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short_name
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entry_type
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int64
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bool
is_llm_reviewed
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abstract
string
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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
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int64
in_entry_list
bool
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short_names_dat_name
string
split_bucket
int64
IPR000686
686
Fanconi anaemia group C protein
FANCC
Family
1,158
false
false
Fanconi anemia (FA) is a human disorder characterised by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. The FA complex repairs the interstrand cross-linking (ICL) lesions and coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesio...
[ "GO:0036297", "GO:0043240" ]
[ "interstrand cross-link repair", "Fanconi anaemia nuclear complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PIRSF", "PRINTS", "PANTHER" ]
[ "PF02106", "PIRSF018417", "PR00494", "PTHR16798" ]
[ "Fanconi_C", "FACC_protein", "FANCONICGENE", "" ]
[ 1153, 497, 997, 1149 ]
4
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-6783310", "R-HSA-6796648", "R-HSA-9833482", "R-MMU-6783310", "R-MMU-9833482", "R-RNO-6783310", "R-RNO-9833482" ]
[ "REACTOME:R-HSA-6783310", "REACTOME:R-HSA-6796648", "REACTOME:R-HSA-9833482", "REACTOME:R-MMU-6783310", "REACTOME:R-MMU-9833482", "REACTOME:R-RNO-6783310", "REACTOME:R-RNO-9833482" ]
7
[ "7kzp", "7kzq", "7kzr", "7kzs", "7kzt", "7kzv" ]
6
[ "PUB00054178", "PUB00089968" ]
[ "20347428", "29017571" ]
[ "A histone-fold complex and FANCM form a conserved DNA-remodeling complex to maintain genome stability.", "DNA damage response and cancer therapeutics through the lens of the Fanconi Anemia DNA repair pathway." ]
[ 2010, 2017 ]
2
[]
[]
0
0
null
[ "Opisthokonta" ]
[ 1158 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 11, 11, 9 ]
4
true
Family
Fanconi anaemia group C protein
Fanconi anaemia group C protein
FANCC
7
IPR000687
687
RIO kinase
RIO_kinase
Domain
17,016
false
false
This entry represents RIO kinase, they exhibit little sequence similarity with eukaryotic protein kinases, and are classified as atypical protein kinases [ ]. The conformation of ATP when bound to the RIO kinases is unique when compared with ePKs, such as serine/threonine kinases or the insulin receptor tyrosine kinase...
[ "GO:0004674", "GO:0005524" ]
[ "protein serine/threonine kinase activity", "ATP binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "SMART" ]
[ "SM00090" ]
[ "RIO" ]
[ 17016 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.11.1", "PDOC00958", "R-BTA-6791226", "R-HSA-6791226", "R-MMU-6791226" ]
[ "EC:2.7.11.1", "PROSITEDOC:PDOC00958", "REACTOME:R-BTA-6791226", "REACTOME:R-HSA-6791226", "REACTOME:R-MMU-6791226" ]
5
[ "1tqi", "1tqm", "1tqp", "1zao", "1zar", "1zp9", "1ztf", "1zth", "3re4", "4gyg", "4gyi", "4jin", "4otp", "6eml", "6fai", "6fdm", "6fdn", "6fdo", "6g18", "6g51", "6g5i", "6hk6", "6rbd", "6y7c", "6zv6", "6zxd", "6zxe", "6zxf", "6zxg", "6zxh", "7vbt", "7wu0"...
39
[ "PUB00005115", "PUB00015362", "PUB00020114", "PUB00033361", "PUB00034898", "PUB00034899" ]
[ "3291115", "12368087", "12471243", "16183636", "15078142", "15320712" ]
[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "Evolution of protein kinase signaling from yeast to man.", "The protein kinase complement of the human genome.", "A family portrait of the RIO kinases.", "High-throughput structural biology in drug discovery: p...
[ 1988, 2002, 2002, 2005, 2004, 2004 ]
6
[ "IPR018934" ]
[ "IPR030484" ]
1
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1584, 3774, 11571, 87 ]
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...
[ 19, 3, 4, 4, 8, 14, 2, 7, 9, 2, 2, 27 ]
12
true
Domain
RIO kinase
RIO kinase
RIO_kinase
3
IPR000688
688
Hydrogenase maturation factor HypA/HybF
HypA/HybF
Family
8,380
false
false
Bacterial membrane-bound nickel-dependent hydrogenases require a number of accessory proteins which are involved in their maturation [ , ]. One of these proteins is generally known as HypA. HypA is a metallochaperone that binds nickel to bring it safely to its target. The nickel coordinates with four nitrogens within t...
[ "GO:0016151", "GO:0051604" ]
[ "nickel cation binding", "protein maturation" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "PIRSF", "PANTHER", "NCBIFAM" ]
[ "MF_00213", "PF01155", "PIRSF004761", "PTHR34535", "TIGR00100" ]
[ "HypA_HybF", "HypA", "Hydrgn_mat_HypA", "", "hypA" ]
[ 7625, 8380, 7937, 8220, 4986 ]
5
[ "PROSITEDOC" ]
[ "PDOC00962" ]
[ "PROSITEDOC:PDOC00962" ]
1
[ "2kdx", "3a43", "3a44", "5aun", "5auo", "5aup", "5yxy", "5yy0", "6g81" ]
9
[ "PUB00000659", "PUB00014664", "PUB00014665", "PUB00088187", "PUB00154481" ]
[ "8305450", "11123699", "12081959", "19621959", "35264792" ]
[ "Nucleotide sequences of two hydrogenase-related genes (hypA and hypB) from Bradyrhizobium japonicum, one of which (hypB) encodes an extremely histidine-rich region and guanine nucleotide-binding domains.", "Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease i...
[ 1994, 2001, 2002, 2009, 2022 ]
5
[]
[ "IPR039002" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 395, 7856, 6, 123 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Hydrogenase maturation factor HypA/HybF
Hydrogenase maturation factor HypA/HybF
HypA/HybF
8
IPR000689
689
Ubiquinone biosynthesis monooxygenase COQ6
UbQ_mOase_COQ6
Family
3,746
false
false
Ubiquinone (Q) functions as an electron carrier in the respiratory chain in mitochondria. Q biosynthesis involves a series of enzymatic steps, which are catalysed by the enzymes COQ1-COQ8 in Saccharomyces cerevisiae (Baker's yeast). COQ6, or ubiquinone biosynthesis monooxygenase, is a flavin-dependent enzyme localised ...
[ "GO:0106364", "GO:0006744" ]
[ "4-hydroxy-3-all-trans-polyprenylbenzoate oxygenase activity", "ubiquinone biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "NCBIFAM" ]
[ "MF_03193", "TIGR01989" ]
[ "COQ6_monooxygenase", "COQ6" ]
[ 3725, 1771 ]
2
[ "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.14.15.45", "1.14.15.46", "R-BTA-2142789", "R-CEL-2142789", "R-DDI-2142789", "R-DME-2142789", "R-DRE-2142789", "R-HSA-2142789", "R-MMU-2142789", "R-RNO-2142789", "R-SCE-2142789", "R-SPO-2142789", "R-XTR-2142789" ]
[ "EC:1.14.15.45", "EC:1.14.15.46", "REACTOME:R-BTA-2142789", "REACTOME:R-CEL-2142789", "REACTOME:R-DDI-2142789", "REACTOME:R-DME-2142789", "REACTOME:R-DRE-2142789", "REACTOME:R-HSA-2142789", "REACTOME:R-MMU-2142789", "REACTOME:R-RNO-2142789", "REACTOME:R-SCE-2142789", "REACTOME:R-SPO-2142789", ...
13
[]
0
[ "PUB00013831", "PUB00013848", "PUB00105224", "PUB00154465" ]
[ "12721307", "11583838", "28927698", "21944752" ]
[ "The Saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-dependent monooxygenase required for coenzyme Q biosynthesis.", "Ubiquinone biosynthesis in microorganisms.", "Biochemistry of Mitochondrial Coenzyme Q Biosynthesis.", "Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation rea...
[ 2003, 2001, 2017, 2011 ]
4
[ "IPR010971" ]
[]
1
0
1
[ "Candidatus Competibacteraceae", "Eukaryota" ]
[ 3, 3743 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 9, 1, 3, 1, 2, 2, 1, 4, 3, 1, 1, 5 ]
12
true
Family
Ubiquinone biosynthesis monooxygenase COQ6
Ubiquinone biosynthesis monooxygenase COQ6
UbQ_mOase_COQ6
9
IPR000690
690
Matrin/U1-C, C2H2-type zinc finger
Matrin/U1-C_Znf_C2H2
Domain
21,241
false
false
Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b...
[ "GO:0003676", "GO:0008270", "GO:0005634" ]
[ "nucleic acid binding", "zinc ion binding", "nucleus" ]
[ "molecular_function", "molecular_function", "cellular_component" ]
3
[ "PROFILE" ]
[ "PS50171" ]
[ "ZF_MATRIN" ]
[ 21241 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50171", "R-BTA-72163", "R-CFA-72163", "R-HSA-381340", "R-HSA-72163", "R-MMU-72163", "R-RNO-72163" ]
[ "PROSITEDOC:PDOC50171", "REACTOME:R-BTA-72163", "REACTOME:R-CFA-72163", "REACTOME:R-HSA-381340", "REACTOME:R-HSA-72163", "REACTOME:R-MMU-72163", "REACTOME:R-RNO-72163" ]
7
[ "2vrd", "3cw1", "4dgw", "4pjo", "5nrl", "5o9z", "5z56", "5z57", "5z58", "5zwm", "5zwn", "5zwo", "6ah0", "6ahd", "6ff4", "6ff7", "6g90", "6n7p", "6n7r", "6n7x", "6qx9", "6y50", "6y53", "6y5q", "7abg", "7abh", "7abi", "7dco", "7evo", "7onb", "7oqb", "7oqc"...
60
[ "PUB00014077", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035808", "PUB00035809", "PUB00035811", "PUB00035812", "PUB00043274" ]
[ "12665246", "17210253", "15963892", "15718139", "10529348", "11361095", "10664601", "10940247", "11179890", "18253864" ]
[ "Zinc fingers--folds for many occasions.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting a grip on RNA.", "Zinc finger peptides for the regulation of gene expression.", "Three classes of C2H2 zinc...
[ 2002, 2007, 2005, 2005, 1999, 2001, 2000, 2000, 2001, 2008 ]
10
[ "IPR003604" ]
[ "IPR013085" ]
1
1
0
[ "Enterobacterales", "Eukaryota", "metagenomes" ]
[ 13, 21224, 4 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 20, 3, 79, 9, 45, 37, 3, 18, 38, 2, 4, 23 ]
12
true
Domain
Matrin/U1-C, C2H2-type zinc finger
Matrin/U1-C, C2H2-type zinc finger
Matrin/U1-C_Znf_C2H2
1
IPR000691
691
Proteinase inhibitor I16, Streptomyces subtilisin-type inhibitor
Prot_inh_I16_SSI
Family
2,074
false
false
The Streptomyces family of bacteria produce a number of proteinase inhibitors, which belong to MEROPS inhibitor family I16, clan IY. They are characterised by their strong activity towards subtilisin (MEROPS peptidase family S8, ) and are collectively known as Streptomyces subtilisin inhibitors (SSI). Some SSI also inh...
[ "GO:0004867" ]
[ "serine-type endopeptidase inhibitor activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "PRINTS" ]
[ "MF_00778", "PR00294" ]
[ "SSI", "SSBTLNINHBTR" ]
[ 761, 2071 ]
2
[ "PROSITEDOC" ]
[ "PDOC00766" ]
[ "PROSITEDOC:PDOC00766" ]
1
[ "2sic", "2tld", "3sic", "3ssi", "4hwx", "4hx2", "4hx3", "5sic", "6i0i" ]
9
[ "PUB00002322", "PUB00002348", "PUB00003205", "PUB00014133" ]
[ "6993452", "1908859", "6387152", "14705960" ]
[ "Importance of the carboxyl-terminal four amino acid residues in the inhibitory activity of Streptomyces subtilisin inhibitor (with a revision of its carboxyl-terminal sequence).", "Inhibition of subtilisin BPN' by reaction site P1 mutants of Streptomyces subtilisin inhibitor.", "Crystal structure at 2.6 A reso...
[ 1980, 1991, 1984, 2004 ]
4
[]
[]
0
0
null
[ "Bacteria", "Fungi incertae sedis" ]
[ 2062, 12 ]
2
[]
[]
0
true
Family
Proteinase inhibitor I16, Streptomyces subtilisin-type inhibitor
Proteinase inhibitor I16, Streptomyces subtilisin-type inhibitor
Prot_inh_I16_SSI
9
IPR000692
692
rRNA 2'-O-methyltransferase fibrillarin-like
Fibrillarin
Family
6,505
false
false
Fibrillarin (rRNA 2'-O-methyltransferase fibrillarin) is a component of a nucleolar small nuclear ribonucleoprotein (SnRNP) [ , ]. It is a S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Site specificity is provided by a guide RNA that base pairs with the su...
[ "GO:0003723", "GO:0008168", "GO:0006364" ]
[ "RNA binding", "methyltransferase activity", "rRNA processing" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "NCBIFAM", "PFAM", "PIRSF", "PRINTS", "SMART" ]
[ "MF_00351", "NF003276", "PF01269", "PIRSF006540", "PR00052", "SM01206" ]
[ "RNA_methyltransf_FlpA", "PRK04266.1-2", "Fibrillarin", "Nop17p", "FIBRILLARIN", "Fibrillarin" ]
[ 5256, 5805, 6493, 3818, 6215, 6387 ]
6
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...
[ "2.1.1.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-5987", "PWY-601", "PWY-6045"...
[ "EC:2.1.1.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", "METACYC:PWY-5729", "METACYC:PWY-5...
156
[ "1fbn", "1g8a", "1g8s", "1nt2", "1pry", "2ipx", "2nnw", "3id5", "3id6", "3nmu", "3nvk", "3nvm", "3pla", "4by9", "4df3", "5gin", "5gio", "5gip", "5jpq", "5oql", "5wlc", "5wyj", "5wyk", "6ke6", "6lqp", "6lqq", "6lqr", "6lqs", "6lqt", "6lqu", "6lqv", "6nd4"...
78
[ "PUB00001181", "PUB00003067", "PUB00004418", "PUB00100520", "PUB00100521", "PUB00100522", "PUB00100523" ]
[ "2686980", "2026646", "8493104", "30540930", "24352239", "1825809", "32017898" ]
[ "A yeast nucleolar protein related to mammalian fibrillarin is associated with small nucleolar RNA and is essential for viability.", "Evolutionary conservation of the human nucleolar protein fibrillarin and its functional expression in yeast.", "Study of multiple fibrillarin mRNAs reveals that 3' end formation ...
[ 1989, 1991, 1993, 2018, 2014, 1991, 2020 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Methanothermobacter phage psiM100", "unclassified sequences" ]
[ 939, 11, 5493, 1, 61 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 12, 1, 1, 3, 11, 4, 1, 8, 9, 1, 1, 28 ]
12
true
Family
rRNA 2'-O-methyltransferase fibrillarin-like
rRNA 2'-O-methyltransferase fibrillarin-like
Fibrillarin
2
IPR000693
693
Sea anemone toxin
Anenome_toxin
Family
40
false
false
Sea anemones produce many different neurotoxins with related structure and function. Proteins belonging to this family include the neurotoxins, of which there are several, including calitoxin and anthopleurin. The neurotoxins bind specifically to the sodium channel, thereby delaying its inactivation during signal trans...
[ "GO:0009966", "GO:0005576" ]
[ "regulation of signal transduction", "extracellular region" ]
[ "biological_process", "cellular_component" ]
2
[ "PIRSF" ]
[ "PIRSF001905" ]
[ "Anenome_toxin" ]
[ 40 ]
1
[]
[]
[]
0
[ "1ahl", "1apf", "1atx", "1sh1", "1shi", "2sh1" ]
6
[ "PUB00023402", "PUB00034660", "PUB00034661", "PUB00103892", "PUB00103893", "PUB00103894" ]
[ "7582896", "6108877", "4019448", "7510258", "22683676", "2567180" ]
[ "Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthopleurin-A.", "Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and A. elegantissima (Brandt).", "Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin-B.", "Isolation a...
[ 1995, 1981, 1985, 1994, 2012, 1989 ]
6
[]
[]
0
0
null
[ "Actiniaria" ]
[ 40 ]
1
[]
[]
0
true
Family
Sea anemone toxin
Sea anemone toxin
Anenome_toxin
9
IPR000697
697
WH1/EVH1 domain
WH1/EVH1_dom
Domain
20,957
false
false
The EVH1 (WH1, RanBP1-WASP) domain is found in multi-domain proteins implicated in a diverse range of signalling, nuclear transport and cytoskeletal events. This domain of around 115 amino acids is present in species ranging from yeast to mammals. Many EVH1-containing proteins associate with actin-based structures and ...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00568", "PS50229", "SM00461" ]
[ "WH1", "WH1", "WH1" ]
[ 19484, 20457, 19293 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50229", "R-BTA-2029482", "R-BTA-203641", "R-BTA-373753", "R-BTA-3928662", "R-BTA-418885", "R-BTA-5663213", "R-BTA-6794361", "R-BTA-8856828", "R-BTA-9013406", "R-BTA-9013424", "R-DDI-446353", "R-DDI-5658442", "R-DME-193648", "R-DME-3928662", "R-DME-3928665", "R-DME-416482", "R-...
[ "PROSITEDOC:PDOC50229", "REACTOME:R-BTA-2029482", "REACTOME:R-BTA-203641", "REACTOME:R-BTA-373753", "REACTOME:R-BTA-3928662", "REACTOME:R-BTA-418885", "REACTOME:R-BTA-5663213", "REACTOME:R-BTA-6794361", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-9013406", "REACTOME:R-BTA-9013424", "REACTOME:R-D...
56
[ "1ddv", "1ddw", "1egx", "1evh", "1i2h", "1i7a", "1mke", "1qc6", "1tj6", "1xod", "2ifs", "2iyb", "2jp2", "2p8v", "2xqn", "3syx", "4my6", "5n91", "5n9c", "5n9p", "5naj", "5nbf", "5nbx", "5nc2", "5nc7", "5ncf", "5ncg", "5ncp", "5nd0", "5ndu", "5neg", "5zz9"...
45
[ "PUB00001307", "PUB00006193", "PUB00006194", "PUB00006195", "PUB00007098" ]
[ "9312002", "9883880", "7724562", "10338211", "11911879" ]
[ "A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family.", "EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family.", "The Ra...
[ 1997, 1998, 1995, 1999, 2002 ]
5
[]
[ "IPR033927", "IPR041937", "IPR044100" ]
0
3
0
[ "Bacillati", "Eukaryota" ]
[ 5, 20952 ]
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)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", ...
[ 8, 85, 25, 58, 44, 1, 5, 79, 1, 1, 13 ]
11
true
Domain
WH1/EVH1 domain
WH1/EVH1 domain
WH1/EVH1_dom
1
IPR000698
698
Arrestin
Arrestin
Family
9,114
false
false
G protein-coupled receptors are a large family of signalling molecules that respond to a wide variety of extracellular stimuli. The receptors relay the information encoded by the ligand through the activation of heterotrimeric G proteins and intracellular effector molecules. To ensure the appropriate regulation of the ...
[ "GO:0007165" ]
[ "signal transduction" ]
[ "biological_process" ]
1
[ "PRINTS", "PANTHER" ]
[ "PR00309", "PTHR11792" ]
[ "ARRESTIN", "" ]
[ 8147, 9092 ]
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-2514859", "R-BTA-418555", "R-BTA-432720", "R-BTA-432722", "R-BTA-456926", "R-BTA-5635838", "R-BTA-5674135", "R-BTA-5689880", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-9839389", "R-CEL-2514859", "R-CEL-432720", "R-CEL-432722", "R-CEL-456926", "R-CEL-5099900", "R-CEL-5674135", ...
[ "REACTOME:R-BTA-2514859", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-432720", "REACTOME:R-BTA-432722", "REACTOME:R-BTA-456926", "REACTOME:R-BTA-5635838", "REACTOME:R-BTA-5674135", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-9839389", "REACTOME:R-...
72
[ "1ayr", "1cf1", "1g4m", "1g4r", "1jsy", "1suj", "1zsh", "2wtr", "3gc3", "3gd1", "3p2d", "3ugu", "3ugx", "4j2q", "4jqi", "4zrg", "4zwj", "5dgy", "5tv1", "5w0p", "6bk9", "6k3f", "6kl7", "6ni2", "6pwc", "6tko", "6u1n", "6up7", "7df9", "7dfa", "7dfb", "7dfc"...
96
[ "PUB00000986", "PUB00001029", "PUB00001684", "PUB00002739", "PUB00004275", "PUB00005126" ]
[ "8452755", "15335861", "7720881", "1517224", "9495348", "2158671" ]
[ "Arrestin-subtypes in insect antennae.", "Arresting G-protein coupled receptor activity.", "The arrestin superfamily: cone arrestins are a fourth family.", "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family.", "X-ray crystal structure of arrestin from bovine rod outer segments.", "A...
[ 1993, 1993, 1995, 1992, 1998, 1990 ]
6
[]
[]
0
0
null
[ "Eukaryota" ]
[ 9114 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 17, 10, 20, 21, 27 ]
6
true
Family
Arrestin
Arrestin
Arrestin
7
IPR000699
699
RIH domain
RIH_dom
Domain
14,973
false
false
Ryanodine (RyR) and Inositol 1,4,5-trisphosphate (IP3) receptors are intracellular Ca 2+ -release channels. The RIH (RyR and IP3R Homology) domain is an extracellular domain from these two types of calcium channels. This domain may form a binding site for IP3 [ ].
[ "GO:0005262", "GO:0070588", "GO:0016020" ]
[ "calcium channel activity", "calcium ion transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF01365" ]
[ "RYDR_ITPR" ]
[ 14973 ]
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-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-HSA-112043", "R-H...
[ "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", "REACTOME:R-DME...
49
[ "1n4k", "2xoa", "3j8h", "3jav", "3t8s", "3uj0", "3uj4", "4i0y", "4i1e", "4i2s", "4i37", "4i3n", "4i6i", "4i7i", "4i8m", "4i96", "4jkq", "4l4h", "4l4i", "4uwa", "4uwe", "5gky", "5gkz", "5gl0", "5gl1", "5go9", "5goa", "5gug", "5j8v", "5l1d", "5t15", "5t9m"...
231
[ "PUB00006473" ]
[ "10664581" ]
[ "Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Eukaryota", "Tenacibaculum skagerrakense", "bird metagenome" ]
[ 14971, 1, 1 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 18, 108, 9, 36, 16, 40 ]
6
true
Domain
RIH domain
RIH domain
RIH_dom
9
IPR000700
700
PAS-associated, C-terminal
PAS-assoc_C
Domain
248,274
false
false
The PAS (Per, Arnt, Sim) domain [ , ] is an approximately 300 amino-acid segment of sequence similarity which is conserved between the Drosophila protein period clock (PER), the Ah receptor nuclear translocator (ARNT) and the Drosophila single-minded (SIM). It is composed of two or more imperfect repeats (PAS-1, PAS-2)...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS50113" ]
[ "PAC" ]
[ 248274 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50112", "R-BTA-1296072", "R-CFA-1296072", "R-CFA-5576890", "R-DME-1296072", "R-HSA-1296072", "R-HSA-5576890", "R-MMU-1296072", "R-MMU-5576890", "R-RNO-1296072", "R-RNO-5576890", "R-SSC-1296072", "R-SSC-5576890" ]
[ "PROSITEDOC:PDOC50112", "REACTOME:R-BTA-1296072", "REACTOME:R-CFA-1296072", "REACTOME:R-CFA-5576890", "REACTOME:R-DME-1296072", "REACTOME:R-HSA-1296072", "REACTOME:R-HSA-5576890", "REACTOME:R-MMU-1296072", "REACTOME:R-MMU-5576890", "REACTOME:R-RNO-1296072", "REACTOME:R-RNO-5576890", "REACTOME:...
13
[ "1byw", "1dp6", "1dp8", "1dp9", "1drm", "1g28", "1jnu", "1lsv", "1lsw", "1lsx", "1lt0", "1n9l", "1n9n", "1n9o", "1xj2", "1xj3", "1xj4", "1xj6", "1y28", "2cmn", "2gj3", "2l0w", "2l1m", "2l4r", "2mwg", "2owh", "2owj", "2pr5", "2pr6", "2v0u", "2v0w", "2v1a"...
238
[ "PUB00005472", "PUB00006196", "PUB00014500" ]
[ "9301332", "9382818", "15009198" ]
[ "PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox.", "PAS: a multifunctional domain family comes to light.", "The PAS fold. A redefinition of the PAS domain based upon structural prediction." ]
[ 1997, 1997, 2004 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 11099, 214931, 19036, 4, 3204 ]
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",...
[ 30, 3, 37, 13, 5, 23, 13, 5, 12, 21, 2, 14 ]
12
true
Domain
PAS-associated, C-terminal
PAS-associated, C-terminal
PAS-assoc_C
3
IPR000701
701
Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit
SuccDH_FuR_B_TM-su
Family
33,281
false
false
Succinate dehydrogenase (SDH) is a membrane-bound complex of two main components: a membrane-extrinsic component composed of an FAD-binding flavoprotein and an iron-sulphur protein, and a hydrophobic component composed of a cytochrome b and a membrane anchor protein. The cytochrome b component is a mono-haem transmembr...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01127" ]
[ "Sdh_cyt" ]
[ 33281 ]
1
[ "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1493", "GenProp1515", "GenProp1693", "PDOC00767", "R-BTA-71403", "R-BTA-9854311", "R-DDI-71403", "R-HSA-611105", "R-HSA-71403", "R-HSA-9854311", "R-MMU-71403", "R-MMU-9854311", "R-SCE-71403", "R-SPO-71403", "R-SSC-71403", "R-SSC-9854311" ]
[ "GP:GenProp1493", "GP:GenProp1515", "GP:GenProp1693", "PROSITEDOC:PDOC00767", "REACTOME:R-BTA-71403", "REACTOME:R-BTA-9854311", "REACTOME:R-DDI-71403", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-71403", "REACTOME:R-HSA-9854311", "REACTOME:R-MMU-71403", "REACTOME:R-MMU-9854311", "REACTOME:R-SCE...
