cytoplasm and inhibiting protein synthesis [ ]. The mechanism of inhibition involves transfer of the ADP-ribose group of NAD to elongatio...
[ "GO:0047286", "GO:0090729", "GO:0005615" ]
[ "NAD+-diphthamide ADP-ribosyltransferase activity", "toxin activity", "extracellular space" ]
[ "molecular_function", "molecular_function", "cellular_component" ]
3
[ "PIRSF", "PRINTS" ]
[ "PIRSF000490", "PR00769" ]
[ "Diphtheria_toxin", "DPTHRIATOXIN" ]
[ 22, 41 ]
2
[ "REACTOME" ]
[ "R-HSA-5336415" ]
[ "REACTOME:R-HSA-5336415" ]
1
[ "1ddt", "1dtp", "1f0l", "1mdt", "1sgk", "1tox", "1xdt", "4ae0", "4ae1", "4ow6", "5i82", "7k7b", "7k7c", "7k7d", "7k7e", "7o4w", "7ri3", "7rrw", "8g0f", "8g0g", "9biw" ]
21
[ "PUB00000429", "PUB00004122" ]
[ "8573568", "1589020" ]
[ "Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide.", "The crystal structure of diphtheria toxin." ]
[ 1996, 1992 ]
2
[]
[]
0
0
null
[ "Actinomycetes", "unclassified Lambdavirus" ]
[ 36, 5 ]
2
[]
[]
0
true
Family
Diphtheria toxin (NAD+-dipthamide ADP-ribosyltransferase)
Diphtheria toxin (NAD+-dipthamide ADP-ribosyltransferase)
Diphtheria_toxin
8
IPR000514
514
Glycoside hydrolase, family 39
Glyco_hydro_39
Family
4,124
false
false
Glycoside hydrolase family 39 ( ) comprises enzymes with several known activities such as alpha-L-iduronidase ( ), beta-xylosidase ( ), and alpha-1,4-L-rhamnosidase [ ]. The most highly conserved regions in these enzymes are located in their N-terminal parts. These contain a glutamic acid residue which, on the basis of...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00745" ]
[ "GLHYDRLASE39" ]
[ 4124 ]
1
[ "CAZY", "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GH39", "3.2.1", "PDOC00787", "R-CFA-2024096", "R-CFA-2024101", "R-DME-2024096", "R-DME-2024101", "R-HSA-2024096", "R-HSA-2024101", "R-HSA-2206302", "R-HSA-9953038", "R-MMU-2024096", "R-MMU-2024101" ]
[ "CAZY:GH39", "EC:3.2.1", "PROSITEDOC:PDOC00787", "REACTOME:R-CFA-2024096", "REACTOME:R-CFA-2024101", "REACTOME:R-DME-2024096", "REACTOME:R-DME-2024101", "REACTOME:R-HSA-2024096", "REACTOME:R-HSA-2024101", "REACTOME:R-HSA-2206302", "REACTOME:R-HSA-9953038", "REACTOME:R-MMU-2024096", "REACTOME...
13
[ "1px8", "1uhv", "1w91", "2bfg", "2bs9", "3w81", "3w82", "4ekj", "4kgj", "4kgl", "4kh2", "4m29", "4mj2", "4mj4", "4obr", "4obs", "5ndx", "6i6r", "6i6x", "6uqj", "6yyh", "6yyi", "8i0j", "8i0x" ]
24
[ "PUB00004870", "PUB00005266", "PUB00093668" ]
[ "7624375", "8535779", "31285597" ]
[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan." ]
[ 1995, 1995, 2019 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halogranum amylolyticum", "metagenomes" ]
[ 2622, 1486, 1, 15 ]
4
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 1, 7, 7, 3 ]
5
true
Family
Glycoside hydrolase, family 39
Glycoside hydrolase, family 39
Glyco_hydro_39
3
IPR000515
515
ABC transporter type 1, transmembrane domain MetI-like
MetI-like
Domain
1,148,743
false
false
This entry recognises ABC transmembrane domains where the TMD is on a separate protein, such as the D-methionine transport system permease protein MetI. The crystal structure of the high-affinity Escherichia coli MetNI methionine uptake transporter has been solved. Each MetI subunit is organised around a core of five t...
[ "GO:0055085", "GO:0016020" ]
[ "transmembrane transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PROFILE", "CDD" ]
[ "PF00528", "PS50928", "cd06261" ]
[ "BPD_transp_1", "ABC_TM1", "TM_PBP2" ]
[ 1131849, 1143256, 1125210 ]
3
[ "GP", "GP", "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME" ]
[ "GenProp1114", "GenProp1124", "GenProp1126", "GenProp1159", "GenProp1204", "PDOC00364", "R-HSA-1222538", "R-HSA-9927020" ]
[ "GP:GenProp1114", "GP:GenProp1124", "GP:GenProp1126", "GP:GenProp1159", "GP:GenProp1204", "PROSITEDOC:PDOC00364", "REACTOME:R-HSA-1222538", "REACTOME:R-HSA-9927020" ]
8
[ "2onk", "2r6g", "3d31", "3dhw", "3fh6", "3puv", "3puw", "3pux", "3puy", "3puz", "3pv0", "3rlf", "3tui", "3tuj", "3tuz", "4jbw", "4khz", "4ki0", "4tqu", "4tqv", "4xig", "4xtc", "4yms", "4ymt", "4ymu", "4ymv", "4ymw", "6cvl", "7ahc", "7ahd", "7ahe", "7ahh"...
70
[ "PUB00003865", "PUB00014769", "PUB00017896", "PUB00051386", "PUB00069748", "PUB00069749", "PUB00096712" ]
[ "7934906", "9873074", "9640644", "18621668", "10809785", "9214624", "29240795" ]
[ "Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins.", "Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.", "ATP-binding-cassette...
[ 1994, 1999, 1998, 2008, 2000, 1997, 2017 ]
7
[]
[ "IPR010065" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Viruses", "unclassified sequences" ]
[ 18510, 1114523, 4060, 1, 12, 11637 ]
6
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 7, 52 ]
2
true
Domain
ABC transporter type 1, transmembrane domain MetI-like
ABC transporter type 1, transmembrane domain MetI-like
MetI-like
3
IPR000516
516
Nickel-dependent hydrogenase b-type cytochrome subunit
Ni-dep_Hydgase_cyt-B
Family
5,387
false
false
Bacterial membrane-bound nickel-dependent hydrogenases [ , , ] seem to be associated with a b-type cytochrome involved in electron transfer from hydrogen to oxygen. This cytochrome is a protein of about 28kDa that seems to have four transmembrane regions, which include several histidine residues that may be involved in...
[ "GO:0005506", "GO:0009055", "GO:0016020" ]
[ "iron ion binding", "electron transfer activity", "membrane" ]
[ "molecular_function", "molecular_function", "cellular_component" ]
3
[ "PRINTS", "PROSITE", "PROSITE", "NCBIFAM" ]
[ "PR00161", "PS00882", "PS00883", "TIGR02125" ]
[ "NIHGNASECYTB", "NI_HGENASE_CYTB_1", "NI_HGENASE_CYTB_2", "CytB-hydogenase" ]
[ 5318, 1250, 1266, 2682 ]
4
[ "GP", "GP", "PROSITEDOC" ]
[ "GenProp1209", "GenProp1582", "PDOC00688" ]
[ "GP:GenProp1209", "GP:GenProp1582", "PROSITEDOC:PDOC00688" ]
3
[ "4gd3", "6g94" ]
2
[ "PUB00001420", "PUB00002184", "PUB00003814" ]
[ "1587288", "1597428", "1791762" ]
[ "The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes.", "Nucleotide sequence and characterization of four additional genes of the hydrogenase structural operon from Rhizobium leguminosarum bv. viciae.", "The hydrogenase structural operon in Rhodobacter capsulatus contains a third gene, hupM, necess...
[ 1992, 1992, 1991 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]
[ 5289, 5, 22, 71 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Nickel-dependent hydrogenase b-type cytochrome subunit
Nickel-dependent hydrogenase b-type cytochrome subunit
Ni-dep_Hydgase_cyt-B
1
IPR000518
518
Metallothionein, family 14, prokaryote
Metalthion_fam14_prok
Family
797
false
false
Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium and nickel. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , , ]. An empirical classification into three classes was proposed by Kojima [ ], with class III MTs incl...
