interpro_id string | interpro_numeric_id int64 | name string | short_name string | entry_type string | protein_count int64 | is_llm bool | is_llm_reviewed bool | abstract string | go_ids list | go_terms list | go_categories list | go_count int64 | member_databases list | member_accessions list | member_names list | member_protein_counts list | member_count int64 | external_databases list | external_accessions list | external_xrefs list | external_xref_count int64 | pdb_ids list | structure_count int64 | publication_ids list | pubmed_ids list | publication_titles list | publication_years list | publication_count int64 | parent_ids list | child_ids list | parent_count int64 | child_count int64 | tree_depth float64 | taxonomy_names list | taxonomy_protein_counts list | taxonomy_count int64 | key_species_names list | key_species_protein_counts list | key_species_count int64 | in_entry_list bool | entry_list_type string | entry_list_name string | names_dat_name string | short_names_dat_name string | split_bucket int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR013711 | 13,711 | Runx, C-terminal domain | RunxI_C_dom | Domain | 3,729 | false | false | This domain lies to the C terminus of Runx-related transcription factors and homologous proteins (AML, CBF-alpha, PEBP2). Its function might be to interact with functional cofactors [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08504"
] | [
"RunxI"
] | [
3729
] | 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-HSA-1912408",
"R-HSA-2032785",
"R-HSA-4411364",
"R-HSA-549127",
"R-HSA-8877330",
"R-HSA-8878166",
"R-HSA-8931987",
"R-HSA-8934593",
"R-HSA-8935964",
"R-HSA-8936459",
"R-HSA-8939236",
"R-HSA-8939242",
"R-HSA-8939243",
"R-HSA-8939245",
"R-HSA-8939246",
"R-HSA-8939247",
"R-HSA-893925... | [
"REACTOME:R-HSA-1912408",
"REACTOME:R-HSA-2032785",
"REACTOME:R-HSA-4411364",
"REACTOME:R-HSA-549127",
"REACTOME:R-HSA-8877330",
"REACTOME:R-HSA-8878166",
"REACTOME:R-HSA-8931987",
"REACTOME:R-HSA-8934593",
"REACTOME:R-HSA-8935964",
"REACTOME:R-HSA-8936459",
"REACTOME:R-HSA-8939236",
"REACTOME... | 67 | [] | 0 | [
"PUB00020842"
] | [
"15713794"
] | [
"Shared and distinct roles mediated through C-terminal subdomains of acute myeloid leukemia/Runt-related transcription factor molecules in murine development."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
3729
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
58,
7,
13,
17
] | 4 | true | Domain | Runx, C-terminal domain | Runx, C-terminal domain | RunxI_C_dom | 4 |
IPR013712 | 13,712 | Mitochondrial Myo2 receptor-related protein 1 | MMR1 | Family | 56 | false | false | Myo2p, a class V myosin, is essential for mitochondrial distribution, class V being vital for organelle distribution in S. cerevisiae. The established mechanism for distribution of cellular components by class V myosins is that they interact with the cargo at the C-terminal tail domain and transport it along the actin ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08505"
] | [
"MMR1"
] | [
56
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00057250"
] | [
"15201867"
] | [
"Mmr1p is a mitochondrial factor for Myo2p-dependent inheritance of mitochondria in the budding yeast."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Saccharomycetaceae"
] | [
56
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Mitochondrial Myo2 receptor-related protein 1 | Mitochondrial Myo2 receptor-related protein 1 | MMR1 | 9 |
IPR013713 | 13,713 | Exportin-2, central domain | XPO2_central | Domain | 10,642 | false | false | Exportin-2, also known as CAS, is an export receptor for importin-alpha [ ]. It binds strongly to importin alpha only in the presence of RanGTP, forming an importin alpha/CAS/RanGTP complex. Exportin-2 mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates have been released into th... | [
"GO:0006886"
] | [
"intracellular protein transport"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF08506"
] | [
"Cse1"
] | [
10642
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5578749",
"R-MMU-5578749",
"R-SPO-5578749"
] | [
"REACTOME:R-HSA-5578749",
"REACTOME:R-MMU-5578749",
"REACTOME:R-SPO-5578749"
] | 3 | [
"1wa5",
"1z3h",
"6n88"
] | 3 | [
"PUB00007252",
"PUB00090423"
] | [
"9323134",
"10394916"
] | [
"Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor.",
"Genetic evidence for interactions between yeast importin alpha (Srp1p) and its nuclear export receptor, Cse1p."
] | [
1997,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Solibaculum mannosilyticum"
] | [
10641,
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... | [
9,
1,
7,
5,
9,
5,
2,
9,
11,
2,
2,
40
] | 12 | true | Domain | Exportin-2, central domain | Exportin-2, central domain | XPO2_central | 9 |
IPR013714 | 13,714 | Golgi apparatus membrane protein TVP15 | Golgi_TVP15 | Family | 2,776 | false | false | Proteins in this family co-localise with COPI vesicle coat proteins [ ]. In yeast it is a Golgi membrane protein involved in vesicular trafficking, interacting with Tvp18 and Tvp23 [ , ]. | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF08507",
"PTHR28128"
] | [
"COPI_assoc",
""
] | [
2731,
1851
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016470",
"PUB00053674",
"PUB00056871"
] | [
"14562095",
"16847258",
"17178117"
] | [
"Global analysis of protein localization in budding yeast.",
"A global topology map of the Saccharomyces cerevisiae membrane proteome.",
"Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the Tlg2-containing Golgi/endosome compartments of Saccharomyces cerevisiae."
] | [
2003,
2006,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2776
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Family | Golgi apparatus membrane protein TVP15 | Golgi apparatus membrane protein TVP15 | Golgi_TVP15 | 1 |
IPR013715 | 13,715 | Domain of unknown function DUF1746 | DUF1746 | Domain | 1,526 | false | false | This is a fungal domain of unknown function. This domain can be found in DSC E3 ubiquitin ligase complex subunit 4 (Dsc4) from S. pombe. It is a component of the DSC E3 ubiquitin ligase complex required for the sre1 transcriptional activator proteolytic cleavage to release the soluble transcription factor from the memb... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08508"
] | [
"DUF1746"
] | [
1526
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00075404",
"PUB00098082"
] | [
"21504829",
"29355480"
] | [
"Yeast SREBP cleavage activation requires the Golgi Dsc E3 ligase complex.",
"Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system."
] | [
2011,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1526
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Domain | Domain of unknown function DUF1746 | Domain of unknown function DUF1746 | DUF1746 | 5 |
IPR013716 | 13,716 | Adenylate cyclase G-alpha binding | Adenylate_cyclase_G-a-bd | Domain | 1,060 | false | false | Adenylate cyclase catalyses the conversion of ATP to 3',5'-cyclic AMP (cAMP) and pyrophosphate. It plays an essential role in the regulation of cellular metabolism by catalysing the synthesis of a second messenger, cAMP. G protein-mediated signalling is implicated in yeast and fungal cAMP pathways. The cAMP-PKA pathway... | [
"GO:0000287",
"GO:0004016",
"GO:0006171"
] | [
"magnesium ion binding",
"adenylate cyclase activity",
"cAMP biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF08509",
"SM00789"
] | [
"Ad_cyc_g-alpha",
"Ad_cyc_g-alpha"
] | [
1018,
757
] | 2 | [
"EC",
"REACTOME"
] | [
"4.6.1.1",
"R-SCE-9696270"
] | [
"EC:4.6.1.1",
"REACTOME:R-SCE-9696270"
] | 2 | [] | 0 | [
"PUB00020890",
"PUB00043455"
] | [
"15831585",
"16924114"
] | [
"Direct activation of fission yeast adenylate cyclase by the Gpa2 Galpha of the glucose signaling pathway.",
"Kelch-repeat proteins interacting with the Galpha protein Gpa2 bypass adenylate cyclase for direct regulation of protein kinase A in yeast."
] | [
2005,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1060
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
1,
1
] | 3 | true | Domain | Adenylate cyclase G-alpha binding | Adenylate cyclase G-alpha binding | Adenylate_cyclase_G-a-bd | 9 |
IPR013717 | 13,717 | PIG-P | PIG-P | Domain | 4,206 | false | false | PIG-P (phosphatidylinositol N-acetylglucosaminyltransferase subunit P) is an enzyme involved in GPI anchor biosynthesis [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08510"
] | [
"PIG-P"
] | [
4206
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-162710",
"R-MMU-162710"
] | [
"REACTOME:R-HSA-162710",
"REACTOME:R-MMU-162710"
] | 2 | [] | 0 | [
"PUB00020925"
] | [
"10944123"
] | [
"Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4206
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
10,
1,
1,
1,
2,
5,
1,
7,
6,
1,
1,
9
] | 12 | true | Domain | PIG-P | PIG-P | PIG-P | 7 |
IPR013718 | 13,718 | COQ9, C-terminal domain | COQ9_C | Domain | 6,012 | false | false | This entry represents the C-terminal region of the globular domain of COQ9 and similar sequences from bacteria and eukaryotes. This domain shows structural homology with the small molecule binding domain members of the TFR family of bacterial transcriptional regulators, adopting an α-helical configuration. It appears s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08511"
] | [
"COQ9"
] | [
6012
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-2142789",
"R-DME-2142789",
"R-HSA-2142789",
"R-MMU-2142789",
"R-RNO-2142789",
"R-SCE-2142789",
"R-SPO-2142789",
"R-XTR-2142789"
] | [
"REACTOME:R-BTA-2142789",
"REACTOME:R-DME-2142789",
"REACTOME:R-HSA-2142789",
"REACTOME:R-MMU-2142789",
"REACTOME:R-RNO-2142789",
"REACTOME:R-SCE-2142789",
"REACTOME:R-SPO-2142789",
"REACTOME:R-XTR-2142789"
] | 8 | [
"3ni7",
"4rhp",
"6awl",
"6dew",
"7ssp",
"7sss"
] | 6 | [
"PUB00020857",
"PUB00103868",
"PUB00103869"
] | [
"16027161",
"25339443",
"30661980"
] | [
"COQ9, a new gene required for the biosynthesis of coenzyme Q in Saccharomyces cerevisiae.",
"Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to enable coenzyme Q biosynthesis.",
"An Isoprene Lipid-Binding Protein Promotes Eukaryotic Coenzyme Q Biosynthesis."