16
[ "1e7p", "1nek", "1nen", "1qlb", "1yq3", "1yq4", "1zoy", "1zp0", "2acz", "2bs2", "2bs3", "2bs4", "2fbw", "2h88", "2h89", "2wdq", "2wdr", "2wdv", "2wp9", "2wqy", "2ws3", "2wu2", "2wu5", "3abv", "3ae1", "3ae2", "3ae3", "3ae4", "3ae5", "3ae6", "3ae7", "3ae8"...
73
[ "PUB00002750", "PUB00003349", "PUB00003763", "PUB00015792", "PUB00152800" ]
[ "1447196", "7616569", "8152421", "9210286", "37490987" ]
[ "Cytochrome b560 (QPs1) of mitochondrial succinate-ubiquinone reductase. Immunochemistry, cloning, and nucleotide sequencing.", "Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus crispus (Gigartinales). Gene content and genome organization.", "Characterization of the Saccharomyces cerevisiae...
[ 1992, 1995, 1994, 1997, 2023 ]
5
[]
[ "IPR004224", "IPR011138", "IPR014312", "IPR014314" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 880, 26831, 5214, 356 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 9, 2, 1, 3, 2, 10, 3, 1, 1, 7, 2, 1, 4 ]
13
true
Family
Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit
Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit
SuccDH_FuR_B_TM-su
8
IPR000704
704
Casein kinase II, regulatory subunit
Casein_kinase_II_reg-sub
Family
9,806
false
false
Casein kinase, a ubiquitous well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Ser or Thr in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha-and 2 beta-subunits [ , ]. However, some species (e.g., mammals) possess 2 related forms of...
[ "GO:0019887", "GO:0005956" ]
[ "protein kinase regulator activity", "protein kinase CK2 complex" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PRINTS", "PROSITE", "PANTHER", "SMART" ]
[ "PF01214", "PR00472", "PS01101", "PTHR11740", "SM01085" ]
[ "CK_II_beta", "CASNKINASEII", "CK2_BETA", "", "CK_II_beta" ]
[ 9791, 9447, 6509, 9589, 9751 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00845", "R-BTA-1483191", "R-BTA-201688", "R-BTA-2514853", "R-BTA-6798695", "R-BTA-6804756", "R-BTA-6814122", "R-BTA-8934903", "R-BTA-8939243", "R-BTA-8948751", "R-BTA-9768727", "R-CEL-1483191", "R-CEL-201688", "R-CEL-445144", "R-CEL-6798695", "R-CEL-6804756", "R-CEL-6814122", ...
[ "PROSITEDOC:PDOC00845", "REACTOME:R-BTA-1483191", "REACTOME:R-BTA-201688", "REACTOME:R-BTA-2514853", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6804756", "REACTOME:R-BTA-6814122", "REACTOME:R-BTA-8934903", "REACTOME:R-BTA-8939243", "REACTOME:R-BTA-8948751", "REACTOME:R-BTA-9768727", "REACTOME:R...
94
[ "1jwh", "1qf8", "1rqf", "2r6m", "3eed", "4dgl", "4md7", "4md8", "4md9", "4nh1" ]
10
[ "PUB00001376", "PUB00002646", "PUB00002858", "PUB00002899" ]
[ "2666134", "1856204", "8027080", "7737972" ]
[ "Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta.", "Structure of the gene encoding human casein kinase II subunit beta.", "Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta'-subunit of Saccharomyces cerevisiae casein k...
[ 1989, 1991, 1994, 1995 ]
4
[]
[]
0
0
null
[ "Eukaryota", "marine sediment metagenome" ]
[ 9805, 1 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 25, 1, 2, 25, 17, 13, 2, 10, 10, 2, 2, 27 ]
12
true
Family
Casein kinase II, regulatory subunit
Casein kinase II, regulatory subunit
Casein_kinase_II_reg-sub
5
IPR000705
705
Galactokinase
Galactokinase
Family
21,881
false
false
Galactokinase catalyses the first reaction in the galactose metabolism pathway, the ATP-dependent phosphorylation of galactose, yielding galactose-1-phosphate [ , ]. Deficiency in this enzyme results in the disease galactosemia, which is responsible for the formation of cataracts in newborn babies, and is possibly resp...
[ "GO:0004335", "GO:0005524", "GO:0006012", "GO:0046835" ]
[ "galactokinase activity", "ATP binding", "galactose metabolic process", "carbohydrate phosphorylation" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]
4
[ "PRINTS", "NCBIFAM" ]
[ "PR00473", "TIGR00131" ]
[ "GALCTOKINASE", "gal_kin" ]
[ 21673, 18426 ]
2
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.1.6", "GenProp0143", "GenProp1310", "GenProp1459", "GenProp1661", "PWY-3821", "PWY-6317", "PWY-6527", "PDOC00099", "R-BTA-70370", "R-CFA-70370", "R-HSA-5609976", "R-HSA-70370", "R-MMU-70370" ]
[ "EC:2.7.1.6", "GP:GenProp0143", "GP:GenProp1310", "GP:GenProp1459", "GP:GenProp1661", "METACYC:PWY-3821", "METACYC:PWY-6317", "METACYC:PWY-6527", "PROSITEDOC:PDOC00099", "REACTOME:R-BTA-70370", "REACTOME:R-CFA-70370", "REACTOME:R-HSA-5609976", "REACTOME:R-HSA-70370", "REACTOME:R-MMU-70370"...
14
[ "1pie", "1s4e", "1wuu", "2a2c", "2a2d", "2aj4", "2cz9", "2dei", "2dej", "3v2u", "3v5r", "6gr2", "6q3w", "6q3x", "6q8z", "6q90", "6q91", "6qje", "6tep", "6teq", "6ter", "6zfh", "6zgv", "6zgw", "6zgx", "6zgy", "6zgz", "6zh0", "7ozx", "7rcl", "7rcm", "7s49"...
34
[ "PUB00003653", "PUB00004765" ]
[ "3062381", "1438294" ]
[ "Yeast regulatory gene GAL3: carbon regulation; UASGal elements in common with GAL1, GAL2, GAL7, GAL10, GAL80, and MEL1; encoded protein strikingly similar to yeast and Escherichia coli galactokinases.", "Cloning of a human galactokinase gene (GK2) on chromosome 15 by complementation in yeast." ]
[ 1988, 1992 ]
2
[ "IPR006206" ]
[ "IPR022963" ]
1
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctmP19", "unclassified sequences" ]
[ 457, 14568, 6622, 1, 233 ]
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, 2, 1, 1, 14, 11, 1, 2, 13, 2, 1, 8 ]
13
true
Family
Galactokinase
Galactokinase
Galactokinase
9
IPR000706
706
N-acetyl-gamma-glutamyl-phosphate reductase, type 1
AGPR_type-1
Family
22,768
false
false
This entry represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of thi...
[ "GO:0003942", "GO:0070401", "GO:0006526" ]
[ "N-acetyl-gamma-glutamyl-phosphate reductase activity", "NADP+ binding", "L-arginine biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "NCBIFAM" ]
[ "MF_00150", "TIGR01850" ]
[ "ArgC_type1", "argC" ]
[ 22447, 22670 ]
2
[ "EC", "EC", "GP", "GP", "GP", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.2.1", "1.2.1.38", "GenProp0118", "GenProp0193", "GenProp1466", "PWY-5154", "PDOC00941", "R-DDI-70635", "R-SCE-70635", "R-SPO-70635" ]
[ "EC:1.2.1", "EC:1.2.1.38", "GP:GenProp0118", "GP:GenProp0193", "GP:GenProp1466", "METACYC:PWY-5154", "PROSITEDOC:PDOC00941", "REACTOME:R-DDI-70635", "REACTOME:R-SCE-70635", "REACTOME:R-SPO-70635" ]
10
[ "1vkn", "1xyg", "2cvo", "2g17", "2i3a", "2i3g", "2nqt", "2ozp", "2q49", "3dr3", "5ein", "5eio", "7nni", "7nnq", "7nnr", "7not", "7nph", "7npj", "8afu", "8afv" ]
20
[ "PUB00002190", "PUB00002893", "PUB00014499", "PUB00015490", "PUB00053254", "PUB00083920", "PUB00083921" ]
[ "1339424", "7907589", "12633501", "10613839", "19620981", "26966182", "23434852" ]
[ "Characterization of the Streptomyces clavuligerus argC gene encoding N-acetylglutamyl-phosphate reductase: expression in Streptomyces lividans and effect on clavulanic acid production.", "A polyprotein precursor of two mitochondrial enzymes in Neurospora crassa. Gene structure and precursor processing.", "N-ac...
[ 1992, 1994, 2003, 1999, 2009, 2016, 2013 ]
7
[ "IPR050085" ]
[ "IPR037535" ]
1
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 804, 19049, 2469, 1, 445 ]
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, 6, 1, 1, 3 ]
7
true
Family
N-acetyl-gamma-glutamyl-phosphate reductase, type 1
N-acetyl-gamma-glutamyl-phosphate reductase, type 1
AGPR_type-1
6
IPR000708
708
Prostanoid EP1 receptor
Prostglndn_EP1_rcpt
Family
183
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004957", "GO:0007186", "GO:0016020" ]
[ "prostaglandin E receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00580" ]
[ "PRSTNOIDEP1R" ]
[ 183 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "340", "R-CFA-391908", "R-CFA-416476", "R-HSA-391908", "R-HSA-416476", "R-MMU-391908", "R-MMU-416476", "R-RNO-391908", "R-RNO-416476" ]
[ "IUPHAR:340", "REACTOME:R-CFA-391908", "REACTOME:R-CFA-416476", "REACTOME:R-HSA-391908", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-391908", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-391908", "REACTOME:R-RNO-416476" ]
9
[ "9m1h" ]
1
[ "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
[ "IPR001244" ]
[]
1
0
1
[ "Theria" ]
[ 183 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 5 ]
3
true
Family
Prostanoid EP1 receptor
Prostanoid EP1 receptor
Prostglndn_EP1_rcpt
3
IPR000709
709
Leu/Ile/Val-binding protein
Leu_Ile_Val-bd
Family
32,302
false
false
Leu/Ile/Val/Thr- and Leu-binding proteins, which share a high degree of sequence similarity, are components of the leucine-specific transport system. This is one of two periplasmic binding protein-dependent systems in the high-affinity transport of branched-chain amino acids in bacteria [ , , ]. A much weaker sequence ...
[ "GO:0006865" ]
[ "amino acid transport" ]
[ "biological_process" ]
1
[ "PRINTS" ]
[ "PR00337" ]
[ "LEUILEVALBP" ]
[ 32302 ]
1
[]
[]
[]
0
[ "1pea", "1qnl", "1qo0", "1usg", "1usi", "1usk", "1z15", "1z16", "1z17", "1z18", "2lbp", "2liv", "3i45", "3ip5", "3ip6", "3ip7", "3ip9", "3ipa", "3ipc", "4evs", "4f06", "4gnr", "4m88", "4mlc", "4mpt", "4n0q", "4q6b", "4q6w", "4xfk", "7jfn", "7ylt", "8q52"...
35
[ "PUB00001238", "PUB00002417", "PUB00003242", "PUB00097187" ]
[ "8253087", "3891753", "2649682", "19597156" ]
[ "Antitermination of amidase expression in Pseudomonas aeruginosa is controlled by a novel cytoplasmic amide-binding protein.", "The complete nucleotide sequences of the Escherichia coli LIV-BP and LS-BP genes. Implications for the mechanism of high-affinity branched-chain amino acid transport.", "Periplasmic bi...
[ 1993, 1985, 1989, 2009 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 133, 31832, 33, 304 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Leu/Ile/Val-binding protein
Leu/Ile/Val-binding protein
Leu_Ile_Val-bd
8
IPR000710
710
Peptidase S6, IgA endopeptidase
Peptidase_S6
Family
975
false
false
This family consists of immunoglobulin A1 protease proteins. The immunoglobulin A1 protease cleaves immunoglobulin IgA and is found in pathogenic bacteria such as Neisseria gonorrhoeae [ ]. Not all of the members of this family are IgA proteases. EspP ( ) from Escherichia coli O157:H7 cleaves human coagulation factor V...
[ "GO:0004252", "GO:0006508" ]
[ "serine-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00921" ]
[ "IGASERPTASE" ]
[ 975 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME" ]
[ "3.4.21.-", "PWY-7884", "R-HSA-9760173", "R-HSA-9927020" ]
[ "EC:3.4.21.-", "METACYC:PWY-7884", "REACTOME:R-HSA-9760173", "REACTOME:R-HSA-9927020" ]
4
[ "1wxr", "3ak5", "3h09", "3syj", "3sze", "5j44", "9mne" ]
7
[ "PUB00008434", "PUB00020059", "PUB00020060" ]
[ "3027577", "9743528", "9194704" ]
[ "Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease.", "Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1.", "EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V...
[ 1987, 1998, 1997 ]
3
[]
[]
0
0
null
[ "Bacteria", "unclassified Caudoviricetes" ]
[ 973, 2 ]
2
[]
[]
0
true
Family
Peptidase S6, IgA endopeptidase
Peptidase S6, IgA endopeptidase
Peptidase_S6
3
IPR000713
713
Mur ligase, N-terminal catalytic domain
Mur_ligase_N
Domain
82,504
false
false
The bacterial cell wall provides strength and rigidity to counteract internal osmotic pressure, and protection against the environment. The peptidoglycan layer gives the cell wall its strength, and helps maintain the overall shape of the cell. The basic peptidoglycan structure of both Gram-positive and Gram-negative ba...
[ "GO:0016881", "GO:0009058" ]
[ "acid-amino acid ligase activity", "biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF01225" ]
[ "Mur_ligase" ]
[ 82504 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC" ]
[ "6.3.2", "6.3.2.8", "PWY-6386", "PWY-6387", "PWY-7953" ]
[ "EC:6.3.2", "EC:6.3.2.8", "METACYC:PWY-6386", "METACYC:PWY-6387", "METACYC:PWY-7953" ]
5
[ "1e8c", "1gg4", "1gqq", "1gqy", "1j6u", "1p31", "1p3d", "2am1", "2am2", "2f00", "2wtz", "2xja", "3eag", "3hn7", "3zl8", "3zm5", "3zm6", "4bub", "4cvk", "4cvl", "4cvm", "4hv4", "4qdi", "4qf5", "4ziy", "5vvw", "6cau", "6x9f", "6x9n", "7b53", "7b60", "7b61"...
61
[ "PUB00035788", "PUB00035789", "PUB00035790", "PUB00035791", "PUB00035792", "PUB00101154" ]
[ "17139082", "17427948", "16595662", "16322581", "16934839", "18974047" ]
[ "Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC).", "Targeted molecular dynamics simulation studies of binding and conformational changes in E. coli MurD.", "The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity.", "Structure of MurF from S...
[ 2006, 2007, 2006, 2005, 2006, 2008 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]
[ 80015, 914, 3, 1572 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 5, 4 ]
2
true
Domain
Mur ligase, N-terminal catalytic domain
Mur ligase, N-terminal catalytic domain
Mur_ligase_N
9
IPR000714
714
Equine herpesvirus protein of unknown function
EHV_Unk
Family
226
false
false
The IR5 open reading frame (ORF) of the Equid herpesvirus 1 (EHV-1) genome maps within the inverted repeat segments. Sequence analyses of the gene region revealed an ORF of 236 amino acids that showed a high degree of similarity to ORF64 of Human herpesvirus 3 (HHV-3) and ORF3 of Equid herpesvirus 4 (EHV-4), both of wh...
[ "GO:0008270" ]
[ "zinc ion binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS" ]
[ "PF02053", "PR00957" ]
[ "Gene66", "GENE66" ]
[ 226, 215 ]
2
[]
[]
[]
0
[]
0
[ "PUB00005585", "PUB00005949" ]
[ "1316680", "1282282" ]
[ "Identification and characterization of an equine herpesvirus 1 late gene encoding a potential zinc finger.", "Sequence determination and genetic content of an 8.9-kb restriction fragment in the short unique region and the internal inverted repeat of Marek's disease virus type 1 DNA." ]
[ 1992, 1992 ]
2
[]
[]
0
0
null
[ "Alphaherpesvirinae", "Streptomyces ramulosus" ]
[ 225, 1 ]
2
[]
[]
0
true
Family
Equine herpesvirus protein of unknown function
Equine herpesvirus protein of unknown function
EHV_Unk
9
IPR000715
715
Glycosyl transferase, family 4
Glycosyl_transferase_4
Family
55,260
false
false
This entry represents a family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P transferases. Members of the family include eukaryotic N-acetylglucosamine-1-phosphate transferases, which catalyse the conversion of UDP-N-acteyl-D-glucosamine and dolichyl phosphate to UMP and N-acetyl-D-glucosaminyl-diphosphodolic...
[ "GO:0016780", "GO:0016020" ]
[ "phosphotransferase activity, for other substituted phosphate groups", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PANTHER" ]
[ "PF00953", "PTHR22926" ]
[ "Glycos_transf_4", "" ]
[ 54883, 50069 ]
2
[ "EC", "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.8", "2.7.8.13", "GenProp1270", "GenProp1398", "GenProp1480", "GenProp1756", "PWY-5265", "PWY-6385", "PWY-6470", "PWY-6471", "R-DDI-446193", "R-HSA-446193", "R-HSA-4549356", "R-MMU-446193", "R-SCE-446193", "R-SPO-446193" ]
[ "EC:2.7.8", "EC:2.7.8.13", "GP:GenProp1270", "GP:GenProp1398", "GP:GenProp1480", "GP:GenProp1756", "METACYC:PWY-5265", "METACYC:PWY-6385", "METACYC:PWY-6470", "METACYC:PWY-6471", "REACTOME:R-DDI-446193", "REACTOME:R-HSA-446193", "REACTOME:R-HSA-4549356", "REACTOME:R-MMU-446193", "REACTOM...
16
[ "4j72", "5ckr", "5jnq", "5lev", "5o5e", "6bw5", "6bw6", "6fm9", "6fwz", "6oyh", "6oyz", "6oz6", "8cxr", "8g01", "8g02", "8tlu", "9b70", "9b71" ]
18
[]
[]
[]
[]
0
[]
[ "IPR003524", "IPR012750", "IPR033895" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 496, 47874, 5658, 1, 1231 ]
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",...
[ 16, 1, 1, 1, 2, 12, 2, 1, 6, 4, 1, 1, 18 ]
13
true
Family
Glycosyl transferase, family 4
Glycosyl transferase, family 4
Glycosyl_transferase_4
6
IPR000716
716
Thyroglobulin type-1
Thyroglobulin_1
Domain
23,591
false
false
Thyroglobulin (Tg) is a large glycoprotein specific to the thyroid gland and is the precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3). The N-terminal section of Tg contains 10 repeats of a domain of about 65 amino acids which is known as the Tg type-1 repeat [ , ]. Such a domain has a...
[]
[]
[]
0
[ "PFAM", "PROSITE", "PROFILE", "SMART", "CDD" ]
[ "PF00086", "PS00484", "PS51162", "SM00211", "cd00191" ]
[ "Thyroglobulin_1", "THYROGLOBULIN_1_1", "THYROGLOBULIN_1_2", "TY", "TY" ]
[ 23126, 19378, 23089, 22352, 21996 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00377", "R-BTA-381426", "R-BTA-6803211", "R-BTA-8957275", "R-DRE-381426", "R-HSA-1474228", "R-HSA-1592389", "R-HSA-202733", "R-HSA-2132295", "R-HSA-3000157", "R-HSA-380994", "R-HSA-381426", "R-HSA-6803211", "R-HSA-8957275", "R-HSA-9615017", "R-HSA-9638630", "R-HSA-9925563", "R...
[ "PROSITEDOC:PDOC00377", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-6803211", "REACTOME:R-BTA-8957275", "REACTOME:R-DRE-381426", "REACTOME:R-HSA-1474228", "REACTOME:R-HSA-1592389", "REACTOME:R-HSA-202733", "REACTOME:R-HSA-2132295", "REACTOME:R-HSA-3000157", "REACTOME:R-HSA-380994", "REACTOME:R-HS...
36
[ "1icf", "1l3h", "1rmj", "1zt3", "1zt5", "2dsq", "2dsr", "2h7t", "4mzv", "6i07", "6o0d", "6o0e", "6o0f", "6scj", "7b75", "7e5m", "7e5n", "7n4y", "7pee", "7qtq", "7ufg", "7wrq", "8d6g", "8d6m", "8d6o", "8d6p", "8d6q", "8d6s", "8d6t", "8d6u", "8r6t", "8v65"...
38
[ "PUB00001151", "PUB00001350", "PUB00001467", "PUB00002700", "PUB00002990", "PUB00004708", "PUB00004834", "PUB00014542" ]
[ "3038530", "3595599", "8797845", "1709161", "9153250", "2333300", "8146142", "12650938" ]
[ "Primary structure of the gene for the murine Ia antigen-associated invariant chains (Ii). An alternatively spliced exon encodes a cysteine-rich domain highly homologous to a repetitive sequence of thyroglobulin.", "Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary ...
[ 1987, 1987, 1996, 1991, 1997, 1990, 1994, 2003 ]
8
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "marine metagenome" ]
[ 14, 23576, 1 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 14, 97, 9, 61, 46, 62 ]
6
true
Domain
Thyroglobulin type-1
Thyroglobulin type-1
Thyroglobulin_1
1
IPR000717
717
Proteasome component (PCI) domain
PCI_dom
Domain
92,784
false
false
The PCI (for Proteasome, COP9, Initiation factor 3) domain (sometimes also referred to as the PINT domain, for Proteasome subunits, Int-6, Nip-1, and Trip-15) is present in six different subunits of 26 proteasome lid, COP9 signalosome (CSN) and eukaryotic translation initiation factor-3 (eIF3) complexes, as well as in ...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF01399", "PS50250", "SM00088" ]
[ "PCI", "PCI", "PINT" ]
[ 72819, 89598, 64744 ]
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-1169091", "R-BTA-1234176", "R-BTA-1236978", "R-BTA-156827", "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-450408", "R-BT...
[ "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1234176", "REACTOME:R-BTA-1236978", "REACTOME:R-BTA-156827", "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-202424", "REACTOME:R-BTA-...
568
[ "1rz4", "1ufm", "2mr3", "2mri", "3chm", "3j8b", "3j8c", "3jap", "3jck", "3jco", "3jcp", "3t5v", "3t5x", "3txm", "3txn", "4b0z", "4cr2", "4cr3", "4cr4", "4d0p", "4d10", "4d18", "4k51", "4lct", "4trq", "4u1c", "4u1d", "4uer", "4wsn", "5a5b", "5a5t", "5g5p"...
193
[ "PUB00005051", "PUB00005480", "PUB00030855", "PUB00051002", "PUB00077378", "PUB00088687" ]
[ "9605331", "9644972", "15180986", "18854373", "23818606", "15790418" ]
[ "Homologues of 26S proteasome subunits are regulators of transcription and translation.", "The PCI domain: a common theme in three multiprotein complexes.", "Crystal structure of human eIF3k, the first structure of eIF3 subunits.", "The Arabidopsis COP9 signalosome subunit 7 is a model PCI domain protein with...
[ 1998, 1998, 2004, 2008, 2013, 2005 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Myoviridae sp. ctXXl13", "metagenomes" ]
[ 7, 35, 92727, 1, 14 ]
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...
[ 126, 22, 40, 33, 138, 89, 17, 88, 115, 14, 21, 248 ]
12
true
Domain
Proteasome component (PCI) domain
Proteasome component (PCI) domain
PCI_dom
3
IPR000718
718
Peptidase M13
Peptidase_M13
Family
47,965
false
false
This group of metallopeptidases belong to the MEROPS peptidase family M13 (neprilysin family, clan MA(E)). The M13 family includes neprilysin (neutral endopeptidase, NEP, enkephalinase, CD10, CALLA, ), endothelin-converting enzyme I (ECE-1, ), erythrocyte surface antigen KELL (ECE-3), phosphate-regulating gene on the X...
[ "GO:0004222", "GO:0006508" ]
[ "metalloendopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PROFILE", "PANTHER", "CDD" ]
[ "PS51885", "PTHR11733", "cd08662" ]
[ "NEPRILYSIN", "", "M13" ]
[ 47813, 45631, 34556 ]
3
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.24", "R-BTA-375276", "R-CEL-2022377", "R-CEL-5578768", "R-CEL-6798695", "R-DME-2022377", "R-DME-5578768", "R-DME-6798695", "R-HSA-2022377", "R-HSA-375276", "R-HSA-5578768", "R-HSA-6798695", "R-HSA-9927432", "R-MMU-2022377", "R-MMU-375276", "R-MMU-5578768", "R-MMU-6798695", "R-...
[ "EC:3.4.24", "REACTOME:R-BTA-375276", "REACTOME:R-CEL-2022377", "REACTOME:R-CEL-5578768", "REACTOME:R-CEL-6798695", "REACTOME:R-DME-2022377", "REACTOME:R-DME-5578768", "REACTOME:R-DME-6798695", "REACTOME:R-HSA-2022377", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-5578768", "REACTOME:R-HSA-6798695...
21
[ "1dmt", "1r1h", "1r1i", "1r1j", "1y8j", "2qpj", "2yb9", "3dwb", "3zuk", "4cth", "4iuw", "4xbh", "4zr5", "5jmy", "5v48", "6gid", "6row", "6sh1", "6sh2", "6suk", "6svy", "6thp", "6xly", "6xvp", "7k1v", "9eyg", "9kn2" ]
27
[ "PUB00000181", "PUB00001657", "PUB00003579", "PUB00011643", "PUB00030479", "PUB00035235", "PUB00038711", "PUB00051515", "PUB00080115", "PUB00080116", "PUB00080117", "PUB00080118", "PUB00080119", "PUB00080120" ]
[ "3555489", "8099556", "7674922", "11223883", "14747736", "15544566", "15893768", "18992253", "10849750", "10698686", "16526590", "16423827", "10791880", "9141502" ]
[ "Molecular cloning and amino acid sequence of rat enkephalinase.", "Substitution of potential metal-coordinating amino acid residues in the zinc-binding site of endopeptidase-24.11.", "Evolutionary families of metallopeptidases.", "The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and functi...