[ "GO:0046872" ]
[ "metal ion binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS" ]
[ "PF02069", "PR00859" ]
[ "Metallothio_Pro", "MTPROKARYOTE" ]
[ 796, 334 ]
2
[]
[]
[]
0
[ "1jjd", "6grv", "6gv6", "6gv7", "6gw8" ]
5
[ "PUB00000300", "PUB00001490", "PUB00003570", "PUB00003571", "PUB00005944" ]
[ "3064814", "2959513", "1779825", "1779826", "2959504" ]
[ "Biochemistry of metallothionein.", "Chemistry and biochemistry of metallothionein.", "Overview of metallothionein.", "Definitions and nomenclature of metallothioneins.", "Nomenclature of metallothionein." ]
[ 1988, 1987, 1991, 1991, 1987 ]
5
[]
[]
0
0
null
[ "Bacteria", "Diploscapter pachys", "marine sediment metagenome" ]
[ 795, 1, 1 ]
3
[]
[]
0
true
Family
Metallothionein, family 14, prokaryote
Metallothionein, family 14, prokaryote
Metalthion_fam14_prok
1
IPR000519
519
P-type trefoil domain
P_trefoil_dom
Domain
11,758
false
false
A cysteine-rich domain of approximately forty five amino-acid residues has been found in some extracellular eukaryotic proteins [ , , , ]. It is known as either the 'P', 'trefoil' or 'TFF' domain, and contains six cysteines linked by three disulphide bonds with connectivity 1-5, 2-4, 3-6. This leads to a characteristic...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART", "CDD" ]
[ "PF00088", "PS51448", "SM00018", "cd00111" ]
[ "Trefoil", "P_TREFOIL_2", "PD", "Trefoil" ]
[ 10807, 11496, 9922, 11392 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00024", "R-BTA-2534343", "R-BTA-6798695", "R-BTA-70221", "R-HSA-189085", "R-HSA-2534343", "R-HSA-5357609", "R-HSA-5659898", "R-HSA-6798695", "R-HSA-70221", "R-HSA-9018519", "R-MMU-2534343", "R-MMU-6798695", "R-MMU-70221", "R-RNO-189085", "R-RNO-6798695", "R-RNO-70221", "R-SSC-...
[ "PROSITEDOC:PDOC00024", "REACTOME:R-BTA-2534343", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-70221", "REACTOME:R-HSA-189085", "REACTOME:R-HSA-2534343", "REACTOME:R-HSA-5357609", "REACTOME:R-HSA-5659898", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-70221", "REACTOME:R-HSA-9018519", "REACTOME:R-MMU...
18
[ "1e9t", "1hi7", "1pcp", "1pe3", "1pos", "1ps2", "1psp", "2psp", "2qly", "2qmj", "3ctt", "3l4t", "3l4u", "3l4v", "3l4w", "3l4x", "3l4y", "3l4z", "3lpo", "3lpp", "3ton", "3top", "5kzw", "5kzx", "5nn3", "5nn4", "5nn5", "5nn6", "5nn8", "6v1c", "6v1d", "7p2z"...
45
[ "PUB00001033", "PUB00001707", "PUB00005012", "PUB00005400" ]
[ "7820556", "9187350", "8518738", "8267796" ]
[ "Trefoil peptides. Coming up clover.", "Rolling in the clover: trefoil factor family (TFF)-domain peptides, cell migration and cancer.", "A trefoil domain in the major rabbit zona pellucida protein.", "The P-domain or trefoil motif: a role in renewal and pathology of mucous epithelia?" ]
[ 1994, 1997, 1993, 1993 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 8, 11750 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 19, 22, 20, 43 ]
5
true
Domain
P-type trefoil domain
P-type trefoil domain
P_trefoil_dom
4
IPR000522
522
ABC transporter, permease protein, BtuC-like
ABC_transptr_permease_BtuC
Family
97,357
false
false
This entry represents a family of ABC transporter permease proteins. It includes the vitamin B12 import system permease protein BtuC, and the Fe(3+) dicitrate transport system permease proteins FecC and FecD, among many others. BtuC is a component of the ABC transporter complex BtuCD, which facilitates uptake of vitami...
[ "GO:0022857", "GO:0016020" ]
[ "transmembrane transporter activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PANTHER" ]
[ "PF01032", "PTHR30472" ]
[ "FecCD", "" ]
[ 97357, 96908 ]
2
[ "GP", "REACTOME", "REACTOME" ]
[ "GenProp0828", "R-HSA-9638334", "R-HSA-9638482" ]
[ "GP:GenProp0828", "REACTOME:R-HSA-9638334", "REACTOME:R-HSA-9638482" ]
3
[ "1l7v", "2nq2", "2qi9", "4dbl", "4fi3", "4g1u", "4r9u", "5b57", "5b58", "7lb8" ]
10
[ "PUB00002077", "PUB00088721" ]
[ "2651410", "16331991" ]
[ "Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli.", "In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B12 uptake." ]
[ 1989, 2005 ]
2
[]
[ "IPR022410", "IPR023691" ]
0
2
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 1854, 94731, 2, 69, 701 ]
5
[ "Escherichia coli (strain K12)" ]
[ 6 ]
1
true
Family
ABC transporter, permease protein, BtuC-like
ABC transporter, permease protein, BtuC-like
ABC_transptr_permease_BtuC
1
IPR000523
523
Magnesium chelatase ChlI-like, catalytic domain
Mg_chelatse_chII-like_cat_dom
Domain
32,572
false
false
This domain can be found in the magnesium chelatase ChlI subunit, the catalytic domain that binds and hydrolyses ATP. This domain contains the nucleotide binding Walker motif [ ] and can also be found in the competence protein ComM from Haemophilus influenzae and Lon proteases from archaea. Magnesium-chelatase is a thr...
[ "GO:0005524" ]
[ "ATP binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF01078" ]
[ "Mg_chelatase" ]
[ 32572 ]
1
[ "EC", "METACYC", "METACYC" ]
[ "6.6.1.1", "PWY-5531", "PWY-7159" ]
[ "EC:6.6.1.1", "METACYC:PWY-5531", "METACYC:PWY-7159" ]
3
[ "1g8p", "2x31", "3k1j", "4zpx", "6l8d", "8osf", "8osg", "8osh", "8rxd", "8rxk", "8rxs", "8rxt" ]
12
[ "PUB00000550", "PUB00002318", "PUB00097705" ]
[ "9359397", "9457877", "17472958" ]
[ "Mechanism and regulation of Mg-chelatase.", "Reconstitution of an active magnesium chelatase enzyme complex from the bchI, -D, and -H gene products of the green sulfur bacterium Chlorobium vibrioforme expressed in Escherichia coli.", "The CHLI1 subunit of Arabidopsis thaliana magnesium chelatase is a target pr...
[ 1997, 1998, 2007 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 1236, 28228, 5, 2529, 574 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Homo sapiens", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 12, 1, 1, 2, 15 ]
5
true
Domain
Magnesium chelatase ChlI-like, catalytic domain
Magnesium chelatase ChlI-like, catalytic domain
Mg_chelatse_chII-like_cat_dom
4
IPR000524
524
Transcription regulator HTH, GntR
Tscrpt_reg_HTH_GntR
Domain
385,258
false
false
Many bacterial transcription regulation proteins bind DNA through a helix-turn-helix (HTH) motif, which can be classified into subfamilies on the basis of sequence similarities. The HTH GntR family has many members distributed among diverse bacterial groups that regulate various biological processes. It was named GntR ...
[ "GO:0003700", "GO:0006355" ]
[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS", "PROFILE", "SMART", "CDD" ]
[ "PF00392", "PR00035", "PS50949", "SM00345", "cd07377" ]
[ "GntR", "HTHGNTR", "HTH_GNTR", "HTH_GNTR", "WHTH_GntR" ]
[ 382367, 217167, 380701, 378371, 342261 ]
5
[ "GP", "GP", "GP", "PROSITEDOC" ]
[ "GenProp0458", "GenProp0713", "GenProp0736", "PDOC00042" ]
[ "GP:GenProp0458", "GP:GenProp0713", "GP:GenProp0736", "PROSITEDOC:PDOC00042" ]
4
[ "1e2x", "1h9g", "1h9t", "1hw1", "1hw2", "1v4r", "2di3", "2du9", "2ek5", "2hs5", "2ra5", "2wv0", "3bwg", "3by6", "3c7j", "3edp", "3eet", "3f8m", "3fms", "3ic7", "3ihu", "3neu", "3sxy", "3tqn", "4egy", "4egz", "4h0e", "4ham", "4mgr", "4n0b", "4p96", "4p9f"...