] | [
2005,
2014,
2019
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
1900,
4091,
21
] | 3 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
5,
1,
2,
5,
3,
1,
3,
4,
1,
1,
5
] | 11 | true | Domain | COQ9, C-terminal domain | COQ9, C-terminal domain | COQ9_C | 9 |
IPR013719 | 13,719 | Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain | RTT106/SPT16-like_middle_dom | Domain | 11,919 | false | false | This entry represents a domain found in the middle region of several eukaryotic proteins [ , ]. It is present in various FACT (facilitates chromatin transactions) complex subunits, such as Spt16 and either Pob3 (yeast) or the related SSRP1 (higher eukaryotes). FACT is a general chromatin factor that acts to reorganise ... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08512",
"SM01287"
] | [
"Rttp106-like_middle",
"Rtt106"
] | [
11885,
11768
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-112382",
"R-CEL-674695",
"R-CEL-6796648",
"R-CEL-6804756",
"R-CEL-75955",
"R-DDI-674695",
"R-DDI-6796648",
"R-DDI-6804756",
"R-DME-112382",
"R-DME-674695",
"R-DME-6796648",
"R-DME-6804756",
"R-DME-75955",
"R-HSA-112382",
"R-HSA-167152",
"R-HSA-167200",
"R-HSA-167238",
"R-HSA... | [
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-6804756",
"REACTOME:R-CEL-75955",
"REACTOME:R-DDI-674695",
"REACTOME:R-DDI-6796648",
"REACTOME:R-DDI-6804756",
"REACTOME:R-DME-112382",
"REACTOME:R-DME-674695",
"REACTOME:R-DME-6796648",
"REACTOME:R-DME... | 41 | [
"2gcj",
"2gcl",
"3fss",
"3gyo",
"3gyp",
"3to1",
"3tvv",
"3tw1",
"4ifs",
"4ioy",
"4kha",
"4kho",
"4pq0",
"4z2m",
"4z2n",
"5ums",
"5umu",
"6l1e",
"6thl",
"6upk",
"6upl",
"7nky",
"7xsx",
"7xt7",
"7xtd",
"7xti",
"8xgc",
"8yjf",
"8yjm",
"9eh2",
"9gw2",
"9rzc"... | 34 | [
"PUB00033392",
"PUB00070237",
"PUB00070238",
"PUB00101031",
"PUB00101032",
"PUB00101033",
"PUB00101034",
"PUB00101035"
] | [
"16157874",
"12815073",
"10413469",
"21454601",
"31775157",
"23417676",
"33846633",
"26687053"
] | [
"Rtt106p is a histone chaperone involved in heterochromatin-mediated silencing.",
"Drosophila FACT contributes to Hox gene expression through physical and functional interactions with GAGA factor.",
"Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-as... | [
2005,
2003,
1999,
2011,
2020,
2013,
2021,
2015
] | 8 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Shewanella",
"bird metagenome"
] | [
11909,
9,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
15,
3,
5,
23,
2,
5,
3,
7,
6,
3,
3,
14
] | 12 | true | Domain | Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain | Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain | RTT106/SPT16-like_middle_dom | 6 |
IPR013721 | 13,721 | STAG | STAG | Domain | 8,699 | false | false | STAG domain proteins are subunits of cohesin complex - a protein complex required for sister chromatid cohesion in eukaryotes. The STAG domain is present in Schizosaccharomyces pombe (Fission yeast) mitotic cohesin Psc3, and the meiosis specific cohesin Rec11. Many organisms express a meiosis-specific STAG protein, for... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08514"
] | [
"STAG"
] | [
8699
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-2468052",
"R-CEL-2470946",
"R-CEL-2500257",
"R-CEL-3108214",
"R-HSA-1221632",
"R-HSA-2467813",
"R-HSA-2468052",
"R-HSA-2470946",
"R-HSA-2500257",
"R-HSA-3108214",
"R-HSA-9018519",
"R-MMU-2467813",
"R-MMU-2468052",
"R-MMU-2470946",
"R-MMU-2500257",
"R-MMU-3108214",
"R-SCE-24680... | [
"REACTOME:R-CEL-2468052",
"REACTOME:R-CEL-2470946",
"REACTOME:R-CEL-2500257",
"REACTOME:R-CEL-3108214",
"REACTOME:R-HSA-1221632",
"REACTOME:R-HSA-2467813",
"REACTOME:R-HSA-2468052",
"REACTOME:R-HSA-2470946",
"REACTOME:R-HSA-2500257",
"REACTOME:R-HSA-3108214",
"REACTOME:R-HSA-9018519",
"REACTOM... | 22 | [
"4pju",
"4pjw",
"4pk7",
"4uvk",
"5qst",
"5qsu",
"5qsv",
"5qsw",
"5qsx",
"6h8q",
"6qb5",
"6qnx",
"6rrc",
"6wg3",
"7w1m",
"7zjs",
"8k4d",
"9ep3",
"9hms",
"9hmv",
"9j0a"
] | 21 | [
"PUB00020823"
] | [
"16043696"
] | [
"Cohesins are required for meiotic DNA breakage and recombination in Schizosaccharomyces pombe."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
8699
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
2,
1,
20,
4,
20,
12,
1,
5,
14,
1,
2,
6
] | 12 | true | Domain | STAG | STAG | STAG | 2 |
IPR013724 | 13,724 | GIT, Spa2 homology (SHD) domain | GIT_SHD | Domain | 7,613 | false | false | This entry represents the Spa2 homology domain (SHD) domain found in the yeast Spa2/Sph1 protein and the mammalian GIT proteins. | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08518",
"SM00555"
] | [
"GIT_SHD",
"GIT"
] | [
7565,
7555
] | 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-DME-3928664",
"R-DME-9013149",
"R-DME-9013404",
"R-DME-9013406",
"R-DME-9013420",
"R-DME-9013423",
"R-DME-9013424",
"R-HSA-3928664",
"R-HSA-9013148",
"R-HSA-9013149",
"R-HSA-9013404",
"R-HSA-9013406",
"R-HSA-9013409",
"R-HSA-9013420",
"R-HSA-9013423",
"R-HSA-9013424",
"R-HSA-96192... | [
"REACTOME:R-DME-3928664",
"REACTOME:R-DME-9013149",
"REACTOME:R-DME-9013404",
"REACTOME:R-DME-9013406",
"REACTOME:R-DME-9013420",
"REACTOME:R-DME-9013423",
"REACTOME:R-DME-9013424",
"REACTOME:R-HSA-3928664",
"REACTOME:R-HSA-9013148",
"REACTOME:R-HSA-9013149",
"REACTOME:R-HSA-9013404",
"REACTOM... | 30 | [
"6jmt",
"6lag"
] | 2 | [
"PUB00020886",
"PUB00075461",
"PUB00075462",
"PUB00075463"
] | [
"12473661",
"12361575",
"9443897",
"11896197"
] | [
"The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo.",
"Spa2p functions as a scaffold-like protein to recruit the Mpk1p MAP kinase module to sites of polarized growth.",
"The Spa2-related protein, Sph1p, is important for polarized growth in yeast.",
"GIT1... | [
2003,
2002,
1998,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
3,
7610
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
1,
14,
1,
15,
11,
1,
13,
2,
1
] | 9 | true | Domain | GIT, Spa2 homology (SHD) domain | GIT, Spa2 homology (SHD) domain | GIT_SHD | 3 |
IPR013725 | 13,725 | DNA replication factor RFC1, C-terminal | DNA_replication_fac_RFC1_C | Domain | 5,380 | false | false | This is the C-terminal domain of replication factor C, RFC1. RFC complexes hydrolyse ATP and load sliding clamps such as PCNA (proliferating cell nuclear antigen) onto double-stranded DNA. RFC1 is essential for RFC function in vivo [ , ]. | [
"GO:0003689",
"GO:0005524",
"GO:0006260",
"GO:0005663"
] | [
"DNA clamp loader activity",
"ATP binding",
"DNA replication",
"DNA replication factor C complex"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF08519"
] | [
"RFC1"
] | [
5380
] | 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-DDI-110314",
"R-DDI-5651801",
"R-DDI-5655862",
"R-DDI-5656169",
"R-DDI-5696397",
"R-DDI-6782135",
"R-DDI-6782210",
"R-DDI-69091",
"R-DME-110312",
"R-DME-110314",
"R-DME-110320",
"R-DME-5651801",
"R-DME-5655862",
"R-DME-5656121",
"R-DME-5656169",
"R-DME-5696397",
"R-DME-5696400",
... | [
"REACTOME:R-DDI-110314",
"REACTOME:R-DDI-5651801",
"REACTOME:R-DDI-5655862",
"REACTOME:R-DDI-5656169",
"REACTOME:R-DDI-5696397",
"REACTOME:R-DDI-6782135",
"REACTOME:R-DDI-6782210",
"REACTOME:R-DDI-69091",
"REACTOME:R-DME-110312",
"REACTOME:R-DME-110314",
"REACTOME:R-DME-110320",
"REACTOME:R-DM... | 69 | [
"1sxj",
"6vvo",
"7tfh",
"7tfi",
"7tfj",
"7tfk",
"7tfl",
"7thj",
"7thv",
"7ti8",
"7tib",
"7tic",
"7tid",
"7tku",
"7u19",
"7u1a",
"7u1p",
"8dqx",
"8dqz",
"8dr0",
"8dr1",
"8dr3",
"8dr4",
"8dr5",
"8dr6",
"8dr7",
"9peo",
"9per",
"9pes",
"9pet",
"9peu",
"9pev"... | 32 | [
"PUB00020875",
"PUB00020937"
] | [
"9092549",
"16040599"
] | [
"Deletion analysis of the large subunit p140 in human replication factor C reveals regions required for complex formation and replication activities.",
"Contrasting effects of Elg1-RFC and Ctf18-RFC inactivation in the absence of fully functional RFC in fission yeast."
] | [
1997,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
15,
5290,
50,
25
] | 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... | [
6,
1,
2,
1,
2,
8,
1,
4,
5,
1,
1,
16
] | 12 | true | Domain | DNA replication factor RFC1, C-terminal | DNA replication factor RFC1, C-terminal | DNA_replication_fac_RFC1_C | 3 |
IPR013726 | 13,726 | Mitofissin | Mitofissin | Family | 1,970 | false | false | This is a family of fungal proteins identified as mitochondrial fission factors (mitofissin, also referred to as Atg44) which are essential for mitophagy. Mitofissin directly binds to lipid membranes to drive mitochondrial fission required for mitophagy [ ]. This intermembrane space protein is essential for the complet... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF08520",
"PTHR28075"
] | [
"Mitofissin",
""
] | [
1969,
1875
] | 2 | [] | [] | [] | 0 | [
"7ydo"
] | 1 | [
"PUB00151415",
"PUB00152781"
] | [
"37192628",
"37540145"
] | [
"The mitochondrial intermembrane space protein mitofissin drives mitochondrial fission required for mitophagy.",
"Completion of mitochondrial division requires the intermembrane space protein Mdi1/Atg44."
] | [
2023,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1970
] | 1 | [
"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)"
] | [
4,
2,
1
] | 3 | true | Family | Mitofissin | Mitofissin | Mitofissin | 7 |
IPR013727 | 13,727 | Two-component sensor kinase, N-terminal | 2CSK_N | Domain | 13,596 | false | false | This domain is found in bacterial two-component sensor kinases towards the N terminus. Proteins containing this domain includes sensor protein QseC, which is a member of a two-component regulatory system QseB/QseC [ ]. It recognises Autotinducer 3 (AI-3), epinephrine, norepinephrine and Fe(III) (Matilla et. al., FEMS M... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08521"
] | [
"2CSK_N"
] | [
13596
] | 1 | [
"EC"
] | [
"2.7.13.3"
] | [
"EC:2.7.13.3"
] | 1 | [
"2kse"
] | 1 | [
"PUB00075428"
] | [
"11929534"
] | [
"Quorum sensing Escherichia coli regulators B and C (QseBC): a novel two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
13493,
7,
96
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Two-component sensor kinase, N-terminal | Two-component sensor kinase, N-terminal | 2CSK_N | 8 |
IPR013728 | 13,728 | BT_3987-like, N-terminal domain | BT_3987-like_N | Domain | 3,760 | false | false | This domain, previously known as DUF1735, is found in a number of proteins mainly found in firmicutes, including BT_3987 ( ) and BT_3044 ( ) from Bacteroides thetaiotaomicron. BT_3987 displays hydrolytic activity against Hy-type N-glycans, probably initiating the degradation of this type of glycan in the human gut [ ].... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08522"
] | [
"BT_3987-like_N"
] | [
3760
] | 1 | [] | [] | [] | 0 | [
"3n91",
"3poh",
"4dqa",
"4jx0",
"6t8i",
"6t8k",
"6t8l",
"6tcv",
"6tcw",
"7nwf",
"8w01",
"8w04"
] | 12 | [
"PUB00152802",
"PUB00152803"
] | [
"34420703",
"34324829"
] | [
"Discrete genetic loci in human gut Bacteroides thetaiotaomicron confer pectin metabolism.",
"GH18 endo-β-N-acetylglucosaminidases use distinct mechanisms to process hybrid-type N-linked glycans."
] | [
2021,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Russula earlei",
"unclassified sequences"
] | [
3706,
2,
52
] | 3 | [] | [] | 0 | true | Domain | BT_3987-like, N-terminal domain | BT_3987-like, N-terminal domain | BT_3987-like_N | 8 |
IPR013730 | 13,730 | Fyv7/TAP26 | Fyv7/TAP26 | Family | 2,701 | false | false | This entry include proteins from the FYV7 and the TAP26 families [ ]. | [] | [] | [] | 0 | [
"PFAM",
"PRINTS"
] | [
"PF08524",
"PR01854"
] | [
"rRNA_processing",
"BR22PROTEIN"
] | [
2588,
1158
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5683826",
"R-HSA-5683826",
"R-MMU-5683826"
] | [
"REACTOME:R-BTA-5683826",
"REACTOME:R-HSA-5683826",
"REACTOME:R-MMU-5683826"
] | 3 | [] | 0 | [
"PUB00014725",
"PUB00042733",
"PUB00053444",
"PUB00053445"
] | [
"12837249",
"12242301",
"12882447",
"16630564"
] | [
"A panoramic view of yeast noncoding RNA processing.",
"Components of an interdependent unit within the SSU processome regulate and mediate its activity.",
"BR22, a 26 kDa thyroid transcription factor-1 associated protein (TAP26), is expressed in human lung cells.",
"The TTF-1/TAP26 complex differentially mod... | [
2003,
2002,
2003,
2006
] | 4 | [] | [
"IPR017265"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
2701
] | 1 | [
"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... | [
4,
1,
1,
2,
2,
1,
2,
2,
1,
1,
7
] | 11 | true | Family | Fyv7/TAP26 | Fyv7/TAP26 | Fyv7/TAP26 | 5 |
IPR013731 | 13,731 | Opacity-associated protein A-like, N-terminal | OapA_N | Domain | 3,161 | false | false | This domain is found in the Haemophilus influenzae opacity-associated protein (OapA) and related proteins. It is required for efficient nasopharyngeal mucosal colonisation, and its expression is associated with a distinctive transparent colony phenotype. OapA is thought to be a secreted protein, and its expression exhi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08525"
] | [
"OapA_N"
] | [
3161
] | 1 | [
"EC",
"METACYC"
] | [
"3.4.24.-",
"PWY-8119"
] | [
"EC:3.4.24.-",
"METACYC:PWY-8119"
] | 2 | [] | 0 | [
"PUB00009909",
"PUB00020973"
] | [
"8830271",
"8559074"
] | [
"Phenotypic switching of Haemophilus influenzae.",
"Identification and characterization of a cell envelope protein of Haemophilus influenzae contributing to phase variation in colony opacity and nasopharyngeal colonization."
] | [
1996,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"human gut metagenome"
] | [
3156,
4,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Opacity-associated protein A-like, N-terminal | Opacity-associated protein A-like, N-terminal | OapA_N | 2 |
IPR013732 | 13,732 | Protein-arginine deiminase (PAD), N-terminal | PAD_N | Domain | 2,690 | false | false | This entry represents the first immunoglobulin-like non-catalytic domain of protein-arginine deiminase. Protein arginine deiminases (PADs) use a nucleophilic cysteine to hydrolyze guanidinium groups on arginine residues to form citrulline. This reaction, known as citrullination or deimination, results in the loss of po... | [
"GO:0005509",
"GO:0005737"
] | [
"calcium ion binding",
"cytoplasm"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF08526"
] | [
"PAD_N"
] | [
2690
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.5.3.15",
"PWY-4921",
"R-HSA-3247509",
"R-HSA-6798695",
"R-MMU-3247509",
"R-MMU-6798695",
"R-RNO-3247509",
"R-RNO-6798695"
] | [
"EC:3.5.3.15",
"METACYC:PWY-4921",
"REACTOME:R-HSA-3247509",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-3247509",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-3247509",
"REACTOME:R-RNO-6798695"
] | 8 | [
"1wd8",
"1wd9",
"1wda",
"2dew",
"2dex",
"2dey",
"2dw5",
"3apm",
"3apn",
"3b1t",
"3b1u",
"4dkt",
"4n20",
"4n22",
"4n24",
"4n25",
"4n26",
"4n28",
"4n2a",
"4n2b",
"4n2c",
"4n2d",
"4n2e",
"4n2f",
"4n2g",
"4n2h",
"4n2i",
"4n2k",
"4n2l",
"4n2m",
"4n2n",
"4x8c"... | 62 | [
"PUB00088282",
"PUB00158973"
] | [
"25621824",
"39286527"
] | [
"Protein arginine deiminase 2 binds calcium in an ordered fashion: implications for inhibitor design.",
"Structural insight into the function of human peptidyl arginine deiminase 6."