[ 1987, 1993, 1995, 2001, 2004, 2004, 2005, 2009, 2000, 2000, 2006, 2006, 2000, 1997 ]
14
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 64, 14230, 33324, 24, 323 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 36, 26, 52, 90, 34, 37 ]
6
true
Family
Peptidase M13
Peptidase M13
Peptidase_M13
6
IPR000719
719
Protein kinase domain
Prot_kinase_dom
Domain
2,246,867
false
false
This entry represents the protein kinase domain containing the catalytic function of protein kinases [ ]. This domain is found in serine/threonine-protein kinases, tyrosine-protein kinases and dual specificity protein kinases. Eukaryotic protein kinases [ , , , , ] are enzymes that belong to a very extensive family of ...
[ "GO:0004672", "GO:0005524", "GO:0006468" ]
[ "protein kinase activity", "ATP binding", "protein phosphorylation" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00069", "PS50011", "SM00220" ]
[ "Pkinase", "PROTEIN_KINASE_DOM", "S_TKc" ]
[ 1576707, 2239617, 1622098 ]
3
[ "EC", "EC", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "2.7.1", "2.7.11", "GenProp1758", "PDOC00100", "R-BTA-110056", "R-BTA-111933", "R-BTA-111995", "R-BTA-112382", "R-BTA-112409", "R-BTA-112411", "R-BTA-114516", "R-BTA-114604", "R-BTA-1169091", "R-BTA-1181150", "R-BTA-1227986", "R-BTA-1257604", "R-BTA-1295596", "R-BTA-141444", "R-B...
[ "EC:2.7.1", "EC:2.7.11", "GP:GenProp1758", "PROSITEDOC:PDOC00100", "REACTOME:R-BTA-110056", "REACTOME:R-BTA-111933", "REACTOME:R-BTA-111995", "REACTOME:R-BTA-112382", "REACTOME:R-BTA-112409", "REACTOME:R-BTA-112411", "REACTOME:R-BTA-114516", "REACTOME:R-BTA-114604", "REACTOME:R-BTA-1169091",...
3,694
[ "1a06", "1a9u", "1ad5", "1agw", "1apm", "1aq1", "1atp", "1b38", "1b39", "1b6c", "1bi7", "1bi8", "1bkx", "1bl6", "1bl7", "1blx", "1bmk", "1buh", "1bx6", "1byg", "1cdk", "1cki", "1ckj", "1ckp", "1cm8", "1cmk", "1csn", "1ctp", "1daw", "1day", "1di8", "1di9"...
7,939
[ "PUB00001530", "PUB00003568", "PUB00003569", "PUB00005115", "PUB00005145", "PUB00015293", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899" ]
[ "7768349", "1835513", "1956325", "3291115", "1862342", "12734000", "12368087", "12471243", "15078142", "15320712" ]
[ "Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.", "Protein kinase classification.", "Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members.", "The ...
[ 1995, 1991, 1991, 1988, 1991, 2003, 2002, 2002, 2004, 2004 ]
10
[]
[ "IPR001245", "IPR015725", "IPR020676", "IPR024105", "IPR026611", "IPR027084", "IPR027916", "IPR028754", "IPR029878", "IPR030611", "IPR033702", "IPR034661", "IPR034668", "IPR034670", "IPR034671", "IPR034672", "IPR034673", "IPR034674", "IPR035014", "IPR035053", "IPR035056", "...
0
69
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 2993, 184410, 2054286, 2531, 2647 ]
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",...
[ 5230, 587, 4230, 1023, 1, 2669, 1794, 132, 4638, 2383, 117, 110, 7686 ]
13
true
Domain
Protein kinase domain
Protein kinase domain
Prot_kinase_dom
2
IPR000720
720
Peptidylglycine alpha-hydroxylating monooxygenase/peptidyl-hydroxyglycine alpha-amidating lyase
PHM/PAL
Family
4,251
false
false
In vertebrates, peptidylglycine alpha-amidating monooxygenase (PAM) is a multifunctional protein found in secretory granules. The protein contains two enzymes, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL), that act sequentially to catalyse the alp...
[ "GO:0003824", "GO:0006518", "GO:0016020" ]
[ "catalytic activity", "peptide metabolic process", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00790" ]
[ "PAMONOXGNASE" ]
[ 4251 ]
1
[ "EC", "EC" ]
[ "1.14.17.3", "4.3.2.5" ]
[ "EC:1.14.17.3", "EC:4.3.2.5" ]
2
[ "1opm", "1phm", "1sdw", "1yi9", "1yip", "1yjk", "1yjl", "3fvz", "3fw0", "3mib", "3mic", "3mid", "3mie", "3mif", "3mig", "3mih", "3mlj", "3mlk", "3mll", "3phm", "4e4z", "5wja", "5wkw", "5wm0", "6ala", "6alv", "6amp", "6an3", "6ao6", "6ay0", "6nck", "8dsj"...
34
[ "PUB00002655", "PUB00003713", "PUB00076896", "PUB00076897", "PUB00076898", "PUB00076899" ]
[ "1988445", "1448112", "11028916", "16301310", "10993678", "15198673" ]
[ "Characterization of novel mRNAs encoding enzymes involved in peptide alpha-amidation.", "The multifunctional peptidylglycine alpha-amidating monooxygenase gene: exon/intron organization of catalytic, processing, and routing domains.", "New insights into copper monooxygenases and peptide amidation: structure, m...
[ 1991, 1992, 2000, 2006, 2000, 2004 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "marine metagenome" ]
[ 72, 4167, 12 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 2, 5, 8, 5, 10 ]
6
true
Family
Peptidylglycine alpha-hydroxylating monooxygenase/peptidyl-hydroxyglycine alpha-amidating lyase
Peptidylglycine alpha-hydroxylating monooxygenase/peptidyl-hydroxyglycine alpha-amidating lyase
PHM/PAL
2
IPR000722
722
RNA polymerase, alpha subunit
RNA_pol_asu
Domain
71,909
false
false
RNA polymerases catalyse the DNA dependent polymerisation of RNA from DNA, using the four ribonucleoside triphosphates as substrates. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial and chloroplast polymerases). Eukaryotic RNA polymerase I is essentially used to ...
[ "GO:0003677", "GO:0003899", "GO:0006351" ]
[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF00623" ]
[ "RNA_pol_Rpb1_2" ]
[ 71909 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.7.6", "R-BTA-112382", "R-BTA-113418", "R-BTA-5578749", "R-BTA-674695", "R-BTA-6781823", "R-BTA-6782135", "R-BTA-6782210", "R-BTA-6796648", "R-BTA-6803529", "R-BTA-6807505", "R-BTA-72086", "R-BTA-72163", "R-BTA-72165", "R-BTA-72203", "R-BTA-73776", "R-BTA-73779", "R-BTA-75953",...
[ "EC:2.7.7.6", "REACTOME:R-BTA-112382", "REACTOME:R-BTA-113418", "REACTOME:R-BTA-5578749", "REACTOME:R-BTA-674695", "REACTOME:R-BTA-6781823", "REACTOME:R-BTA-6782135", "REACTOME:R-BTA-6782210", "REACTOME:R-BTA-6796648", "REACTOME:R-BTA-6803529", "REACTOME:R-BTA-6807505", "REACTOME:R-BTA-72086",...
209
[ "1hqm", "1i3q", "1i50", "1i6h", "1i6v", "1iw7", "1k83", "1l9u", "1l9z", "1nik", "1nt9", "1pqv", "1r5u", "1r9s", "1r9t", "1sfo", "1smy", "1twa", "1twc", "1twf", "1twg", "1twh", "1wcm", "1y1v", "1y1w", "1y1y", "1y77", "1ynj", "1ynn", "1zyr", "2a68", "2a69"...
1,220
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 966, 26633, 43100, 467, 743 ]
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",...
[ 32, 3, 5, 8, 1, 15, 14, 3, 28, 8, 3, 3, 81 ]
13
true
Domain
RNA polymerase, alpha subunit
RNA polymerase, alpha subunit
RNA_pol_asu
6
IPR000723
723
G protein-coupled receptor 3/6/12 orphan
GPR_3/6/12_orphan
Family
2,941
false
false
Amongst the rhodopsin-like GPCRs are a family of orphan receptors whose members are designated GPR3, GPR6 and GPR12. Whilst these receptors do show sequence similarity to other rhodopsin-class GPCRs, the overall degree of similarity is very low, and evidence that they are functional GPCRs has not yet been gathered expe...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR00644" ]
[ "GPRORPHANR" ]
[ 2941 ]
1
[]
[]
[]
0
[ "7y3g", "8t1v", "8t1w", "8tf5", "8tyw", "8u8f", "8ww2", "8x2k", "9lyb", "9lyc", "9lyd", "9m88", "9m8p", "9m8v" ]
14
[]
[]
[]
[]
0
[ "IPR000276" ]
[ "IPR000599", "IPR000984", "IPR001151" ]
1
3
0
[ "Vertebrata" ]
[ 2941 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 12, 6, 7 ]
4
true
Family
G protein-coupled receptor 3/6/12 orphan
G protein-coupled receptor 3/6/12 orphan
GPR_3/6/12_orphan
5
IPR000724
724
IgG-binding B
IgG-bd_B
Domain
44
false
false
This domain is found as a tandem repeat in Streptococcal cell surface proteins, such as the IgG binding proteins G. These proteins are type I membrane proteins that bind to the constant Fc region of IgG with high affinity.
[ "GO:0005618" ]
[ "cell wall" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF01378" ]
[ "IgG_binding_B" ]
[ 44 ]
1
[]
[]
[]
0
[ "1em7", "1fcc", "1fcl", "1fd6", "1gb1", "1gb4", "1ibx", "1igc", "1igd", "1mhx", "1mi0", "1mpe", "1mvk", "1p7e", "1p7f", "1pga", "1pgb", "1pgx", "1pn5", "1q10", "1qkz", "1uwx", "2cwb", "2den", "2gb1", "2gi9", "2i2y", "2i38", "2igd", "2igg", "2igh", "2j52"...
169
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacillota", "Human immunodeficiency virus type 1" ]
[ 43, 1 ]
2
[]
[]
0
true
Domain
IgG-binding B
IgG-binding B
IgG-bd_B
2
IPR000725
725
Olfactory receptor
Olfact_rcpt
Family
175,194
false
false
The olfactory system is a highly specialised chemical recognition system that, like the immune system, is capable of discriminating with tremendous sensitivity between numerous foreign molecules in the environment. Olfactory transduction is believed to be initiated by the binding of odorants to specific receptor protei...
[ "GO:0004984", "GO:0007186", "GO:0016020" ]
[ "olfactory receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PRINTS" ]
[ "PF13853", "PR00245" ]
[ "7tm_4", "OLFACTORYR" ]
[ 172737, 169648 ]
2
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-381753", "R-HSA-9752946", "R-MMU-381753" ]
[ "REACTOME:R-HSA-381753", "REACTOME:R-HSA-9752946", "REACTOME:R-MMU-381753" ]
3
[ "8f76", "8hti", "8j46", "8uxv", "8uxy", "8uy0", "8uyq", "8w77" ]
8
[ "PUB00001028", "PUB00004960", "PUB00004961", "PUB00066999", "PUB00067000", "PUB00158910" ]
[ "15335857", "8386361", "8170923", "14507991", "10089886", "36922591" ]
[ "Olfactory receptors.", "Design of a discriminating fingerprint for G-protein-coupled receptors.", "Fingerprinting G-protein-coupled receptors.", "Evolution of olfactory receptor genes in the human genome.", "Combinatorial receptor codes for odors.", "Structural basis of odorant recognition by a human odo...
[ 1993, 1993, 1994, 2003, 1999, 2023 ]
6
[ "IPR000276" ]
[ "IPR047132", "IPR047940", "IPR050402" ]
1
3
0
[ "Eumetazoa", "bird metagenome" ]
[ 175192, 2 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 170, 1276, 2312, 1974 ]
4
true
Family
Olfactory receptor
Olfactory receptor
Olfact_rcpt
8
IPR000726
726
Glycoside hydrolase, family 19, catalytic
Glyco_hydro_19_cat
Domain
17,875
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0004568", "GO:0006032", "GO:0016998" ]
[ "chitinase activity", "chitin catabolic process", "cell wall macromolecule catabolic process" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM", "PROSITE", "PROSITE" ]
[ "PF00182", "PS00773", "PS00774" ]
[ "Glyco_hydro_19", "CHITINASE_19_1", "CHITINASE_19_2" ]
[ 17860, 4706, 5257 ]
3
[ "CAZY", "EC", "METACYC", "METACYC", "METACYC", "PROSITEDOC" ]
[ "GH19", "3.2.1.14", "PWY-6855", "PWY-6902", "PWY-7822", "PDOC00620" ]
[ "CAZY:GH19", "EC:3.2.1.14", "METACYC:PWY-6855", "METACYC:PWY-6902", "METACYC:PWY-7822", "PROSITEDOC:PDOC00620" ]
6
[ "1cns", "1dxj", "1wvu", "1wvv", "2baa", "2cjl", "2dbt", "2dkv", "2z37", "2z38", "2z39", "3cql", "3hbd", "3hbe", "3hbh", "3iwr", "3w3e", "3wh1", "4dwx", "4dyg", "4ij4", "4j0l", "4mck", "4mst", "4ok7", "4tx7", "5h7t", "6lnr", "7f88", "7r6s", "7v91", "7v92"...
40
[ "PUB00000503", "PUB00001488", "PUB00004870", "PUB00005266", "PUB00036615", "PUB00079509", "PUB00079510", "PUB00079511", "PUB00080039", "PUB00080040" ]
[ "1747104", "1516675", "7624375", "8535779", "10957628", "9723170", "8564539", "12369923", "10906956", "10906957" ]
[ "A classification of glycosyl hydrolases based on amino acid sequence similarities.", "What's new in chitinase research?", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "Structure of jack...
[ 1991, 1992, 1995, 1995, 2000, 1998, 1996, 2000, 1999, 1999 ]
10
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 7670, 9809, 379, 17 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 61, 6, 32, 72 ]
4
true
Domain
Glycoside hydrolase, family 19, catalytic
Glycoside hydrolase, family 19, catalytic
Glyco_hydro_19_cat
9
IPR000727
727
Target SNARE coiled-coil homology domain
T_SNARE_dom
Domain
106,690
false
false
The process of vesicular fusion with target membranes depends on a set of SNAREs (SNAP-Receptors), which are associated with the fusing membranes [ , ]. These proteins are classified as v-SNAREs and t-SNAREs based on their localisation on vesicle or target membrane while another classification scheme defines R-SNAREs a...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF05739", "PS50192", "SM00397" ]
[ "SNARE", "T_SNARE", "t_SNARE" ]
[ 39740, 102111, 68487 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50192", "R-BTA-181429", "R-BTA-181430", "R-BTA-204005", "R-BTA-210500", "R-BTA-212676", "R-BTA-264642", "R-BTA-449836", "R-BTA-5682910", "R-BTA-5694530", "R-BTA-6798695", "R-BTA-6807878", "R-BTA-6811438", "R-BTA-888590", "R-BTA-8980692", "R-BTA-9013106", "R-BTA-9013408", "R-BT...
[ "PROSITEDOC:PDOC50192", "REACTOME:R-BTA-181429", "REACTOME:R-BTA-181430", "REACTOME:R-BTA-204005", "REACTOME:R-BTA-210500", "REACTOME:R-BTA-212676", "REACTOME:R-BTA-264642", "REACTOME:R-BTA-449836", "REACTOME:R-BTA-5682910", "REACTOME:R-BTA-5694530", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6...
205
[ "1fio", "1gl2", "1hvv", "1jth", "1kil", "1l4a", "1n7s", "1nhl", "1sfc", "1urq", "1xtg", "2ch7", "2m8r", "2n1t", "2nps", "2xhe", "3b5n", "3c98", "3hd7", "3ipd", "3j96", "3j97", "3j98", "3j99", "3ja6", "3p8c", "3rk2", "3rk3", "3rl0", "3zur", "3zus", "4jeh"...
92
[ "PUB00005782", "PUB00005792", "PUB00005793", "PUB00018360" ]
[ "9096343", "9232812", "9239749", "9861047" ]
[ "A conserved domain is present in different families of vesicular fusion proteins: a new superfamily.", "Neurotransmitter release - four years of SNARE complexes.", "Immunocytochemical localization of synaptic proteins at vesicular organelles in PC12 cells.", "Conserved structural features of the synaptic fus...
[ 1997, 1997, 1997, 1998 ]
4
[]
[ "IPR028671", "IPR028676", "IPR031186", "IPR039077", "IPR041875", "IPR042781", "IPR044766", "IPR061287", "IPR061288" ]
0
9
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 267, 18631, 87553, 61, 178 ]
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...
[ 158, 16, 148, 30, 123, 93, 12, 84, 139, 16, 10, 135 ]
12
true
Domain
Target SNARE coiled-coil homology domain
Target SNARE coiled-coil homology domain
T_SNARE_dom
8
IPR000730
730
Proliferating cell nuclear antigen, PCNA
Pr_cel_nuc_antig
Family
7,864
false
false
Proliferating cell nuclear antigen (PCNA), or cyclin, is a non-histone acidic nuclear protein [ ] that plays a key role in the control of eukaryotic DNA replication [ ]. It acts as a co-factor for DNA polymerase delta, which is responsible for leading strand DNA replication [ ]. The sequence of PCNA is well conserved b...
[ "GO:0003677", "GO:0030337", "GO:0006275" ]
[ "DNA binding", "DNA polymerase processivity factor activity", "regulation of DNA replication" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PRINTS", "PANTHER", "NCBIFAM" ]
[ "MF_00317", "PR00339", "PTHR11352", "TIGR00590" ]
[ "DNApol_clamp_arch", "PCNACYCLIN", "", "pcna" ]
[ 5975, 7087, 7784, 6303 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00265", "R-BTA-110312", "R-BTA-110314", "R-BTA-110320", "R-BTA-174411", "R-BTA-174414", "R-BTA-174417", "R-BTA-174437", "R-BTA-4615885", "R-BTA-5358565", "R-BTA-5651801", "R-BTA-5655862", "R-BTA-5656121", "R-BTA-5656169", "R-BTA-5685942", "R-BTA-5696397", "R-BTA-5696400", "R-B...
[ "PROSITEDOC:PDOC00265", "REACTOME:R-BTA-110312", "REACTOME:R-BTA-110314", "REACTOME:R-BTA-110320", "REACTOME:R-BTA-174411", "REACTOME:R-BTA-174414", "REACTOME:R-BTA-174417", "REACTOME:R-BTA-174437", "REACTOME:R-BTA-4615885", "REACTOME:R-BTA-5358565", "REACTOME:R-BTA-5651801", "REACTOME:R-BTA-5...
209
[ "1axc", "1ge8", "1isq", "1iz4", "1iz5", "1plq", "1plr", "1rwz", "1rxm", "1rxz", "1sxj", "1u76", "1u7b", "1ud9", "1ul1", "1vyj", "1vym", "1w60", "2hii", "2hik", "2ijx", "2io4", "2ix2", "2izo", "2nti", "2od8", "2zvk", "2zvl", "2zvm", "2zvv", "2zvw", "3a2f"...
229
[ "PUB00001160", "PUB00001388", "PUB00001407", "PUB00002545", "PUB00059204", "PUB00059205" ]
[ "2884104", "1671766", "1346518", "2565339", "10438605", "10542158" ]
[ "Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin.", "Highly conserved structure of proliferating cell nuclear antigen (DNA polymerase delta auxiliary protein) gene in plants.", "Identification of carrot cDNA clones encoding a second putative proliferating cell-nuclear a...
[ 1987, 1991, 1992, 1989, 1999, 1999 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria candidate phyla", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1262, 2, 6044, 140, 416 ]
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...
[ 6, 1, 1, 3, 7, 4, 1, 1, 3, 1, 1, 9 ]
12
true
Family
Proliferating cell nuclear antigen, PCNA
Proliferating cell nuclear antigen, PCNA
Pr_cel_nuc_antig
4
IPR000731
731
Sterol-sensing domain
SSD
Domain
86,609
false
false
The sterol-sensing domain (SSD) is an around 180 residues long cluster of five membrane-spanning segments. The SSD domain is conserved across phyla and confers sensitivity to regulation by sterol. It 'senses' the presence of sterol substrates through interactions and may modulate protein behaviours with changing sterol...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS50156" ]
[ "SSD" ]
[ 86609 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50156", "R-BTA-191273", "R-CEL-5632684", "R-CEL-8963678", "R-CEL-8964038", "R-DME-191273", "R-DME-209338", "R-DME-209471", "R-DME-5610787", "R-DME-5632681", "R-DME-5632684", "R-DME-8963678", "R-DRE-5362798", "R-HSA-1655829", "R-HSA-191273", "R-HSA-1989781", "R-HSA-2426168", "R...
[ "PROSITEDOC:PDOC50156", "REACTOME:R-BTA-191273", "REACTOME:R-CEL-5632684", "REACTOME:R-CEL-8963678", "REACTOME:R-CEL-8964038", "REACTOME:R-DME-191273", "REACTOME:R-DME-209338", "REACTOME:R-DME-209471", "REACTOME:R-DME-5610787", "REACTOME:R-DME-5632681", "REACTOME:R-DME-5632684", "REACTOME:R-DM...
42
[ "3aqp", "3jd8", "4mt1", "5jnx", "5khn", "5khs", "5lq3", "5t0o", "5u73", "5u74", "5xam", "5xan", "5xap", "5yhf", "6dmb", "6dmo", "6dmy", "6e1h", "6m49", "6mg8", "6n7g", "6n7h", "6n7k", "6oeu", "6oev", "6r4l", "6rmg", "6rvd", "6tbu", "6td6", "6uox", "6v3f"...
85
[ "PUB00007099", "PUB00018156", "PUB00018157", "PUB00154365", "PUB00154366" ]
[ "11932020", "9642295", "10821832", "35012873", "29954986" ]
[ "The sterol-sensing domain: multiple families, a unique role?", "Topology of SREBP cleavage-activating protein, a polytopic membrane protein with a sterol-sensing domain.", "Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical t...
[ 2002, 1998, 2000, 2022, 2018 ]
5
[]
[ "IPR003392", "IPR053958" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Myoviridae sp. ctcaJ26", "unclassified sequences" ]
[ 1612, 50896, 33155, 1, 945 ]
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...
[ 14, 39, 36, 13, 43, 30, 3, 4, 43, 3, 2, 6 ]
12
true
Domain
Sterol-sensing domain
Sterol-sensing domain
SSD
2
IPR000732
732
Rhodopsin
Rhodopsin
Family
13,571
false
false
The photoreceptor rhodopsin is a complex of the vision protein opsin and the chromophore 11-cis-retinal (derived from vitamin A). Light-sensitive pigments occur in both the rod cells (black and white vision) and cone cells (colour vision) in the retina at the back of the eye. Although related, the differences in sequen...
[ "GO:0007186", "GO:0007602", "GO:0016020" ]
[ "G protein-coupled receptor signaling pathway", "phototransduction", "membrane" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00579" ]
[ "RHODOPSIN" ]
[ 13571 ]
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-2453902", "R-BTA-2485179", "R-BTA-2514859", "R-BTA-418594", "R-BTA-419771", "R-BTA-5620916", "R-DRE-2453902", "R-DRE-2485179", "R-DRE-2514859", "R-DRE-418594", "R-DRE-419771", "R-DRE-5620916", "R-HSA-2453902", "R-HSA-2485179", "R-HSA-2514859", "R-HSA-418594", "R-HSA-419771", ...
[ "REACTOME:R-BTA-2453902", "REACTOME:R-BTA-2485179", "REACTOME:R-BTA-2514859", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-419771", "REACTOME:R-BTA-5620916", "REACTOME:R-DRE-2453902", "REACTOME:R-DRE-2485179", "REACTOME:R-DRE-2514859", "REACTOME:R-DRE-418594", "REACTOME:R-DRE-419771", "REACTOME:R-...
36
[ "1edx", "1f88", "1gzm", "1hzx", "1jfp", "1l9h", "1ln6", "1u19", "2g87", "2hpy", "2i35", "2i36", "2i37", "2j4y", "2ped", "2x72", "3c9l", "3c9m", "3cap", "3dqb", "3oax", "3pqr", "3pxo", "4a4m", "4bey", "4bez", "4j4q", "4pxf", "4x1h", "5dys", "5en0", "5te3"...
67
[]
[]
[]
[]
0
[ "IPR001760" ]
[]
1
0
1
[ "Bilateria" ]
[ 13571 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 11, 4, 3, 4 ]
4
true
Family
Rhodopsin
Rhodopsin
Rhodopsin
8
IPR000734
734
Triacylglycerol lipase family
TAG_lipase
Family
23,406
false
false
Triglyceride lipases ( ) are lipolytic enzymes that hydrolyse ester linkages of triglycerides [ ]. Lipases are widely distributed in animals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each ot...
[ "GO:0016298" ]
[ "lipase activity" ]
[ "molecular_function" ]
1
[ "PRINTS", "PANTHER" ]
[ "PR00821", "PTHR11610" ]
[ "TAGLIPASE", "" ]
[ 19502, 23235 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.1.1", "R-BTA-192456", "R-BTA-8963889", "R-BTA-8963901", "R-BTA-8964026", "R-BTA-975634", "R-DME-1483166", "R-DRE-1482801", "R-DRE-1483166", "R-GGA-8963889", "R-HSA-1482801", "R-HSA-1483166", "R-HSA-192456", "R-HSA-381340", "R-HSA-8963889", "R-HSA-8963901", "R-HSA-8964026", "R-HS...