78
[ "PUB00001726", "PUB00015228", "PUB00015265" ]
[ "2060763", "11013219", "11756427" ]
[ "A new family of bacterial regulatory proteins.", "Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold.", "Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies." ]
[ 1991, 2000, 2002 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "Sym plasmid", "unclassified sequences" ]
[ 126, 382958, 8, 213, 2, 1951 ]
6
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 1, 21 ]
2
true
Domain
Transcription regulator HTH, GntR
Transcription regulator HTH, GntR
Tscrpt_reg_HTH_GntR
6
IPR000525
525
Initiator Rep protein, WH1 domain
Initiator_Rep_WH1
Domain
10,455
false
false
This entry represents the WH1 domain found in the initiator of plasmid replication proteins, RepA and related sequences. RepA is a protein from Escherichia coli involved in plasmid replication. The RepA protein binds to DNA repeats that flank the repA gene [ , ]. A similar RepA family of proteins with wider distributio...
[ "GO:0003887", "GO:0006270" ]
[ "DNA-directed DNA polymerase activity", "DNA replication initiation" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF01051" ]
[ "Rep3_N" ]
[ 10455 ]
1
[]
[]
[]
0
[ "1hkq", "1rep", "2nra", "2z9o", "6h24", "7rva", "7sdp", "7sgc", "7soz", "7spm", "7u6k", "7u7o", "7ufx", "7uog", "7ur0", "7uv6", "7uv7", "7uxy", "8aan", "8ac8", "8d86", "8d8m", "8tip", "8tiq", "8tir", "8tis", "8tit", "8tiu", "8tiv", "8tiw", "8tix", "8tiy"...
35
[ "PUB00002219", "PUB00002431", "PUB00050250" ]
[ "8320218", "3949778", "18000058" ]
[ "Regulatory interactions between RepA, an essential replication protein, and the DNA repeats of RepFIB from plasmid P307.", "P1 plasmid replication. Purification and DNA-binding activity of the replication protein RepA.", "Structural basis for regulation of bifunctional roles in replication initiator protein." ...
[ 1993, 1986, 2007 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 6, 10142, 85, 23, 8, 191 ]
6
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Domain
Initiator Rep protein, WH1 domain
Initiator Rep protein, WH1 domain
Initiator_Rep_WH1
3
IPR000526
526
Auxin-binding protein
Auxin-bd
Family
891
false
false
Auxin binding protein is located in the lumen of the endoplasmic reticulum (ER). The primary structure contains an N-terminal hydrophobic leader sequence of 30-40 amino acids, which could represent a signal for translocation of the protein to the ER [ , ]. The mature protein comprises around 165 residues, and contains ...
[ "GO:0010011" ]
[ "auxin binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF02041", "PR00655", "PTHR37236" ]
[ "Auxin_BP", "AUXINBINDNGP", "" ]
[ 866, 797, 777 ]
3
[]
[]
[]
0
[ "1lr5", "1lrh" ]
2
[ "PUB00001170", "PUB00004518" ]
[ "2555179", "1321684" ]
[ "Molecular cloning and structural analysis of a gene from Zea mays (L.) coding for a putative receptor for the plant hormone auxin.", "Molecular analysis of an auxin binding protein gene located on chromosome 4 of Arabidopsis." ]
[ 1989, 1992 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 7, 98, 784, 2 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 5, 6, 24 ]
3
true
Family
Auxin-binding protein
Auxin-binding protein
Auxin-bd
7
IPR000527
527
Flagellar L-ring protein
Flag_Lring
Family
10,453
false
false
The flgH, flgI and fliF genes of Salmonella typhimurium encode the major proteins for the L, P and M rings of the flagellar basal body [ ]. In fact, the basal body consists of four rings (L,P,S and M) surrounding the flagellar rod, which is believed to transmit motor rotation to the filament [ ]. The M ring is integral...
[ "GO:0003774", "GO:0071973", "GO:0009427" ]
[ "cytoskeletal motor activity", "bacterial-type flagellum-dependent cell motility", "bacterial-type flagellum basal body, distal rod, L ring" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PFAM", "PRINTS", "PANTHER" ]
[ "MF_00415", "PF02107", "PR01008", "PTHR34933" ]
[ "FlgH", "FlgH", "FLGLRINGFLGH", "" ]
[ 9319, 10452, 10038, 10396 ]
4
[ "GP" ]
[ "GenProp0880" ]
[ "GP:GenProp0880" ]
1
[ "7bgl", "7cbl", "7cgo", "7clr", "7nvg", "8wht", "8wl2", "8wle", "8wlt", "8wo5", "8woe", "8z5n", "8z60" ]
13
[ "PUB00002086", "PUB00003254" ]
[ "2544561", "2129540" ]
[ "L-, P-, and M-ring proteins of the flagellar basal body of Salmonella typhimurium: gene sequences and deduced protein sequences.", "FlgB, FlgC, FlgF and FlgG. A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium." ]
[ 1989, 1990 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 10280, 28, 145 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Flagellar L-ring protein
Flagellar L-ring protein
Flag_Lring
9
IPR000528
528
Plant non-specific lipid-transfer protein/Par allergen
Plant_nsLTP
Family
14,440
false
false
Plant cells contain proteins, called non-specific lipid-transfer proteins (nsLTPs) [ , , , ], which transfer phospholipids, glycolipids, fatty acids and sterols from liposomes or microsomes to mitochondria [ ] and are thought to be involved in plant defense. These proteins, expressed throughout the plant tissues but pr...
[ "GO:0008289", "GO:0006869" ]
[ "lipid binding", "lipid transport" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS", "PROSITE", "PANTHER" ]
[ "PR00382", "PS00597", "PTHR33076" ]
[ "LIPIDTRNSFER", "PLANT_LTP", "" ]
[ 13746, 3878, 9475 ]
3
[ "PROSITEDOC" ]
[ "PDOC00516" ]
[ "PROSITEDOC:PDOC00516" ]
1
[ "1afh", "1be2", "1bv2", "1bwo", "1cz2", "1fk0", "1fk1", "1fk2", "1fk3", "1fk4", "1fk5", "1fk6", "1fk7", "1gh1", "1jtb", "1lip", "1mid", "1mzl", "1mzm", "1rzl", "1siy", "1t12", "1uva", "1uvb", "1uvc", "2alg", "2b5s", "2mal", "2n2z", "2n81", "3gsh", "4xuw"...
43
[ "PUB00000081", "PUB00000619", "PUB00001487", "PUB00004991", "PUB00096612" ]
[ "1883207", "1901223", "2193821", "8066090", "26417906" ]
[ "Phospholipid transfer proteins.", "The genetics of plant lipids.", "Lipid transfer in plants.", "Crystallization and preliminary X-ray crystallographic analysis of phospholipid transfer protein from maize seedlings.", "Structural and Functional Characterization of the Hazelnut Allergen Cor a 8." ]
[ 1991, 1991, 1990, 1994, 2015 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 6, 14434 ]
2
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 92, 86, 85 ]
3
true
Family
Plant non-specific lipid-transfer protein/Par allergen
Plant non-specific lipid-transfer protein/Par allergen
Plant_nsLTP
2
IPR000529
529
Small ribosomal subunit protein bS6
Ribosomal_bS6
Family
29,569
false
false
The small subunits of bacterial and eukaryotic ribosomes have the same overall shapes (with structural elements described as head, body, platform, beak and shoulder). Ribosomal protein bS6 is one of the proteins from the small ribosomal subunit. [ ]. In Escherichia coli, bS6 is known to bind together with bS18 to 16S r...
[ "GO:0003735", "GO:0019843", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "rRNA binding", "translation", "ribosome" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PANTHER", "NCBIFAM" ]
[ "PF01250", "PTHR21011", "TIGR00166" ]
[ "Ribosomal_S6", "", "S6" ]
[ 29508, 27731, 26148 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00805", "R-BTA-5389840", "R-BTA-5419276", "R-BTA-9937383", "R-DME-5389840", "R-DME-5419276", "R-DME-9937383", "R-HSA-5368286", "R-HSA-5389840", "R-HSA-5419276", "R-HSA-9937383", "R-MMU-5389840", "R-MMU-5419276", "R-MMU-9937383" ]
[ "PROSITEDOC:PDOC00805", "REACTOME:R-BTA-5389840", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-9937383", "REACTOME:R-DME-5389840", "REACTOME:R-DME-5419276", "REACTOME:R-DME-9937383", "REACTOME:R-HSA-5368286", "REACTOME:R-HSA-5389840", "REACTOME:R-HSA-5419276", "REACTOME:R-HSA-9937383", "REACTOME:...
14
[ "1cqm", "1cqn", "1eg0", "1fjg", "1fka", "1g1x", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1lou", "1ml5", "1n32", "1n33", "1n34", "1n36", "1qd7", "1qjh", "1ris", "1vmb", "1vvj"...