] | [
2015,
2024
] | 2 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
2690
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
16,
10,
17
] | 4 | true | Domain | Protein-arginine deiminase (PAD), N-terminal | Protein-arginine deiminase (PAD), N-terminal | PAD_N | 8 |
IPR013733 | 13,733 | Protein-arginine deiminase (PAD), central domain | Prot_Arg_deaminase_cen_dom | Domain | 2,974 | false | false | Peptidylarginine deiminase (PAD) enzymes catalyse the conversion of protein-bound arginine to citrulline. There are five types of PADs known in humans, PAD1-PAD4 and PAD6 [ ]. PAD6 does not bind Ca2+ and is inactive in vitro assays against standard PADs substrate [ ]. This entry represents the central non-catalytic dom... | [
"GO:0005509",
"GO:0005737"
] | [
"calcium ion binding",
"cytoplasm"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF08527"
] | [
"PAD_M"
] | [
2974
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.5.3.15",
"PWY-4921",
"R-HSA-3247509",
"R-HSA-6798695",
"R-MMU-3247509",
"R-MMU-6798695",
"R-RNO-3247509",
"R-RNO-6798695"
] | [
"EC:3.5.3.15",
"METACYC:PWY-4921",
"REACTOME:R-HSA-3247509",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-3247509",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-3247509",
"REACTOME:R-RNO-6798695"
] | 8 | [
"1wd8",
"1wd9",
"1wda",
"2dew",
"2dex",
"2dey",
"2dw5",
"3apm",
"3apn",
"3b1t",
"3b1u",
"4dkt",
"4n20",
"4n22",
"4n24",
"4n25",
"4n26",
"4n28",
"4n2a",
"4n2b",
"4n2c",
"4n2d",
"4n2e",
"4n2f",
"4n2g",
"4n2h",
"4n2i",
"4n2k",
"4n2l",
"4n2m",
"4n2n",
"4x8c"... | 62 | [
"PUB00014094",
"PUB00047245",
"PUB00158973"
] | [
"14579251",
"16567635",
"39286527"
] | [
"PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease.",
"Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4.",
"Structural insight into the function of human peptidyl arginine deiminase 6."
] | [
2003,
2006,
2024
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bilateria"
] | [
53,
2921
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
6,
11,
19
] | 4 | true | Domain | Protein-arginine deiminase (PAD), central domain | Protein-arginine deiminase (PAD), central domain | Prot_Arg_deaminase_cen_dom | 9 |
IPR013734 | 13,734 | Transcription factor Nrm1/Whi5 | TF_Nrm1/Whi5 | Conserved_site | 2,682 | false | false | This is a short conserved sequence found in the Nrm1/Whi5 transcription factors. Nrm1 is a negative regulatory component of the MBF complex involved in cell-cycle-dependent transcription [ ]. Whi5 is a transcriptional repressor that negatively regulates G1-specific, SBF- and MBF-dependent transcription [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08528"
] | [
"Whi5"
] | [
2682
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00033694",
"PUB00045170",
"PUB00053853"
] | [
"15210111",
"15210110",
"16916637"
] | [
"CDK activity antagonizes Whi5, an inhibitor of G1/S transcription in yeast.",
"Cln3 activates G1-specific transcription via phosphorylation of the SBF bound repressor Whi5.",
"Constraining G1-specific transcription to late G1 phase: the MBF-associated corepressor Nrm1 acts via negative feedback."
] | [
2004,
2004,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2682
] | 1 | [
"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)"
] | [
5,
2,
2
] | 3 | true | Conserved_site | Transcription factor Nrm1/Whi5 | Transcription factor Nrm1/Whi5 | TF_Nrm1/Whi5 | 3 |
IPR013735 | 13,735 | Transcription factor NusA, N-terminal | TF_NusA_N | Domain | 25,034 | false | false | This entry represents the N-terminal RNA polymerase-binding domain of bacterial transcription factors such as NusA (N-utilising substance A). NusA is involved in transcriptional pausing, termination and anti-termination. NusA from Thermotoga maritima contains an N-terminal domain and three RNA-binding domains (one S1 d... | [
"GO:0003700",
"GO:0031554"
] | [
"DNA-binding transcription factor activity",
"regulation of termination of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08529"
] | [
"NusA_N"
] | [
25034
] | 1 | [] | [] | [] | 0 | [
"1hh2",
"1k0r",
"1l2f",
"2kwp",
"2mt4",
"4mtn",
"5lm7",
"5lm9",
"5ms0",
"6flq",
"6gov",
"6j9e",
"6tqn",
"6tqo",
"6x6t",
"6x7f",
"6x7k",
"6x9q",
"6xas",
"6xav",
"6xdq",
"6z9p",
"6z9q",
"6z9r",
"6z9s",
"6z9t",
"7adb",
"7adc",
"7add",
"7ade",
"7py3",
"7py5"... | 63 | [
"PUB00026894"
] | [
"14621988"
] | [
"Crystal structure of NusA from Thermotoga maritima and functional implication of the N-terminal domain."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
24447,
77,
510
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Transcription factor NusA, N-terminal | Transcription factor NusA, N-terminal | TF_NusA_N | 7 |
IPR013736 | 13,736 | Xaa-Pro dipeptidyl-peptidase, C-terminal | Xaa-Pro_dipept_C | Domain | 28,933 | false | false | This domain is found at the C terminus of cocaine esterase CocE, several glutaryl-7-ACA acylases, and the putative diester hydrolase NonD of Streptomyces griseus (all hydrolases). The domain, which is a β sandwich, is also found in serine peptidases belonging to MEROPS peptidase family S15: Xaa-Pro dipeptidyl-peptidase... | [
"GO:0008239"
] | [
"dipeptidyl-peptidase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF08530",
"SM00939"
] | [
"PepX_C",
"PepX_C"
] | [
28427,
28350
] | 2 | [
"EC"
] | [
"3.4.14.11"
] | [
"EC:3.4.14.11"
] | 1 | [
"1ju3",
"1ju4",
"1l7q",
"1l7r",
"1lns",
"1mpx",
"1nx9",
"1ryy",
"2b4k",
"2b9v",
"3i2f",
"3i2g",
"3i2h",
"3i2i",
"3i2j",
"3i2k",
"3ib3",
"3ida",
"3iii",
"3puh",
"3pui",
"4p08",
"4pf1",
"6nff",
"7f65",
"8yzn",
"8yzo",
"9k48"
] | 28 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Harvfovirus sp.",
"unclassified sequences"
] | [
204,
23594,
4826,
1,
308
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Domain | Xaa-Pro dipeptidyl-peptidase, C-terminal | Xaa-Pro dipeptidyl-peptidase, C-terminal | Xaa-Pro_dipept_C | 6 |
IPR013737 | 13,737 | Bacterial alpha-L-rhamnosidase N-terminal | Bac_rhamnosid_N | Domain | 13,248 | false | false | This domain is found in bacterial rhamnosidase A and B enzymes and is probably involved in substrate recognition. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08531"
] | [
"Bac_rhamnosid_N"
] | [
13248
] | 1 | [
"EC",
"METACYC"
] | [
"3.2.1.40",
"PWY-7134"
] | [
"EC:3.2.1.40",
"METACYC:PWY-7134"
] | 2 | [
"2okx",
"3w5m",
"3w5n",
"6gsz",
"6i60"
] | 5 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
77,
10366,
2696,
3,
106
] | 5 | [
"Arabidopsis thaliana",
"Homo sapiens"
] | [
1,
2
] | 2 | true | Domain | Bacterial alpha-L-rhamnosidase N-terminal | Bacterial alpha-L-rhamnosidase N-terminal | Bac_rhamnosid_N | 9 |
IPR013738 | 13,738 | Beta-galactosidase trimerisation | Beta_galactosidase_Trimer | Domain | 13,305 | 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:0004565",
"GO:0005975"
] | [
"beta-galactosidase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08532"
] | [
"Glyco_hydro_42M"
] | [
13305
] | 1 | [
"EC",
"METACYC"
] | [
"3.2.1.23",
"PWY-6807"
] | [
"EC:3.2.1.23",
"METACYC:PWY-6807"
] | 2 | [
"1kwg",
"1kwk",
"3tts",
"3tty",
"4oif",
"4ucf",
"4uni",
"4uoq",
"4uoz",
"4uzs",
"5dfa",
"5e9a",
"5vym",
"5xb7",
"6lvw",
"6t5o",
"6t6g",
"6t75",
"6t7g",
"6tvk",
"6y2k",
"7omi",
"7oms",
"8ibr",
"8ibs",
"8ibt"
] | 26 | [
"PUB00004870",
"PUB00005266"
] | [
"7624375",
"8535779"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1995,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
113,
12931,
188,
73
] | 4 | [
"Arabidopsis thaliana"
] | [
1
] | 1 | true | Domain | Beta-galactosidase trimerisation | Beta-galactosidase trimerisation | Beta_galactosidase_Trimer | 6 |
IPR013739 | 13,739 | Beta-galactosidase C-terminal | Beta_galactosidase_C | Domain | 7,808 | 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:0004565",
"GO:0006012"
] | [
"beta-galactosidase activity",
"galactose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08533"
] | [
"Glyco_hydro_42C"
] | [
7808
] | 1 | [
"EC",
"METACYC"
] | [
"3.2.1.23",
"PWY-6807"
] | [
"EC:3.2.1.23",
"METACYC:PWY-6807"
] | 2 | [
"1kwg",
"1kwk",
"3tts",
"3tty",
"4oif",
"4ucf",
"4uni",
"4uoq",
"4uoz",
"4uzs",
"5dfa",
"5e9a"
] | 12 | [
"PUB00004870",
"PUB00005266",
"PUB00020891"
] | [
"7624375",
"8535779",
"12215416"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex... | [
1995,
1995,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
7713,
14,
53,
28
] | 4 | [] | [] | 0 | true | Domain | Beta-galactosidase C-terminal | Beta-galactosidase C-terminal | Beta_galactosidase_C | 3 |
IPR013740 | 13,740 | Redoxin | Redoxin | Domain | 66,263 | false | false | This redoxin domain is found in peroxiredoxin, thioredoxin and glutaredoxin proteins. Peroxiredoxins (Prxs) constitute a family of thiol peroxidases that reduce hydrogen peroxide, peroxinitrite, and hydroperoxides using a strictly conserved cysteine [ , ]. Chloroplast thioredoxin systems in plants regulate the enzymes ... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08534"
] | [
"Redoxin"
] | [
66263
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.11.1",
"1.11.1.24",
"R-BTA-3299685",
"R-BTA-5628897",
"R-HSA-1222538",
"R-HSA-1222541",
"R-HSA-3299685",
"R-HSA-5628897",
"R-MMU-3299685",
"R-MMU-5628897",
"R-RNO-3299685",
"R-RNO-5628897",
"R-SCE-3299685",
"R-SCE-5628897",
"R-SPO-3299685",
"R-SPO-5628897"
] | [
"EC:1.11.1",
"EC:1.11.1.24",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-5628897",
"REACTOME:R-HSA-1222538",
"REACTOME:R-HSA-1222541",
"REACTOME:R-HSA-3299685",
"REACTOME:R-HSA-5628897",
"REACTOME:R-MMU-3299685",
"REACTOME:R-MMU-5628897",
"REACTOME:R-RNO-3299685",
"REACTOME:R-RNO-5628897",
"RE... | 16 | [
"1h4o",
"1hd2",
"1jfu",
"1kng",
"1nm3",
"1oc3",
"1psq",
"1q98",
"1qxh",
"1tp9",
"1urm",
"1xiy",
"1xvq",
"1y25",
"1z5y",
"2b1k",
"2b1l",
"2fy6",
"2g0f",
"2h30",
"2jsy",
"2jsz",
"2jzr",
"2jzs",
"2k9f",
"2l5o",
"2lja",
"2ls5",
"2pwj",
"2vl2",
"2vl3",
"2vl9"... | 94 | [
"PUB00037757",
"PUB00043349",
"PUB00043350",
"PUB00094316"
] | [
"15697201",
"18047840",
"17103236",
"27624005"
] | [
"Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.",
"Glutaredoxins and thioredoxins in plants.",
"Cadmium response and redoxin targets in Chlamydomonas reinhardtii: a proteomic approach.",
"The ... | [
2005,
2008,
2006,
2016
] | 4 | [
"IPR013766"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
432,
56445,
18,
8429,
939
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae... | [
26,
1,
1,
2,
2,
9,
2,
7,
8,
1,
1,
14
] | 12 | true | Domain | Redoxin | Redoxin | Redoxin | 3 |
IPR013742 | 13,742 | Whirly transcription factor | Whirly | Family | 1,610 | false | false | The whirly family members are plant transcription factors that bind to single-stranded DNA and regulate defense gene expression [ , , ]. They may contribute to plastid genome stability by protecting against illegitimate repeat-mediated recombination [ , ]. | [
"GO:0003697",
"GO:0006355",
"GO:0006952"
] | [
"single-stranded DNA binding",
"regulation of DNA-templated transcription",
"defense response"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF08536",
"PTHR31745"
] | [
"Whirly",
""
] | [
1581,
1542
] | 2 | [] | [] | [] | 0 | [
"1l3a",
"3n1h",
"3n1i",
"3n1j",
"3n1k",
"3n1l",
"3r9y",
"3r9z",
"3ra0",
"4koo",
"4kop",
"4koq"
] | 12 | [
"PUB00011849",
"PUB00045171",
"PUB00058744",
"PUB00084346",
"PUB00101210"
] | [
"12080340",
"15708347",
"20551348",
"19666500",
"24192350"
] | [
"A new family of plant transcription factors displays a novel ssDNA-binding surface.",
"Whirly transcription factors: defense gene regulation and beyond.",
"Crystal structures of DNA-Whirly complexes and their role in Arabidopsis organelle genome repair.",
"Whirly proteins maintain plastid genome stability in... | [
2002,
2005,
2010,
2009,
2013
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"uncultured Caudovirales phage"
] | [
51,
1558,
1
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
12,
5,
14
] | 3 | true | Family | Whirly transcription factor | Whirly transcription factor | Whirly | 5 |
IPR013743 | 13,743 | NBP1/CSA1 | NBP1/CSA1 | Family | 88 | false | false | This family includes CDC5 pindle pole body anchor protein 1 (CSA1/YPR174C) and NAP1-binding protein (NBP1) from yeast, which are paralogues. Both proteins bind to the nuclear membrane. NBP1 has been shown in Saccharomyces cerevisiae to function in spindle pole body duplication [ ] and CSA1 is a specialised component of... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08537"
] | [
"NBP1"
] | [
88
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00074978",
"PUB00074979",
"PUB00158958"
] | [
"21785410",
"15282802",
"32553169"
] | [
"Targeting of Nbp1 to the inner nuclear membrane is essential for spindle pole body duplication.",
"Localization of proteins that are coordinately expressed with Cln2 during the cell cycle.",