[ "EC:3.1.1", "REACTOME:R-BTA-192456", "REACTOME:R-BTA-8963889", "REACTOME:R-BTA-8963901", "REACTOME:R-BTA-8964026", "REACTOME:R-BTA-975634", "REACTOME:R-DME-1483166", "REACTOME:R-DRE-1482801", "REACTOME:R-DRE-1483166", "REACTOME:R-GGA-8963889", "REACTOME:R-HSA-1482801", "REACTOME:R-HSA-1483166"...
38
[ "1bu8", "1eth", "1gpl", "1hpl", "1lpa", "1lpb", "1n8s", "1rp1", "1w52", "2oxe", "2ppl", "2pvs", "4qnn", "6e7k", "6oau", "6oaz", "6ob0", "6u7m", "8erl", "9nrn" ]
20
[ "PUB00000684", "PUB00001369", "PUB00004054", "PUB00004617" ]
[ "3147715", "2917565", "2304545", "3458198" ]
[ "Minireview on pancreatic lipase and colipase.", "Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase.", "Enzymology. More of the catalytic triad.", "Clonin...
[ 1988, 1989, 1990, 1986 ]
4
[]
[ "IPR002334", "IPR016272" ]
0
2
0
[ "Adenoviridae", "Bacteria", "Eukaryota" ]
[ 40, 62, 23304 ]
3
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 66, 53, 38, 36 ]
5
true
Family
Triacylglycerol lipase family
Triacylglycerol lipase family
TAG_lipase
1
IPR000735
735
Alpha 2C adrenoceptor
ADRA2C_rcpt
Family
1,056
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:0004938", "GO:0006940", "GO:0007186", "GO:0019229", "GO:0030168", "GO:0016020" ]
[ "alpha2-adrenergic receptor activity", "regulation of smooth muscle contraction", "G protein-coupled receptor signaling pathway", "regulation of vasoconstriction", "platelet activation", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
6
[ "PRINTS" ]
[ "PR00560" ]
[ "ADRENRGCA2CR" ]
[ 1056 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "27", "R-DRE-390696", "R-DRE-392023", "R-DRE-400042", "R-DRE-418594", "R-HSA-390696", "R-HSA-392023", "R-HSA-400042", "R-HSA-418594", "R-HSA-418597", "R-HSA-5683826", "R-MMU-390696", "R-MMU-392023", "R-MMU-400042", "R-MMU-418594", "R-MMU-418597", "R-MMU-5683826", "R-RNO-390696", ...
[ "IUPHAR:27", "REACTOME:R-DRE-390696", "REACTOME:R-DRE-392023", "REACTOME:R-DRE-400042", "REACTOME:R-DRE-418594", "REACTOME:R-HSA-390696", "REACTOME:R-HSA-392023", "REACTOME:R-HSA-400042", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-418597", "REACTOME:R-HSA-5683826", "REACTOME:R-MMU-390696", "RE...
23
[ "6kuw" ]
1
[ "PUB00066376", "PUB00066377", "PUB00066395", "PUB00066396", "PUB00066462", "PUB00066463", "PUB00066464", "PUB00066465", "PUB00066466", "PUB00066467", "PUB00066468", "PUB00066471", "PUB00066472" ]
[ "18882199", "2855960", "2887122", "9280371", "9605427", "9760042", "9824686", "8670422", "15684247", "2574568", "10215710", "7812219", "7684725" ]
[ "A study of the adrenotropic receptors.", "Subtypes of alpha 2-adrenoceptors: pharmacological and molecular biological evidence converge.", "Coronary vasoconstriction mediated by alpha 1- and alpha 2-adrenoceptors in conscious dogs.", "Alpha-adrenoceptors in equine digital veins: evidence for the presence of ...
[ 1948, 1988, 1987, 1997, 1998, 1998, 1998, 1996, 2004, 1989, 1999, 1994, 1993 ]
13
[ "IPR002233" ]
[]
1
0
1
[ "Vertebrata" ]
[ 1056 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 1, 2 ]
4
true
Family
Alpha 2C adrenoceptor
Alpha 2C adrenoceptor
ADRA2C_rcpt
5
IPR000737
737
Proteinase inhibitor I7, squash
Prot_inh_squash
Family
73
false
false
The squash inhibitors form one of a number of serine proteinase inhibitor families. They belong to MEROPS inhibitor family I7, clan IE. They are generally annotated as either trypsin or elastase inhibitors (MEROPS peptidase family S1, ). The proteins, found exclusively in the seeds of the cucurbitaceae, e.g. Citrullus ...
[ "GO:0004867" ]
[ "serine-type endopeptidase inhibitor activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROSITE", "CDD" ]
[ "PF00299", "PR00293", "PS00286", "cd00150" ]
[ "Squash", "SQUASHINHBTR", "SQUASH_INHIBITOR", "PlantTI" ]
[ 67, 30, 63, 68 ]
4
[ "PROSITEDOC" ]
[ "PDOC00258" ]
[ "PROSITEDOC:PDOC00258" ]
1
[ "1cti", "1f2s", "1h9h", "1h9i", "1ha9", "1ib9", "1lu0", "1mct", "1mcv", "1ppe", "1w7z", "2btc", "2c4b", "2cti", "2eti", "2it7", "2it8", "2let", "2ljs", "2m7t", "2m86", "2mt8", "2n8b", "2n8c", "2po8", "2sta", "2stb", "2v1v", "3cti", "4gux", "5wov", "5wow"...
44
[ "PUB00000373", "PUB00001564" ]
[ "1731946", "2914611" ]
[ "Two-dimensional NMR studies of squash family inhibitors. Sequence-specific proton assignments and secondary structure of reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III.", "The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor ...
[ 1992, 1989 ]
2
[]
[]
0
0
null
[ "Eukaryota", "Xanthomonas citri pv. citri" ]
[ 72, 1 ]
2
[]
[]
0
true
Family
Proteinase inhibitor I7, squash
Proteinase inhibitor I7, squash
Prot_inh_squash
4
IPR000738
738
WHEP-TRS domain
WHEP-TRS_dom
Domain
11,298
false
false
A conserved domain of 46 amino acids, called WHEP-TRS has been shown [ ] to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases. This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates t...
[ "GO:0004812", "GO:0005524", "GO:0006418" ]
[ "aminoacyl-tRNA ligase activity", "ATP binding", "tRNA aminoacylation for protein translation" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PROSITE", "PROFILE", "SMART" ]
[ "PF00458", "PS00762", "PS51185", "SM00991" ]
[ "WHEP-TRS", "WHEP_TRS_1", "WHEP_TRS_2", "WHEP-TRS" ]
[ 9752, 6426, 11029, 10109 ]
4
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.1.1", "PDOC00614", "R-DME-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-379726", "R-HSA-6782315", "R-HSA-9856649", "R-MMU-9856649" ]
[ "EC:6.1.1", "PROSITEDOC:PDOC00614", "REACTOME:R-DME-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-6782315", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649" ]
9
[ "1d2d", "1fyj", "1r1b", "1r6t", "1x59", "2azx", "2djv", "2lw7", "2pme", "2pmf", "2q5h", "2q5i", "2quh", "2qui", "2quj", "2quk", "2zt5", "2zt6", "2zt7", "2zt8", "2zxf", "4g85", "4kqe", "4phc", "4x5o", "5e6m", "5ujj", "6o76", "8yor", "8yp1" ]
30
[ "PUB00001214", "PUB00002829", "PUB00013215", "PUB00033807" ]
[ "1756734", "8463296", "11123902", "9556618" ]
[ "A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase.", "Primary structure of the gene for glycyl-tRNA synthetase from Bombyx mori.", "Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and fun...
[ 1991, 1993, 2000, 1998 ]
4
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati", "bird metagenome" ]
[ 11286, 11, 1 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 13, 5, 9, 7, 58, 18, 5, 21, 1, 14 ]
10
true
Domain
WHEP-TRS domain
WHEP-TRS domain
WHEP-TRS_dom
6
IPR000740
740
GrpE nucleotide exchange factor
GrpE
Family
37,147
false
false
Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-...
[ "GO:0000774", "GO:0042803", "GO:0051087", "GO:0006457" ]
[ "adenyl-nucleotide exchange factor activity", "protein homodimerization activity", "protein-folding chaperone binding", "protein folding" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "HAMAP", "PFAM", "PRINTS", "PROSITE", "PANTHER", "CDD" ]
[ "MF_01151", "PF01025", "PR00773", "PS01071", "PTHR21237", "cd00446" ]
[ "GrpE", "GrpE", "GRPEPROTEIN", "GRPE", "", "GrpE" ]
[ 34477, 37097, 34834, 28326, 35281, 33994 ]
6
[ "GP", "PROSITEDOC", "REACTOME" ]
[ "GenProp0244", "PDOC00822", "R-HSA-1268020" ]
[ "GP:GenProp0244", "PROSITEDOC:PDOC00822", "REACTOME:R-HSA-1268020" ]
3
[ "1dkg", "3a6m", "4ani", "8gb3", "9bls", "9blt", "9blu" ]
7
[ "PUB00000100", "PUB00014966", "PUB00054469", "PUB00079903", "PUB00079904", "PUB00079905", "PUB00079906", "PUB00079907", "PUB00079908", "PUB00079909", "PUB00079910" ]
[ "8280473", "15136046", "20036249", "14984054", "22544739", "11580258", "12369934", "10430558", "22683810", "24269840", "19075746" ]
[ "Role of the major heat shock proteins as molecular chaperones.", "Mutational analysis of the energetics of the GrpE.DnaK binding interface: equilibrium association constants by sedimentation velocity analytical ultracentrifugation.", "Crystal structure of a thermophilic GrpE protein: insight into thermosensing...
[ 1993, 2004, 2010, 2003, 2012, 2001, 2001, 1999, 2012, 2014, 2008 ]
11
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 731, 28205, 7562, 8, 641 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 17, 1, 2, 3, 1, 5, 6, 1, 10, 11, 1, 1, 20 ]
13
true
Family
GrpE nucleotide exchange factor
GrpE nucleotide exchange factor
GrpE
1
IPR000741
741
Fructose-bisphosphate aldolase, class-I
FBA_I
Family
17,296
false
false
Fructose-bisphosphate aldolase ( ) [ , ] is a glycolytic enzyme that catalyses the reversible aldol cleavage or condensation of fructose-1,6-bisphosphate into dihydroxyacetone-phosphate and glyceraldehyde 3-phosphate. There are two classes of fructose-bisphosphate aldolases with different catalytic mechanisms: class I ...
[ "GO:0004332", "GO:0006096" ]
[ "fructose-bisphosphate aldolase activity", "glycolytic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PANTHER" ]
[ "PF00274", "PTHR11627" ]
[ "Glycolytic", "" ]
[ 17262, 17073 ]
2
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...
[ "4.1.2.13", "GenProp0120", "GenProp0691", "GenProp1599", "GenProp1612", "PWY-1042", "PWY-1861", "PWY-5484", "PWY-6142", "PWY-7385", "PWY-8178", "PWY-8404", "PDOC00143", "R-CEL-114608", "R-CEL-6798695", "R-CEL-70171", "R-CEL-70263", "R-CEL-70350", "R-DDI-114608", "R-DDI-6798695"...
[ "EC:4.1.2.13", "GP:GenProp0120", "GP:GenProp0691", "GP:GenProp1599", "GP:GenProp1612", "METACYC:PWY-1042", "METACYC:PWY-1861", "METACYC:PWY-5484", "METACYC:PWY-6142", "METACYC:PWY-7385", "METACYC:PWY-8178", "METACYC:PWY-8404", "PROSITEDOC:PDOC00143", "REACTOME:R-CEL-114608", "REACTOME:R-...
58
[ "1a5c", "1ado", "1ald", "1epx", "1ewd", "1ewe", "1ex5", "1f2j", "1fba", "1fdj", "1j4e", "1qo5", "1xdl", "1xdm", "1xfb", "1zah", "1zai", "1zaj", "1zal", "2ald", "2eph", "2iqt", "2ot0", "2ot1", "2pc4", "2qap", "2qdg", "2qdh", "2qut", "2quu", "2quv", "3b8d"...
89
[ "PUB00000463", "PUB00000567", "PUB00005383", "PUB00070914", "PUB00070915" ]
[ "3355497", "2199259", "1412694", "14766013", "15880727" ]
[ "The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase.", "The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.", "Fructose-bisphosphate aldolases: an evolutionary history.", "Human aldolase A natural mutants: relationship between flexibility of the C-t...
[ 1988, 1990, 1992, 2004, 2005 ]
5
[]
[ "IPR023014" ]
0
1
0
[ "Bacteria", "Eukaryota", "Methanobacteriati", "Prochlorococcus phage P-TIM68", "unclassified sequences" ]
[ 5157, 11932, 23, 1, 183 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 38, 2, 12, 9, 33, 16, 26, 34, 49 ]
9
true
Family
Fructose-bisphosphate aldolase, class-I
Fructose-bisphosphate aldolase, class-I
FBA_I
2
IPR000742
742
EGF-like domain
EGF
Domain
448,905
false
false
This entry represents the EGF domain found in Cueball proteins, Prostaglandins and related proteins. A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown [ , , , , ] to be present in a large number of membrane-bound and extracellular, mostly animal, proteins. Many of these...
[]
[]
[]
0
[ "PFAM", "PROSITE", "PROSITE", "PROFILE", "SMART" ]
[ "PF00008", "PS00022", "PS01186", "PS50026", "SM00181" ]
[ "EGF", "EGF_1", "EGF_2", "EGF_3", "EGF" ]
[ 120917, 258247, 290948, 358923, 342611 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00021", "R-BTA-114608", "R-BTA-140834", "R-BTA-140837", "R-BTA-140875", "R-BTA-1474228", "R-BTA-1566948", "R-BTA-159740", "R-BTA-159763", "R-BTA-159782", "R-BTA-166665", "R-BTA-1971475", "R-BTA-2022870", "R-BTA-2022923", "R-BTA-2024101", "R-BTA-202733", "R-BTA-210993", "R-BTA-...
[ "PROSITEDOC:PDOC00021", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-140834", "REACTOME:R-BTA-140837", "REACTOME:R-BTA-140875", "REACTOME:R-BTA-1474228", "REACTOME:R-BTA-1566948", "REACTOME:R-BTA-159740", "REACTOME:R-BTA-159763", "REACTOME:R-BTA-159782", "REACTOME:R-BTA-166665", "REACTOME:R-BTA-19...
679
[ "1a3p", "1apo", "1apq", "1aut", "1bf9", "1c5m", "1ccf", "1cqe", "1cvu", "1cx2", "1dan", "1ddx", "1diy", "1dqb", "1dva", "1dx5", "1ebv", "1edm", "1egf", "1emn", "1emo", "1epg", "1eph", "1epi", "1epj", "1eqg", "1eqh", "1esl", "1ezq", "1f0r", "1f0s", "1f7e"...
580
[ "PUB00000923", "PUB00001555", "PUB00002741", "PUB00003983", "PUB00004321", "PUB00004609", "PUB00004964" ]
[ "7606779", "3282918", "1527084", "6607417", "2288911", "6334307", "3534958" ]
[ "The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions.", "Structure and function of epidermal growth factor-like regions in proteins.", "How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of...
[ 1995, 1988, 1992, 1984, 1990, 1984, 1986 ]
7
[]
[ "IPR001881", "IPR056588", "IPR056943", "IPR060322" ]
0
4
0
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 349, 448234, 301, 21 ]
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...
[ 89, 232, 1501, 277, 1141, 782, 2, 278, 1152, 1, 198 ]
11
true
Domain
EGF-like domain
EGF-like domain
EGF
1
IPR000743
743
Glycoside hydrolase, family 28
Glyco_hydro_28
Family
55,967
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0004650", "GO:0005975" ]
[ "polygalacturonase activity", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROSITE" ]
[ "PF00295", "PS00502" ]
[ "Glyco_hydro_28", "POLYGALACTURONASE" ]
[ 55961, 25915 ]
2
[ "CAZY", "EC", "PROSITEDOC" ]
[ "GH28", "3.2.1", "PDOC00415" ]
[ "CAZY:GH28", "EC:3.2.1", "PROSITEDOC:PDOC00415" ]
3
[ "1bhe", "1czf", "1hg8", "1ia5", "1ib4", "1k5c", "1kcc", "1kcd", "1nhc", "1rmg", "2iq7", "2uve", "2uvf", "3jur", "4c2l", "4mxn", "5olp", "6kve", "6kvh", "7b7a", "7b8b", "7e56", "8ikw", "8ikx" ]
24
[ "PUB00000607", "PUB00002110", "PUB00002118", "PUB00004870", "PUB00005266" ]
[ "2400785", "2193922", "2168372", "7624375", "8535779" ]
[ "Cloning and DNA sequence analysis of a polygalacturonase cDNA from Aspergillus niger RH5344.", "DNA sequence analysis of pglA and mechanism of export of its polygalacturonase product from Pseudomonas solanacearum.", "Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-alpha-...
[ 1990, 1990, 1990, 1995, 1995 ]
5
[]
[ "IPR050434" ]
0
1
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 89, 11816, 9, 43964, 89 ]
5
[ "Arabidopsis thaliana", "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)", "Zea mays" ]
[ 331, 2, 140, 1, 320 ]
5
true
Family
Glycoside hydrolase, family 28
Glycoside hydrolase, family 28
Glyco_hydro_28
8
IPR000744
744
NSF attachment protein
NSF_attach
Family
12,787
false
false
Regulated exocytosis of neurotransmitters and hormones, as well as intracellular traffic, requires fusion of two lipid bilayers. SNARE proteins are thought to form a protein bridge, the SNARE complex, between an incoming vesicle and the acceptor compartment. SNARE proteins contribute to the specificity of membrane fusi...
[ "GO:0006886" ]
[ "intracellular protein transport" ]
[ "biological_process" ]
1
[ "PFAM", "PRINTS", "PANTHER", "CDD" ]
[ "PF14938", "PR00448", "PTHR13768", "cd15832" ]
[ "SNAP", "NSFATTACHMNT", "", "SNAP" ]
[ 12618, 6874, 10676, 7034 ]
4
[ "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-204005", "R-BTA-6807878", "R-BTA-6811434", "R-BTA-6811438", "R-BTA-6811440", "R-DDI-204005", "R-DDI-6807878", "R-DDI-6811434", "R-DDI-6811438", "R-DDI-6811440", "R-DME-204005", "R-DME-6807878", "R-DME-6811434", "R-DME-6811438", "R-DME-6811440", "R-HSA-204005", "R-HSA-432722", ...
[ "REACTOME:R-BTA-204005", "REACTOME:R-BTA-6807878", "REACTOME:R-BTA-6811434", "REACTOME:R-BTA-6811438", "REACTOME:R-BTA-6811440", "REACTOME:R-DDI-204005", "REACTOME:R-DDI-6807878", "REACTOME:R-DDI-6811434", "REACTOME:R-DDI-6811438", "REACTOME:R-DDI-6811440", "REACTOME:R-DME-204005", "REACTOME:R...
43
[ "1qqe", "2ifu", "3j96", "3j97", "3j98", "3j99", "6ip1", "6mdm", "6mdn", "9cru", "9crx", "9n22", "9ng2", "9nlu", "9nlw", "9nly", "9nlz", "9ojz", "9ok3", "9olo", "9om6", "9paf", "9pag", "9pb9", "9pba", "9pbf", "9pbv", "9pc3", "9pcx", "9pcz", "9pd1", "9pd8"...
35
[ "PUB00005430", "PUB00007100", "PUB00022550", "PUB00047702", "PUB00080103", "PUB00080104", "PUB00080105", "PUB00080106", "PUB00080107", "PUB00080108" ]
[ "7846761", "12140265", "10445030", "17634982", "16981829", "17397838", "23836889", "19762473", "12730228", "8455721" ]
[ "A TPR domain in the SNAP secretory proteins.", "Plasma membrane targeting of SNAP-25 increases its local concentration and is necessary for SNARE complex formation and regulated exocytosis.", "Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembl...
[ 1994, 2002, 1999, 2008, 2006, 2007, 2013, 2009, 2003, 1993 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Nucleocytoviricota", "metagenomes" ]
[ 18, 628, 12058, 31, 52 ]
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...
[ 16, 2, 35, 4, 14, 10, 1, 14, 16, 1, 1, 25 ]
12
true
Family
NSF attachment protein
NSF attachment protein
NSF_attach
7
IPR000745
745
Hepatitis C virus, Non-structural protein NS4a
HCV_NS4a
Domain
17,541
false
false
NS4a (non-structural protein) forms an integral part of the NS3 serine protease in Hepatitis C virus, as it is required in a number of cases as a cofactor of cleavage [ , ]. It has also been reported that NS4a interacts with NS4b and NS3 to form a multi-subunit replicase complex [ ].
[ "GO:0016032", "GO:0044423" ]
[ "viral process", "virion component" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF01006" ]
[ "HCV_NS4a" ]
[ 17541 ]
1
[ "EC", "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME" ]
[ "2.7.7.48", "3.4.21.98", "3.4.22.-", "3.6.1.15", "3.6.4.13", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210", "R-HSA-5621480", "R-HSA-8854214" ]
[ "EC:2.7.7.48", "EC:3.4.21.98", "EC:3.4.22.-", "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", "REACTOME:R-HSA-5621480", "REACTOME:R-HSA-8854214" ]
12
[]
0
[ "PUB00003532", "PUB00005057" ]
[ "9261364", "9568891" ]
[ "The hepatitis C virus NS4A protein: interactions with the NS4B and NS5A proteins.", "Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2 A resolution structure in a hexagonal crystal form." ]
[ 1997, 1998 ]
2
[]
[]
0
0
null
[ "Flaviviridae" ]
[ 17541 ]
1
[]
[]
0
true
Domain
Hepatitis C virus, Non-structural protein NS4a
Hepatitis C virus, Non-structural protein NS4a
HCV_NS4a
7
IPR000747
747
Homeodomain engrailed
HD_engrailed
Domain
2,295
false
false
Proteins that regulate developmental gene expression are nuclear proteins [ ] that contain a conserved domain known as the homedomain (HD), the flanking sequences of which differ considerably among different proteins. The HD includes the helix-turn-helix (HTH) motif which binds to DNA [ ]. Most proteins which contain a...
[ "GO:0003677", "GO:0007275", "GO:0005634" ]
[ "DNA binding", "multicellular organism development", "nucleus" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00026" ]
[ "ENGRAILED" ]
[ 2295 ]
1
[ "PROSITEDOC" ]
[ "PDOC00033" ]
[ "PROSITEDOC:PDOC00033" ]
1
[]
0
[ "PUB00000591", "PUB00001890", "PUB00004373", "PUB00005101" ]
[ "2568852", "2566559", "1970866", "2884726" ]
[ "The structure and function of the homeodomain.", "Progressively restricted expression of a homeo box gene within the aboral ectoderm of developing sea urchin embryos.", "Specific DNA binding of the two chicken Deformed family homeodomain proteins, Chox-1.4 and Chox-a.", "Homeo boxes in the study of developme...
[ 1989, 1989, 1990, 1987 ]
4
[ "IPR020479" ]
[]
1
0
1
[ "Bilateria" ]
[ 2295 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 5, 2, 3, 4 ]
5
true
Domain
Homeodomain engrailed
Homeodomain engrailed
HD_engrailed
4
IPR000748
748
Pseudouridine synthase, RsuA/RluB/E/F
PsdUridine_synth_RsuA/RluB/E/F
Family
53,420
false
false
Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine (Psi) in a variety of RNA molecules, and may function as RNA chaperones. Pseudouridine is the most abundant modified nucleotide found in all cellular RNAs. There are four distinct families of pseudouridine synthases that share no global sequ...
[ "GO:0003723", "GO:0016866", "GO:0001522", "GO:0009451" ]
[ "RNA binding", "intramolecular transferase activity", "pseudouridine synthesis", "RNA modification" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]
4
[ "NCBIFAM" ]
[ "TIGR00093" ]
[ "" ]
[ 53420 ]
1
[ "EC", "PROSITEDOC" ]
[ "5.4.99", "PDOC00885" ]
[ "EC:5.4.99", "PROSITEDOC:PDOC00885" ]
2
[ "1ksk", "1ksl", "1ksv", "1vio", "2gml", "2olw", "2oml", "3dh3", "4lab", "4lgt", "9cl9" ]
11
[ "PUB00018355", "PUB00037953", "PUB00045922", "PUB00092579" ]
[ "11953756", "16511038", "10529181", "19664587" ]
[ "Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP.", "Structure of the pseudouridine synthase RsuA from Haemophilus influenzae.", "Role of cysteine residues in pseudouridine synthases of different families.", "Enzymatic characterization and mutational studies of TruD--the fifth fa...
[ 2002, 2005, 1999, 2009 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Thermoplasmatota", "unclassified sequences" ]
[ 52173, 592, 7, 648 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 1, 4, 1, 2 ]
4
true
Family
Pseudouridine synthase, RsuA/RluB/E/F
Pseudouridine synthase, RsuA/RluB/E/F
PsdUridine_synth_RsuA/RluB/E/F
7
IPR000749
749
ATP:guanido phosphotransferase
ATP-guanido_PTrfase
Family
23,088
false
false
ATP:guanido phosphotransferases are a family of structurally and functionally related enzymes [ , ] that reversibly catalyse the transfer of phosphate between ATP and various phosphogens. The enzymes belonging to this family include: Glycocyamine kinase ( ), which catalyses the transfer of phosphate from ATP to guanido...
[ "GO:0016775", "GO:0046314" ]
[ "phosphotransferase activity, nitrogenous group as acceptor", "phosphocreatine biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER" ]
[ "PTHR11547" ]
[ "" ]
[ 23088 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00103", "R-BTA-71288", "R-BTA-9696264", "R-CFA-71288", "R-CFA-9696264", "R-GGA-71288", "R-GGA-9696264", "R-HSA-71288", "R-HSA-9696264", "R-MMU-71288", "R-MMU-9696264", "R-RNO-71288", "R-RNO-9696264", "R-SSC-71288" ]
[ "PROSITEDOC:PDOC00103", "REACTOME:R-BTA-71288", "REACTOME:R-BTA-9696264", "REACTOME:R-CFA-71288", "REACTOME:R-CFA-9696264", "REACTOME:R-GGA-71288", "REACTOME:R-GGA-9696264", "REACTOME:R-HSA-71288", "REACTOME:R-HSA-9696264", "REACTOME:R-MMU-71288", "REACTOME:R-MMU-9696264", "REACTOME:R-RNO-7128...