1,302
[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00101116" ]
[ "11297922", "11290319", "11114498", "18042701" ]
[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Cryo-EM study of the spinach chloroplast ribosome reveals the structural and functional roles of plastid-specific ribosomal proteins." ]
[ 2001, 2001, 2000, 2007 ]
4
[]
[ "IPR020814" ]
0
1
0
[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 23616, 5487, 1, 465 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 10, 1, 1, 2, 1, 4, 3, 1, 10, 2, 1, 1, 8 ]
13
true
Family
Small ribosomal subunit protein bS6
Small ribosomal subunit protein bS6
Ribosomal_bS6
9
IPR000530
530
Small ribosomal subunit protein eS12
Ribosomal_eS12
Family
5,781
false
false
A number of eukaryotic ribosomal proteins can be grouped on the basis of sequence similarities. The small ribosomal subunit protein eS12 contains 130-150 amino acid residues, and is thought to be involved in the translation initiation step. This family consists of eukaryotic S12 ribosomal proteins, including those from...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00972" ]
[ "RIBSOMALS12E" ]
[ 5781 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00915", "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72649", "R-BTA-72689", "R-BTA-72695", "R-BTA-72702", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72649", "R-CEL-72689", "R-CEL-72695", "R-CEL-72702", "R-CEL-72706", "R...
[ "PROSITEDOC:PDOC00915", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72695", "REACTOME:R-BTA-72702", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827"...
109
[ "3j6x", "3j6y", "3j77", "3j78", "3j7a", "3j7p", "3j7r", "3j80", "3j81", "3jag", "3jah", "3jai", "3jaj", "3jam", "3jan", "3jap", "3jbn", "3jbo", "3jbp", "4d5l", "4d61", "4kzx", "4kzy", "4kzz", "4u3m", "4u3n", "4u3u", "4u4n", "4u4o", "4u4q", "4u4r", "4u4u"...
465
[ "PUB00002442", "PUB00003617", "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "3308890", "8433721", "11297922", "11290319", "11114498" ]
[ "The primary structure of rat ribosomal protein S12. The relationship of rat S12 to other ribosomal proteins and a correlation of the amino acid sequences of rat and yeast ribosomal proteins.", "A ribosomal S12-like gene of Trypanosoma brucei.", "Atomic structures at last: the ribosome in 2000.", "The ribosom...
[ 1987, 1993, 2001, 2001, 2000 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 3, 5778 ]
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...
[ 5, 1, 1, 1, 1, 3, 1, 7, 20, 1, 2, 19 ]
12
true
Family
Small ribosomal subunit protein eS12
Small ribosomal subunit protein eS12
Ribosomal_eS12
4
IPR000531
531
TonB-dependent receptor-like, beta-barrel
Beta-barrel_TonB
Domain
278,842
false
false
This entry represents the β-barrel domain which contains the plug domain ( ). This β-barrel domain is also found in vitamin B12 transporter BtuB [ ] and ferric citrate outer membrane transporter FecA [ ], among others. TonB proteins are bacterial membrane proteins that play a crucial role in energy-dependent active tra...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00593" ]
[ "TonB_dep_Rec_b-barrel" ]
[ 278842 ]
1
[ "GP", "REACTOME", "REACTOME" ]
[ "GenProp0543", "R-HSA-9638334", "R-HSA-9638482" ]
[ "GP:GenProp0543", "REACTOME:R-HSA-9638334", "REACTOME:R-HSA-9638482" ]
3
[ "1by3", "1by5", "1fcp", "1fep", "1fi1", "1kmo", "1kmp", "1nqe", "1nqf", "1nqg", "1nqh", "1pnz", "1po0", "1po3", "1qff", "1qfg", "1qjq", "1qkc", "1ujw", "1xkh", "1xkw", "2fcp", "2grx", "2gsk", "2guf", "2hdf", "2hdi", "2iah", "2o5p", "2w16", "2w6t", "2w6u"...
141
[ "PUB00006673", "PUB00014980", "PUB00014981", "PUB00014984", "PUB00014986", "PUB00035726", "PUB00035727", "PUB00050147", "PUB00089681" ]
[ "9886293", "14499604", "9865695", "12652322", "11872840", "15993072", "12957833", "17548346", "17056600" ]
[ "Crystal structure of the outer membrane active transporter FepA from Escherichia coli.", "The Escherichia coli outer membrane cobalamin transporter BtuB: structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation.", "Transmembrane sig...
[ 1999, 2003, 1998, 2003, 2002, 2005, 2003, 2007, 2007 ]
9
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 6, 275562, 451, 15, 2808 ]
5
[ "Escherichia coli (strain K12)" ]
[ 8 ]
1
true
Domain
TonB-dependent receptor-like, beta-barrel
TonB-dependent receptor-like, beta-barrel
Beta-barrel_TonB
1
IPR000532
532
Glucagon/GIP/secretin/VIP
Glucagon_GIP_secretin_VIP
Domain
5,784
false
false
A number of polypeptidic hormones, mainly expressed in the intestine or the pancreas, belong to a group of structurally related peptides [ , ]. Once such hormone, glucagon is widely distributed and produced in the alpha-cells of pancreatic islets [ ]. It affects glucose metabolism in the liver [ ] by inhibiting glycoge...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PRINTS", "PROSITE", "SMART" ]
[ "PF00123", "PR00275", "PS00260", "SM00070" ]
[ "Hormone_2", "GLUCAGON", "GLUCAGON", "GLUCA" ]
[ 5727, 1998, 5194, 5654 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00233", "R-BTA-163359", "R-BTA-381676", "R-BTA-381771", "R-BTA-416476", "R-BTA-418555", "R-BTA-420092", "R-BTA-422085", "R-GGA-163359", "R-GGA-381771", "R-GGA-416476", "R-GGA-418555", "R-GGA-420092", "R-GGA-422085", "R-HSA-163359", "R-HSA-187024", "R-HSA-381676", "R-HSA-381771...
[ "PROSITEDOC:PDOC00233", "REACTOME:R-BTA-163359", "REACTOME:R-BTA-381676", "REACTOME:R-BTA-381771", "REACTOME:R-BTA-416476", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-420092", "REACTOME:R-BTA-422085", "REACTOME:R-GGA-163359", "REACTOME:R-GGA-381771", "REACTOME:R-GGA-416476", "REACTOME:R-GGA-4185...
45
[ "1bh0", "1d0r", "1gcn", "1gea", "1jrj", "1kx6", "1nau", "1t5q", "2b4n", "2d2p", "2g49", "2l63", "2l64", "2l70", "2l71", "2m5p", "2m5q", "2mj9", "2naw", "2obu", "2qkh", "2rrh", "2rri", "3iol", "4apd", "4zgm", "5bqm", "5niq", "5ott", "5otu", "5otv", "5otw"...
110
[ "PUB00000024", "PUB00000025", "PUB00001745", "PUB00002491", "PUB00004603" ]
[ "3133967", "3291691", "4076759", "3260236", "6577439" ]
[ "Vasoactive intestinal polypeptide and related peptides. Isolation and chemistry.", "Glucagon and related peptides. Molecular structure and biological specificity.", "Primary structure of glucagon from an elasmobranchian fish. Torpedo marmorata.", "Isolation of peptide hormones from the pancreas of the bullfr...
[ 1988, 1988, 1985, 1988, 1983 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 11, 5773 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 11, 10, 17, 23 ]
4
true
Domain
Glucagon/GIP/secretin/VIP
Glucagon/GIP/secretin/VIP
Glucagon_GIP_secretin_VIP
9
IPR000533
533
Tropomyosin
Tropomyosin
Family
19,313
false
false
Tropomyosins [ ], are a family of closely related proteins present in muscle and non-muscle cells. In striated muscle, tropomyosin mediate the interactions between the troponin complex and actin so as to regulate muscle contraction [ ]. The role of tropomyosin in smooth muscle and non-muscle tissues is not clear. Tropo...
[]
[]
[]
0
[ "PFAM", "PRINTS", "PROSITE" ]
[ "PF00261", "PR00194", "PS00326" ]
[ "Tropomyosin", "TROPOMYOSIN", "TROPOMYOSIN" ]
[ 19197, 15930, 13503 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00290", "R-BTA-390522", "R-BTA-445355", "R-BTA-9013424", "R-CEL-445355", "R-CEL-9013424", "R-DME-445355", "R-DME-9013424", "R-GGA-390522", "R-GGA-445355", "R-HSA-390522", "R-HSA-445355", "R-HSA-9013424", "R-HSA-9725370", "R-MMU-390522", "R-MMU-445355", "R-MMU-9013424", "R-RNO-...
[ "PROSITEDOC:PDOC00290", "REACTOME:R-BTA-390522", "REACTOME:R-BTA-445355", "REACTOME:R-BTA-9013424", "REACTOME:R-CEL-445355", "REACTOME:R-CEL-9013424", "REACTOME:R-DME-445355", "REACTOME:R-DME-9013424", "REACTOME:R-GGA-390522", "REACTOME:R-GGA-445355", "REACTOME:R-HSA-390522", "REACTOME:R-HSA-4...