"Proline-Rich Motifs Control G2-CDK Target Phosphorylation and Priming an Anchoring Protein for Polo Kinase Localization... | [
2011,
2004,
2020
] | 3 | [] | [] | 0 | 0 | null | [
"saccharomyceta"
] | [
88
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
2
] | 1 | true | Family | NBP1/CSA1 | NBP1/CSA1 | NBP1/CSA1 | 9 |
IPR013744 | 13,744 | Fusarinine C esterase SidJ | SidJ | Family | 3,219 | false | false | This entry includes fusarinine C esterase SidJ from the yeast Neosartorya fumigata . Fusarinine C is an intracellular siderophore (an iron-chelating compound that transports iron across membranes) that is crucial for virulence. The closely related siderophore triacetylfusarinine C is not hydrolysed by SidJ [ ]. Homolog... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF08538",
"PTHR31591"
] | [
"DUF1749",
""
] | [
3188,
3041
] | 2 | [] | [] | [] | 0 | [
"2q0x",
"6gup"
] | 2 | [
"PUB00089632"
] | [
"24038704"
] | [
"Aspergillus fumigatus SidJ mediates intracellular siderophore hydrolysis."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
11,
186,
3020,
2
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
4,
1,
4,
1,
3
] | 5 | true | Family | Fusarinine C esterase SidJ | Fusarinine C esterase SidJ | SidJ | 9 |
IPR013745 | 13,745 | TORC2 component Bit61/PRR5 | Bit61/PRR5 | Family | 4,414 | false | false | This entry includes PRR5 (also known as PROTOR1) from animals, Bit61 and its paralogue-Bit2 from budding yeasts [ , ]. They are part of the Target Of Rapamycin Complex 2 (TORC2) complex, which plays an essential role in signal transduction [ ]. The mammalian TORC2 consists of mTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPT... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF08539",
"PTHR32428"
] | [
"HbrB",
""
] | [
4069,
4251
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-HSA-1257604",
"R-HSA-389357",
"R-HSA-5218920",
"R-HSA-5674400",
"R-HSA-6804757",
"R-HSA-9856530",
"R-MMU-1257604",
"R-MMU-389357",
"R-MMU-5218920",
"R-MMU-6804757",
"R-MMU-9856530",
"R-RNO-1257604",
"R-RNO-389357",
"R-RNO-5218920",
"R-RNO-6804757",
"R-RNO-9856530",
"R-SCE-1257604"... | [
"REACTOME:R-HSA-1257604",
"REACTOME:R-HSA-389357",
"REACTOME:R-HSA-5218920",
"REACTOME:R-HSA-5674400",
"REACTOME:R-HSA-6804757",
"REACTOME:R-HSA-9856530",
"REACTOME:R-MMU-1257604",
"REACTOME:R-MMU-389357",
"REACTOME:R-MMU-5218920",
"REACTOME:R-MMU-6804757",
"REACTOME:R-MMU-9856530",
"REACTOME:... | 26 | [] | 0 | [
"PUB00044891",
"PUB00057948",
"PUB00061649",
"PUB00075519",
"PUB00075520",
"PUB00075521",
"PUB00075523",
"PUB00075524",
"PUB00078108",
"PUB00078112"
] | [
"14736892",
"16962653",
"15689497",
"15988011",
"16919458",
"23762398",
"17043309",
"17303383",
"26700129",
"17461779"
] | [
"TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates with Ssd1p to maintain cellular integrity in Saccharomyces cerevisiae.",
"SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity.",
"The pleckstrin homology domain proteins Slm1 and... | [
2004,
2006,
2005,
2005,
2006,
2013,
2006,
2007,
2015,
2007
] | 10 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4414
] | 1 | [
"Danio rerio",
"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 (strain 972 / ATCC 24843)"
] | [
19,
13,
5,
1,
6,
2,
2
] | 7 | true | Family | TORC2 component Bit61/PRR5 | TORC2 component Bit61/PRR5 | Bit61/PRR5 | 9 |
IPR013746 | 13,746 | Hydroxymethylglutaryl-coenzyme A synthase, C-terminal domain | HMG_CoA_synt_C_dom | Domain | 11,214 | false | false | Hydroxymethylglutaryl-CoA synthase ( ) catalyses the condensation of acetyl-CoA with acetoacetyl-CoA to produce HMG-CoA and CoA, the second reaction in the mevalonate-dependent isoprenoid biosynthesis pathway. HMG-CoA synthase contains an important catalytic cysteine residue that acts as a nucleophile in the first step... | [
"GO:0004421",
"GO:0006084",
"GO:0010142"
] | [
"hydroxymethylglutaryl-CoA synthase activity",
"acetyl-CoA metabolic process",
"farnesyl diphosphate biosynthetic process, mevalonate pathway"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF08540"
] | [
"HMG_CoA_synt_C"
] | [
11214
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"2.3.3.10",
"PWY-6174",
"PWY-7391",
"PWY-7524",
"PWY-7571",
"PWY-8125",
"PWY-922",
"R-BTA-77111",
"R-BTA-9837999",
"R-CEL-191273",
"R-CEL-77111",
"R-CEL-9837999",
"R-DDI-191273",
"R-DDI-77111",
"R-DDI-9837999",
"R-HSA-191273",
"R-HSA-1989781",
"R-HSA-2426168",
"R-HSA-77111",
"R... | [
"EC:2.3.3.10",
"METACYC:PWY-6174",
"METACYC:PWY-7391",
"METACYC:PWY-7524",
"METACYC:PWY-7571",
"METACYC:PWY-8125",
"METACYC:PWY-922",
"REACTOME:R-BTA-77111",
"REACTOME:R-BTA-9837999",
"REACTOME:R-CEL-191273",
"REACTOME:R-CEL-77111",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-191273",
"REACT... | 34 | [
"1tvz",
"1txt",
"1x9e",
"1xpk",
"1xpl",
"1xpm",
"1ysl",
"2f82",
"2f9a",
"2fa0",
"2fa3",
"2hdb",
"2p8u",
"2wya",
"3leh",
"3sqz",
"3v4n",
"3v4x",
"4yxq",
"4yxt",
"4yxv",
"5hwo",
"5hwp",
"5hwq",
"5hwr",
"5kp5",
"5kp6",
"5kp7",
"5kp8",
"7cqt",
"8s81"
] | 31 | [
"PUB00036056",
"PUB00036057",
"PUB00036058",
"PUB00036059",
"PUB00036060"
] | [
"15498869",
"15546978",
"16640729",
"17128980",
"16245942"
] | [
"3-hydroxy-3-methylglutaryl-CoA synthase intermediate complex observed in \"real-time\".",
"An atomic-resolution mechanism of 3-hydroxy-3-methylglutaryl-CoA synthase.",
"Isolation, endocrine regulation and mRNA distribution of the 3-hydroxy-3-methylglutaryl coenzyme A synthase (HMG-S) gene from the pine engrave... | [
2004,
2004,
2006,
2006,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
417,
3507,
7258,
32
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
2,
1,
3,
1,
7,
10,
1,
8,
7,
1,
1,
28
] | 12 | true | Domain | Hydroxymethylglutaryl-coenzyme A synthase, C-terminal domain | Hydroxymethylglutaryl-coenzyme A synthase, C-terminal domain | HMG_CoA_synt_C_dom | 6 |
IPR013747 | 13,747 | Beta-ketoacyl-[acyl-carrier-protein] synthase III, C-terminal | ACP_syn_III_C | Domain | 62,941 | false | false | This entry represents the C-terminal domain in beta-ketoacyl-[acyl-carrier-protein] synthase III (also known as 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III), the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria [ ]. Beta-ketoacyl-[acyl-carrier-protein] s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08541"
] | [
"ACP_syn_III_C"
] | [
62941
] | 1 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC"
] | [
"2.3.1",
"2.3.1.180",
"GenProp1364",
"GenProp1473",
"GenProp1562",
"GenProp1569",
"PWY-4381"
] | [
"EC:2.3.1",
"EC:2.3.1.180",
"GP:GenProp1364",
"GP:GenProp1473",
"GP:GenProp1562",
"GP:GenProp1569",
"METACYC:PWY-4381"
] | 7 | [
"1ebl",
"1hn9",
"1hnd",
"1hnh",
"1hnj",
"1hnk",
"1hzp",
"1m1m",
"1mzj",
"1mzs",
"1u6e",
"1u6s",
"1ub7",
"1zow",
"2ahb",
"2aj9",
"2ebd",
"2eft",
"2gyo",
"2qnx",
"2qny",
"2qnz",
"2qo0",
"2qo1",
"2qx1",
"2x3e",
"3fk5",
"3gwa",
"3gwe",
"3h76",
"3h77",
"3h78"... | 127 | [
"PUB00007690",
"PUB00021033",
"PUB00163228"
] | [
"10629181",
"10600651",
"14523010"
] | [
"beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis.",
"Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme.",
"Beta-ketoacyl-acyl carrie... | [
2000,
2000,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified bacterial viruses",
"unclassified sequences"
] | [
604,
48718,
12828,
2,
789
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
84,
1,
72,
106
] | 4 | true | Domain | Beta-ketoacyl-[acyl-carrier-protein] synthase III, C-terminal | Beta-ketoacyl-[acyl-carrier-protein] synthase III, C-terminal | ACP_syn_III_C | 6 |
IPR013748 | 13,748 | Replication factor C, C-terminal | Rep_factorC_C | Domain | 15,204 | false | false | This is the C-terminal domain of RFC (replication factor-C) protein of the clamp loader complex which binds to the DNA sliding clamp (proliferating cell nuclear antigen, PCNA). The five modules of RFC assemble into a right-handed spiral, which results in only three of the five RFC subunits (RFC-A, RFC-B and RFC-C) maki... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08542"
] | [
"Rep_fac_C"
] | [
15204
] | 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-110312",
"R-BTA-110314",
"R-BTA-110320",
"R-BTA-174411",
"R-BTA-176187",
"R-BTA-5651801",
"R-BTA-5655862",
"R-BTA-5656121",
"R-BTA-5656169",
"R-BTA-5685938",
"R-BTA-5685942",
"R-BTA-5693607",
"R-BTA-5696397",
"R-BTA-5696400",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6804756",
... | [
"REACTOME:R-BTA-110312",
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-110320",
"REACTOME:R-BTA-174411",
"REACTOME:R-BTA-176187",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5655862",
"REACTOME:R-BTA-5656121",
"REACTOME:R-BTA-5656169",
"REACTOME:R-BTA-5685938",
"REACTOME:R-BTA-5685942",
"REACTOME:R-B... | 161 | [
"1iqp",
"1sxj",
"2chq",
"2chv",
"6vvo",
"7sgz",
"7sh2",
"7st9",
"7stb",
"7ste",
"7tfh",
"7tfi",
"7tfj",
"7tfk",
"7tfl",
"7thj",
"7thv",
"7ti8",
"7tib",
"7tic",
"7tid",
"7tku",
"7u19",
"7u1a",
"7u1p",
"7z6h",
"8dqw",
"8dqx",
"8dqz",
"8dr0",
"8dr1",
"8dr3"... | 68 | [
"PUB00031233"
] | [
"15201901"
] | [
"Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Thermodesulfobacterium geofontis",
"Viruses",
"unclassified sequences"
] | [
1393,
13541,
1,
118,
151
] | 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... | [
11,
2,
7,
3,
13,
10,
3,
6,
11,
3,
3,
11
] | 12 | true | Domain | Replication factor C, C-terminal | Replication factor C, C-terminal | Rep_factorC_C | 4 |
IPR013749 | 13,749 | Pyridoxamine kinase/Phosphomethylpyrimidine kinase | PM/HMP-P_kinase-1 | Domain | 46,112 | false | false | Enzymes in this family belong to the ribokinase superfamily. Pyridoxamine kinase phosphorylates B6 vitamers and functions in a salvage pathway [ , ]. Phosphomethylpyrimidine kinase is part of the thiamine pyrophosphate (TPP) synthesis pathway. TPP is an essential cofactor for many enzymes [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08543"
] | [
"Phos_pyr_kin"
] | [
46112
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.35",
"GenProp1266",
"GenProp1289",
"GenProp1590",
"PWY-7204",
"PWY-7282",
"R-BTA-6798695",
"R-BTA-964975",
"R-DDI-6798695",
"R-DDI-964975",
"R-HSA-6798695",
"R-HSA-964975",
"R-MMU-6798695",
"R-MMU-964975",
"R-RNO-6798695",
"R-RNO-964975",
"R-SCE-6798695",
"R-SCE-964975",
"... | [
"EC:2.7.1.35",
"GP:GenProp1266",
"GP:GenProp1289",
"GP:GenProp1590",
"METACYC:PWY-7204",
"METACYC:PWY-7282",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-964975",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-964975",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-964975",
"REACTOME:R-MMU-6798695",
"R... | 20 | [
"1jxh",
"1jxi",
"1lhp",
"1lhr",
"1rft",
"1rfu",
"1rfv",
"1td2",
"1ub0",
"1vi9",
"1ygj",
"1ygk",
"1yhj",
"2ajp",
"2ddm",
"2ddo",
"2ddw",
"2f7k",
"2i5b",
"2yxt",
"2yxu",
"3fhx",
"3fhy",
"3h74",
"3hyo",
"3ibq",
"3keu",
"3mbh",
"3mbj",
"3pzs",
"3rm5",
"3zs7"... | 64 | [
"PUB00017544",
"PUB00020971",
"PUB00031417"
] | [
"9537380",
"9244280",
"15547280"
] | [
"Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12.",
"Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis.",
"Crystal struc... | [
1998,
1997,
2004
] | 3 | [] | [
"IPR004399"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
902,
37010,
7860,
340
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae... | [
6,
8,
3,
3,
4,
1,
3,
7,
9,
5,
5,
15
] | 12 | true | Domain | Pyridoxamine kinase/Phosphomethylpyrimidine kinase | Pyridoxamine kinase/Phosphomethylpyrimidine kinase | PM/HMP-P_kinase-1 | 8 |
IPR013751 | 13,751 | Beta-ketoacyl-[acyl-carrier-protein] synthase III, N-terminal | ACP_syn_III_N | Domain | 47,792 | false | false | This entry represents the N-terminal domain in beta-ketoacyl-[acyl-carrier-protein] synthase III (also known as 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III), the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria [ ]. Beta-ketoacyl-[acyl-carrier-protein] s... | [
"GO:0004315",
"GO:0006633"
] | [
"3-oxoacyl-[acyl-carrier-protein] synthase activity",
"fatty acid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08545"
] | [
"ACP_syn_III"
] | [
47792
] | 1 | [
"EC",
"EC",
"GP",
"GP",
"METACYC"
] | [
"2.3.1",
"2.3.1.180",
"GenProp1473",
"GenProp1562",
"PWY-4381"
] | [
"EC:2.3.1",
"EC:2.3.1.180",
"GP:GenProp1473",
"GP:GenProp1562",
"METACYC:PWY-4381"
] | 5 | [
"1ebl",
"1hn9",
"1hnd",
"1hnh",
"1hnj",
"1hnk",
"1hzp",
"1m1m",
"1mzj",
"1mzs",
"1u6e",
"1u6s",
"1ub7",
"1zow",
"2ahb",
"2aj9",
"2ebd",
"2eft",
"2gyo",
"2qnx",
"2qny",
"2qnz",
"2qo0",
"2qo1",
"2qx1",
"2x3e",
"3fk5",
"3gwa",
"3gwe",
"3h76",
"3h77",
"3h78"... | 106 | [
"PUB00007690",
"PUB00021033",
"PUB00025721",
"PUB00033354",
"PUB00033355",
"PUB00163228"
] | [
"10629181",
"10600651",
"11243824",
"12429097",
"15952903",
"14523010"
] | [
"beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis.",
"Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme.",
"Refined structures of bet... | [
2000,
2000,
2001,
2002,
2005,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified bacterial viruses",
"unclassified sequences"
] | [
125,
45547,
1436,
2,
682
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
4,
16
] | 4 | true | Domain | Beta-ketoacyl-[acyl-carrier-protein] synthase III, N-terminal | Beta-ketoacyl-[acyl-carrier-protein] synthase III, N-terminal | ACP_syn_III_N | 1 |
IPR013752 | 13,752 | Ketopantoate reductase, C-terminal domain | KPR_C | Domain | 36,011 | false | false | This entry represents the C-terminal domain of KPR. Ketopantoate reductase (KPR; ), also known as 2-dehydropantoate 2-reductase or ApbA/PanE, catalyses the NADPH-dependent reduction of ketopantoate to pantoate, an essential step in the biosynthesis of pantothenate (vitamin B5) and coenzyme A [ ]. The enzyme consists of... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08546"
] | [
"ApbA_C"
] | [
36011
] | 1 | [
"EC",
"METACYC"
] | [
"1.1.1.169",
"PWY-6654"
] | [
"EC:1.1.1.169",
"METACYC:PWY-6654"
] | 2 | [
"1ks9",
"1yjq",
"1yon",
"2ew2",
"2ofp",
"2qyt",
"3ego",
"3g17",
"3ghy",
"3hn2",
"3hwr",
"3i83",
"3wfi",
"3wfj",
"4ol9",
"4s3m",
"4yca",
"5ayv",
"5hws",
"5x20",
"5zik",
"5zix",
"6k1r",
"8iwg",
"8iwq",
"8ix9",
"8ixh",
"8ixm",
"8wl1",
"8wl3",
"8wl4"
] | 31 | [
"PUB00020970",
"PUB00020974",
"PUB00028857",
"PUB00104842"
] | [
"9488683",
"9721324",
"11724562",
"25946571"
] | [
"ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway.",
"The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is allelic to apbA in Salmonella typhimurium.",
"Crystal structure of Escher... | [
1998,
1998,
2001,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
671,
26362,
8628,
350
] | 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,
7,
5,
3
] | 4 | true | Domain | Ketopantoate reductase, C-terminal domain | Ketopantoate reductase, C-terminal domain | KPR_C | 6 |
IPR013755 | 13,755 | Flaviviral glycoprotein E, central domain, subdomain 1 | Flav_gly_cen_dom_subdom1 | Homologous_superfamily | 36,111 | false | false | Flaviviruses are small, enveloped RNA viruses that use arthropods such as mosquitoes for transmission to their vertebrate hosts, and include Yellow fever virus (YFV), West Nile virus (WNV), Tick-borne encephalitis virus, Japanese encephalitis virus (JE) and Dengue virus 2 viruses [ ]. Flaviviruses consist of three stru... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.387.10"
] | [
""
] | [
36111
] | 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 | [
"1k4r",
"1n6g",
"1na4",
"1oan",
"1ok8",
"1oke",
"1p58",
"1svb",
"1tg8",
"1tge",
"1thd",
"1urz",
"1uzg",
"2b6b",
"2hg0",
"2i69",
"2of6",
"2r6p",
"3c5x",
"3c6d",
"3c6e",
"3c6r",
"3g7t",
"3i50",
"3ixx",
"3ixy",
"3iya",
"3iyw",
"3j05",
"3j0b",
"3j27",
"3j2p"... | 201 | [
"PUB00004210",
"PUB00015617",
"PUB00015627"
] | [
"7753193",
"15378043",
"12759475"
] | [
"The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution.",
"Transmission cycles, host range, evolution and emergence of arboviral disease.",
"A ligand-binding pocket in the dengue virus envelope glycoprotein."
] | [
1995,
2004,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Elysia marginata",
"Riboviria"
] | [
1,
36110
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Flaviviral glycoprotein E, central domain, subdomain 1 | Flaviviral glycoprotein E, central domain, subdomain 1 | Flav_gly_cen_dom_subdom1 | 9 |
IPR013756 | 13,756 | Flaviviral glycoprotein E, central domain, subdomain 2 | GlyE_cen_dom_subdom2 | Homologous_superfamily | 35,886 | false | false | Flaviviruses are small, enveloped RNA viruses that use arthropods such as mosquitoes for transmission to their vertebrate hosts, and include Yellow fever virus (YFV), West Nile virus (WNV), Tick-borne encephalitis virus, Japanese encephalitis virus (JE) and Dengue virus 2 viruses [ ]. Flaviviruses consist of three stru... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.67.10"
] | [
""
] | [
35886
] | 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 | [
"1k4r",
"1n6g",
"1na4",
"1oan",
"1ok8",
"1oke",
"1p58",
"1svb",
"1tg8",
"1tge",
"1thd",
"1urz",
"1uzg",
"2b6b",
"2hg0",
"2i69",
"2of6",
"2r6p",
"3c5x",
"3c6d",
"3c6e",
"3c6r",
"3g7t",
"3i50",
"3ixx",
"3ixy",
"3iya",
"3iyw",
"3j05",
"3j0b",
"3j27",
"3j2p"... | 201 | [
"PUB00004210",
"PUB00015617",
"PUB00015627"
] | [
"7753193",
"15378043",
"12759475"
] | [
"The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution.",
"Transmission cycles, host range, evolution and emergence of arboviral disease.",
"A ligand-binding pocket in the dengue virus envelope glycoprotein."
] | [
1995,
2004,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Riboviria"
] | [
35886
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Flaviviral glycoprotein E, central domain, subdomain 2 | Flaviviral glycoprotein E, central domain, subdomain 2 | GlyE_cen_dom_subdom2 | 3 |
IPR013758 | 13,758 | DNA topoisomerase, type IIA, domain A, alpha-beta | Topo_IIA_A/C_ab | Homologous_superfamily | 65,094 | false | false | DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single-or double-strand breaks, crossing the strands through one another, then resealing the breaks [ ]. These enzymes have several functions: to remove DNA supercoi... | [
"GO:0003677",
"GO:0003918",
"GO:0005524",
"GO:0006259",
"GO:0006265"
] | [
"DNA binding",
"DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity",
"ATP binding",
"DNA metabolic process",
"DNA topological change"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 5 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.199.10"
] | [
""
] | [
65094
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"REACTOME:R-SPO-4615... | 13 | [
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"4bul"... | 172 | [
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"PUB00016842",
"PUB00020793",
"PUB00020794",
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"7770916",
"11395412",
"12596227",
"12042765",
"7980433",
"16023670",
"8982450"
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"The mechanisms of DNA topoisomerases.",
"DNA topoisomerases: structure, function, and mechanism.",
"Phylogenomics of type II DNA topoisomerases.",
"Cellular roles of DNA topoisomerases: a molecular perspective.",
"Structure and function of type II DNA topoisomerases.",
"The structural basis for substrate... | [
1995,
2001,
2003,
2002,
1994,
2005,
1996
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
557,
53408,
9070,
732,
1327
] | 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,
3,
5,
1,
2,
10,
5,
2,
7,
8,
1,
1,
69
] | 13 | true | Homologous_superfamily | DNA topoisomerase, type IIA, domain A, alpha-beta | DNA topoisomerase, type IIA, domain A, alpha-beta | Topo_IIA_A/C_ab | 9 |
IPR013759 | 13,759 | DNA topoisomerase, type IIA, subunit B, C-terminal | Topo_IIA_B_C | Homologous_superfamily | 71,029 | false | false | DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single-or double-strand breaks, crossing the strands through one another, then resealing the breaks [ ]. These enzymes have several functions: to remove DNA supercoi... | [
"GO:0003677",
"GO:0003918",
"GO:0005524",
"GO:0006265"
] | [
"DNA binding",
"DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity",
"ATP binding",
"DNA topological change"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.50.670"
] | [
""
] | [
71029
] | 1 | [
"EC",
"REACTOME",
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"REACTOME",
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"R-SSC-4615885"
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"REACTOME:R-RNO-4615885",
"REACTOME:R-SCE-4615885",
"REACTOME:R-SPO-4615... | 13 | [
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"3ig0",
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"3ksa",
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"3l4j",
"3l4k",
"3ltn",
"3m4i",
"3nuh",
"3qx3",
"3rad",
"3rae",
"3raf",
"4bul",
"4fm9",
"4g0u",
"4g0v",
"4g0w",
"4gfh"... | 159 | [
"PUB00005437",
"PUB00016842",
"PUB00020793",
"PUB00020794",
"PUB00020795",
"PUB00020802",
"PUB00020803"
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"7770916",
"11395412",
"12596227",
"12042765",
"7980433",
"16023670",
"8982450"
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"The mechanisms of DNA topoisomerases.",
"DNA topoisomerases: structure, function, and mechanism.",
"Phylogenomics of type II DNA topoisomerases.",
"Cellular roles of DNA topoisomerases: a molecular perspective.",
"Structure and function of type II DNA topoisomerases.",
"The structural basis for substrate... | [
1995,
2001,
2003,
2002,
1994,
2005,
1996
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
566,
58079,
10267,
764,
1353
] | 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",... | [
15,
4,
5,
1,
2,
9,
5,
2,
7,
7,
1,
1,
59
] | 13 | true | Homologous_superfamily | DNA topoisomerase, type IIA, subunit B, C-terminal | DNA topoisomerase, type IIA, subunit B, C-terminal | Topo_IIA_B_C | 8 |
IPR013761 | 13,761 | Sterile alpha motif/pointed domain superfamily | SAM/pointed_sf | Homologous_superfamily | 222,972 | false | false | Sterile alpha motif (SAM) domains are known to be involved in diverse protein-protein interactions, associating with both SAM-containing and non-SAM-containing proteins pathway [ ]. SAM domains exhibit a conserved structure, consisting of a 4-5-helical bundle of two orthogonally packed α-hairpins. However SAM domains d... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.150.50",
"SSF47769"
] | [
"",
""
] | [
211578,
208451
] | 2 | [
"REACTOME",
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"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-2559585",
"R-BTA-8956319",
"R-CEL-1660661",
"R-CEL-181429",
"R-CEL-181430",
"R-CEL-210500",
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"R-CEL-6794361",
"R-CEL-983695",
"R-CFA-1660499",
"R-CFA-1855204",
"R-CFA-912526",
"... | [
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"REACTOME:R-CEL-181429",
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"REACTOME:R-CEL-210500",
"REACTOME:R-CEL-212676",
"REACTOME:R-CEL-2559580",
"REACTOME:R-CEL-264642",
"REACTOME:R-CEL-388844",
"REACTOME:R-CEL-5578775",
"REACTOME:R-CE... | 279 | [
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"1v38",
"1v85",
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"1x40",
"1x66",
"1x9x",
"1z1v",
"2b6g",
"2d3d",
"2d8c",
"2dkx"... | 221 | [
"PUB00014041",
"PUB00014042",
"PUB00014043",
"PUB00014044",
"PUB00014045",
"PUB00014046",
"PUB00014047",
"PUB00014048"
] | [
"14659692",
"12858164",
"14704859",
"9031109",
"12577325",
"12389031",
"14659698",
"14499651"
] | [
"SAM domains: uniform structure, diversity of function.",
"The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators.",
"The Ets-1 transcription factor is involved in the development and invasion of malignant melanoma.",
"ETV6 gene rearrangements in hematopoietic malignant di... | [
2003,
2003,
2004,
1996,
2003,
2002,
2003,
2003
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
949,
221964,
41,
18
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
63,
53,
1110,
148,
509,
392,
9,
36,
513,
6,
5,
96
] | 12 | true | Homologous_superfamily | Sterile alpha motif/pointed domain superfamily | Sterile alpha motif/pointed domain superfamily | SAM/pointed_sf | 8 |
IPR013762 | 13,762 | Integrase-like, catalytic domain superfamily | Integrase-like_cat_sf | Homologous_superfamily | 321,243 | false | false | Phage integrases are enzymes that mediate unidirectional site-specific recombination between two DNA recognition sequences, the phage attachment site, attP, and the bacterial attachment site, attB [ ]. Integrases may be grouped into two major families, the tyrosine recombinases and the serine recombinases, based on the... | [
"GO:0003677",
"GO:0006310",
"GO:0015074"
] | [
"DNA binding",
"DNA recombination",
"DNA integration"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.443.10"
] | [
""
] | [
321243
] | 1 | [] | [] | [] | 0 | [
"1a0p",
"1ae9",
"1aih",
"1crx",
"1drg",
"1f44",
"1flo",
"1kbu",
"1m6x",
"1ma7",
"1nzb",
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"1p4e",
"1p7d",
"1pvp",
"1pvq",
"1pvr",
"1q3u",
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"1xns",
"1xo0",
"1z19",
"1z1b",
"1z1g",
"2a3v",
"2crx",
"2hof",
"2hoi",
"3c28",
"3c29",
"3crx",
"3mgv"... | 57 | [
"PUB00014061",
"PUB00014062"
] | [
"14687564",
"12560475"
] | [
"Phage integrases: biology and applications.",
"Conservation of structure and function among tyrosine recombinases: homology-based modeling of the lambda integrase core-binding domain."