14
[ "1bg0", "1crk", "1g0w", "1i0e", "1m15", "1p50", "1p52", "1qh4", "1qk1", "1rl9", "1sd0", "1u6r", "1vrp", "2crk", "2j1q", "3b6r", "3drb", "3dre", "3jpz", "3jq3", "3ju5", "3ju6", "3l2d", "3l2e", "3m10", "4am1", "4bg4", "4bhl", "4gvy", "4gvz", "4gw0", "4gw2"...
73
[ "PUB00000040", "PUB00000670", "PUB00002616", "PUB00002619" ]
[ "3896131", "7819288", "2324092", "2324105" ]
[ "The creatine-creatine phosphate energy shuttle.", "Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues.", "A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni has a novel duplicated str...
[ 1985, 1995, 1990, 1990 ]
4
[]
[ "IPR023660" ]
0
1
0
[ "Bacteria", "Eukaryota", "Thermococcus litoralis", "metagenomes" ]
[ 3209, 19819, 1, 59 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Zea mays" ]
[ 6, 19, 10, 37, 12, 17, 1 ]
7
true
Family
ATP:guanido phosphotransferase
ATP:guanido phosphotransferase
ATP-guanido_PTrfase
8
IPR000750
750
Proenkephalin B
Proenkphlin_B
Family
643
false
false
Vertebrate endogenous opioid neuropeptides are released by post-translational proteolytic cleavage of precursor proteins. The precursors consist of the following components: a signal sequence that precedes a conserved region of about 50 residues; a variable-length region; and the sequence of the neuropeptide itself. Th...
[ "GO:0007218" ]
[ "neuropeptide signaling pathway" ]
[ "biological_process" ]
1
[ "PRINTS" ]
[ "PR01030" ]
[ "PENKBPRCRSR" ]
[ 643 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-111885", "R-HSA-202040", "R-HSA-375276", "R-HSA-418594", "R-MMU-111885", "R-MMU-202040", "R-MMU-375276", "R-MMU-418594", "R-RNO-111885", "R-RNO-202040", "R-RNO-375276", "R-RNO-418594" ]
[ "REACTOME:R-HSA-111885", "REACTOME:R-HSA-202040", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-111885", "REACTOME:R-MMU-202040", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-111885", "REACTOME:R-RNO-202040", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418...
12
[]
0
[ "PUB00003982", "PUB00004901" ]
[ "6316163", "8710928" ]
[ "Isolation and structural organization of the human preproenkephalin B gene.", "Structure, tissue distribution, and chromosomal localization of the prepronociceptin gene." ]
[ 1983, 1996 ]
2
[ "IPR006024" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 643 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 11, 4, 3 ]
4
true
Family
Proenkephalin B
Proenkephalin B
Proenkphlin_B
6
IPR000751
751
M-phase inducer phosphatase
MPI_Phosphatase
Family
6,314
false
false
M-phase inducer phosphatases function as dosage-dependent inducers in mitotic control [ , , , ]. They are tyrosine protein phosphatases required for progression of the cell cycle. They may directly dephosphorylate p34(cdc2) and activate p34(cdc2) kinase activity. They catalyse the reaction: protein tyrosine phosphate +...
[ "GO:0004725", "GO:0006470", "GO:1902751" ]
[ "protein tyrosine phosphatase activity", "protein dephosphorylation", "positive regulation of cell cycle G2/M phase transition" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM", "PRINTS", "CDD" ]
[ "PF06617", "PR00716", "cd01530" ]
[ "M-inducer_phosp", "MPIPHPHTASE", "Cdc25" ]
[ 2311, 6172, 5032 ]
3
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.1.3.48", "R-BTA-156711", "R-BTA-5625740", "R-BTA-5689880", "R-BTA-6804115", "R-BTA-69202", "R-BTA-69273", "R-BTA-69601", "R-BTA-69656", "R-BTA-75035", "R-CEL-156711", "R-CEL-176187", "R-CEL-5625740", "R-CEL-5689880", "R-CEL-69202", "R-CEL-69273", "R-CEL-69601", "R-CEL-69656", ...
[ "EC:3.1.3.48", "REACTOME:R-BTA-156711", "REACTOME:R-BTA-5625740", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-6804115", "REACTOME:R-BTA-69202", "REACTOME:R-BTA-69273", "REACTOME:R-BTA-69601", "REACTOME:R-BTA-69656", "REACTOME:R-BTA-75035", "REACTOME:R-CEL-156711", "REACTOME:R-CEL-176187", "REA...
88
[ "1c25", "1cwr", "1cws", "1cwt", "1qb0", "1ym9", "1ymd", "1ymk", "1yml", "1ys0", "2a2k", "2ifd", "2ifv", "2uzq", "3op3", "4wh7", "4wh9", "5m36", "8roz" ]
19
[ "PUB00000857", "PUB00001196", "PUB00001247", "PUB00003627" ]
[ "1836978", "2120044", "8156993", "1392080" ]
[ "Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins.", "Complementation of fission yeast cdc2ts and cdc25ts mutants identifies two cell cycle genes from Drosophila: a cdc2 homologue and string.", "Cdc25A is a novel phosphatase functioning early i...
[ 1991, 1990, 1994, 1992 ]
4
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati" ]
[ 6305, 9 ]
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...
[ 6, 5, 4, 20, 11, 1, 21, 1, 1 ]
9
true
Family
M-phase inducer phosphatase
M-phase inducer phosphatase
MPI_Phosphatase
9
IPR000752
752
Flavivirus non-structural protein NS2A
Flavi_NS2A
Domain
11,514
false
false
NS2A is a hydrophobic protein about 25kDa in size, which is cleaved from NS1 by a membrane bound host protease [ ]. NS2A has been found to associate with the dsRNA within the vesicle packages. It has also been found that NS2A associates with the known replicase components and so NS2A has been postulated to be part of t...
[ "GO:0003725" ]
[ "double-stranded RNA binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF01005" ]
[ "Flavi_NS2A" ]
[ 11514 ]
1
[ "EC", "EC", "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.1.1.56", "2.1.1.57", "2.7.7.48", "3.4.21.91", "3.6.1.15", "3.6.4.13", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210", "PWY-7375", "PWY-7379" ]
[ "EC:2.1.1.56", "EC:2.1.1.57", "EC:2.7.7.48", "EC:3.4.21.91", "EC:3.6.1.15", "EC:3.6.4.13", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7185", "METACYC:PWY-7198", "METACYC:PWY-7210", "METACYC:PWY-7375", "METACYC:PWY-7379" ]
13
[ "2m0s", "8cxg", "8cxh", "8cxi" ]
4
[ "PUB00003517", "PUB00005629" ]
[ "7474145", "9636360" ]
[ "Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum.", "Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A." ]
[ 1995, 1998 ]
2
[]
[]
0
0
null
[ "Orthornavirae" ]
[ 11514 ]
1
[]
[]
0
true
Domain
Flavivirus non-structural protein NS2A
Flavivirus non-structural protein NS2A
Flavi_NS2A
3
IPR000753
753
Clusterin-like
Clusterin-like
Family
1,942
false
false
Clusterin (Clu), also known as apolipoprotein J, is a vertebrate glycoprotein [ ]. Clusterin expression is complex, appearing as different forms in different cell compartments. One set of proteins is directed for secretion, and other clusterin species are expressed in the cytoplasm and nucleus. The secretory form of th...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF01093", "PTHR10970" ]
[ "Clusterin", "" ]
[ 1941, 1921 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00431", "R-BTA-114608", "R-BTA-166665", "R-BTA-6803157", "R-BTA-977606", "R-CFA-114608", "R-CFA-166665", "R-CFA-977606", "R-HSA-114608", "R-HSA-166665", "R-HSA-6803157", "R-HSA-977606", "R-MMU-114608", "R-MMU-166665", "R-MMU-6803157", "R-MMU-977606", "R-RNO-114608", "R-RNO-680...
[ "PROSITEDOC:PDOC00431", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-166665", "REACTOME:R-BTA-6803157", "REACTOME:R-BTA-977606", "REACTOME:R-CFA-114608", "REACTOME:R-CFA-166665", "REACTOME:R-CFA-977606", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-166665", "REACTOME:R-HSA-6803157", "REACTOME:R-HSA-97...
23
[ "7zet", "7zeu" ]
2
[ "PUB00005386", "PUB00010653", "PUB00081944", "PUB00081945", "PUB00081946", "PUB00081947", "PUB00081948", "PUB00081949", "PUB00081950", "PUB00081951", "PUB00081952" ]
[ "1585460", "12551933", "10675623", "14507903", "21953454", "22588555", "21505792", "19535339", "22025968", "11720815", "27148688" ]
[ "Clusterin: the intriguing guises of a widely expressed glycoprotein.", "Synthesis and functional analyses of nuclear clusterin, a cell death protein.", "Molecular cloning, characterization and expression of a novel retinal clusterin-like protein cDNA.", "Comparative analysis and expression of CLUL1, a cone p...
[ 1992, 2003, 2000, 2003, 2011, 2012, 2011, 2009, 2011, 2001, 2016 ]
11
[]
[ "IPR016016" ]
0
1
0
[ "Eumetazoa", "bird metagenome" ]
[ 1939, 3 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 21, 10, 10 ]
4
true
Family
Clusterin-like
Clusterin-like
Clusterin-like
4
IPR000754
754
Small ribosomal subunit protein uS9
Ribosomal_uS9
Family
36,819
false
false
uS9 proteins adopt a β/α/β fold similar to that found in numerous RNA/DNA-binding proteins, as well as in kinases from the GHMP kinase family [ ]. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This le...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER" ]
[ "PF00380", "PTHR21569" ]
[ "Ribosomal_S9", "" ]
[ 36799, 36295 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00311", "R-BTA-156827", "R-BTA-1799339", "R-BTA-5389840", "R-BTA-5419276", "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-BTA-9937383", "R-CEL-156827", "R-CEL-1799339", "R-CEL-5389840", "R-CEL-5419...
[ "PROSITEDOC:PDOC00311", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-5389840", "REACTOME:R-BTA-5419276", "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-97595...
116
[ "1fjg", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xmo", "1xmq", "1xnq", "1xnr", "2e5l", "2f4v"...
1,901
[ "PUB00001585", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00034480" ]
[ "2332055", "11297922", "11290319", "11114498", "8722013" ]
[ "The primary structure of rat ribosomal protein S16.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Structures of prokaryotic ribosomal proteins: implications for RNA binding and evolution." ]
[ 1990, 2001, 2001, 2000, 1995 ]
5
[]
[ "IPR019958", "IPR023035" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 911, 23680, 11650, 578 ]
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",...
[ 20, 2, 2, 3, 1, 9, 9, 2, 10, 16, 3, 3, 18 ]
13
true
Family
Small ribosomal subunit protein uS9
Small ribosomal subunit protein uS9
Ribosomal_uS9
3
IPR000755
755
D-alanyl-D-alanine dipeptidase
A_A_dipeptidase
Family
9,900
false
false
This group of metallopeptidases belong to MEROPS peptidase family M15 (clan MD), subfamily M15D (vanX D-Ala-D-Ala dipeptidase). The D-alanyl-D-alanine dipeptidase enzyme from Enterococcus faecalis is also known as the vancomycin resistance protein VanX, and hydrolyses D-ala-D-ala [ , ]. It has a 250-fold differential i...
[ "GO:0008237", "GO:0016805", "GO:0006508" ]
[ "metallopeptidase activity", "dipeptidase activity", "proteolysis" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PFAM", "PIRSF", "PANTHER" ]
[ "MF_01924", "PF01427", "PIRSF026671", "PTHR43126" ]
[ "A_A_dipeptidase", "Peptidase_M15", "AA_dipeptidase", "" ]
[ 9010, 9820, 7174, 9746 ]
4
[ "EC", "METACYC", "METACYC" ]
[ "3.4.13.22", "PWY-6454", "PWY-6455" ]
[ "EC:3.4.13.22", "METACYC:PWY-6454", "METACYC:PWY-6455" ]
3
[ "1r44", "8xz2" ]
2
[ "PUB00027914", "PUB00027959" ]
[ "7873524", "7854121" ]
[ "Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147.", "Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine." ]
[ 1995, 1994 ]
2
[]
[ "IPR058213" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 3, 9699, 100, 98 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 1, 1 ]
2
true
Family
D-alanyl-D-alanine dipeptidase
D-alanyl-D-alanine dipeptidase
A_A_dipeptidase
1
IPR000756
756
Diacylglycerol kinase, accessory domain
Diacylglycerol_kin_accessory
Domain
26,598
false
false
Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The DAG kinase domain is assumed to be an accessory domain. Upon cell stimulation, DAG kinase converts DAG into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. It catalyses...
[ "GO:0004143", "GO:0007200" ]
[ "ATP-dependent diacylglycerol kinase activity", "phospholipase C-activating G protein-coupled receptor signaling pathway" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "SMART" ]
[ "PF00609", "SM00045" ]
[ "DAGK_acc", "DAGKa" ]
[ 26485, 25611 ]
2
[ "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.1.107", "PWY-7039", "PWY-7817", "R-BTA-114508", "R-CEL-114508", "R-DDI-114508", "R-DME-114508", "R-HSA-114508", "R-MMU-114508", "R-RNO-114508", "R-SSC-114508" ]
[ "EC:2.7.1.107", "METACYC:PWY-7039", "METACYC:PWY-7817", "REACTOME:R-BTA-114508", "REACTOME:R-CEL-114508", "REACTOME:R-DDI-114508", "REACTOME:R-DME-114508", "REACTOME:R-HSA-114508", "REACTOME:R-MMU-114508", "REACTOME:R-RNO-114508", "REACTOME:R-SSC-114508" ]
11
[]
0
[ "PUB00005115", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899" ]
[ "3291115", "12368087", "12471243", "15078142", "15320712" ]
[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "Evolution of protein kinase signaling from yeast to man.", "The protein kinase complement of the human genome.", "High-throughput structural biology in drug discovery: protein kinases.", "Creating chemical dive...
[ 1988, 2002, 2002, 2004, 2004 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 100, 26490, 8 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 34, 15, 158, 29, 41, 31, 31, 55, 57 ]
9
true
Domain
Diacylglycerol kinase, accessory domain
Diacylglycerol kinase, accessory domain
Diacylglycerol_kin_accessory
9
IPR000757
757
Beta-glucanase-like, N-terminal domain
Beta-glucanase-like
Domain
71,089
false
false
This entry represents the N-terminal domain in members of the glycoside hydrolase family 16 (GH16), including Beta-glucanase, Crh-like protein 1, Xyloglucan endotransglucosylase/hydrolase and related proteins. The glycosyl hydrolases family 16 (GH16) [ ] contains functionally heterogeneous members, including lichenase ...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE" ]
[ "PF00722", "PS51762" ]
[ "Glyco_hydro_16", "GH16_2" ]
[ 52592, 69537 ]
2
[ "CAZY" ]
[ "GH16" ]
[ "CAZY:GH16" ]
1
[ "1ajk", "1ajo", "1axk", "1byh", "1cpm", "1cpn", "1dyp", "1gbg", "1glh", "1mac", "1mve", "1o4y", "1o4z", "1u0a", "1umz", "1un1", "1ups", "1urx", "1zm1", "2ayh", "2cl2", "2hyk", "2r49", "2uwa", "2uwb", "2uwc", "2vh9", "2vy0", "2w39", "2w52", "2wlq", "2wne"...
119
[ "PUB00000503", "PUB00002845", "PUB00010686", "PUB00029321" ]
[ "1747104", "8182059", "11435116", "12970344" ]
[ "A classification of glycosyl hydrolases based on amino acid sequence similarities.", "Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed mutagenesis.", "The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active...
[ 1991, 1994, 2001, 2003 ]
4
[]
[ "IPR035806" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 102, 21543, 49185, 23, 236 ]
5
[ "Arabidopsis thaliana", "Drosophila melanogaster", "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" ]
[ 136, 10, 15, 100, 5, 3, 133 ]
7
true
Domain
Beta-glucanase-like, N-terminal domain
Beta-glucanase-like, N-terminal domain
Beta-glucanase-like
6
IPR000758
758
Virulence-related outer membrane protein
Enterovir_OMP
Family
6,584
false
false
Virulence-related outer membrane proteins are expressed in Gram-negative bacteria and are essential to bacterial survival within macrophages and for eukaryotic cell invasion. Members of this group include: PagC, required by Salmonella typhimurium for survival in macrophages and for virulence in mice [ ] Rck outer membr...
[ "GO:0044384" ]
[ "host outer membrane" ]
[ "cellular_component" ]
1
[ "PFAM", "PRINTS", "PROSITE", "PROSITE" ]
[ "PF06316", "PR00316", "PS00694", "PS00695" ]
[ "Ail_Lom", "ENTEROVIROMP", "ENT_VIR_OMP_1", "ENT_VIR_OMP_2" ]
[ 2066, 4165, 2588, 5202 ]
4
[ "PROSITEDOC" ]
[ "PDOC00582" ]
[ "PROSITEDOC:PDOC00582" ]
1
[ "1orm", "1q9f", "1q9g", "1qj8", "1qj9", "2m06", "2m07", "2mnh", "2n2l", "2n2m", "3qra", "3qrc", "5vj8", "8qpv", "8qpw" ]
15
[ "PUB00002097", "PUB00002133", "PUB00002159", "PUB00006270", "PUB00006349", "PUB00006456" ]
[ "1688838", "1987115", "1846140", "1766380", "8675302", "10545325" ]
[ "Nucleotide sequence of the Yersinia enterocolitica ail gene and characterization of the Ail protein product.", "Molecular characterization of an Enterobacter cloacae outer membrane protein (OmpX).", "A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacte...
[ 1990, 1991, 1991, 1991, 1996, 1999 ]
6
[]
[]
0
0
null
[ "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 6471, 80, 19, 14 ]
4
[ "Escherichia coli (strain K12)", "Mus musculus" ]
[ 2, 1 ]
2
true
Family
Virulence-related outer membrane protein
Virulence-related outer membrane protein
Enterovir_OMP
2
IPR000760
760
Inositol monophosphatase-like
Inositol_monophosphatase-like
Family
84,121
false
false
It has been shown that several proteins share two sequence motifs [ ]. Two of these proteins, vertebrate and plant inositol monophosphatase ( ), and vertebrate inositol polyphosphate 1-phosphatase ( ), are enzymes of the inositol phosphate second messenger signalling pathway, and share similar enzyme activity. Both enz...
[]
[]
[]
0
[ "PFAM", "PRINTS" ]
[ "PF00459", "PR00377" ]
[ "Inositol_P", "IMPHPHTASES" ]
[ 84094, 70036 ]
2
[ "EC", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.3", "GenProp1244", "GenProp1605", "PDOC00547", "R-BTA-156584", "R-BTA-1855183", "R-CEL-1855183", "R-DDI-156584", "R-DDI-1855183", "R-DME-156584", "R-DRE-156584", "R-HSA-156584", "R-HSA-1855183", "R-MMU-156584", "R-MMU-1855183", "R-MTU-879299", "R-MTU-936635", "R-RNO-156584", ...
[ "EC:3.1.3", "GP:GenProp1244", "GP:GenProp1605", "PROSITEDOC:PDOC00547", "REACTOME:R-BTA-156584", "REACTOME:R-BTA-1855183", "REACTOME:R-CEL-1855183", "REACTOME:R-DDI-156584", "REACTOME:R-DDI-1855183", "REACTOME:R-DME-156584", "REACTOME:R-DRE-156584", "REACTOME:R-HSA-156584", "REACTOME:R-HSA-1...
22
[ "1awb", "1dk4", "1g0h", "1g0i", "1ima", "1imb", "1imc", "1imd", "1ime", "1imf", "1inp", "1jp4", "1k9y", "1k9z", "1ka0", "1ka1", "1lbv", "1lbw", "1lbx", "1lby", "1lbz", "1qgx", "1vdw", "1xi6", "2bji", "2czh", "2czi", "2czk", "2ddk", "2fvz", "2hhm", "2p3n"...
102
[ "PUB00000822", "PUB00001628", "PUB00004864" ]
[ "2553271", "1660408", "7761465" ]
[ "Neural and developmental actions of lithium: a unifying hypothesis.", "Diverse proteins homologous to inositol monophosphatase.", "Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure." ]
[ 1989, 1991, 1995 ]
3
[]
[ "IPR006239", "IPR006240", "IPR011809", "IPR033942" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1244, 60157, 21387, 1333 ]
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",...
[ 39, 4, 10, 16, 2, 34, 21, 5, 30, 28, 3, 1, 36 ]
13
true
Family
Inositol monophosphatase-like
Inositol monophosphatase-like
Inositol_monophosphatase-like
4
IPR000761
761
Melanocyte-stimulating hormone receptor
MSH_rcpt
Family
2,474
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:0004980", "GO:0007186", "GO:0016020" ]
[ "melanocyte-stimulating hormone receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00536" ]
[ "MELNOCYTESHR" ]
[ 2474 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "282", "R-BTA-375276", "R-BTA-418555", "R-HSA-375276", "R-HSA-418555", "R-HSA-9856649", "R-MMU-375276", "R-MMU-418555" ]
[ "IUPHAR:282", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-418555", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418555" ]
8
[ "7f4d", "7f4f", "7f4h", "7f4i", "9k3p" ]
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
[ "IPR001671" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 2474 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 65, 25, 2 ]
4
true
Family
Melanocyte-stimulating hormone receptor
Melanocyte-stimulating hormone receptor
MSH_rcpt
2
IPR000762
762
Midkine heparin-binding growth factor
Midkine_heparin-bd_GF
Family
2,356
false
false
Several extracellular heparin-binding proteins involved in regulation of growth and differentiation belong to a new family of growth factors. These growth factors are highly related proteins of about 140 amino acids that contain 10 conserved cysteines probably involved in disulphide bonds, and include pleiotrophin [ ] ...
[ "GO:0008083" ]
[ "growth factor activity" ]
[ "molecular_function" ]
1
[ "PRINTS", "PANTHER", "SMART" ]
[ "PR00269", "PTHR13850", "SM00193" ]
[ "PTNMIDKINE", "", "PTN" ]
[ 2288, 2333, 2302 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00540", "R-BTA-201556", "R-BTA-9851151", "R-GGA-201556", "R-GGA-9851151", "R-HSA-201556", "R-HSA-2979096", "R-HSA-9851151", "R-MMU-201556", "R-MMU-9851151", "R-RNO-201556", "R-RNO-9851151", "R-SSC-201556", "R-SSC-9851151", "R-XTR-2979096" ]
[ "PROSITEDOC:PDOC00540", "REACTOME:R-BTA-201556", "REACTOME:R-BTA-9851151", "REACTOME:R-GGA-201556", "REACTOME:R-GGA-9851151", "REACTOME:R-HSA-201556", "REACTOME:R-HSA-2979096", "REACTOME:R-HSA-9851151", "REACTOME:R-MMU-201556", "REACTOME:R-MMU-9851151", "REACTOME:R-RNO-201556", "REACTOME:R-RNO...
15
[ "1mkc", "1mkn", "2lut", "2luu", "2n6f", "8voh", "8voi" ]
7
[ "PUB00015070", "PUB00015071", "PUB00015072" ]
[ "15047154", "7796887", "15121180" ]
[ "Midkine, a heparin-binding cytokine, plays key roles in intraperitoneal adhesions.", "Retinoic acid-induced heparin binding protein (RIHB) binds to embryonal chondrocytes and cartilage primarily via proteoglycans.", "HB-GAM inhibits proliferation and enhances differentiation of neural stem cells." ]
[ 2004, 1995, 2004 ]
3
[]
[]
0
0
null
[ "Bilateria", "Ciceribacter ferrooxidans" ]
[ 2355, 1 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 8, 11, 10 ]
4
true
Family
Midkine heparin-binding growth factor
Midkine heparin-binding growth factor
Midkine_heparin-bd_GF
2
IPR000763
763
Catalase-peroxidase haem
Catalase_peroxidase
Family
16,940
false
false
Haem-containing catalase-peroxidases are bifunctional antioxidant enzymes that exhibit both catalase ( ) and peroxidase ( ) activity, and which are present predominantly in bacterial species [ ]. Several evolutionary lineages are present also in archaeal, fungal, and protistan species. These enzymes provide protection ...
[ "GO:0004096", "GO:0004601", "GO:0020037", "GO:0006979" ]
[ "catalase activity", "peroxidase activity", "heme binding", "response to oxidative stress" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "HAMAP", "PRINTS", "PANTHER", "NCBIFAM" ]
[ "MF_01961", "PR00460", "PTHR30555", "TIGR00198" ]
[ "Catal_peroxid", "BPEROXIDASE", "", "cat_per_HPI" ]
[ 15164, 15874, 16937, 15398 ]
4
[ "EC", "GP", "GP", "METACYC", "REACTOME" ]
[ "1.11.1.21", "GenProp0213", "GenProp1598", "PWY-5506", "R-HSA-1222387" ]
[ "EC:1.11.1.21", "GP:GenProp0213", "GP:GenProp1598", "METACYC:PWY-5506", "REACTOME:R-HSA-1222387" ]
5
[ "1itk", "1sj2", "1u2j", "1u2k", "1u2l", "1ub2", "2cca", "2ccd", "3ut2", "3uw8", "3vlh", "3vli", "3vlj", "3vlk", "3vll", "3vlm", "3wnu", "3wxo", "3x16", "4c50", "4c51", "4pae", "5cjh", "5jhx", "5jhy", "5jhz", "5kq0", "5kq2", "5kq3", "5kq6", "5kqh", "5kqi"...