25
[ "1c1g", "1ic2", "2b9c", "2d3e", "2efr", "2efs", "2tma", "2w49", "2w4u", "3u1a", "3u1c", "3u59", "4a7f", "4a7h", "4a7l", "6kn7", "6kn8", "6otn", "6x5z", "7bjg", "7bjn", "7bjs", "7ko4", "7ko5", "7ko7", "7kon", "7kor", "7nep", "7uti", "7utl", "8dd0", "8efh"...
77
[ "PUB00000703", "PUB00002384", "PUB00015281", "PUB00056059" ]
[ "3606587", "6993480", "12690456", "7844152" ]
[ "Genetic origin of diversity of human cytoskeletal tropomyosins.", "The amino acid sequence of rabbit cardiac tropomyosin.", "The role of tropomyosin in the regulation of myocardial contraction and relaxation.", "Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions." ]
[ 1987, 1980, 2003, 1995 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses" ]
[ 4, 64, 19243, 2 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 15, 46, 18, 77, 40, 2, 51, 2, 1 ]
9
true
Family
Tropomyosin
Tropomyosin
Tropomyosin
2
IPR000534
534
Semialdehyde dehydrogenase, NAD-binding
Semialdehyde_DH_NAD-bd
Domain
69,028
false
false
The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase [ ], an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Ar...
[ "GO:0016620", "GO:0051287" ]
[ "oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor", "NAD binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "SMART" ]
[ "PF01118", "SM00859" ]
[ "Semialdhyde_dh", "Semialdhyde_dh" ]
[ 64635, 68212 ]
2
[ "EC", "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.2.1", "1.2.1.38", "PWY-5154", "R-DDI-70635", "R-SCE-70635", "R-SPO-70635" ]
[ "EC:1.2.1", "EC:1.2.1.38", "METACYC:PWY-5154", "REACTOME:R-DDI-70635", "REACTOME:R-SCE-70635", "REACTOME:R-SPO-70635" ]
6
[ "1brm", "1gl3", "1mb4", "1mc4", "1nvm", "1nwc", "1nwh", "1nx6", "1oza", "1pqp", "1pqu", "1pr3", "1ps8", "1pu2", "1q2x", "1t4b", "1t4d", "1ta4", "1tb4", "1vkn", "1xyg", "1ys4", "2cvo", "2ep5", "2fmu", "2g17", "2gyy", "2gz1", "2gz2", "2gz3", "2hjs", "2i3a"...
92
[ "PUB00016262" ]
[ "10369777" ]
[ "Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Viruses", "unclassified sequences" ]
[ 1724, 60127, 6019, 1, 3, 1154 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Escherichia coli (strain K12)", "Mus musculus", "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 pomb...
[ 12, 1, 5, 2, 2, 9, 2, 2, 8 ]
9
true
Domain
Semialdehyde dehydrogenase, NAD-binding
Semialdehyde dehydrogenase, NAD-binding
Semialdehyde_DH_NAD-bd
9
IPR000535
535
Major sperm protein (MSP) domain
MSP_dom
Domain
25,663
false
false
Nematode sperm are unusual amoeboid cells in which motility is not based on actin, but instead on the major sperm protein (MSP). MSP is a dimeric molecule that polymerises to form non-polar filaments constructed from two helical subfilaments that wind round one another. The filaments then assemble into larger macromole...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF00635", "PS50202" ]
[ "Motile_Sperm", "MSP" ]
[ 23125, 24327 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50202", "R-BTA-1660661", "R-BTA-6798695", "R-BTA-8980692", "R-BTA-9013106", "R-BTA-9013404", "R-BTA-9013405", "R-BTA-9013408", "R-BTA-9609523", "R-HSA-1660661", "R-HSA-6798695", "R-HSA-8980692", "R-HSA-9013106", "R-HSA-9013404", "R-HSA-9013405", "R-HSA-9013408", "R-HSA-9609523",...
[ "PROSITEDOC:PDOC50202", "REACTOME:R-BTA-1660661", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8980692", "REACTOME:R-BTA-9013106", "REACTOME:R-BTA-9013404", "REACTOME:R-BTA-9013405", "REACTOME:R-BTA-9013408", "REACTOME:R-BTA-9609523", "REACTOME:R-HSA-1660661", "REACTOME:R-HSA-6798695", "REACTOME:...
41
[ "1grw", "1m1s", "1msp", "1row", "1wic", "1z9l", "1z9o", "2bvu", "2cri", "2mdk", "2msp", "2rr3", "3ikk", "3msp", "6lp4", "6tqr", "6tqs", "6tqt", "6tqu", "7x14", "8hqu", "8hs7", "9jui" ]
23
[ "PUB00003372", "PUB00016286", "PUB00018203", "PUB00018204", "PUB00018205", "PUB00018206", "PUB00018207" ]
[ "8913307", "12051923", "9878374", "9641981", "9920726", "10733941", "9537365" ]
[ "2.5 A resolution crystal structure of the motile major sperm protein (MSP) of Ascaris suum.", "2.6 A resolution crystal structure of helices of the motile major sperm protein (MSP) of Caenorhabditis elegans.", "Solution structure of the motile major sperm protein (MSP) of Ascaris suum - evidence for two mangan...
[ 1996, 2002, 1998, 1998, 1999, 2000, 1998 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Mimiviridae sp. ChoanoV1", "ecological metagenomes" ]
[ 2, 163, 25491, 1, 6 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 51, 90, 10, 19, 17, 15, 1, 63, 29, 2, 2, 111 ]
12
true
Domain
Major sperm protein (MSP) domain
Major sperm protein (MSP) domain
MSP_dom
2
IPR000536
536
Nuclear hormone receptor, ligand-binding domain
Nucl_hrmn_rcpt_lig-bd
Domain
96,153
false
false
Nuclear receptors (NRs), such as the receptors for steroids and thyroid hormones, retinoids and vitamin D3, are one of the most abundant classes of transcriptional regulators in animals (metazoans). They regulate diverse functions, such as homeostasis, reproduction, development and metabolism. The most prominent featur...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00104", "PS51843", "SM00430" ]
[ "Hormone_recep", "NR_LBD", "HOLI" ]
[ 91026, 95028, 84444 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-1251985", "R-BTA-1257604", "R-BTA-381340", "R-BTA-383280", "R-BTA-4090294", "R-BTA-5362517", "R-BTA-5689896", "R-BTA-6811558", "R-BTA-8866427", "R-BTA-8866910", "R-BTA-8931987", "R-BTA-8939211", "R-BTA-9009391", "R-BTA-9018519", "R-BTA-9029569", "R-BTA-9623433", "R-BTA-9841251...
[ "REACTOME:R-BTA-1251985", "REACTOME:R-BTA-1257604", "REACTOME:R-BTA-381340", "REACTOME:R-BTA-383280", "REACTOME:R-BTA-4090294", "REACTOME:R-BTA-5362517", "REACTOME:R-BTA-5689896", "REACTOME:R-BTA-6811558", "REACTOME:R-BTA-8866427", "REACTOME:R-BTA-8866910", "REACTOME:R-BTA-8931987", "REACTOME:...
220
[ "1a28", "1a52", "1bsx", "1db1", "1dkf", "1e3g", "1e3k", "1ere", "1err", "1exa", "1exx", "1fby", "1fcx", "1fcy", "1fcz", "1fd0", "1fm6", "1fm9", "1g1u", "1g2n", "1g50", "1g5y", "1gs4", "1gwq", "1gwr", "1gwx", "1h9u", "1hg4", "1hj1", "1i37", "1i38", "1i7g"...
1,992
[ "PUB00088675", "PUB00088676", "PUB00088677", "PUB00088678", "PUB00088679", "PUB00088680", "PUB00088681" ]
[ "12538758", "15105832", "24844133", "24361687", "11050318", "9640540", "20723571" ]
[ "The nuclear receptor superfamily.", "Signature of the oligomeric behaviour of nuclear receptors at the sequence and structural level.", "Molecular cloning and tissue distribution of peroxisome proliferator-activated receptor-alpha (PPARα) and gamma (PPARγ) in the pigeon (Columba livia domestica).", "Local mo...