] | [
2004,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"other sequences",
"unclassified sequences"
] | [
6059,
283607,
22586,
3025,
8,
5958
] | 6 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Mus musculus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
29,
15,
1,
1
] | 4 | true | Homologous_superfamily | Integrase-like, catalytic domain superfamily | Integrase-like, catalytic domain superfamily | Integrase-like_cat_sf | 2 |
IPR013763 | 13,763 | Cyclin-like domain | Cyclin-like_dom | Domain | 97,386 | false | false | This cyclin-like domain is found in cyclins, but it is also found as the core domain in transcription factor IIB (TFIIB) [ ] and in the retinoblastoma tumour suppressor [ ]. It consists of a duplication of a fold consisting of 5 helices, one of them surrounded by the others. | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00385"
] | [
"CYCLIN"
] | [
97386
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-112382",
"R-BTA-1538133",
"R-BTA-174048",
"R-BTA-176408",
"R-BTA-176412",
"R-BTA-176417",
"R-BTA-187577",
"R-BTA-212436",
"R-BTA-2173796",
"R-BTA-2299718",
"R-BTA-2500257",
"R-BTA-2559586",
"R-BTA-2565942",
"R-BTA-2980767",
"R-BTA-2995383",
"R-BTA-3301854",
"R-BTA-4419969",
... | [
"REACTOME:R-BTA-112382",
"REACTOME:R-BTA-1538133",
"REACTOME:R-BTA-174048",
"REACTOME:R-BTA-176408",
"REACTOME:R-BTA-176412",
"REACTOME:R-BTA-176417",
"REACTOME:R-BTA-187577",
"REACTOME:R-BTA-212436",
"REACTOME:R-BTA-2173796",
"REACTOME:R-BTA-2299718",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA... | 500 | [
"1ais",
"1bu2",
"1c9b",
"1d3u",
"1e9h",
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"1fin",
"1fvv",
"1g3n",
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"1jst",
"1jsu",
"1kxu",
"1n4m",
"1o9k",
"1ogu",
"1oi9",
"1oiu",
"1oiy"... | 481 | [
"PUB00022837",
"PUB00049281"
] | [
"7675079",
"17974914"
] | [
"Crystal structure of a TFIIB-TBP-TATA-element ternary complex.",
"Structure of the retinoblastoma protein bound to adenovirus E1A reveals the molecular basis for viral oncoprotein inactivation of a tumor suppressor."
] | [
1995,
2007
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3933,
10,
93087,
118,
238
] | 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... | [
228,
24,
103,
44,
117,
108,
8,
110,
130,
17,
13,
367
] | 12 | true | Domain | Cyclin-like domain | Cyclin-like domain | Cyclin-like_dom | 9 |
IPR013765 | 13,765 | DNA recombination and repair protein RecA | DNA_recomb/repair_RecA | Family | 49,545 | false | false | The recA gene product is a multifunctional enzyme that plays a role in homologous recombination, DNA repair and induction of the SOS response [ ]. In homologous recombination, the protein functions as a DNA-dependent ATPase, promoting synapsis, heteroduplex formation and strand exchange between homologous DNAs [ ]. Rec... | [
"GO:0003697",
"GO:0005524",
"GO:0006281"
] | [
"single-stranded DNA binding",
"ATP binding",
"DNA repair"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"MF_00268",
"PR00142",
"PTHR45900",
"TIGR02012"
] | [
"RecA",
"RECA",
"",
"tigrfam_recA"
] | [
28203,
47994,
49479,
35699
] | 4 | [
"GP"
] | [
"GenProp0215"
] | [
"GP:GenProp0215"
] | 1 | [
"1aa3",
"1g18",
"1g19",
"1mo3",
"1mo4",
"1mo5",
"1mo6",
"1n03",
"1rea",
"1u94",
"1u98",
"1u99",
"1ubc",
"1ube",
"1ubf",
"1ubg",
"1xms",
"1xmv",
"1xp8",
"2g88",
"2odn",
"2odw",
"2oe2",
"2oep",
"2oes",
"2ofo",
"2reb",
"2rec",
"2zr0",
"2zr7",
"2zr9",
"2zra"... | 87 | [
"PUB00002285",
"PUB00003439",
"PUB00003747",
"PUB00004797",
"PUB00004946",
"PUB00043276"
] | [
"7592482",
"8587109",
"1896024",
"1518831",
"9187054",
"12045091"
] | [
"Bacterial classifications derived from recA protein sequence comparisons.",
"The RecA protein as a model molecule for molecular systematic studies of bacteria: comparison of trees of RecAs and 16S rRNAs from the same species.",
"Characterization of recA genes and recA mutants of Rhizobium meliloti and Rhizobiu... | [
1995,
1995,
1991,
1992,
1997,
2002
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
10,
44775,
2872,
1005,
883
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
21,
1,
13,
28
] | 4 | true | Family | DNA recombination and repair protein RecA | DNA recombination and repair protein RecA | DNA_recomb/repair_RecA | 2 |
IPR013766 | 13,766 | Thioredoxin domain | Thioredoxin_domain | Domain | 508,468 | false | false | This entry represents the thioredoxin domain. Thioredoxins [ , , , ] are small disulphide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on r... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00085",
"PS51352"
] | [
"Thioredoxin",
"THIOREDOXIN_2"
] | [
201353,
474244
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1614558",
"R-BTA-2559580",
"R-BTA-3299685",
"R-BTA-499943",
"R-BTA-5628897",
"R-BTA-5676934",
"R-BTA-6798695",
"R-BTA-844456",
"R-BTA-9818027",
"R-BTA-9864848",
"R-CEL-1614558",
"R-CEL-1650814",
"R-CEL-2559580",
"R-CEL-264876",
"R-CEL-3299685",
"R-CEL-381426",
"R-CEL-499943",
... | [
"REACTOME:R-BTA-1614558",
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-499943",
"REACTOME:R-BTA-5628897",
"REACTOME:R-BTA-5676934",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-844456",
"REACTOME:R-BTA-9818027",
"REACTOME:R-BTA-9864848",
"REACTOME:R-CEL-1614558",
"REACTOME:... | 199 | [
"1a23",
"1a24",
"1a2j",
"1a2l",
"1a2m",
"1ac1",
"1acv",
"1aiu",
"1auc",
"1bed",
"1bq7",
"1cqg",
"1cqh",
"1dby",
"1dsb",
"1e2y",
"1eej",
"1ep7",
"1ep8",
"1ert",
"1eru",
"1erv",
"1erw",
"1ewx",
"1ezk",
"1f6m",
"1f9m",
"1faa",
"1fb0",
"1fb6",
"1fg4",
"1fo5"... | 1,072 | [
"PUB00000038",
"PUB00000561",
"PUB00001458",
"PUB00001495",
"PUB00002504",
"PUB00002862",
"PUB00002883",
"PUB00005250",
"PUB00005258",
"PUB00005259",
"PUB00005423"
] | [
"3896121",
"3371540",
"7635143",
"2537773",
"2668278",
"7913469",
"7983029",
"8590004",
"7788289",
"7788290",
"7940678"
] | [
"Thioredoxin.",
"Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins.",
"Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese.",
"Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multif... | [
1985,
1988,
1995,
1989,
1989,
1994,
1994,
1995,
1995,
1995,
1994
] | 11 | [] | [
"IPR000866",
"IPR005788",
"IPR013740",
"IPR035671",
"IPR035673",
"IPR035674",
"IPR037463",
"IPR043361",
"IPR045870",
"IPR046374"
] | 0 | 10 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
7929,
335268,
158292,
801,
6178
] | 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",... | [
361,
60,
72,
76,
11,
196,
122,
16,
164,
165,
17,
13,
477
] | 13 | true | Domain | Thioredoxin domain | Thioredoxin domain | Thioredoxin_domain | 2 |
IPR013767 | 13,767 | PAS fold | PAS_fold | Domain | 163,879 | false | false | PAS domains are involved in many signalling proteins where they are used as a signal sensor domain [ ]. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in dif... | [
"GO:0006355"
] | [
"regulation of DNA-templated transcription"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00989"
] | [
"PAS"
] | [
163879
] | 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-1234158",
"R-CEL-1234176",
"R-CEL-5689880",
"R-CEL-8951664",
"R-CEL-9768919",
"R-DME-1234158",
"R-DME-1234176",
"R-DME-211945",
"R-DME-418555",
"R-DME-432395",
"R-DME-432408",
"R-DME-432490",
"R-DME-432501",
"R-DME-432524",
"R-DME-432553",
"R-DME-432560",
"R-DME-432620",
"R-... | [
"REACTOME:R-CEL-1234158",
"REACTOME:R-CEL-1234176",
"REACTOME:R-CEL-5689880",
"REACTOME:R-CEL-8951664",
"REACTOME:R-CEL-9768919",
"REACTOME:R-DME-1234158",
"REACTOME:R-DME-1234176",
"REACTOME:R-DME-211945",
"REACTOME:R-DME-418555",
"REACTOME:R-DME-432395",
"REACTOME:R-DME-432408",
"REACTOME:R-... | 128 | [
"1d06",
"1d7e",
"1dp6",
"1dp8",
"1dp9",
"1drm",
"1ew0",
"1f98",
"1f9i",
"1gsv",
"1gsw",
"1gsx",
"1kou",
"1lsv",
"1lsw",
"1lsx",
"1lt0",
"1mzu",
"1nwz",
"1odv",
"1ot6",
"1ot9",
"1ota",
"1otb",
"1otd",
"1ote",
"1oti",
"1s1y",
"1s1z",
"1s4r",
"1s4s",
"1t18"... | 208 | [
"PUB00005472",
"PUB00014500",
"PUB00014501",
"PUB00015791"
] | [
"9301332",
"15009198",
"12377121",
"10357859"
] | [
"PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox.",
"The PAS fold. A redefinition of the PAS domain based upon structural prediction.",
"Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation.",
"PAS domains: internal sensors of oxyg... | [
1997,
2004,
2002,
1999
] | 4 | [
"IPR000014"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4767,
114657,
43037,
7,
1411
] | 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",... | [
114,
5,
107,
29,
7,
80,
71,
1,
43,
84,
72
] | 11 | true | Domain | PAS fold | PAS fold | PAS_fold | 4 |
IPR013768 | 13,768 | Intercellular adhesion molecule, N-terminal | ICAM_N | Domain | 2,703 | false | false | Intercellular adhesion molecules (ICAMs) and vascular cell adhesion molecule-1 (VCAM-1) are part of the immunoglobulin superfamily. They are important in inflammation, immune responses and in intracellular signalling events [ ]. The ICAM family consists of five members, designated ICAM-1 to ICAM-5. They are known to bi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03921"
] | [
"ICAM_N"
] | [
2703
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CFA-198933",
"R-CFA-216083",
"R-HSA-198933",
"R-HSA-216083",
"R-HSA-5621575",
"R-HSA-6783783",
"R-HSA-6785807",
"R-HSA-877300",
"R-MMU-198933",
"R-MMU-216083",
"R-MMU-5621575",
"R-RNO-198933",
"R-RNO-216083"
] | [
"REACTOME:R-CFA-198933",
"REACTOME:R-CFA-216083",
"REACTOME:R-HSA-198933",
"REACTOME:R-HSA-216083",
"REACTOME:R-HSA-5621575",
"REACTOME:R-HSA-6783783",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-877300",
"REACTOME:R-MMU-198933",