96
[ "PUB00000617", "PUB00015058", "PUB00027476", "PUB00053578", "PUB00053579", "PUB00053580", "PUB00053582" ]
[ "1954228", "12172540", "12628252", "19129167", "18498226", "20062977", "15291807" ]
[ "Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily.", "The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui.", "Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution.", "Occurrence, phylogeny, structure, and function of ...
[ 1991, 2002, 2003, 2009, 2008, 2010, 2004 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 427, 14508, 1755, 250 ]
4
[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1, 1 ]
2
true
Family
Catalase-peroxidase haem
Catalase-peroxidase haem
Catalase_peroxidase
4
IPR000764
764
Uridine kinase-like
Uridine_kinase-like
Family
20,133
false
false
This entry represents the uridine kinase like proteins.
[]
[]
[]
0
[ "NCBIFAM", "CDD" ]
[ "TIGR00235", "cd02023" ]
[ "udk", "UMPK" ]
[ 16031, 20133 ]
2
[ "EC", "GP", "GP", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.1.48", "GenProp1369", "GenProp1384", "PWY-7193", "R-CEL-73614", "R-DDI-196807", "R-DDI-73614", "R-DME-73614", "R-DRE-73614", "R-HSA-73614", "R-MMU-73614", "R-RNO-73614", "R-SCE-73614", "R-SPO-73614", "R-XTR-73614" ]
[ "EC:2.7.1.48", "GP:GenProp1369", "GP:GenProp1384", "METACYC:PWY-7193", "REACTOME:R-CEL-73614", "REACTOME:R-DDI-196807", "REACTOME:R-DDI-73614", "REACTOME:R-DME-73614", "REACTOME:R-DRE-73614", "REACTOME:R-HSA-73614", "REACTOME:R-MMU-73614", "REACTOME:R-RNO-73614", "REACTOME:R-SCE-73614", "R...
15
[ "1udw", "1uei", "1uej", "1ufq", "1uj2", "1xrj", "2jeo", "2uvq", "3asy", "3asz", "3w34", "3w8r", "6n53", "6n54", "6n55", "6pwz", "7sql" ]
17
[ "PUB00000165" ]
[ "8951040" ]
[ "Cloning and expression of a cDNA encoding uridine kinase from mouse brain." ]
[ 1996 ]
1
[]
[ "IPR026008" ]
0
1
0
[ "Bacteria", "Eukaryota", "Halobacteriales", "Mimiviridae", "unclassified sequences" ]
[ 8396, 11437, 201, 9, 90 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 22, 5, 15, 6, 1, 9, 13, 1, 11, 16, 1, 1, 32 ]
13
true
Family
Uridine kinase-like
Uridine kinase-like
Uridine_kinase-like
6
IPR000766
766
Galactose-1-phosphate uridyl transferase, class II
GalP_uridyl_Trfase_II
Family
4,142
false
false
Galactose-1-phosphate uridyl transferase (GalT) catalyses the transfer of an uridyldiphosphate group on galactose (or glucose) 1-phosphate. During the reaction, the uridyl moiety links to a histidine residue. In the Escherichia coli enzyme, it has been shown [ ] that two histidine residues separated by a single proline...
[ "GO:0008108", "GO:0006012", "GO:0005737" ]
[ "UDP-glucose:hexose-1-phosphate uridylyltransferase activity", "galactose metabolic process", "cytoplasm" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PIRSF", "PANTHER", "NCBIFAM" ]
[ "MF_00571", "PIRSF006005", "PTHR39191", "TIGR01239" ]
[ "GalP_UDP_trans", "GalT_BS", "", "galT_2" ]
[ 3982, 3663, 4141, 2872 ]
4
[ "EC", "GP", "METACYC", "METACYC", "PROSITEDOC" ]
[ "2.7.7.12", "GenProp0143", "PWY-6317", "PWY-6527", "PDOC00108" ]
[ "EC:2.7.7.12", "GP:GenProp0143", "METACYC:PWY-6317", "METACYC:PWY-6527", "PROSITEDOC:PDOC00108" ]
5
[]
0
[ "PUB00002146", "PUB00004352" ]
[ "2066342", "2845364" ]
[ "Galactose utilization in Lactobacillus helveticus: isolation and characterization of the galactokinase (galK) and galactose-1-phosphate uridyl transferase (galT) genes.", "Conservation of short patches of amino acid sequence amongst proteins with a common function but evolutionarily distinct origins: implication...
[ 1991, 1988 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 4107, 13, 22 ]
3
[]
[]
0
true
Family
Galactose-1-phosphate uridyl transferase, class II
Galactose-1-phosphate uridyl transferase, class II
GalP_uridyl_Trfase_II
1
IPR000768
768
NAD:arginine ADP-ribosyltransferase, ART
ART
Family
15,327
false
false
Mono-ADP-ribosylation is a post-translational modification of proteins in which the ADP-ribose moiety of NAD is transferred to proteins. This process is responsible for the toxicity of some bacterial toxins (e.g., cholera and pertussis toxins). Mono (ADP-ribosyl) transferases exist in vertebrates that transfer ADP-ribo...
[ "GO:0106274" ]
[ "NAD+-protein-arginine ADP-ribosyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROSITE" ]
[ "PF01129", "PR00970", "PS01291" ]
[ "ART", "RIBTRNSFRASE", "ART" ]
[ 15324, 4848, 3180 ]
3
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.4.2.31", "PDOC00993", "R-HSA-1462054", "R-HSA-163125", "R-MMU-1462054", "R-MMU-163125" ]
[ "EC:2.4.2.31", "PROSITEDOC:PDOC00993", "REACTOME:R-HSA-1462054", "REACTOME:R-HSA-163125", "REACTOME:R-MMU-1462054", "REACTOME:R-MMU-163125" ]
6
[ "1gxy", "1gxz", "1gy0", "1og1", "1og3", "1og4", "6dre", "6drh", "6k93", "6k94", "6kly" ]
11
[ "PUB00000393", "PUB00002966", "PUB00095655", "PUB00095656" ]
[ "7947688", "8703012", "21901419", "17928361" ]
[ "Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases.", "Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase.", "Glucagon like-peptide-1 receptor is covalently modified by endoge...
[ 1994, 1996, 2012, 2008 ]
4
[ "IPR050999" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 527, 14770, 27, 3 ]
4
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 20, 31, 26, 32 ]
4
true
Family
NAD:arginine ADP-ribosyltransferase, ART
NAD:arginine ADP-ribosyltransferase, ART
ART
8
IPR000769
769
Regulatory protein Rop
Regulatory_Rop
Family
972
false
false
The Rop protein regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. Rop increases the affinity of RNAI for RNAII and thus decreases the rate of re...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PRINTS" ]
[ "PF01815", "PIRSF003229", "PR00835" ]
[ "Rop", "Rop_reg", "ROPREGULATRY" ]
[ 972, 846, 950 ]
3
[]
[]
[]
0
[ "1b6q", "1f4m", "1f4n", "1gmg", "1gto", "1nkd", "1qx8", "1rop", "1rpo", "1rpr", "1yo7", "2ghy", "2ijh", "2iji", "2ijj", "2ijk", "3k79", "4do2", "7kae" ]
19
[ "PUB00000328", "PUB00003045", "PUB00003223" ]
[ "2223771", "1841691", "3681971" ]
[ "Proton nuclear magnetic resonance assignments and secondary structure determination of the ColE1 rop (rom) protein.", "The structure of ColE1 rop in solution.", "Structure of the ColE1 rop protein at 1.7 A resolution." ]
[ 1990, 1991, 1987 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "plasmids", "uncultured prokaryote" ]
[ 956, 6, 2, 2, 6 ]
5
[]
[]
0
true
Family
Regulatory protein Rop
Regulatory protein Rop
Regulatory_Rop
4
IPR000770
770
SAND domain
SAND_dom
Domain
8,102
false
false
The SAND domain (named after Sp100, AIRE-1, NucP41/75, DEAF-1) is a conserved ~80 residue region found in a number of nuclear proteins, many of which function in chromatin-dependent transcriptional control. These include proteins linked to various human diseases, such as the Sp100 (Speckled protein 100kDa) [ ], NUDR (N...
[ "GO:0003677" ]
[ "DNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF01342", "PS50864", "SM00258" ]
[ "SAND", "SAND", "SAND" ]
[ 7415, 8016, 7259 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50864", "R-HSA-3108214", "R-HSA-877300", "R-MMU-3108214" ]
[ "PROSITEDOC:PDOC50864", "REACTOME:R-HSA-3108214", "REACTOME:R-HSA-877300", "REACTOME:R-MMU-3108214" ]
4
[ "1h5p", "1oqj", "1ufn", "8j70", "8j71" ]
5
[ "PUB00005483", "PUB00007101", "PUB00056637", "PUB00097269" ]
[ "9697411", "11427895", "10894151", "9636146" ]
[ "The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor.", "The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation.", "Properties of the glucocorticoid modulatory element binding proteins GMEB-1 and -2: pote...
[ 1998, 2001, 2000, 1998 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "viral metagenome" ]
[ 7, 8094, 1 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus" ]
[ 6, 4, 60, 5, 36, 34, 2, 46 ]
8
true
Domain
SAND domain
SAND domain
SAND_dom
2
IPR000771
771
Fructose-bisphosphate aldolase, class-II
FBA_II
Family
40,199
false
false
Class-II aldolases [ ], mainly found in prokaryotes and fungi, are homodimeric enzymes, which require a divalent metal ion, generally zinc, for their activity. They include fructose-bisphosphate aldolase [ , ], a glycolytic enzyme that catalyses the reversible aldol cleavage or condensation of fructose-1,6-bisphosphate...
[ "GO:0008270", "GO:0016832", "GO:0005975" ]
[ "zinc ion binding", "aldehyde-lyase activity", "carbohydrate metabolic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PIRSF", "PROSITE", "PROSITE", "NCBIFAM", "CDD" ]
[ "PF01116", "PIRSF001359", "PS00602", "PS00806", "TIGR00167", "cd00947" ]
[ "F_bP_aldolase", "F_bP_aldolase_II", "ALDOLASE_CLASS_II_1", "ALDOLASE_CLASS_II_2", "cbbA", "TBP_aldolase_IIB" ]
[ 40103, 37167, 20492, 24083, 33554, 23801 ]
6
[ "EC", "GP", "GP", "GP", "GP", "GP", "PROSITEDOC" ]
[ "4.1.2", "GenProp1286", "GenProp1306", "GenProp1344", "GenProp1407", "GenProp1705", "PDOC00523" ]
[ "EC:4.1.2", "GP:GenProp1286", "GP:GenProp1306", "GP:GenProp1344", "GP:GenProp1407", "GP:GenProp1705", "PROSITEDOC:PDOC00523" ]
7
[ "1b57", "1dos", "1gvf", "1gyn", "1rv8", "1rvg", "1zen", "2fjk", "2isv", "2isw", "3c4u", "3c52", "3c56", "3ekl", "3ekz", "3elf", "3gak", "3gay", "3gb6", "3n9r", "3n9s", "3ohi", "3pm6", "3q94", "3qm3", "4a21", "4a22", "4def", "4del", "4lv4", "4to8", "5gk3"...
64
[ "PUB00000567", "PUB00001651", "PUB00005383" ]
[ "2199259", "8436219", "1412694" ]
[ "The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.", "Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.", "Fructose-bisphosphate aldolases: an evolutionary history." ]
[ 1990, 1993, 1992 ]
3
[]
[ "IPR006411", "IPR006412", "IPR011288" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 150, 33758, 5712, 1, 578 ]
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" ]
[ 10, 4, 2, 6, 1, 1, 29 ]
7
true
Family
Fructose-bisphosphate aldolase, class-II
Fructose-bisphosphate aldolase, class-II
FBA_II
7
IPR000772
772
Ricin B, lectin domain
Ricin_B_lectin
Domain
81,554
false
false
Ricin is a legume lectin from the seeds of the castor bean plant, Ricinus communis. The seeds are poisonous to people, animals and insects and just one milligram of ricin can kill an adult. Primary structure analysis has shown the presence of a similar domain in many carbohydrate-recognition proteins like plant and bac...
[]
[]
[]
0
[ "PFAM", "PFAM", "PFAM", "SMART" ]
[ "PF00652", "PF14200", "PF24562", "SM00458" ]
[ "Ricin_B_lectin", "RicinB_lectin_2", "CysR_MRC2_N", "RICIN" ]
[ 55009, 20194, 5705, 65189 ]
4
[ "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...
[ "GenProp0707", "GenProp1712", "PDOC50231", "R-BTA-1482788", "R-BTA-1482801", "R-BTA-1482839", "R-BTA-1482922", "R-BTA-1482925", "R-BTA-1483166", "R-BTA-6811436", "R-BTA-913709", "R-CEL-6811436", "R-CEL-913709", "R-DME-190372", "R-DME-6811436", "R-DME-913709", "R-HSA-1236978", "R-HS...
[ "GP:GenProp0707", "GP:GenProp1712", "PROSITEDOC:PDOC50231", "REACTOME:R-BTA-1482788", "REACTOME:R-BTA-1482801", "REACTOME:R-BTA-1482839", "REACTOME:R-BTA-1482922", "REACTOME:R-BTA-1482925", "REACTOME:R-BTA-1483166", "REACTOME:R-BTA-6811436", "REACTOME:R-BTA-913709", "REACTOME:R-CEL-6811436", ...
45
[ "1abr", "1ce7", "1dqg", "1dqo", "1fwu", "1fwv", "1ggp", "1hwm", "1hwn", "1hwo", "1hwp", "1isv", "1isw", "1isx", "1isy", "1isz", "1it0", "1knl", "1knm", "1m2t", "1mc9", "1onk", "1oql", "1pc8", "1pum", "1puu", "1qxm", "1rzo", "1sz6", "1tfm", "1v6u", "1v6v"...
243
[ "PUB00006197", "PUB00006198", "PUB00006199", "PUB00006200", "PUB00006201", "PUB00024297", "PUB00036748", "PUB00155593", "PUB00155594", "PUB00155595", "PUB00155596" ]
[ "9603958", "8844840", "7664090", "1881882", "3561502", "10748229", "11152606", "26481812", "27247422", "29225077", "12972549" ]
[ "Novel galactose-binding proteins in Annelida. Characterization of 29-kDa tandem repeat-type lectins from the earthworm Lumbricus terrestris.", "The (QxW)3 domain: a flexible lectin scaffold.", "A mosquitocidal toxin with a ricin-like cell-binding domain.", "Structure of ricin B-chain at 2.5 A resolution.", ...
[ 1998, 1996, 1995, 1991, 1987, 2000, 2001, 2015, 2016, 2018, 2003 ]
11
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 162, 38620, 42678, 49, 45 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Zea mays" ]
[ 13, 12, 103, 21, 86, 60, 1, 90, 6 ]
9
true
Domain
Ricin B, lectin domain
Ricin B, lectin domain
Ricin_B_lectin
4
IPR000773
773
Granulocyte-macrophage colony-stimulating factor
GM_colony-stim-fac
Family
224
false
false
Granulocyte-macrophage colony-stimulating factor (GMCSF) is a cytokine that acts in hematopoiesis to stimulate growth and differentiation of hematopoietic precursor cells from various lineages including granulocytes, macrophages, eosinophils and erythrocytes [ , ]. GMCSF is a glycoprotein of ~120 residues that contains...
[ "GO:0005129", "GO:0008083", "GO:0006955", "GO:0005576" ]
[ "granulocyte macrophage colony-stimulating factor receptor binding", "growth factor activity", "immune response", "extracellular region" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PRINTS", "PROSITE", "PANTHER", "SMART", "CDD" ]
[ "PF01109", "PR00693", "PS00702", "PTHR10059", "SM00040", "cd00040" ]
[ "GM_CSF", "GMCSFACTOR", "GM_CSF", "", "CSF2", "CSF2" ]
[ 214, 212, 155, 214, 213, 154 ]
6
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00584", "R-BTA-512988", "R-BTA-5673001", "R-BTA-912526", "R-CFA-512988", "R-CFA-5673001", "R-CFA-912526", "R-HSA-512988", "R-HSA-5673001", "R-HSA-6783783", "R-HSA-8939246", "R-HSA-912526", "R-MMU-512988", "R-MMU-5673001", "R-MMU-912526", "R-RNO-512988", "R-RNO-5673001", "R-RNO...
[ "PROSITEDOC:PDOC00584", "REACTOME:R-BTA-512988", "REACTOME:R-BTA-5673001", "REACTOME:R-BTA-912526", "REACTOME:R-CFA-512988", "REACTOME:R-CFA-5673001", "REACTOME:R-CFA-912526", "REACTOME:R-HSA-512988", "REACTOME:R-HSA-5673001", "REACTOME:R-HSA-6783783", "REACTOME:R-HSA-8939246", "REACTOME:R-HSA...
21
[ "1csg", "2gmf", "4nkq", "4rs1", "5c7x", "5d22", "5d28", "5d70", "5d71", "5d72", "6bfq", "6bfs" ]
12
[ "PUB00000780", "PUB00003283" ]
[ "2458827", "1569568" ]
[ "Hemopoietic growth factors: a review.", "Three-dimensional structure of recombinant human granulocyte-macrophage colony-stimulating factor." ]
[ 1988, 1992 ]
2
[]
[]
0
0
null
[ "Eukaryota", "Haloquadratum walsbyi J07HQW1", "Pseudomonadati" ]
[ 220, 1, 3 ]
3
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 3 ]
3
true
Family
Granulocyte-macrophage colony-stimulating factor
Granulocyte-macrophage colony-stimulating factor
GM_colony-stim-fac
5
IPR000774
774
Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal
PPIase_FKBP_N
Domain
15,495
false
false
Peptidyl-prolyl cis-trans isomerase (PPIase) catalyses the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [ ]. This α helical domain is found at the N terminus of proteins belonging to the FKBP-type peptidyl-prolyl cis-trans isomerase family. Peptidyl-prolyl cis-trans isomerase has been shown ...
[ "GO:0006457" ]
[ "protein folding" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF01346" ]
[ "FKBP_N" ]
[ 15495 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "5.2.1.8", "R-HSA-1236974", "R-HSA-166058", "R-HSA-168188", "R-HSA-5602498", "R-HSA-5603041", "R-HSA-9760173" ]
[ "EC:5.2.1.8", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-166058", "REACTOME:R-HSA-168188", "REACTOME:R-HSA-5602498", "REACTOME:R-HSA-5603041", "REACTOME:R-HSA-9760173" ]
7
[ "1fd9", "1q6h", "1q6i", "1q6u", "2uz5", "2vcd", "3b09", "4qcc", "7dek", "8bjc", "8bjd", "8bje", "8bk5", "8r39", "8ruo" ]
15
[ "PUB00034654", "PUB00034655", "PUB00034656", "PUB00034657" ]
[ "2644542", "6395866", "3306408", "3277061" ]
[ "Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin.", "[Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides]", "Catalysis of protein folding by prolyl isomerase.", "Protein-disulphide isomerase and prolyl iso...
[ 1989, 1984, 1987, 1988 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 14907, 403, 185 ]
3
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Domain
Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal
Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal
PPIase_FKBP_N
1
IPR000775
775
Bindin
Bindin
Family
643
false
false
Bindin, the major protein component of the acrosome granule of sea urchin sperm, mediates species-specific adhesion of sperm to the egg surface during fertilisation [ , ]. The protein coats the acrosomal process after externalisation by the acrosome reaction; it binds to sulphated, fucose-containing polysaccharides on ...
[ "GO:0007342" ]
[ "fusion of sperm to egg plasma membrane involved in single fertilization" ]
[ "biological_process" ]
1
[ "PFAM", "PRINTS" ]
[ "PF02084", "PR00761" ]
[ "Bindin", "BINDIN" ]
[ 638, 415 ]
2
[]
[]
[]
0
[]
0
[ "PUB00001098", "PUB00003633" ]
[ "1991551", "1775065" ]
[ "The sequence of the Arbacia punctulata bindin cDNA and implications for the structural basis of species-specific sperm adhesion and fertilization.", "Comparison of the bindin proteins of Strongylocentrotus franciscanus, S. purpuratus, and Lytechinus variegatus: sequences involved in the species specificity of fe...
[ 1991, 1991 ]
2
[]
[]
0
0
null
[ "Eukaryota", "Paenibacillus montanisoli" ]
[ 642, 1 ]
2
[]
[]
0
true
Family
Bindin
Bindin
Bindin
6
IPR000776
776
Precursor fusion glycoprotein F0, Paramyxoviridae
Fusion_F0_Paramyxovir
Family
17,287
false
false
The fusion glycoproteins from this family are found in ssRNA negative-strand viruses. This protein directs fusion of viral and cellular membranes, resulting in viral penetration, and can direct fusion of infected cells with adjoining cells, resulting in the formation of syncytia. The mature form is a dimer of polypepti...
[ "GO:0019064" ]
[ "fusion of virus membrane with host plasma membrane" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF00523" ]
[ "Fusion_gly" ]
[ 17287 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-9820960", "R-HSA-9820962", "R-HSA-9828721", "R-HSA-9828806", "R-HSA-9833110" ]
[ "REACTOME:R-HSA-9820960", "REACTOME:R-HSA-9820962", "REACTOME:R-HSA-9828721", "REACTOME:R-HSA-9828806", "REACTOME:R-HSA-9833110" ]
5
[ "1g2c", "1g5g", "1svf", "1wp7", "1wp8", "1ztm", "2b9b", "2fyz", "3kpe", "3maw", "3n27", "3rki", "3rrr", "3rrt", "4ccf", "4dag", "4gip", "4jhw", "4mmq", "4mmr", "4mms", "4mmt", "4mmu", "4mmv", "4wsg", "4zyp", "5c69", "5c6b", "5ea3", "5ea4", "5ea5", "5ea6"...
214
[ "PUB00028095" ]
[ "3776349" ]
[ "Nucleotide sequence of the gene encoding the Newcastle disease virus fusion protein and comparisons of paramyxovirus fusion protein sequences." ]
[ 1986 ]
1
[]
[]
0
0
null
[ "Bifidobacterium breve", "Euteleostomi", "Mononegavirales" ]
[ 1, 17, 17269 ]
3
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Precursor fusion glycoprotein F0, Paramyxoviridae
Precursor fusion glycoprotein F0, Paramyxoviridae
Fusion_F0_Paramyxovir
3
IPR000777
777
Human immunodeficiency virus 1, envelope glycoprotein Gp120
HIV1_Gp120
Domain
268,775
false
false
The envelope glycoprotein Gp160 of HIV1 is cleaved into the surface protein Gp120 and the transmembrane protein Gp41. The entry of HIV requires interaction of viral Gp120 with the CD4 glycoprotein and a chemokine receptor on the cell surface [ ]. This entry represents the GP120 core protein, which is released after Gp1...
[ "GO:0019031" ]
[ "viral envelope" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF00516" ]
[ "GP120" ]
[ 268775 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1462054", "R-HSA-162588", "R-HSA-171286", "R-HSA-173107", "R-HSA-175474", "R-HSA-5621480" ]
[ "REACTOME:R-HSA-1462054", "REACTOME:R-HSA-162588", "REACTOME:R-HSA-171286", "REACTOME:R-HSA-173107", "REACTOME:R-HSA-175474", "REACTOME:R-HSA-5621480" ]
6
[ "1ce4", "1g9m", "1g9n", "1gc1", "1rzj", "1rzk", "1yyl", "1yym", "2b4c", "2bf1", "2i5y", "2i60", "2nxy", "2nxz", "2ny0", "2ny1", "2ny2", "2ny3", "2ny4", "2ny5", "2ny6", "2ny7", "2qad", "3dnl", "3dnn", "3dno", "3fus", "3hi1", "3idx", "3idy", "3j5m", "3j70"...
663
[ "PUB00004281", "PUB00039508" ]
[ "9641677", "16284180" ]
[ "Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody.", "Structure of a V3-containing HIV-1 gp120 core." ]
[ 1998, 2005 ]
2
[]
[]
0
0
null
[ "Homo sapiens", "Lentivirus" ]
[ 1, 268774 ]
2
[ "Homo sapiens" ]
[ 1 ]
1
true
Domain
Human immunodeficiency virus 1, envelope glycoprotein Gp120
Human immunodeficiency virus 1, envelope glycoprotein Gp120
HIV1_Gp120
2
IPR000778
778
Cytochrome b245, heavy chain
Cyt_b245_heavy_chain
Family
12,104
false
false
Phagocytes form the first line of defence against invasion by micro-organisms. Engulfing of bacteria by neutrophils during phagocytosis is accompanied by a respiratory burst. Defects in phagocytosis involving the lack of a respiratory burst give rise to chronic granulomatous disease (CGD) [ ]. Proteins in this entry ar...
[ "GO:0016491", "GO:0016020" ]
[ "oxidoreductase activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR00466" ]
[ "GP91PHOX" ]
[ 12104 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "1.6.3.-", "R-BTA-1222556", "R-BTA-1236973", "R-BTA-3299685", "R-BTA-4420097", "R-BTA-5668599", "R-BTA-6798695", "R-BTA-9013149", "R-BTA-9013404", "R-BTA-9013423", "R-DDI-209968", "R-DDI-3299685", "R-DDI-6798695", "R-HSA-1222556", "R-HSA-1236973", "R-HSA-3299685", "R-HSA-4420097", ...
[ "EC:1.6.3.-", "REACTOME:R-BTA-1222556", "REACTOME:R-BTA-1236973", "REACTOME:R-BTA-3299685", "REACTOME:R-BTA-4420097", "REACTOME:R-BTA-5668599", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-9013149", "REACTOME:R-BTA-9013404", "REACTOME:R-BTA-9013423", "REACTOME:R-DDI-209968", "REACTOME:R-DDI-32996...
46
[ "3a1f", "5o0x", "8cak", "8cal", "8cao", "8cap", "8cb0", "8gz3", "8kei", "8wej", "8x2l" ]
11
[ "PUB00003781", "PUB00005005", "PUB00158913", "PUB00158914", "PUB00158915", "PUB00158916" ]
[ "8796870", "8251942", "15338276", "36241643", "36413210", "38355798" ]
[ "The NADPH oxidase and chronic granulomatous disease.", "A structural model for the nucleotide binding domains of the flavocytochrome b-245 beta-chain.", "Functional analysis of two-amino acid substitutions in gp91 phox in a patient with X-linked flavocytochrome b558-positive chronic granulomatous disease by me...