[ 2003, 2004, 2014, 2014, 2000, 1998, 2010 ]
7
[]
[ "IPR041889", "IPR044114", "IPR047158", "IPR048008", "IPR048246", "IPR049635" ]
0
6
0
[ "Avian erythroblastosis virus", "Eukaryota", "unclassified sequences" ]
[ 4, 96147, 2 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 416, 340, 53, 336, 181, 261 ]
6
true
Domain
Nuclear hormone receptor, ligand-binding domain
Nuclear hormone receptor, ligand-binding domain
Nucl_hrmn_rcpt_lig-bd
4
IPR000537
537
UbiA prenyltransferase
UbiA_prenyltransferase
Family
90,791
false
false
The UbiA family of prenyltransferases includes bacterial 4-hydroxybenzoate octaprenyltransferase (gene ubiA); yeast mitochondrial para-hydroxybenzoate--polyprenyltransferase (gene COQ2); protohaem IX farnesyltransferase (haem O synthase) from yeast and mammals (gene COX10), and from bacteria (genes cyoE or ctaB) [ , ];...
[ "GO:0016765", "GO:0016020" ]
[ "transferase activity, transferring alkyl or aryl (other than methyl) groups", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF01040" ]
[ "UbiA" ]
[ 90791 ]
1
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...
[ "2.5.1", "GenProp1291", "GenProp1337", "GenProp1355", "GenProp1498", "GenProp1585", "GenProp1694", "GenProp1724", "GenProp1744", "PDOC00727", "R-CEL-1268020", "R-CEL-2142789", "R-DDI-1268020", "R-DDI-189451", "R-DDI-2142789", "R-DDI-6806664", "R-DME-1268020", "R-DME-2142789", "R-...
[ "EC:2.5.1", "GP:GenProp1291", "GP:GenProp1337", "GP:GenProp1355", "GP:GenProp1498", "GP:GenProp1585", "GP:GenProp1694", "GP:GenProp1724", "GP:GenProp1744", "PROSITEDOC:PDOC00727", "REACTOME:R-CEL-1268020", "REACTOME:R-CEL-2142789", "REACTOME:R-DDI-1268020", "REACTOME:R-DDI-189451", "REAC...
36
[ "4od4", "4od5", "4tq3", "4tq4", "4tq5", "4tq6", "6m31", "6m34", "7bpu", "8djk", "8djm", "8j8j", "8j8k" ]
13
[ "PUB00000664", "PUB00003867", "PUB00060544", "PUB00085659", "PUB00085660" ]
[ "8155731", "7885224", "21840984", "25564559", "22166201" ]
[ "Characterization of polyprenyldiphosphate: 4-hydroxybenzoate polyprenyltransferase from Escherichia coli.", "Biosynthesis and functional role of haem O and haem A.", "Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in Halobacterium salinarum.", "A heteromeric membrane-bound prenyltransferas...
[ 1994, 1994, 2011, 2015, 2012 ]
5
[]
[ "IPR006369", "IPR026046", "IPR039653", "IPR044502", "IPR050475" ]
0
5
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 3786, 65585, 19778, 6, 1636 ]
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, 2, 4, 3, 3, 10, 7, 3, 22, 10, 2, 2, 72 ]
13
true
Family
UbiA prenyltransferase
UbiA prenyltransferase
UbiA_prenyltransferase
7
IPR000538
538
Link domain
Link_dom
Domain
15,543
false
false
The link domain [ ] is a hyaluronan(HA)-binding region found in proteins of vertebrates that are involved in the assembly of extracellular matrix, cell adhesion, and migration. The structure has been shown [ ] to consist of two α helices and two antiparallel β sheets arranged around a large hydrophobic core similar to ...
[ "GO:0005540", "GO:0007155" ]
[ "hyaluronic acid binding", "cell adhesion" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS", "PROSITE", "PROFILE", "SMART" ]
[ "PF00193", "PR01265", "PS01241", "PS50963", "SM00445" ]
[ "Xlink", "LINKMODULE", "LINK_1", "LINK_2", "LINK" ]
[ 15438, 12063, 13078, 15501, 15326 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00955", "R-BTA-1971475", "R-BTA-2022870", "R-BTA-2022923", "R-BTA-2024101", "R-BTA-2142845", "R-BTA-2160916", "R-BTA-3000178", "R-BTA-381426", "R-BTA-8957275", "R-GGA-3000178", "R-HSA-1474228", "R-HSA-1971475", "R-HSA-2022854", "R-HSA-2022857", "R-HSA-2022870", "R-HSA-2022923", ...
[ "PROSITEDOC:PDOC00955", "REACTOME:R-BTA-1971475", "REACTOME:R-BTA-2022870", "REACTOME:R-BTA-2022923", "REACTOME:R-BTA-2024101", "REACTOME:R-BTA-2142845", "REACTOME:R-BTA-2160916", "REACTOME:R-BTA-3000178", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-8957275", "REACTOME:R-GGA-3000178", "REACTOME:R...
76
[ "1o7b", "1o7c", "1poz", "1uuh", "2i83", "2jcp", "2jcq", "2jcr", "2n40", "2pf5", "4mrd", "4mre", "4mrf", "4mrg", "4mrh", "4np2", "4np3", "4pz3", "4pz4", "5bzc", "5bze", "5bzf", "5bzg", "5bzh", "5bzi", "5bzj", "5bzk", "5bzl", "5bzm", "5bzn", "5bzo", "5bzp"...
66
[ "PUB00000527", "PUB00000941", "PUB00001702" ]
[ "8318021", "8797823", "8690089" ]
[ "Evolution of the hyaluronan-binding module of link protein.", "Solution structure of the link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration.", "The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of link protein, aggrecan and CD44 is...
[ 1993, 1996, 1996 ]
3
[]
[ "IPR042059" ]
0
1
0
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 21, 15313, 11, 198 ]
4
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 54, 56, 47, 73 ]
4
true
Domain
Link domain
Link domain
Link_dom
5
IPR000539
539
Frizzled/Smoothened, 7TM
Frizzled/Smoothened_7TM
Domain
15,471
false
false
This domain is the membrane spanning region of frizzled and smoothened receptors. This membrane region is predicted to contain seven transmembrane α-helices. Proteins related to Drosophila frizzled ( ) are receptors for Wnt (mediating the beta-catenin signalling pathway) [ ], but also the planar cell polarity (PCP) pat...
[ "GO:0007166", "GO:0016020" ]
[ "cell surface receptor signaling pathway", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PRINTS", "SMART" ]
[ "PF01534", "PR00489", "SM01330" ]
[ "Frizzled", "FRIZZLED", "Frizzled" ]
[ 15336, 14492, 14873 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-CEL-4086398", "R-CEL-4086400", "R-CEL-4608870", "R-CEL-4641262", "R-CEL-4641263", "R-CEL-5140745", "R-DME-209214", "R-DME-209338", "R-DME-209387", "R-DME-209440", "R-DME-209472", "R-DME-216119", "R-DME-216217", "R-DME-350368", "R-DME-350376", "R-DME-350379", "R-DME-350411", "R-D...
[ "REACTOME:R-CEL-4086398", "REACTOME:R-CEL-4086400", "REACTOME:R-CEL-4608870", "REACTOME:R-CEL-4641262", "REACTOME:R-CEL-4641263", "REACTOME:R-CEL-5140745", "REACTOME:R-DME-209214", "REACTOME:R-DME-209338", "REACTOME:R-DME-209387", "REACTOME:R-DME-209440", "REACTOME:R-DME-209472", "REACTOME:R-D...
78
[ "4jkv", "4n4w", "4o9r", "4qim", "4qin", "5l7d", "5l7i", "5v56", "5v57", "6bd4", "6d32", "6d35", "6o3c", "6ot0", "6ww2", "6xbj", "6xbk", "6xbl", "6xbm", "7zi0", "8cxo", "8j9n", "8j9o", "8jh7", "8jhb", "8jhc", "8jhi", "8qeo", "8qw4", "8wm9", "8wma", "8yy8"...
34
[ "PUB00001104", "PUB00004238", "PUB00019581" ]
[ "9811578", "8717036", "15239825" ]
[ "In vivo evidence that Patched and Smoothened constitute distinct binding and transducing components of a Hedgehog receptor complex.", "A new member of the frizzled family from Drosophila functions as a Wingless receptor.", "The Frizzled family: receptors for multiple signal transduction pathways." ]
[ 1998, 1996, 2004 ]
3
[ "IPR017981" ]
[ "IPR026543", "IPR026551", "IPR035683", "IPR047105" ]
1
4
0
[ "Bacteria", "Eukaryota" ]
[ 7, 15464 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 24, 13, 24, 30, 32 ]
6
true
Domain
Frizzled/Smoothened, 7TM
Frizzled/Smoothened, 7TM
Frizzled/Smoothened_7TM
4
IPR000541
541
Cytoplasmic tRNA 2-thiolation protein 1
Ncs6/Tuc1/Ctu1
Family
4,537
false
false
Cytoplasmic tRNA 2-thiolation protein 1 (also known as Ncs6/Tuc1 in budding yeasts) is responsible for 2-thiolation of mcm5S2U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln) [ , ]. It directly binds tRNAs and probably acts by catalysing adenylation of tRNAs, an intermediate required for 2-thiolation. It...