"REACTOME:R-MMU-216083",
"REACTOME:R-MMU-5621575",
"REACTOME:R-RNO... | 13 | [
"1d3e",
"1d3i",
"1d3l",
"1iam",
"1ic1",
"1mq8",
"1t0p",
"1z7z",
"1zxq",
"3bn3",
"3tcx",
"4oi9",
"4oia",
"4oib",
"5mza",
"6eit",
"6s8u",
"7bg7"
] | 18 | [
"PUB00007637",
"PUB00007638",
"PUB00007639",
"PUB00007640",
"PUB00007641",
"PUB00007642",
"PUB00009398",
"PUB00009399",
"PUB00009400"
] | [
"10352278",
"10725740",
"10846180",
"10741396",
"11133225",
"7531291",
"9151947",
"10998349",
"9539703"
] | [
"ICAM-2 and a peptide from its binding domain are efficient activators of leukocyte adhesion and integrin affinity.",
"Shear and time-dependent changes in Mac-1, LFA-1, and ICAM-3 binding regulate neutrophil homotypic adhesion.",
"Binding sites of leukocyte beta 2 integrins (LFA-1, Mac-1) on the human ICAM-4/LW... | [
1999,
2000,
2000,
2000,
2001,
1995,
1997,
2000,
1998
] | 9 | [] | [] | 0 | 0 | null | [
"Gnathostomata",
"Leptospira"
] | [
2701,
2
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
29,
24,
17
] | 4 | true | Domain | Intercellular adhesion molecule, N-terminal | Intercellular adhesion molecule, N-terminal | ICAM_N | 8 |
IPR013769 | 13,769 | Band 3 cytoplasmic domain | Band3_cytoplasmic_dom | Domain | 21,913 | false | false | This entry contains the cytoplasmic domain of the Band 3 anion exchange proteins that exchange Cl-/HCO3-. Band 3 constitutes the most abundant polypeptide in the red blood cell membrane, comprising 25% of the total membrane protein. The cytoplasmic domain of band 3 functions primarily as an anchoring site for other mem... | [
"GO:0008509",
"GO:0006820",
"GO:0016020"
] | [
"monoatomic anion transmembrane transporter activity",
"monoatomic anion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF07565"
] | [
"Band_3_cyto"
] | [
21913
] | 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-425381",
"R-HSA-1237044",
"R-HSA-1247673",
"R-HSA-425381",
"R-HSA-5619050",
"R-HSA-5619054",
"R-HSA-9013405",
"R-HSA-9013406",
"R-HSA-9013407",
"R-HSA-9013409",
"R-HSA-9035034",
"R-HSA-9925563",
"R-MMU-1237044",
"R-MMU-1247673",
"R-MMU-425381",
"R-MMU-9013405",
"R-MMU-9013406"... | [
"REACTOME:R-BTA-425381",
"REACTOME:R-HSA-1237044",
"REACTOME:R-HSA-1247673",
"REACTOME:R-HSA-425381",
"REACTOME:R-HSA-5619050",
"REACTOME:R-HSA-5619054",
"REACTOME:R-HSA-9013405",
"REACTOME:R-HSA-9013406",
"REACTOME:R-HSA-9013407",
"REACTOME:R-HSA-9013409",
"REACTOME:R-HSA-9035034",
"REACTOME:... | 26 | [
"1hyn",
"4ky9",
"4yzf",
"5jho",
"6caa",
"7tvz",
"7tw0",
"7tw1",
"7tw2",
"7tw3",
"7tw5",
"7tw6",
"7ty4",
"7ty6",
"7ty7",
"7ty8",
"7tya",
"7uz3",
"7uzu",
"7uzv",
"7v07",
"7v0k",
"7v0m",
"7v0t",
"7v0u",
"7v0y",
"7v19",
"8crq",
"8crr",
"8crt",
"8cs9",
"8csl"... | 58 | [
"PUB00014719"
] | [
"11049968"
] | [
"Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
21912,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
118,
21,
47,
78,
70
] | 6 | true | Domain | Band 3 cytoplasmic domain | Band 3 cytoplasmic domain | Band3_cytoplasmic_dom | 4 |
IPR013776 | 13,776 | Alpha-amylase, thermostable | A-amylase_thermo | Family | 5,746 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005509",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"calcium ion binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF001021"
] | [
"Alph-amls_thrmst"
] | [
5746
] | 1 | [
"EC"
] | [
"3.2.1.1"
] | [
"EC:3.2.1.1"
] | 1 | [
"1bli",
"1e3x",
"1e3z",
"1e40",
"1e43",
"1hvx",
"1mwo",
"1mxd",
"1mxg",
"1ob0",
"1ud2",
"1ud3",
"1ud4",
"1ud5",
"1ud6",
"1ud8",
"1vjs",
"1w9x",
"1wp6",
"1wpc",
"2d3l",
"2d3n",
"2die",
"2gjp",
"2gjr",
"3bh4",
"3qgv",
"4uzu",
"6ag0",
"6gxv",
"6gya",
"6toy"... | 39 | [
"PUB00004870",
"PUB00005266",
"PUB00016829",
"PUB00016862",
"PUB00027666",
"PUB00027689"
] | [
"7624375",
"8535779",
"15274613",
"12915728",
"11141191",
"15990960"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Structural stability and unfolding properties of thermostable bacterial alpha-amylases: a comparative study of homologous enzymes.",
"Alpha-am... | [
1995,
1995,
2004,
2003,
2001,
2005
] | 6 | [
"IPR006046"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Siphoviridae sp. ctYaH2",
"unclassified sequences"
] | [
4237,
1438,
64,
1,
6
] | 5 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1,
1
] | 2 | true | Family | Alpha-amylase, thermostable | Alpha-amylase, thermostable | A-amylase_thermo | 8 |
IPR013777 | 13,777 | Alpha-amylase-like | A-amylase-like | Family | 3,025 | false | false | This entry includes alpha-amylases and related proteins [ , ]. Alpha-amylase is classified as family 13 ( ) of the glycosyl hydrolases and is present in archaea, bacteria, fungi, plants and animals. Alpha-amylase is an essential enzyme in alpha-glucan metabolism, acting to catalyse the hydrolysis of alpha-1,4-glucosidi... | [
"GO:0004556",
"GO:0005509",
"GO:0005975"
] | [
"alpha-amylase activity",
"calcium ion binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF001024"
] | [
"Alph-amyl_fung"
] | [
3025
] | 1 | [
"EC"
] | [
"3.2.1.1"
] | [
"EC:3.2.1.1"
] | 1 | [
"2aaa",
"2guy",
"2gvy",
"2taa",
"3kwx",
"3vm7",
"3vx0",
"3vx1",
"4e2o",
"5a2a",
"5a2b",
"5a2c",
"6sao",
"6sau",
"6sav",
"6taa",
"6wni",
"6wnu",
"6xsj",
"6xsv",
"6yq7",
"6yq9",
"6yqa",
"6yqb",
"6yqc",
"7p4w",
"7taa"
] | 27 | [
"PUB00000325",
"PUB00004870",
"PUB00005266",
"PUB00027666",
"PUB00027691"
] | [
"2207069",
"7624375",
"8535779",
"11141191",
"9283074"
] | [
"Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Evolution of alpha-amyla... | [
1990,
1995,
1995,
2001,
1997
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanolobus sediminis"
] | [
452,
2572,
1
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
5
] | 2 | true | Family | Alpha-amylase-like | Alpha-amylase-like | A-amylase-like | 4 |
IPR013783 | 13,783 | Immunoglobulin-like fold | Ig-like_fold | Homologous_superfamily | 1,992,832 | false | false | This superfamily represents domains with an immunoglobulin-like (Ig-like) fold, which consists of a β-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals, occurring in a variety of different proteins. These domains are of... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.40.10"
] | [
""
] | [
1992832
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-1236974",
"R-BTA-1236977",
"R-BTA-1257604",
"R-BTA-1266695",
"R-BTA-140834",
"R-BTA-163125",
"R-BTA-1632852",
"R-BTA-1660661",
"R-BTA-173736",
"R-BTA-174577",
"R-BTA-1971475",
"R-BTA-198933",
"R-BTA-2022870",
"R-BTA-2022923",
"R-BTA-2024101",
"R-BTA-202424",
... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1236974",
"REACTOME:R-BTA-1236977",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-140834",
"REACTOME:R-BTA-163125",
"REACTOME:R-BTA-1632852",
"REACTOME:R-BTA-1660661",
"REACTOME:R-BTA-173736",
"REACTOME:R-BTA-174577",
"REACTOME:R-B... | 1,752 | [
"12e8",
"15c8",
"1a02",
"1a0q",
"1a14",
"1a1m",
"1a1n",
"1a1o",
"1a21",
"1a22",
"1a2y",
"1a3l",
"1a3q",
"1a3r",
"1a47",
"1a4j",
"1a4k",
"1a5f",
"1a64",
"1a6a",
"1a6p",
"1a6t",
"1a6u",
"1a6v",
"1a6w",
"1a6z",
"1a7b",
"1a7n",
"1a7o",
"1a7p",
"1a7q",
"1a7r"... | 16,402 | [
"PUB00003330",
"PUB00015110",
"PUB00018310",
"PUB00027656",
"PUB00027700"
] | [
"7932691",
"15327963",
"10436082",
"10698639",
"7994575"
] | [
"The immunoglobulin fold. Structural classification, sequence patterns and common core.",
"Protein--protein recognition: juxtaposition of domain and interface cores in immunoglobulins and other sandwich-like proteins.",
"The immunoglobulin fold family: sequence analysis and 3D structure comparisons.",
"Immuno... | [
1994,
2004,
1999,
2000,
1994
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
16509,
605160,
1353202,
7144,
10817
] | 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",... | [
334,
384,
5622,
964,
26,
39600,
4673,
34,
251,
4310,
15,
7,
655
] | 13 | true | Homologous_superfamily | Immunoglobulin-like fold | Immunoglobulin-like fold | Ig-like_fold | 1 |
IPR013784 | 13,784 | Carbohydrate-binding-like fold | Carb-bd-like_fold | Homologous_superfamily | 60,772 | false | false | This superfamily represents domains with a carbohydrate-binding-like fold, which consists of a seven-stranded β-sandwich with a Greek key topology, although some members may have 1-2 extra strands. These domains are present as carbohydrate-binding modules in a number of glycosyl hydrolases, often at the C-terminal end,... | [
"GO:0030246"
] | [
"carbohydrate binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF49452"
] | [
""
] | [
60772
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1483115",
"R-HSA-1483152",
"R-HSA-3322077",
"R-HSA-3785653",
"R-HSA-6798695",
"R-HSA-8980692",
"R-HSA-9013404",
"R-HSA-9013405",
"R-HSA-9013408",
"R-HSA-9013423",
"R-MMU-6798695",
"R-MMU-8980692",
"R-MMU-9013404",
"R-MMU-9013405",
"R-MMU-9013408",
"R-MMU-9013423",
"R-RNO-67986... | [
"REACTOME:R-HSA-1483115",
"REACTOME:R-HSA-1483152",
"REACTOME:R-HSA-3322077",
"REACTOME:R-HSA-3785653",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-9013404",
"REACTOME:R-HSA-9013405",
"REACTOME:R-HSA-9013408",
"REACTOME:R-HSA-9013423",
"REACTOME:R-MMU-6798695",
"REACTOM... | 21 | [
"1a47",
"1ac0",
"1acz",
"1cdg",
"1cgt",
"1cgu",
"1cgv",
"1cgw",
"1cgx",
"1cgy",
"1ciu",
"1cqy",
"1cxe",
"1cxf",
"1cxh",
"1cxi",
"1cxk",
"1cxl",
"1cyg",
"1d3c",
"1d7f",
"1ded",
"1dtu",
"1eo5",
"1eo7",
"1gcy",
"1i75",
"1kck",
"1kcl",
"1kul",
"1kum",
"1nkg"... | 115 | [
"PUB00021848",
"PUB00027701"
] | [
"12741813",
"15135077"
] | [
"Crystal structure of a catalytic site mutant of beta-amylase from Bacillus cereus var. mycoides cocrystallized with maltopentaose.",
"Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4."