[ 1996, 1993, 2004, 2022, 2022, 2024 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "marine metagenome" ]
[ 45, 12056, 3 ]
3
[ "Arabidopsis thaliana", "Danio rerio", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 81, 8, 21, 11, 28, 21, 1, 92 ]
8
true
Family
Cytochrome b245, heavy chain
Cytochrome b245, heavy chain
Cyt_b245_heavy_chain
1
IPR000779
779
Interleukin-2
IL-2
Family
310
false
false
T-Lymphocytes regulate the growth and differentiation of certain lymphopoietic and haemopoietic cells through the release of various secreted protein factors [ ]. These factors, which include interleukin-2 (IL2), are secreted by lectin- or antigen-stimulated T-cells, and have various physiological effects. IL2 is a lym...
[ "GO:0005134", "GO:0008083", "GO:0006955", "GO:0005576" ]
[ "interleukin-2 receptor binding", "growth factor activity", "immune response", "extracellular region" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PRINTS", "PANTHER", "SMART" ]
[ "PF00715", "PR00265", "PTHR48487", "SM00189" ]
[ "IL2", "INTERLEUKIN2", "", "IL2" ]
[ 310, 295, 307, 293 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00349", "R-BTA-5673001", "R-BTA-9020558", "R-BTA-912526", "R-CFA-5673001", "R-CFA-9020558", "R-CFA-912526", "R-HSA-5673001", "R-HSA-8877330", "R-HSA-9020558", "R-HSA-912526", "R-MMU-5673001", "R-MMU-9020558", "R-MMU-912526", "R-RNO-5673001", "R-RNO-9020558", "R-RNO-912526", "R...
[ "PROSITEDOC:PDOC00349", "REACTOME:R-BTA-5673001", "REACTOME:R-BTA-9020558", "REACTOME:R-BTA-912526", "REACTOME:R-CFA-5673001", "REACTOME:R-CFA-9020558", "REACTOME:R-CFA-912526", "REACTOME:R-HSA-5673001", "REACTOME:R-HSA-8877330", "REACTOME:R-HSA-9020558", "REACTOME:R-HSA-912526", "REACTOME:R-M...
20
[ "1irl", "1m47", "1m48", "1m49", "1m4a", "1m4b", "1m4c", "1nbp", "1pw6", "1py2", "1qvn", "1z92", "2b5i", "2erj", "3ink", "3qaz", "3qb1", "4nej", "4nem", "4yqx", "4yue", "4zf7", "5lqb", "5m5e", "5utz", "6vwu", "6x97", "6ye3", "7dr4", "7m2g", "7ra9", "7raa"...
36
[ "PUB00000368", "PUB00004612", "PUB00004618" ]
[ "1510960", "3918306", "3517854" ]
[ "Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.", "Use of a cDNA expression vector for isolation of mouse interleukin 2 cDNA clones: expression of T-cell growth-factor activity after transfection of monkey cells.", "Cloning, sequence, and expression of bovine interleukin 2." ]
[ 1992, 1985, 1986 ]
3
[]
[]
0
0
null
[ "Theria" ]
[ 310 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 12, 10, 2 ]
3
true
Family
Interleukin-2
Interleukin-2
IL-2
8
IPR000780
780
MCP methyltransferase, CheR-type
CheR_MeTrfase
Domain
30,357
false
false
CheR proteins are part of the chemotaxis signaling mechanism in bacteria. Flagellated bacteria swim towards favourable chemicals and away from deleterious ones. Sensing of chemoeffector gradients involves chemotaxis receptors, transmembrane (TM) proteins that detect stimuli through their periplasmic domains and transdu...
[ "GO:0008757" ]
[ "S-adenosylmethionine-dependent methyltransferase activity" ]
[ "molecular_function" ]
1
[ "PRINTS", "PROFILE", "SMART" ]
[ "PR00996", "PS50123", "SM00138" ]
[ "CHERMTFRASE", "CHER", "MeTrc" ]
[ 29758, 30342, 30011 ]
3
[ "EC", "PROSITEDOC" ]
[ "2.1.1.80", "PDOC50123" ]
[ "EC:2.1.1.80", "PROSITEDOC:PDOC50123" ]
2
[ "1af7", "1bc5", "5ftw", "5xlx", "5xly", "5y4r", "5y4s" ]
7
[ "PUB00003960", "PUB00005291" ]
[ "9628482", "9115443" ]
[ "Chemotaxis receptor recognition by protein methyltransferase CheR.", "Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine." ]
[ 1998, 1997 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 589, 29379, 52, 337 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
MCP methyltransferase, CheR-type
MCP methyltransferase, CheR-type
CheR_MeTrfase
3
IPR000781
781
Enhancer of rudimentary
ERH
Family
3,030
false
false
The Drosophila protein 'enhancer of rudimentary' (gene (e(r)) is a small protein of 104 residues whose function is not yet clear. From an evolutionary point of view, it is highly conserved [ ] and has been found to exist in probably all multicellular eukaryotic organisms. ERH has been implicated in the regulation of py...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PROSITE", "PANTHER" ]
[ "PF01133", "PIRSF016393", "PS01290", "PTHR12373" ]
[ "ER", "Enh_rudimentary", "ER", "" ]
[ 3028, 2142, 1684, 2887 ]
4
[ "PROSITEDOC" ]
[ "PDOC00992" ]
[ "PROSITEDOC:PDOC00992" ]
1
[ "1w9g", "1wwq", "1wz7", "2nml", "6akj", "6s2w", "7cnc", "7ejo", "7ejs", "7o6l", "7o6n", "7x39" ]
12
[ "PUB00001871", "PUB00093060", "PUB00093061", "PUB00093062", "PUB00093063", "PUB00094514" ]
[ "9074495", "27830090", "26942678", "28627136", "29424342", "31974447" ]
[ "The putative cell cycle gene, enhancer of rudimentary, encodes a highly conserved protein found in plants and animals.", "Drosophila Enhancer of Rudimentary Homolog, ERH, Is a Binding Partner of RPS3, RPL19, and DDIT4, Suggesting a Mechanism for the Nuclear Localization of ERH.", "Enhancer of Rudimentary Coope...
[ 1997, 2016, 2016, 2017, 2018, 2020 ]
6
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3030 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 3, 2, 1, 2, 2, 8, 6, 8, 1, 6 ]
10
true
Family
Enhancer of rudimentary
Enhancer of rudimentary
ERH
3
IPR000782
782
FAS1 domain
FAS1_domain
Domain
51,546
false
false
The FAS1 (fasciclin-like) domain is an extracellular module of about 140 amino acid residues. It has been suggested that the FAS1 domain represents an ancient cell adhesion domain common to plants and animals [ ]; related FAS1 domains are also found in bacteria [ ]. The crystal structure of FAS1 domains 3 and 4 of fasc...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF02469", "PS50213", "SM00554" ]
[ "Fasciclin", "FAS1", "FAS1" ]
[ 49014, 49927, 44503 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50213", "R-HSA-2142845", "R-HSA-2160916", "R-HSA-3000497", "R-HSA-977225", "R-MMU-2142845", "R-MMU-2160916", "R-MMU-3000497" ]
[ "PROSITEDOC:PDOC50213", "REACTOME:R-HSA-2142845", "REACTOME:R-HSA-2160916", "REACTOME:R-HSA-3000497", "REACTOME:R-HSA-977225", "REACTOME:R-MMU-2142845", "REACTOME:R-MMU-2160916", "REACTOME:R-MMU-3000497" ]
8
[ "1nyo", "1o70", "1w7d", "1w7e", "1x3b", "2ltb", "2ltc", "2mxa", "2vxp", "5n86", "5nv6", "5wt7", "5y6p", "5yjg", "5yjh", "6kgx", "6tjv", "7as7", "7asc", "7asg", "7ezx", "7y4l", "7y5e", "7y7a", "8c18", "8hga", "8hia", "9g6k", "9i05" ]
29
[ "PUB00005952", "PUB00011804", "PUB00011805", "PUB00011806", "PUB00044561", "PUB00044562", "PUB00044563", "PUB00044564" ]
[ "7822037", "7925267", "10906123", "12575939", "16944204", "15345724", "7871388", "18450759" ]
[ "Relationship of secretion pattern and MPB70 homology with osteoblast-specific factor 2 to osteitis following Mycobacterium bovis BCG vaccination.", "Algal-CAMs: isoforms of a cell adhesion molecule in embryos of the alga Volvox with homology to Drosophila fasciclin I.", "Identification of motifs for cell adhes...
[ 1995, 1994, 2000, 2003, 2006, 2004, 1995, 2008 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 378, 17147, 33836, 11, 174 ]
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...
[ 98, 2, 31, 23, 24, 28, 3, 70, 23, 2, 2, 90 ]
12
true
Domain
FAS1 domain
FAS1 domain
FAS1_domain
7
IPR000783
783
RNA polymerase, subunit H/Rpb5 C-terminal
RNA_pol_subH/Rpb5_C
Domain
7,492
false
false
Prokaryotes contain a single DNA-dependent RNA polymerase (RNAP; ) that is responsible for the transcription of all genes, while eukaryotes have three classes of RNAPs (I-III) that transcribe different sets of genes. Each class of RNA polymerase is an assemblage of ten to twelve different polypeptides. Certain subunits...
[ "GO:0003677", "GO:0003899", "GO:0006351" ]
[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF01191" ]
[ "RNA_pol_Rpb5_C" ]
[ 7492 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.7.6", "PDOC00854", "R-CEL-112382", "R-CEL-113418", "R-CEL-5250924", "R-CEL-5578749", "R-CEL-674695", "R-CEL-6781823", "R-CEL-6782135", "R-CEL-6782210", "R-CEL-6796648", "R-CEL-6803529", "R-CEL-6807505", "R-CEL-72086", "R-CEL-72163", "R-CEL-72165", "R-CEL-72203", "R-CEL-73762",...
[ "EC:2.7.7.6", "PROSITEDOC:PDOC00854", "REACTOME:R-CEL-112382", "REACTOME:R-CEL-113418", "REACTOME:R-CEL-5250924", "REACTOME:R-CEL-5578749", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-6781823", "REACTOME:R-CEL-6782135", "REACTOME:R-CEL-6782210", "REACTOME:R-CEL-6796648", "REACTOME:R-CEL-6803529",...
193
[ "1dzf", "1eik", "1hmj", "1i3q", "1i50", "1i6h", "1k83", "1nik", "1nt9", "1pqv", "1r5u", "1r9s", "1r9t", "1sfo", "1twa", "1twc", "1twf", "1twg", "1twh", "1wcm", "1y1v", "1y1w", "1y1y", "1y77", "2b63", "2b8k", "2e2h", "2e2i", "2e2j", "2ja5", "2ja6", "2ja7"...
548
[ "PUB00003393", "PUB00004780", "PUB00008455", "PUB00008456" ]
[ "10191143", "1729711", "10841537", "10841538" ]
[ "RNA polymerase subunit H features a beta-ribbon motif within a novel fold that is present in archaea and eukaryotes.", "Component H of the DNA-dependent RNA polymerases of Archaea is homologous to a subunit shared by the three eucaryal nuclear RNA polymerases.", "Crystal structure of RPB5, a universal eukaryot...
[ 1999, 1992, 2000, 2000 ]
4
[]
[]
0
0
null
[ "Archaea", "Candidatus Staskawiczbacteria bacterium RIFCSPHIGHO2_01_FULL_41_41", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 901, 1, 6185, 123, 282 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 22, 1, 3, 1, 6, 3, 1, 13, 7, 1, 1, 13 ]
12
true
Domain
RNA polymerase, subunit H/Rpb5 C-terminal
RNA polymerase, subunit H/Rpb5 C-terminal
RNA_pol_subH/Rpb5_C
1
IPR000784
784
Late protein L2
Late_L2
Family
3,914
false
false
This family includes the L2 minor capsid protein, a late protein from Human papillomavirus (HPV). HPV are dsDNA viruses with no RNA stage in their replication cycle. Their dsDNA is contained within a capsid composed of 72 L1 capsomers and about 36 L2 minor capsid proteins. L2 minor capsid proteins enter the nucleus twi...
[ "GO:0005198", "GO:0019028" ]
[ "structural molecule activity", "viral capsid" ]
[ "molecular_function", "cellular_component" ]
2
[ "HAMAP", "PFAM" ]
[ "MF_04003", "PF00513" ]
[ "PPV_L2", "Late_protein_L2" ]
[ 3692, 3914 ]
2
[]
[]
[]
0
[]
0
[ "PUB00035300", "PUB00035301" ]
[ "16873281", "15507604" ]
[ "The l2 minor capsid protein of low-risk human papillomavirus type 11 interacts with host nuclear import receptors and viral DNA.", "The l2 minor capsid protein of human papillomavirus type 16 interacts with a network of nuclear import receptors." ]
[ 2006, 2004 ]
2
[]
[]
0
0
null
[ "Bilateria", "Papillomaviridae" ]
[ 2, 3912 ]
2
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Late protein L2
Late protein L2
Late_L2
8
IPR000785
785
Herpsevirus envelope glycoprotein M
Herpes_glycop_M
Family
540
false
false
Envelope glycoprotein M (gM) is well conserved across the herpesvirus family. It is important for virion assembly and egress [ ].
[]
[]
[]
0
[ "HAMAP", "PFAM", "PRINTS" ]
[ "MF_04035", "PF01528", "PR00333" ]
[ "HSV_GM", "Herpes_glycop", "HSVINTEGRLMP" ]
[ 429, 540, 431 ]
3
[ "REACTOME", "REACTOME" ]
[ "R-HSA-9609690", "R-HSA-9610379" ]
[ "REACTOME:R-HSA-9609690", "REACTOME:R-HSA-9610379" ]
2
[]
0
[ "PUB00082557" ]
[ "12771417" ]
[ "Glycoproteins M and N of human herpesvirus 8 form a complex and inhibit cell fusion." ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Amniota", "Corallococcus aberystwythensis", "Herpesvirales" ]
[ 2, 1, 537 ]
3
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Herpsevirus envelope glycoprotein M
Herpsevirus envelope glycoprotein M
Herpes_glycop_M
4
IPR000786
786
Green fluorescent protein, GFP
Green_fluorescent_prot
Family
258
false
false
The green fluorescent protein (GFP) is found in the jellyfish (Aequorea victoria), and functions as an energy-transfer acceptor. It fluoresces in vivo upon receiving energy from the Ca 2+ -activated photoprotein aequorin. The protein absorbs light maximally at 395 nm and exhibits a smaller absorbance peak at 470 nm. Th...
[ "GO:0006091" ]
[ "generation of precursor metabolites and energy" ]
[ "biological_process" ]
1
[ "PRINTS" ]
[ "PR01229" ]
[ "GFLUORESCENT" ]
[ 258 ]
1
[]
[]
[]
0
[ "1b9c", "1bfp", "1c4f", "1cv7", "1ema", "1emb", "1emc", "1eme", "1emf", "1emg", "1emk", "1eml", "1emm", "1f09", "1f0b", "1g7k", "1gfl", "1ggx", "1h6r", "1hcj", "1huy", "1jby", "1jbz", "1jc0", "1jc1", "1kp5", "1kyp", "1kyr", "1kys", "1myw", "1oxd", "1oxe"...
1,219
[ "PUB00020644", "PUB00020645" ]
[ "12325128", "10852900" ]
[ "Family of the green fluorescent protein: journey to the end of the rainbow.", "Natural animal coloration can Be determined by a nonfluorescent green fluorescent protein homolog." ]
[ 2002, 2000 ]
2
[ "IPR011584" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "Viruses" ]
[ 26, 213, 19 ]
3
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Green fluorescent protein, GFP
Green fluorescent protein, GFP
Green_fluorescent_prot
8
IPR000787
787
Peptidase M29
Peptidase_M29
Family
11,204
false
false
This group of metallopeptidases belong to MEROPS peptidase family M29 (aminopeptidase T family, clan M-). The protein fold of the peptidase domain and the active site residues are not known for any members of the thermophilic metallo-aminopeptidases family [ ].
[ "GO:0004177", "GO:0006508" ]
[ "aminopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS" ]
[ "PF02073", "PR00919" ]
[ "Peptidase_M29", "THERMOPTASE" ]
[ 11204, 7351 ]
2
[ "EC", "METACYC", "METACYC", "METACYC" ]
[ "3.4.11.-", "PWY-6423", "PWY-7694", "PWY-7954" ]
[ "EC:3.4.11.-", "METACYC:PWY-6423", "METACYC:PWY-7694", "METACYC:PWY-7954" ]
4
[ "1zjc", "2ayi", "4icq", "4icr", "4ics" ]
5
[ "PUB00063613" ]
[ "10406960" ]
[ "PepS from Streptococcus thermophilus. A new member of the aminopeptidase T family of thermophilic bacteria." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ct3es5", "unclassified sequences" ]
[ 826, 10186, 14, 1, 177 ]
5
[]
[]
0
true
Family
Peptidase M29
Peptidase M29
Peptidase_M29
3
IPR000788
788
Ribonucleotide reductase large subunit, C-terminal
RNR_lg_C
Domain
49,756
false
false
Ribonucleotide reductase (RNR, ) [ , ] catalyses the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs divide into three classes on the basis of their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, bact...
[]
[]
[]
0
[ "PFAM", "PRINTS" ]
[ "PF02867", "PR01183" ]
[ "Ribonuc_red_lgC", "RIBORDTASEM1" ]
[ 49753, 45104 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.17.4.1", "PWY-6545", "PWY-7184", "PWY-7198", "PWY-7210", "PWY-7220", "PWY-7222", "PWY-7226", "PWY-7227", "PDOC00084", "R-CEL-499943", "R-DDI-499943", "R-DME-499943", "R-DRE-499943", "R-HSA-499943", "R-HSA-5213460", "R-HSA-9609690", "R-HSA-9610379", "R-HSA-9686347", "R-MMU-49...
[ "EC:1.17.4.1", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7198", "METACYC:PWY-7210", "METACYC:PWY-7220", "METACYC:PWY-7222", "METACYC:PWY-7226", "METACYC:PWY-7227", "PROSITEDOC:PDOC00084", "REACTOME:R-CEL-499943", "REACTOME:R-DDI-499943", "REACTOME:R-DME-499943", "REACTOME:R-DRE-...
22
[ "1pem", "1peo", "1peq", "1peu", "1r1r", "1rlr", "1xje", "1xjf", "1xjg", "1xjj", "1xjk", "1xjm", "1xjn", "1zyz", "1zzd", "2bq1", "2cvs", "2cvt", "2cvu", "2cvv", "2cvw", "2cvx", "2cvy", "2eud", "2r1r", "2wgh", "2x0x", "2xak", "2xap", "2xav", "2xaw", "2xax"...
144
[ "PUB00000559", "PUB00005164", "PUB00005953", "PUB00005954", "PUB00007088" ]
[ "3286319", "8511586", "9309223", "8052308", "11875520" ]
[ "Structure-function studies of the large subunit of ribonucleotide reductase from Escherichia coli.", "From RNA to DNA, why so many ribonucleotide reductases?", "Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.", "Structure ...
[ 1988, 1993, 1997, 1994, 2002 ]
5
[]
[ "IPR013346" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1001, 36072, 7871, 3580, 1232 ]
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",...
[ 6, 1, 2, 1, 2, 11, 4, 1, 6, 4, 2, 1, 11 ]
13
true
Domain
Ribonucleotide reductase large subunit, C-terminal
Ribonucleotide reductase large subunit, C-terminal
RNR_lg_C
8
IPR000789
789
Cyclin-dependent kinase, regulatory subunit
Cyclin-dep_kinase_reg-sub
Family
6,111
false
false
In eukaryotes, cyclin-dependent protein kinases interact with cyclins to regulate cell cycle progression, and are required for the G1 and G2 stages of cell division [ ]. The proteins bind to a regulatory subunit, cyclin-dependent kinase regulatory subunit (CKS), which is essential for their function. This regulatory su...
[ "GO:0016538" ]
[ "cyclin-dependent protein serine/threonine kinase regulator activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROSITE", "PROSITE", "SMART" ]
[ "PF01111", "PR00296", "PS00944", "PS00945", "SM01084" ]
[ "CKS", "CYCLINKINASE", "CKS_1", "CKS_2", "CKS" ]
[ 6093, 5690, 3383, 3968, 6058 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00728", "R-BTA-187577", "R-BTA-69231", "R-CEL-187577", "R-CEL-69231", "R-DDI-69231", "R-DME-187577", "R-DME-69231", "R-HSA-187577", "R-HSA-69231", "R-MMU-187577", "R-MMU-69231" ]
[ "PROSITEDOC:PDOC00728", "REACTOME:R-BTA-187577", "REACTOME:R-BTA-69231", "REACTOME:R-CEL-187577", "REACTOME:R-CEL-69231", "REACTOME:R-DDI-69231", "REACTOME:R-DME-187577", "REACTOME:R-DME-69231", "REACTOME:R-HSA-187577", "REACTOME:R-HSA-69231", "REACTOME:R-MMU-187577", "REACTOME:R-MMU-69231" ]
12
[ "1buh", "1cks", "1dks", "1dkt", "1puc", "1qb3", "1sce", "2ass", "2ast", "3qy2", "4lpa", "4y72", "4yc3", "4yc6", "5hq0", "5lqf", "6gu2", "6gu3", "6gu4", "6gu6", "6gu7", "7b5l", "7b5m", "7b5r", "7nj0", "8bya", "8byl", "8or0", "8or4" ]
29
[ "PUB00001157", "PUB00001914", "PUB00005179" ]
[ "3322810", "8491379", "8211159" ]
[ "p13suc1 acts in the fission yeast cell division cycle as a component of the p34cdc2 protein kinase.", "The Cdk-associated protein Cks1 functions both in G1 and G2 in Saccharomyces cerevisiae.", "Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control." ]
[ 1987, 1993, 1993 ]
3
[]
[]
0
0
null
[ "Eukaryota", "Limosilactobacillus" ]
[ 6106, 5 ]
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...
[ 4, 2, 3, 3, 5, 7, 1, 1, 8, 1, 1, 11 ]
12
true
Family
Cyclin-dependent kinase, regulatory subunit
Cyclin-dependent kinase, regulatory subunit
Cyclin-dep_kinase_reg-sub
6
IPR000791
791
Acetate transporter GPR1/Ato2/SatP-like
Gpr1/Fun34/SatP-like
Family
13,466
false
false
This family of evolutionary related proteins includes Yarrowia lipolytica (Candida lipolytica) glyxoxylate pathway regulator GPR1 [ , ], Saccharomyces cerevisiae Ady2, Fun34/Ato2 and Ato3 [ ]; fission yeast Mug86 (also known as SpAC5D6.09c); Escherichia coli SatP (YaaH) [ ]; and the Acetate transporter protein patA fro...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF01184" ]
[ "Gpr1_Fun34_YaaH" ]
[ 13466 ]
1
[ "PROSITEDOC" ]
[ "PDOC00890" ]
[ "PROSITEDOC:PDOC00890" ]
1
[ "5ys3", "5ys8", "5zug" ]
3
[ "PUB00019653", "PUB00071881", "PUB00071882", "PUB00071883", "PUB00078051", "PUB00091330", "PUB00150976", "PUB00150978", "PUB00150979", "PUB00150980", "PUB00150981", "PUB00160069" ]
[ "14968426", "18302536", "1349449", "12634328", "23844911", "30100914", "30333234", "17233767", "12429834", "30680886", "19383676", "39062536" ]
[ "Ady2p is essential for the acetate permease activity in the yeast Saccharomyces cerevisiae.", "AcpA, a member of the GPR1/FUN34/YaaH membrane protein family, is essential for acetate permease activity in the hyphal fungus Aspergillus nidulans.", "Characterization of mutants of the yeast Yarrowia lipolytica def...
[ 2004, 2008, 1992, 2003, 2013, 2018, 2018, 2007, 2002, 2019, 2009, 2024 ]
12
[]
[ "IPR047623" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 315, 4676, 8421, 54 ]
4
[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1, 1, 3, 1 ]
4
true
Family
Acetate transporter GPR1/Ato2/SatP-like
Acetate transporter GPR1/Ato2/SatP-like
Gpr1/Fun34/SatP-like
8
IPR000792
792
Transcription regulator LuxR, C-terminal
Tscrpt_reg_LuxR_C
Domain
382,305
false
false
This domain is a DNA-binding, helix-turn-helix (HTH) domain of about 65 amino acids, present in transcription regulators of the LuxR/FixJ family of response regulators. The domain is named after Vibrio fischeri luxR, a transcriptional activator for quorum-sensing control of luminescence. LuxR-type HTH domain proteins o...
[ "GO:0006355" ]
[ "regulation of DNA-templated transcription" ]
[ "biological_process" ]
1
[ "PFAM", "PRINTS", "PROSITE", "PROFILE", "SMART", "CDD" ]
[ "PF00196", "PR00038", "PS00622", "PS50043", "SM00421", "cd06170" ]
[ "GerE", "HTHLUXR", "HTH_LUXR_1", "HTH_LUXR_2", "HTH_LUXR", "LuxR_C_like" ]
[ 358233, 330574, 196016, 344875, 374110, 336814 ]
6
[ "PROSITEDOC" ]
[ "PDOC00542" ]
[ "PROSITEDOC:PDOC00542" ]
1
[ "1a04", "1fse", "1h0m", "1je8", "1l3l", "1p4w", "1rnl", "1x3u", "1yio", "1zg1", "1zg5", "1zlj", "1zlk", "1zn2", "2jpc", "2krf", "2q0o", "2rnj", "3c3w", "3c57", "3clo", "3kln", "3klo", "3p7n", "3qp5", "3qp6", "3szt", "3ulq", "4gvp", "4hye", "4if4", "4ldz"...