[ "GO:0000049", "GO:0002098", "GO:0034227" ]
[ "tRNA binding", "tRNA wobble uridine modification", "tRNA thio-modification" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "HAMAP", "NCBIFAM" ]
[ "MF_03053", "TIGR00269" ]
[ "CTU1", "" ]
[ 3151, 2847 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME" ]
[ "2.7.7.-", "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", "PDOC00971", "R-HSA-6782315" ]
[ "EC:2.7.7.-", "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", "METACYC:PWY-7...
20
[ "3vrh", "5b4e", "5b4f", "5gha", "5mko", "5mkp", "5mkq", "5ztb", "6scy" ]
9
[ "PUB00045305", "PUB00069585", "PUB00069587", "PUB00087328" ]
[ "18391219", "18664566", "19151091", "28655838" ]
[ "The conserved Wobble uridine tRNA thiolase Ctu1-Ctu2 is required to maintain genome integrity.", "Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems.", "Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridi...
[ 2008, 2008, 2009, 2017 ]
4
[ "IPR035107" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1051, 135, 3323, 28 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 10, 1, 3, 1, 1, 1, 1, 3, 1, 1, 1, 4 ]
12
true
Family
Cytoplasmic tRNA 2-thiolation protein 1
Cytoplasmic tRNA 2-thiolation protein 1
Ncs6/Tuc1/Ctu1
6
IPR000542
542
Acyltransferase ChoActase/COT/CPT
Carn_acyl_trans
Family
24,563
false
false
A number of eukaryotic acetyltransferases can, on the basis of sequence similarities, be grouped together into a family. These enzymes include: Choline o-acetyltransferase , an enzyme that catalyses the biosynthesis of the neurotransmitter acetylcholine [ ]. Carnitine o-acetyltransferase [ ]. Peroxisomal carnitine octa...
[ "GO:0016746" ]
[ "acyltransferase activity" ]
[ "molecular_function" ]
1
[ "PROSITE", "PROSITE", "PANTHER" ]
[ "PS00439", "PS00440", "PTHR22589" ]
[ "ACYLTRANSF_C_1", "ACYLTRANSF_C_2", "" ]
[ 11374, 16643, 24118 ]
3
[ "EC", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...
[ "2.3.1", "GenProp1413", "PDOC00402", "R-BTA-200425", "R-BTA-389887", "R-BTA-9033241", "R-CEL-1483191", "R-CEL-264642", "R-DME-1483191", "R-DME-264642", "R-DRE-1483191", "R-DRE-200425", "R-DRE-264642", "R-HSA-1483191", "R-HSA-1989781", "R-HSA-200425", "R-HSA-264642", "R-HSA-389887",...
[ "EC:2.3.1", "GP:GenProp1413", "PROSITEDOC:PDOC00402", "REACTOME:R-BTA-200425", "REACTOME:R-BTA-389887", "REACTOME:R-BTA-9033241", "REACTOME:R-CEL-1483191", "REACTOME:R-CEL-264642", "REACTOME:R-DME-1483191", "REACTOME:R-DME-264642", "REACTOME:R-DRE-1483191", "REACTOME:R-DRE-200425", "REACTOME...
33
[ "1ndb", "1ndf", "1ndi", "1nm8", "1q6x", "1s5o", "1t1u", "1t7n", "1t7o", "1t7q", "1xl7", "1xl8", "1xmc", "1xmd", "2deb", "2fw3", "2fy2", "2fy3", "2fy4", "2fy5", "2fyo", "2h3p", "2h3u", "2h3w", "2h4t", "2rcu", "4ep9", "4eph", "4eyw", "7amd", "9f84", "9f85"...
32
[ "PUB00000301", "PUB00002800", "PUB00002825", "PUB00004650" ]
[ "3233218", "8420957", "8449948", "3480542" ]
[ "Cloning, sequencing, and regulation of rat liver carnitine octanoyltransferase: transcriptional stimulation of the enzyme during peroxisome proliferation.", "Cloning and sequencing of a cDNA encoding Saccharomyces cerevisiae carnitine acetyltransferase. Use of the cDNA in gene disruption studies.", "Cloning, s...
[ 1988, 1993, 1993, 1987 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 647, 23912, 4 ]
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", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 15, 37, 14, 42, 31, 2, 33, 3 ]
8
true
Family
Acyltransferase ChoActase/COT/CPT
Acyltransferase ChoActase/COT/CPT
Carn_acyl_trans
1
IPR000545
545
Lactalbumin
Lactalbumin
Family
350
false
false
Alpha-lactalbumin comprises 15 percent of the total human milk protein and is essential for lactose production [ ]. It is a globular calcium-binding metalloprotein secreted in the lactating mammary gland [ ], the calcium being bound in a novel binding loop that is superficially similar to the classic EF-hand motif. Lac...
[ "GO:0004461", "GO:0005509", "GO:0005989" ]
[ "lactose synthase activity", "calcium ion binding", "lactose biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PRINTS" ]
[ "PR00136" ]
[ "LACTALBUMIN" ]
[ 350 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-5653890", "R-MMU-5653890", "R-SSC-5653890" ]
[ "REACTOME:R-HSA-5653890", "REACTOME:R-MMU-5653890", "REACTOME:R-SSC-5653890" ]
3
[ "1a4v", "1alc", "1b9o", "1f6r", "1f6s", "1fkq", "1fkv", "1hfx", "1hfy", "1hfz", "1hmk", "1hml", "1nf5", "1nhe", "1nkh", "1nmm", "1nqi", "1nwg", "1o23", "1oqm", "1pzy", "1yro", "2fyc", "2fyd", "2g4n", "3b0i", "3b0k", "3b0o", "4l41", "6ip9", "7eka", "7wqg"...
33
[ "PUB00000468", "PUB00002403", "PUB00003274", "PUB00003998" ]
[ "2845947", "6715332", "1920433", "3785375" ]
[ "Structure and expression of the guinea-pig alpha-lactalbumin gene.", "Evolution of alpha-lactalbumins. The complete amino acid sequence of the alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat alpha-lactalbumins.", "Crystal structure of human al...
[ 1988, 1984, 1991, 1986 ]
4
[ "IPR001916" ]
[]
1
0
1
[ "Amniota" ]
[ 350 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 2, 4 ]
3
true
Family
Lactalbumin
Lactalbumin
Lactalbumin
3
IPR000547
547
Clathrin, heavy chain/VPS, 7-fold repeat
Clathrin_H-chain/VPS_repeat
Repeat
30,136
false
false
Clathrin is a triskelion-shaped cytoplasmic protein that polymerises into a polyhedral lattice on intracellular membranes to form protein-coated membrane vesicles. Lattice formation induces the sorting of membrane proteins during endocytosis and organelle biogenesis by interacting with membrane-associated adaptor molec...
[ "GO:0006886", "GO:0016192" ]
[ "intracellular protein transport", "vesicle-mediated transport" ]
[ "biological_process", "biological_process" ]
2
[ "PROFILE", "SMART" ]
[ "PS50236", "SM00299" ]
[ "CHCR", "CLH" ]
[ 30044, 15729 ]
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-177504", "R-BTA-190873", "R-BTA-196025", "R-BTA-2132295", "R-BTA-432720", "R-BTA-432722", "R-BTA-437239", "R-BTA-5099900", "R-BTA-5140745", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-8866427", "R-BTA-8964038", "R-BTA-9013420", "R-BTA-9013424", "R-CEL-190873", "R-CEL-196025", "...
[ "REACTOME:R-BTA-177504", "REACTOME:R-BTA-190873", "REACTOME:R-BTA-196025", "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-432720", "REACTOME:R-BTA-432722", "REACTOME:R-BTA-437239", "REACTOME:R-BTA-5099900", "REACTOME:R-BTA-5140745", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BT...
115
[ "1b89", "1xi4", "1xi5", "3iyv", "3lvg", "3lvh", "3qil", "5ods", "6sct", "6wcj", "6yai", "7zu0", "8dit", "8qx8" ]
14
[ "PUB00023546", "PUB00068728", "PUB00068729", "PUB00068730", "PUB00068731", "PUB00160303" ]
[ "10360576", "11160821", "12906858", "11448994", "17702618", "21330665" ]
[ "Clathrin self-assembly is mediated by a tandemly repeated superhelix.", "Vps41p function in the alkaline phosphatase pathway requires homo-oligomerization and interaction with AP-3 through two distinct domains.", "Isolation and characterization of human and mouse WDR19,a novel WD-repeat protein exhibiting andr...