89
[ "PUB00016941", "PUB00016942", "PUB00016943", "PUB00016944", "PUB00016945", "PUB00016946", "PUB00016947" ]
[ "11243786", "12352954", "12162958", "15255890", "11931562", "12087407", "12740396" ]
[ "Crystal structure of GerE, the ultimate transcriptional regulator of spore formation in Bacillus subtilis.", "Dimerization allows DNA target site recognition by the NarL response regulator.", "Insights into signal transduction revealed by the low resolution structure of the FixJ response regulator.", "Chemic...
[ 2001, 2002, 2002, 2004, 2002, 2002, 2003 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 164, 378614, 641, 129, 2757 ]
5
[ "Escherichia coli (strain K12)" ]
[ 20 ]
1
true
Domain
Transcription regulator LuxR, C-terminal
Transcription regulator LuxR, C-terminal
Tscrpt_reg_LuxR_C
3
IPR000793
793
ATP synthase, alpha subunit, C-terminal
ATP_synth_asu_C
Domain
48,731
false
false
Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ...
[ "GO:0015986" ]
[ "proton motive force-driven ATP synthesis" ]
[ "biological_process" ]
1
[ "PFAM", "CDD" ]
[ "PF00306", "cd18113" ]
[ "ATP-synt_ab_C", "ATP-synt_F1_alpha_C" ]
[ 48693, 47157 ]
2
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...
[ "7.1.2.2", "PWY-7980", "R-CEL-163210", "R-CEL-8949613", "R-CEL-9837999", "R-DDI-9837999", "R-DME-163210", "R-DME-8949613", "R-DME-9837999", "R-HSA-1268020", "R-HSA-163210", "R-HSA-8949613", "R-HSA-9837999", "R-MMU-163210", "R-MMU-8949613", "R-MMU-9837999", "R-RNO-163210", "R-RNO-89...
[ "EC:7.1.2.2", "METACYC:PWY-7980", "REACTOME:R-CEL-163210", "REACTOME:R-CEL-8949613", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-163210", "REACTOME:R-DME-8949613", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-1268020", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "...
24
[ "1bmf", "1cow", "1e1q", "1e1r", "1e79", "1efr", "1fx0", "1h8e", "1h8h", "1kmh", "1mab", "1nbm", "1ohh", "1qo1", "1sky", "1w0j", "1w0k", "2ck3", "2f43", "2hld", "2jdi", "2jiz", "2jj1", "2jj2", "2qe7", "2r9v", "2v7q", "2w6e", "2w6f", "2w6g", "2w6h", "2w6i"...
349
[ "PUB00004187", "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020609", "PUB00020611", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]
[ "8065448", "11309608", "15473999", "15078220", "15629643", "12745923", "20450191", "18937357", "1385979", "9741106" ]
[ "Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.", "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.", "Mechan...
[ 1994, 2001, 2004, 2004, 2005, 2003, 2010, 2008, 1992, 1998 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 29, 25479, 22749, 474 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 12, 1, 1, 1, 1, 2, 3, 1, 12, 11, 1, 1, 9 ]
13
true
Domain
ATP synthase, alpha subunit, C-terminal
ATP synthase, alpha subunit, C-terminal
ATP_synth_asu_C
3
IPR000795
795
Translational (tr)-type GTP-binding domain
T_Tr_GTP-bd_dom
Domain
385,220
false
false
Translational GTPases (trGTPases) are a family of proteins in which GTPase activity is stimulated by the large ribosomal subunit. This family includes translation initiation, elongation, and release factors and contains four subfamilies that are widespread, if not ubiquitous, in all three superkingdoms [ ]. The trGTPas...
[ "GO:0003924", "GO:0005525" ]
[ "GTPase activity", "GTP binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "PRINTS", "PROFILE" ]
[ "PF00009", "PR00315", "PS51722" ]
[ "GTP_EFTU", "ELONGATNFCT", "G_TR_2" ]
[ 385040, 305404, 363051 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00273", "R-BTA-156827", "R-BTA-156842", "R-BTA-156902", "R-BTA-3371511", "R-BTA-381042", "R-BTA-382556", "R-BTA-5358493", "R-BTA-5419276", "R-BTA-6798695", "R-BTA-72649", "R-BTA-72695", "R-BTA-72702", "R-BTA-72731", "R-BTA-8876725", "R-BTA-9840373", "R-CEL-156902", "R-CEL-3371...
[ "PROSITEDOC:PDOC00273", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-156842", "REACTOME:R-BTA-156902", "REACTOME:R-BTA-3371511", "REACTOME:R-BTA-381042", "REACTOME:R-BTA-382556", "REACTOME:R-BTA-5358493", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-7...
184
[ "1aip", "1b23", "1d2e", "1d8t", "1dar", "1dg1", "1efc", "1efg", "1efm", "1eft", "1efu", "1elo", "1etu", "1exm", "1f60", "1fnm", "1g7c", "1g7r", "1g7s", "1g7t", "1ha3", "1ije", "1ijf", "1jny", "1jqm", "1kjz", "1kk0", "1kk1", "1kk2", "1kk3", "1ktv", "1ls2"...
726
[ "PUB00000682", "PUB00000882", "PUB00001272", "PUB00002632", "PUB00002900", "PUB00004050", "PUB00013952", "PUB00038060", "PUB00074802" ]
[ "3126836", "1394434", "7556078", "1709933", "7737996", "2531290", "11916378", "15616587", "24686316" ]
[ "A conserved amino acid sequence around Arg-68 of Artemia elongation factor 1 alpha is involved in the binding of guanine nucleotides and aminoacyl transfer RNAs.", "The translation machinery and 70 kd heat shock protein cooperate in protein synthesis.", "The products of the SUP45 (eRF1) and SUP35 genes interac...
[ 1987, 1992, 1995, 1991, 1995, 1989, 2002, 2005, 2014 ]
9
[]
[ "IPR035531", "IPR041709", "IPR041732", "IPR041757", "IPR044121", "IPR044128", "IPR047041" ]
0
7
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 4627, 197565, 178965, 126, 3937 ]
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",...
[ 157, 22, 68, 44, 9, 139, 87, 17, 90, 89, 14, 16, 244 ]
13
true
Domain
Translational (tr)-type GTP-binding domain
Translational (tr)-type GTP-binding domain
T_Tr_GTP-bd_dom
4
IPR000796
796
Aspartate/other aminotransferase
Asp_trans
Family
28,012
false
false
Aspartate aminotransferase is important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism. The enzyme catalyses the reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate Aminotransferases...
[ "GO:0008483", "GO:0006520" ]
[ "transaminase activity", "amino acid metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS", "PANTHER" ]
[ "PR00799", "PTHR11879" ]
[ "TRANSAMINASE", "" ]
[ 25956, 27973 ]
2
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.6.1", "2.6.1.1", "PWY-6638", "PWY-6642", "PWY-6643", "PWY-7115", "PWY-7117", "PWY-7383", "R-BTA-389661", "R-BTA-8963693", "R-BTA-8964539", "R-BTA-9856872", "R-CEL-8963693", "R-CEL-9856872", "R-DDI-389661", "R-DDI-8963693", "R-DDI-8964539", "R-DDI-9856872", "R-GGA-352875", "R...
[ "EC:2.6.1", "EC:2.6.1.1", "METACYC:PWY-6638", "METACYC:PWY-6642", "METACYC:PWY-6643", "METACYC:PWY-7115", "METACYC:PWY-7117", "METACYC:PWY-7383", "REACTOME:R-BTA-389661", "REACTOME:R-BTA-8963693", "REACTOME:R-BTA-8964539", "REACTOME:R-BTA-9856872", "REACTOME:R-CEL-8963693", "REACTOME:R-CEL...
50
[ "1aam", "1aat", "1aaw", "1ahe", "1ahf", "1ahg", "1ahx", "1ahy", "1aia", "1aib", "1aic", "1ajr", "1ajs", "1aka", "1akb", "1akc", "1ama", "1amq", "1amr", "1ams", "1arg", "1arh", "1ari", "1ars", "1art", "1asa", "1asb", "1asc", "1asd", "1ase", "1asf", "1asg"...
182
[ "PUB00002679", "PUB00153740", "PUB00153741" ]
[ "1990006", "10074065", "37607357" ]
[ "Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization.", "Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae.", "Biosynthesis of <i>p</i>-Terphenyls in <i>Asperg...
[ 1991, 1999, 2023 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "metagenomes" ]
[ 12614, 15324, 2, 72 ]
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",...
[ 30, 3, 4, 9, 2, 11, 4, 3, 14, 19, 2, 2, 30 ]
13
true
Family
Aspartate/other aminotransferase
Aspartate/other aminotransferase
Asp_trans
8
IPR000797
797
Bunyavirus non-structural protein NS-s
Bunya_NSs
Family
464
false
false
The NSS proteins are encoded in the S RNA from ssRNA negative-strand viruses [ ]. The S RNA also codes for the nucleoprotein N. The two main products are read from overlapping reading frames in the viral complementary sequence.
[ "GO:0016032" ]
[ "viral process" ]
[ "biological_process" ]
1
[ "PFAM", "PIRSF" ]
[ "PF01104", "PIRSF003954" ]
[ "Bunya_NS-S", "NS-S_OrthobunV" ]
[ 464, 406 ]
2
[ "GP" ]
[ "GenProp1007" ]
[ "GP:GenProp1007" ]
1
[]
0
[ "PUB00003165" ]
[ "8760423" ]
[ "The S RNA genomic sequences of Inkoo, San Angelo, Serra do Navio, South River and Tahyna bunyaviruses." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Orthobunyavirus" ]
[ 464 ]
1
[]
[]
0
true
Family
Bunyavirus non-structural protein NS-s
Bunyavirus non-structural protein NS-s
Bunya_NSs
3
IPR000798
798
Ezrin/radixin/moesin-like
Ez/rad/moesin-like
Family
32,941
false
false
This entry represents the ERM family consisting of three closely related proteins, ezrin, radixin, and moesin, that work as cross-linkers between plasma membranes and actin-based cytoskeletons as well as taking part in signal transduction. The ERM family consists of three closely-related proteins, ezrin, radixin and mo...
[ "GO:0008092" ]
[ "cytoskeletal protein binding" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR00661" ]
[ "ERMFAMILY" ]
[ 32941 ]
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-373752", "R-BTA-6794361", "R-DME-2029482", "R-DME-373752", "R-DME-5627123", "R-HSA-2029482", "R-HSA-373752", "R-HSA-399719", "R-HSA-399955", "R-HSA-437239", "R-HSA-5627123", "R-HSA-6794361", "R-HSA-8866427", "R-HSA-8950505", "R-HSA-8980692", "R-HSA-9013148", "R-HSA-9013149", ...
[ "REACTOME:R-BTA-373752", "REACTOME:R-BTA-6794361", "REACTOME:R-DME-2029482", "REACTOME:R-DME-373752", "REACTOME:R-DME-5627123", "REACTOME:R-HSA-2029482", "REACTOME:R-HSA-373752", "REACTOME:R-HSA-399719", "REACTOME:R-HSA-399955", "REACTOME:R-HSA-437239", "REACTOME:R-HSA-5627123", "REACTOME:R-HS...
48
[ "1e5w", "1ef1", "1gc6", "1gc7", "1gg3", "1h4r", "1isn", "1j19", "1ni2", "1sgh", "2d10", "2d11", "2d2q", "2ems", "2emt", "2he7", "2i1j", "2i1k", "2yvc", "2zpy", "3bin", "3qij", "3u8z", "3wa0", "3x23", "4p7i", "4rm8", "4rm9", "4rma", "4yl8", "4zri", "4zrj"...
104
[ "PUB00000467", "PUB00003053", "PUB00003059", "PUB00005477", "PUB00041575", "PUB00095065", "PUB00095066", "PUB00098656", "PUB00098657", "PUB00098658" ]
[ "3046603", "6885906", "2500445", "9048483", "17134719", "27405666", "21167305", "9298994", "9616160", "17061246" ]
[ "A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation.", "Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells.", "A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-c...
[ 1988, 1983, 1989, 1997, 2007, 2016, 2011, 1997, 1998, 2007 ]
10
[]
[ "IPR011174" ]
0
1
0
[ "Eukaryota" ]
[ 32941 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 14, 287, 18, 103, 92, 99 ]
7
true
Family
Ezrin/radixin/moesin-like
Ezrin/radixin/moesin-like
Ez/rad/moesin-like
6
IPR000799
799
Steroidogenic acute regulatory protein-like
StAR-like
Family
3,518
false
false
This entry represents subsets of the steroidogenic acute regulatory (StAR) proteins from animals. Proteins in this family contain a START domain, which binds lipids, including sterols [ ].
[ "GO:0008289" ]
[ "lipid binding" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR00978" ]
[ "STARPROTEIN" ]
[ 3518 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-196108", "R-BTA-9837999", "R-DRE-196108", "R-DRE-9837999", "R-GGA-196108", "R-GGA-9837999", "R-HSA-196108", "R-HSA-9837999", "R-MMU-159418", "R-MMU-196108", "R-MMU-9837999", "R-RNO-196108", "R-RNO-9837999" ]
[ "REACTOME:R-BTA-196108", "REACTOME:R-BTA-9837999", "REACTOME:R-DRE-196108", "REACTOME:R-DRE-9837999", "REACTOME:R-GGA-196108", "REACTOME:R-GGA-9837999", "REACTOME:R-HSA-196108", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-159418", "REACTOME:R-MMU-196108", "REACTOME:R-MMU-9837999", "REACTOME:R-RN...
13
[ "1em2", "5brl", "5i9j", "7ztq", "7ztr", "7ztu", "7zvq", "7zvr", "8aaq" ]
9
[ "PUB00070951" ]
[ "15976441" ]
[ "Give lipids a START: the StAR-related lipid transfer (START) domain in mammals." ]
[ 2005 ]
1
[]
[ "IPR029866" ]
0
1
0
[ "Eukaryota" ]
[ 3518 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 7, 2, 10, 11, 11 ]
6
true
Family
Steroidogenic acute regulatory protein-like
Steroidogenic acute regulatory protein-like
StAR-like
7
IPR000800
800
Notch domain
Notch_dom
Domain
10,867
false
false
The Notch domain is also called the 'DSL' domain or the Lin-12/Notch repeat (LNR). The LNR region is present only in Notch related proteins C-terminal to EGF repeats. The lin-12/Notch proteins act as transmembrane receptors for intercellular signals that specify cell fates during animal development. In response to a li...
[]
[]
[]
0
[ "PFAM", "PRINTS", "PROFILE", "SMART" ]
[ "PF00066", "PR01452", "PS50258", "SM00004" ]
[ "Notch", "LNOTCHREPEAT", "LNR", "NL" ]
[ 9072, 5396, 7403, 10485 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50258", "R-CEL-1912420", "R-CEL-9013700", "R-CEL-9604323", "R-HSA-1912399", "R-HSA-1912408", "R-HSA-1912420", "R-HSA-210744", "R-HSA-2122947", "R-HSA-2122948", "R-HSA-2197563", "R-HSA-2644606", "R-HSA-2644607", "R-HSA-2660826", "R-HSA-2691232", "R-HSA-2894862", "R-HSA-2979096", ...
[ "PROSITEDOC:PDOC50258", "REACTOME:R-CEL-1912420", "REACTOME:R-CEL-9013700", "REACTOME:R-CEL-9604323", "REACTOME:R-HSA-1912399", "REACTOME:R-HSA-1912408", "REACTOME:R-HSA-1912420", "REACTOME:R-HSA-210744", "REACTOME:R-HSA-2122947", "REACTOME:R-HSA-2122948", "REACTOME:R-HSA-2197563", "REACTOME:R...
51
[ "1pb5", "2oo4", "3eto", "3i08", "3l95", "4zlp", "5czv", "5czx", "6xsw", "7abv", "7dxi", "7s05", "7s06", "7ufg", "7y5n", "7y5q", "8a7d", "8a7e", "8d8o", "8hgg", "8hgh", "8sl1", "9bgf" ]
23
[ "PUB00000815", "PUB00000917", "PUB00004172" ]
[ "3119223", "7697721", "8139658" ]
[ "Mutations altering the structure of epidermal growth factor-like coding sequences at the Drosophila Notch locus.", "Jagged: a mammalian ligand that activates Notch1.", "Sequence of C. elegans lag-2 reveals a cell-signalling domain shared with Delta and Serrate of Drosophila." ]
[ 1987, 1995, 1994 ]
3
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati", "metagenomes" ]
[ 10863, 2, 2 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 25, 5, 39, 12, 32 ]
6
true
Domain
Notch domain
Notch domain
Notch_dom
7
IPR000801
801
Esterase-like
Esterase-like
Family
72,147
false
false
This family contains several seemingly unrelated proteins, including human esterase D ; mycobacterial antigen 85 [ ], which is responsible for the high affinity of mycobacteria to fibronectin; Corynebacterium glutamicum major secreted protein PS1; and a number of proteins from Escherichia coli, yeast, mycobacteria and ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00756" ]
[ "Esterase" ]
[ 72147 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1578", "R-BTA-156590", "R-HSA-156590", "R-HSA-9638334", "R-MMU-156590", "R-RNO-156590", "R-SCE-156590", "R-SSC-156590" ]
[ "GP:GenProp1578", "REACTOME:R-BTA-156590", "REACTOME:R-HSA-156590", "REACTOME:R-HSA-9638334", "REACTOME:R-MMU-156590", "REACTOME:R-RNO-156590", "REACTOME:R-SCE-156590", "REACTOME:R-SSC-156590" ]
8
[ "1dqy", "1dqz", "1f0n", "1f0p", "1gkk", "1gkl", "1jjf", "1jt2", "1pv1", "1r88", "1sfr", "1va5", "1wb4", "1wb5", "1wb6", "2b20", "2gzr", "2gzs", "2qm0", "2uz0", "3c6b", "3c87", "3c8d", "3c8h", "3e4d", "3fcx", "3gff", "3hrh", "3i6y", "3ls2", "3mga", "3s8y"...
95
[ "PUB00024304", "PUB00041225", "PUB00097189" ]
[ "10655617", "16922493", "16076215" ]
[ "Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines.", "Structural characterization of enterobactin hydrolase IroE.", "In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes." ]
[ 2000, 2006, 2005 ]
3
[]
[ "IPR014186" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Moumouvirus sp. 'Monve'", "unclassified sequences" ]
[ 153, 65099, 6400, 1, 494 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 4, 1, 1, 3, 4, 5, 8, 1, 5, 8, 1, 11 ]
12
true
Family
Esterase-like
Esterase-like
Esterase-like
2
IPR000802
802
Arsenical pump membrane protein, ArsB
Arsenical_pump_ArsB
Family
16,075
false
false
Arsenic is a toxic metalloid whose trivalent and pentavalent ions inhibit a variety of biochemical processes. Operons that encode arsenic resistance have been found in multicopy plasmids from both Gram-positive and Gram-negative bacteria [ ]. The resistance mechanism is encoded from a single operon, which houses an ani...
[ "GO:0015105", "GO:0015700", "GO:0016020" ]
[ "arsenite transmembrane transporter activity", "arsenite transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PRINTS", "NCBIFAM", "CDD" ]
[ "PF02040", "PR00758", "TIGR00935", "cd01118" ]
[ "ArsB", "ARSENICPUMP", "2a45", "ArsB_permease" ]
[ 6911, 15684, 5118, 6793 ]
4
[ "GP" ]
[ "GenProp0474" ]
[ "GP:GenProp0474" ]
1
[]
0
[ "PUB00002267", "PUB00002587" ]
[ "7721697", "1688427" ]
[ "An Escherichia coli chromosomal ars operon homolog is functional in arsenic detoxification and is conserved in gram-negative bacteria.", "Molecular characterization of an anion pump. The ArsB protein is the membrane anchor for the ArsA protein." ]
[ 1995, 1990 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 377, 15041, 492, 164, 1 ]
5
[ "Escherichia coli (strain K12)", "Zea mays" ]
[ 1, 1 ]
2
true
Family
Arsenical pump membrane protein, ArsB
Arsenical pump membrane protein, ArsB
Arsenical_pump_ArsB
4
IPR000804
804
Clathrin adaptor complex, small chain
Clathrin_sm-chain_CS
Conserved_site
12,873
false
false
Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. This traffic is bidirectional, to ensure that proteins required to form vesicles ar...
[ "GO:0006886", "GO:0016192", "GO:0030117" ]
[ "intracellular protein transport", "vesicle-mediated transport", "membrane coat" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "PROSITE" ]
[ "PS00989" ]
[ "CLAT_ADAPTOR_S" ]
[ 12873 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00760", "R-BTA-177504", "R-BTA-2132295", "R-BTA-416993", "R-BTA-432720", "R-BTA-432722", "R-BTA-437239", "R-BTA-5099900", "R-BTA-5140745", "R-BTA-6807878", "R-BTA-6811434", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-8866427", "R-BTA-8964038", "R-CEL-6807878", "R-CEL-6811434", "R...
[ "PROSITEDOC:PDOC00760", "REACTOME:R-BTA-177504", "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-416993", "REACTOME:R-BTA-432720", "REACTOME:R-BTA-432722", "REACTOME:R-BTA-437239", "REACTOME:R-BTA-5099900", "REACTOME:R-BTA-5140745", "REACTOME:R-BTA-6807878", "REACTOME:R-BTA-6811434", "REACTOME:R-BTA...
71
[ "1w63", "2hf6", "2jkr", "2jkt", "2vgl", "2xa7", "3tjz", "4hmy", "4nee", "4p6z", "4uqi", "5a1u", "5a1v", "5a1w", "5a1x", "5a1y", "5mc7", "5nzr", "5nzs", "5nzt", "5nzu", "5nzv", "6cm9", "6cri", "6d83", "6d84", "6dff", "6owo", "6owt", "6oxl", "6qh5", "6qh6"...
68
[ "PUB00000652", "PUB00001249", "PUB00003074", "PUB00029720", "PUB00030524", "PUB00035753", "PUB00035768", "PUB00035769", "PUB00035771", "PUB00035772" ]
[ "8373805", "8157009", "8276893", "12858162", "14690497", "17449236", "17041781", "15261670", "9002613", "14729954" ]
[ "Cloning of the YAP19 gene encoding a putative yeast homolog of AP19, the mammalian small chain of the clathrin-assembly proteins.", "The Saccharomyces cerevisiae APS1 gene encodes a homolog of the small subunit of the mammalian clathrin AP-1 complex: evidence for functional interaction with clathrin at the Golgi...
[ 1993, 1994, 1993, 2003, 2004, 2007, 2006, 2004, 1996, 2004 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 2, 20, 12849, 2 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea ma...
[ 13, 4, 23, 8, 45, 22, 10, 38, 3, 2, 35 ]
11
true
Conserved_site
Clathrin adaptor complex, small chain
Clathrin adaptor complex, small chain
Clathrin_sm-chain_CS
9
IPR000805
805
Glycoside hydrolase family 26
Glyco_hydro_26
Family
8,123
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0016985", "GO:0006080" ]
[ "mannan endo-1,4-beta-mannosidase activity", "substituted mannan metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS", "PANTHER" ]
[ "PR00739", "PTHR40079" ]
[ "GLHYDRLASE26", "" ]
[ 3992, 8054 ]
2
[ "CAZY", "EC", "METACYC" ]
[ "GH26", "3.2.1.78", "PWY-7456" ]
[ "CAZY:GH26", "EC:3.2.1.78", "METACYC:PWY-7456" ]
3
[ "1gvy", "1gw1", "1j9y", "1odz", "1r7o", "2bv9", "2bvd", "2bvt", "2bvy", "2cip", "2cit", "2ddx", "2qha", "2v3g", "2vi0", "2vx4", "2vx5", "2vx6", "2vx7", "2whk", "2whm", "2x2y", "3cbw", "3tp4", "3vpl", "3wdq", "3wdr", "3zm8", "4cd4", "4cd5", "4yn5", "4zxo"...
44
[ "PUB00000537", "PUB00004870", "PUB00005266" ]
[ "7848261", "7624375", "8535779" ]
[ "A non-modular endo-beta-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa.", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases." ]
[ 1995, 1995, 1995 ]
3
[]
[ "IPR016714" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 76, 6695, 1287, 1, 64 ]
5
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Family
Glycoside hydrolase family 26
Glycoside hydrolase family 26
Glyco_hydro_26
4
IPR000806
806
Rab GDI protein
RabGDI
Family
7,650
false
false
null
[ "GO:0005093", "GO:0015031" ]
[ "Rab GDP-dissociation inhibitor activity", "protein transport" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00892" ]
[ "RABGDI" ]
[ 7650 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-8876198", "R-CEL-6803205", "R-CEL-8873719", "R-CEL-8876198", "R-HSA-6798695", "R-HSA-8876198", "R-MMU-6798695", "R-MMU-8876198", "R-RNO-6798695", "R-RNO-8876198", "R-SCE-6798695", "R-SCE-8876198", "R-SPO-6798695", "R-SPO-8876198" ]
[ "REACTOME:R-BTA-8876198", "REACTOME:R-CEL-6803205", "REACTOME:R-CEL-8873719", "REACTOME:R-CEL-8876198", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-8876198", "REACTOME:R-MMU-6798695", "REACTOME:R-MMU-8876198", "REACTOME:R-RNO-6798695", "REACTOME:R-RNO-8876198", "REACTOME:R-SCE-6798695", "REACTOM...
14
[ "1d5t", "1gnd", "1lv0", "1ukv", "2bcg", "3cph", "3cpi", "3cpj", "3p1w", "6c87" ]
10
[ "PUB00000785", "PUB00004235" ]
[ "7585614", "8609986" ]
[ "Cloning of a brain-type isoform of human Rab GDI and its expression in human neuroblastoma cell lines and tumor specimens.", "Structure and mutational analysis of Rab GDP-dissociation inhibitor." ]
[ 1995, 1996 ]
2
[ "IPR018203" ]
[]
1
0
1
[ "Eukaryota", "marine sediment metagenome" ]
[ 7649, 1 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 10, 4, 3, 2, 15, 10, 1, 9, 9, 1, 1, 56 ]
12
true
Family
Rab GDI protein
Rab GDI protein
RabGDI
6