[ 1999, 2001, 2003, 2001, 2007, 2011 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 42, 30094 ]
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...
[ 26, 3, 31, 7, 47, 26, 5, 20, 25, 6, 6, 244 ]
12
true
Repeat
Clathrin, heavy chain/VPS, 7-fold repeat
Clathrin, heavy chain/VPS, 7-fold repeat
Clathrin_H-chain/VPS_repeat
5
IPR000548
548
Myelin basic protein
Myelin_BP
Family
2,434
false
false
The myelin sheath is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the velocity of axonal impulse conduction [ ]. Myelin basic protein (MBP) [ , ] is a hydrophilic protein that may function to maintain the correct structure of myelin, interacting with the lip...
[ "GO:0019911" ]
[ "structural constituent of myelin sheath" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROSITE", "PANTHER" ]
[ "PF01669", "PR00212", "PS00569", "PTHR11429" ]
[ "Myelin_MBP", "MYELINMBP", "MYELIN_MBP", "" ]
[ 2208, 1954, 1128, 2324 ]
4
[ "PROSITEDOC", "REACTOME" ]
[ "PDOC00492", "R-HSA-9619665" ]
[ "PROSITEDOC:PDOC00492", "REACTOME:R-HSA-9619665" ]
2
[ "1bx2", "1fv1", "1ymm", "2lug", "3pl6" ]
5
[ "PUB00000989", "PUB00002447", "PUB00003466" ]
[ "1710177", "2435734", "1710279" ]
[ "Central nervous system myelin: structure, function, and pathology.", "Complete amino acid sequence of PO protein in bovine peripheral nerve myelin.", "Folding and function of the myelin proteins from primary sequence data." ]
[ 1991, 1987, 1991 ]
3
[]
[]
0
0
null
[ "Eukaryota", "Kangiella spongicola" ]
[ 2433, 1 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 26, 7, 14 ]
4
true
Family
Myelin basic protein
Myelin basic protein
Myelin_BP
5
IPR000549
549
Photosystem I reaction center subunit V/PsaK
PSI_PsaG/PsaK
Family
2,200
false
false
This entry represents Photosystem I reaction centre subunits V (PsaG) and PsaK from Cyanobacteria, Rhodophyta (red algae) and plants. Photosystem I (PSI) [ ] is an integral membrane protein complex that uses light energy to mediate electron transfer from plastocyanin to ferredoxin. It is found in the chloroplasts of pl...
[ "GO:0015979", "GO:0009522", "GO:0016020" ]
[ "photosynthesis", "photosystem I", "membrane" ]
[ "biological_process", "cellular_component", "cellular_component" ]
3
[ "PFAM", "PROSITE" ]
[ "PF01241", "PS01026" ]
[ "PSI_PSAK", "PHOTOSYSTEM_I_PSAGK" ]
[ 2196, 1500 ]
2
[ "PROSITEDOC" ]
[ "PDOC00786" ]
[ "PROSITEDOC:PDOC00786" ]
1
[ "1jb0", "2o01", "2wsc", "2wse", "2wsf", "3lw5", "3pcq", "4fe1", "4kt0", "4l6v", "4rku", "4xk8", "4y28", "5l8r", "5oy0", "5zf0", "5zgb", "5zgh", "5zji", "6fos", "6hqb", "6igz", "6ijj", "6ijo", "6jeo", "6jo5", "6jo6", "6k33", "6k61", "6kif", "6kig", "6kmx"...
123
[ "PUB00000583", "PUB00002802", "PUB00100153", "PUB00152828" ]
[ "3333014", "8360180", "11687207", "33846594" ]
[ "Structure, function and organization of the Photosystem I reaction center complex.", "The PSI-K subunit of photosystem I from barley (Hordeum vulgare L.). Evidence for a gene duplication of an ancestral PSI-G/K gene.", "Role of subunits in eukaryotic Photosystem I.", "Structural insights into photosystem II ...
[ 1987, 1993, 2001, 2021 ]
4
[]
[ "IPR016370", "IPR017492" ]
0
2
0
[ "Bacteria", "Eukaryota", "Viruses", "marine metagenome" ]
[ 684, 1511, 4, 1 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 9, 5, 6 ]
3
true
Family
Photosystem I reaction center subunit V/PsaK
Photosystem I reaction center subunit V/PsaK
PSI_PsaG/PsaK
6
IPR000550
550
7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK
Hppk
Domain
30,226
false
false
All organisms require reduced folate cofactors for the synthesis of a variety of metabolites. Most microorganisms must synthesise folate de novo because they lack the active transport system of higher vertebrate cells which allows these organisms to use dietary folates. Enzymes involved in folate biosynthesis are there...
[ "GO:0003848", "GO:0009396" ]
[ "2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity", "folic acid-containing compound biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROSITE", "NCBIFAM", "CDD" ]
[ "PF01288", "PS00794", "TIGR01498", "cd00483" ]
[ "HPPK", "HPPK", "folK", "HPPK" ]
[ 30213, 20103, 28995, 28231 ]
4
[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC" ]
[ "2.7.6.3", "GenProp0038", "GenProp1332", "PWY-6147", "PWY-6148", "PWY-6797", "PWY-7539", "PWY-7852", "PWY-7853", "PDOC00631" ]
[ "EC:2.7.6.3", "GP:GenProp0038", "GP:GenProp1332", "METACYC:PWY-6147", "METACYC:PWY-6148", "METACYC:PWY-6797", "METACYC:PWY-7539", "METACYC:PWY-7852", "METACYC:PWY-7853", "PROSITEDOC:PDOC00631" ]
10
[ "1cbk", "1dy3", "1eq0", "1eqm", "1ex8", "1f9h", "1g4c", "1hka", "1hq2", "1im6", "1kbr", "1q0n", "1rao", "1rb0", "1rtz", "1ru1", "1ru2", "1tmj", "1tmm", "2bmb", "2cg8", "2f63", "2f65", "2qx0", "3hcx", "3hd1", "3hd2", "3hsd", "3hsg", "3hsj", "3hsz", "3ht0"...
94
[ "PUB00001816", "PUB00002198" ]
[ "1313386", "1325970" ]
[ "The multifunctional folic acid synthesis fas gene of Pneumocystis carinii appears to encode dihydropteroate synthase and hydroxymethyldihydropterin pyrophosphokinase.", "Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinas...
[ 1992, 1992 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 10, 26726, 2873, 8, 609 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 8, 1, 1, 7, 1, 1, 2 ]
7
true
Domain
7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK
7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK
Hppk
8
IPR000551
551
MerR-type HTH domain
MerR-type_HTH_dom
Domain
184,607
false
false
The merR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 70 residues present in the merR family of transcriptional regulators [ ]. MerR-type regulators are present in diverse bacterial genera, in the cytoplasm. The helix-turn-helix DNA-binding motif is located in the N-terminal part of ...
[ "GO:0003677", "GO:0006355" ]
[ "DNA binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PFAM", "PRINTS", "PROSITE", "PROFILE", "SMART" ]
[ "PF00376", "PF13411", "PR00040", "PS00552", "PS50937", "SM00422" ]
[ "MerR", "MerR_1", "HTHMERR", "HTH_MERR_1", "HTH_MERR_2", "HTH_MERR" ]
[ 30340, 152084, 80766, 50994, 175894, 170167 ]
6
[ "PROSITEDOC" ]
[ "PDOC00477" ]
[ "PROSITEDOC:PDOC00477" ]
1
[ "1exi", "1exj", "1jbg", "1q05", "1q06", "1q07", "1q08", "1q09", "1q0a", "1r8d", "1r8e", "2dg6", "2jml", "2vz4", "2zhg", "2zhh", "3d6y", "3d6z", "3d70", "3d71", "3gp4", "3gpv", "3hh0", "3iao", "3q1m", "3q2y", "3q3d", "3q5p", "3q5r", "3q5s", "3qao", "3whp"...
76
[ "PUB00002075", "PUB00017958", "PUB00066804", "PUB00070201", "PUB00070202", "PUB00070203" ]
[ "2492496", "12829265", "12186881", "21502508", "23512413", "18315685" ]
[ "Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons.", "The MerR family of transcriptional regulators.", "Structural biology of bacterial multidrug resistance gene regulators.", "Light-dependent gene regulation by a coen...
[ 1989, 2003, 2002, 2011, 2013, 2008 ]
6
[]
[ "IPR037392", "IPR048225" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 197, 181709, 641, 204, 4, 1852 ]
6
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Homo sapiens" ]
[ 1, 5, 1 ]
3
true
Domain
MerR-type HTH domain
MerR-type HTH domain
MerR-type_HTH_dom
5