] | [
2003,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
703,
33756,
25675,
9,
629
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
79,
2,
17,
20,
24,
13,
4,
43,
17,
85
] | 10 | true | Homologous_superfamily | Carbohydrate-binding-like fold | Carbohydrate-binding-like fold | Carb-bd-like_fold | 6 |
IPR013785 | 13,785 | Aldolase-type TIM barrel | Aldolase_TIM | Homologous_superfamily | 1,728,958 | false | false | This entry represents the TIM β/α barrel found in aldolase and in related proteins. This TIM barrel usually covers the entire protein structure. Proteins containing this TIM barrel domain include class I aldolases, class I DAHP synthases, class II fructose-bisphosphate aldolases (FBP aldolases), and 5-aminolevulinate d... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.20.20.70"
] | [
""
] | [
1728958
] | 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-189451",
"R-BTA-196780",
"R-BTA-2142845",
"R-BTA-2160916",
"R-BTA-389661",
"R-BTA-390918",
"R-BTA-4085001",
"R-BTA-6798695",
"R-BTA-70263",
"R-BTA-70268",
"R-BTA-71336",
"R-BTA-73817",
"R-BTA-77111",
"R-BTA-9033241",
"R-BTA-947581",
"R-BTA-9748787",
"R-BTA-9857492",
"R-CEL-1... | [
"REACTOME:R-BTA-189451",
"REACTOME:R-BTA-196780",
"REACTOME:R-BTA-2142845",
"REACTOME:R-BTA-2160916",
"REACTOME:R-BTA-389661",
"REACTOME:R-BTA-390918",
"REACTOME:R-BTA-4085001",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70263",
"REACTOME:R-BTA-70268",
"REACTOME:R-BTA-71336",
"REACTOME:R-BTA-73... | 219 | [
"1a50",
"1a53",
"1a5a",
"1a5b",
"1a5c",
"1a5s",
"1ado",
"1ag1",
"1ak5",
"1al7",
"1al8",
"1ald",
"1amk",
"1aw1",
"1aw2",
"1aw5",
"1b3o",
"1b4e",
"1b4k",
"1b57",
"1b9b",
"1beu",
"1bks",
"1btm",
"1bwk",
"1bwl",
"1c29",
"1c8v",
"1c9d",
"1ci1",
"1cw2",
"1cx9"... | 3,695 | [
"PUB00023436",
"PUB00027702",
"PUB00027703"
] | [
"9406553",
"12741828",
"15476818"
] | [
"X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase.",
"Quaternary structure of aldolase leads to differences in its folding and unfolding intermediates.",
"Analysis of the class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase at 0.99A ... | [
1997,
2003,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"other sequences",
"unclassified sequences"
] | [
39296,
1350542,
306481,
2067,
8,
30564
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
474,
44,
119,
62,
74,
293,
163,
65,
338,
248,
45,
34,
995
] | 13 | true | Homologous_superfamily | Aldolase-type TIM barrel | Aldolase-type TIM barrel | Aldolase_TIM | 2 |
IPR013786 | 13,786 | Acyl-CoA dehydrogenase/oxidase, N-terminal | AcylCoA_DH/ox_N | Domain | 292,335 | false | false | This entry represents the N-terminal α-helical domain found in medium chain acyl-CoA dehydrogenases, as well as in the related peroxisomal acyl-CoA oxidase-II enzymes. Acyl-CoA oxidase (ACO; ) catalyses the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids [ ]. Acyl-CoA dehydrogenases ( )... | [
"GO:0016627",
"GO:0050660"
] | [
"oxidoreductase activity, acting on the CH-CH group of donors",
"flavin adenine dinucleotide binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF02771"
] | [
"Acyl-CoA_dh_N"
] | [
292335
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"1.3.8",
"GenProp1510",
"GenProp1533",
"GenProp1562",
"GenProp1572",
"GenProp1673",
"GenProp1717",
"R-BTA-70895",
"R-BTA-71064",
"R-BTA-77288",
"R-BTA-77305",
"R-BTA-77346",
"R-BTA-77348",
"R-BTA-9837999",
"R-CEL-71064",
"R-DDI-70895",
"R-DDI-71064",
"R-DDI-9837999",
"R-DME-77288... | [
"EC:1.3.8",
"GP:GenProp1510",
"GP:GenProp1533",
"GP:GenProp1562",
"GP:GenProp1572",
"GP:GenProp1673",
"GP:GenProp1717",
"REACTOME:R-BTA-70895",
"REACTOME:R-BTA-71064",
"REACTOME:R-BTA-77288",
"REACTOME:R-BTA-77305",
"REACTOME:R-BTA-77346",
"REACTOME:R-BTA-77348",
"REACTOME:R-BTA-9837999",
... | 67 | [
"1buc",
"1egc",
"1egd",
"1ege",
"1ivh",
"1jqi",
"1r2j",
"1rx0",
"1siq",
"1sir",
"1t9g",
"1udy",
"1ukw",
"1ws9",
"2a1t",
"2c0u",
"2c12",
"2cx9",
"2d29",
"2dvl",
"2eba",
"2ix5",
"2ix6",
"2jbr",
"2jbs",
"2jbt",
"2jif",
"2pg0",
"2r0m",
"2r0n",
"2reh",
"2rfq"... | 152 | [
"PUB00013228",
"PUB00013229",
"PUB00026133",
"PUB00032141"
] | [
"11812788",
"9214289",
"11872165",
"15581893"
] | [
"Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.",
"Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.",
"Three-dimensional structure of the flavoenzyme acyl-... | [
2002,
1997,
2002,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
3539,
244646,
40296,
3,
4,
3847
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
10,
21,
16,
12,
3,
106,
34,
8,
8,
51,
38
] | 11 | true | Domain | Acyl-CoA dehydrogenase/oxidase, N-terminal | Acyl-CoA dehydrogenase/oxidase, N-terminal | AcylCoA_DH/ox_N | 5 |
IPR013788 | 13,788 | Hemocyanin/hexamerin | Hemocyanin/hexamerin | Family | 5,125 | false | false | Crustacean and cheliceratan hemocyanins (oxygen-transport proteins) and insect hexamerins (storage proteins) are homologous gene products, although the latter do not bind oxygen [ ]. Haemocyanins are found in the haemolymph of many invertebrates. They are divided into 2 main groups, arthropodan and molluscan. These hav... | [] | [] | [] | 0 | [
"PRINTS",
"PROSITE",
"PROSITE",
"PANTHER"
] | [
"PR00187",
"PS00209",
"PS00210",
"PTHR11511"
] | [
"HAEMOCYANIN",
"HEMOCYANIN_1",
"HEMOCYANIN_2",
""
] | [
3492,
1986,
3565,
4557
] | 4 | [] | [] | [] | 0 | [
"1hc1",
"1hcy",
"1ll1",
"1lla",
"1nol",
"1oxy",
"2p3x",
"3gwj",
"3hhs",
"3ixv",
"3ixw",
"3wjm",
"3wky",
"4l37",
"4yzw",
"5yy2",
"5yy3",
"6l8s",
"7ze1",
"8ca9",
"8cad",
"8can",
"8ji8",
"8jib",
"8po9"
] | 25 | [
"PUB00000297",
"PUB00059233",
"PUB00082624",
"PUB00100820"
] | [
"3207675",
"8015442",
"25251934",
"25859931"
] | [
"cDNA cloning of the Octopus dofleini hemocyanin: sequence of the carboxyl-terminal domain.",
"Evolution of arthropod hemocyanins and insect storage proteins (hexamerins).",
"Non-heme dioxygenase catalyzes atypical oxidations of 6,7-bicyclic systems to form the 6,6-quinolone core of viridicatin-type fungal alka... | [
1988,
1994,
2014,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
223,
4892,
10
] | 3 | [
"Caenorhabditis elegans",
"Drosophila melanogaster",
"Zea mays"
] | [
1,
20,
3
] | 3 | true | Family | Hemocyanin/hexamerin | Hemocyanin/hexamerin | Hemocyanin/hexamerin | 7 |
IPR013789 | 13,789 | Phosphotransferase system, mannose family IIA component | PTS_EIIA_man | Domain | 3,159 | false | false | Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Man family is unique in several respects among PTS permease families: It is the only PTS family in which members possess a IID protein. It is the only PTS famil... | [
"GO:0016773",
"GO:0008643",
"GO:0005737"
] | [
"phosphotransferase activity, alcohol group as acceptor",
"carbohydrate transport",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00824"
] | [
"EIIA-man"
] | [
3159
] | 1 | [
"GP"
] | [
"GenProp0119"
] | [
"GP:GenProp0119"
] | 1 | [
"1pdo",
"1vrc",
"1vsq",
"2jzn",
"2jzo",
"6fmg"
] | 6 | [
"PUB00017927"
] | [
"8676384"
] | [
"Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 angstroms resolution."
] | [
1996
] | 1 | [
"IPR004701"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta",
"bioreactor metagenome"
] | [
3153,
3,
3
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Phosphotransferase system, mannose family IIA component | Phosphotransferase system, mannose family IIA component | PTS_EIIA_man | 2 |
IPR013790 | 13,790 | SMAD/Dwarfins | SMAD/Dwarfins | Family | 16,130 | false | false | Receptor-regulated SMAD (R-SMAD) proteins, also known as mammalian dwarfins, are intracellular signal transducers and transcriptional modulators that are phosphorylated in response to transforming growth factor-beta (TGF-β) and activin type I receptor kinases and are implicated in the control of cell growth. They bind ... | [
"GO:0006355"
] | [
"regulation of DNA-templated transcription"
] | [
"biological_process"
] | 1 | [
"PANTHER"
] | [
"PTHR13703"
] | [
""
] | [
16130
] | 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-201451",
"R-BTA-5689880",
"R-BTA-8941326",
"R-CEL-1181150",
"R-CEL-1502540",
"R-CEL-201451",
"R-CEL-2173788",
"R-CEL-2173789",
"R-CEL-2173795",
"R-CEL-2173796",
"R-CEL-5689880",
"R-CEL-8941326",
"R-CEL-8941855",
"R-CEL-9617828",
"R-DME-1181150",
"R-DME-1502540",
"R-DME-201451"... | [
"REACTOME:R-BTA-201451",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-8941326",
"REACTOME:R-CEL-1181150",
"REACTOME:R-CEL-1502540",
"REACTOME:R-CEL-201451",
"REACTOME:R-CEL-2173788",
"REACTOME:R-CEL-2173789",
"REACTOME:R-CEL-2173795",
"REACTOME:R-CEL-2173796",
"REACTOME:R-CEL-5689880",
"REACTOME:... | 98 | [
"1dd1",
"1dev",
"1g88",
"1khu",
"1khx",
"1mhd",
"1mjs",
"1mk2",
"1mr1",
"1ozj",
"1u7f",
"1u7v",
"1ygs",
"3dit",
"3gmj",
"3kmp",
"3qsv",
"5c4v",
"5mey",
"5mez",
"5mf0",
"5nm9",
"5od6",
"5odg",
"5x6g",
"5x6h",
"5x6m",
"5xoc",
"5xod",
"5zoj",
"5zok",
"6fzs"... | 41 | [
"PUB00004255",
"PUB00004902",
"PUB00017916",
"PUB00019858",
"PUB00097244",
"PUB00097246",
"PUB00097247",
"PUB00097248",
"PUB00097273",
"PUB00157972"
] | [
"9230443",
"8799132",
"14631647",
"11532220",
"19218245",
"22359515",
"10625546",
"1408209",
"17507407",
"8752209"
] | [
"Drosophila Mad binds to DNA and directly mediates activation of vestigial by Decapentaplegic.",
"Mammalian dwarfins are phosphorylated in response to transforming growth factor beta and are implicated in control of cell growth.",
"Relationship between the DNA binding domains of SMAD and NFI/CTF transcription f... | [
1997,
1996,
2003,
2001,
2009,
2012,
2000,
1992,
2007,
1996
] | 10 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
16126,
4
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
27,
10,
72,
34,
43
] | 6 | true | Family | SMAD/Dwarfins | SMAD/Dwarfins | SMAD/Dwarfins | 6 |
IPR013791 | 13,791 | RNA 3'-terminal phosphate cyclase, insert domain | RNA3'-term_phos_cycl_insert | Domain | 8,749 | false | false | RNA cyclases are a family of RNA-modifying enzymes that are conserved in eukaryotes, bacteria and archaea. RNA 3'-terminal phosphate cyclase ( ) [ , ] catalyses the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyc... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF05189"
] | [
"RTC_insert"
] | [
8749
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.5.1.4",
"R-BTA-6791226",
"R-CEL-6791226",
"R-DDI-6791226",
"R-DME-6791226",
"R-HSA-6790901",
"R-HSA-6791226",
"R-MMU-6791226",
"R-SCE-6791226",
"R-SPO-6791226"
] | [
"EC:6.5.1.4",
"REACTOME:R-BTA-6791226",
"REACTOME:R-CEL-6791226",
"REACTOME:R-DDI-6791226",
"REACTOME:R-DME-6791226",
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-6791226",
"REACTOME:R-SCE-6791226",
"REACTOME:R-SPO-6791226"
] | 10 | [
"1qmh",
"1qmi",
"3kgd",
"3pqv",
"3tut",
"3tux",
"3tv1",
"3tw3",
"4clq",
"4o89",
"4o8j",
"5jpq",
"5oql",
"5tzs",
"5wlc",
"5wyj",
"5wyk",
"6ke6",
"6lqp",
"6lqq",
"6lqr",
"6lqs",
"6lqt",
"6lqu",
"6lqv",
"6rxt",
"6rxu",
"6rxv",
"6rxx",
"6rxy",
"6rxz",
"6zqa"... | 65 | [
"PUB00001300",
"PUB00003565",
"PUB00006476"
] | [
"9184239",
"2199762",
"10673421"
] | [
"The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea.",
"RNA 3'-terminal phosphate cyclase from HeLa cells.",
"Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology."
] | [
1997,
1990,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
607,
1697,
6417,
28
] | 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",... | [
5,
1,
2,
3,
1,
5,
9,
1,
3,
10,
1,
1,
6
] | 13 | true | Domain | RNA 3'-terminal phosphate cyclase, insert domain | RNA 3'-terminal phosphate cyclase, insert domain | RNA3'-term_phos_cycl_insert | 4 |
IPR013792 | 13,792 | RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta | RNA3'P_cycl/enolpyr_Trfase_a/b | Homologous_superfamily | 77,275 | false | false | This superfamily represents an α/β domain consisting of alternating β-strands and α helices in two layer. This domain is found in RNA 3'-terminal phosphate cyclase (RPTC), where it occurs as a duplication of three repeats of this fold packed together around a pseudo three-fold axis [ ]. RNA cyclases are a family of RNA... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF55205"
] | [
""
] | [
77275
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.5.1",
"R-BTA-5689880",
"R-BTA-6791226",
"R-CEL-6791226",
"R-DDI-6791226",
"R-DME-6791226",
"R-HSA-2173788",
"R-HSA-5689603",
"R-HSA-5689880",
"R-HSA-6790901",
"R-HSA-6791226",
"R-MMU-5689880",
"R-MMU-6791226",
"R-MTU-964903",
"R-RNO-5689880",
"R-SCE-6791226",
"R-SPO-6791226"
] | [
"EC:2.5.1",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-6791226",
"REACTOME:R-CEL-6791226",
"REACTOME:R-DDI-6791226",
"REACTOME:R-DME-6791226",
"REACTOME:R-HSA-2173788",
"REACTOME:R-HSA-5689603",
"REACTOME:R-HSA-5689880",
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-568988... | 17 | [
"1a2n",
"1dlg",
"1ejc",
"1ejd",
"1eps",
"1eyn",
"1g6s",
"1g6t",
"1mi4",
"1naw",
"1p88",
"1p89",
"1q36",
"1q3g",
"1qmh",
"1qmi",
"1rf4",
"1rf5",
"1rf6",
"1ryw",
"1uae",
"1x8r",
"1x8t",
"1ybg",
"2aa9",
"2aay",
"2bjb",
"2gg4",
"2gg6",
"2gga",
"2ggd",
"2o0b"... | 188 | [
"PUB00006476",
"PUB00028019",
"PUB00028020"
] | [
"10673421",
"9485407",
"15995357"
] | [
"Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology.",
"Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound ... | [
2000,
1998,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1529,
61624,
12522,
2,
1598
] | 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,
3,
9,
13,
4,
9,
16,
3,
2,
19
] | 13 | true | Homologous_superfamily | RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta | RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta | RNA3'P_cycl/enolpyr_Trfase_a/b | 8 |
IPR013793 | 13,793 | Porin, Gram-negative type, conserved site | Porin_Gram-ve_CS | Conserved_site | 7,188 | false | false | Porins are found in the outer membranes of Gram-negative bacteria, mitochondria and chloroplasts, where they form ion-selective channels for small hydrophilic molecules (up to ~600 D) [ , ]. X-ray structure analyses of several bacterial porins [ , , ] have revealed a large 16-stranded anti-parallel β-barrel structure e... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00576"
] | [
"GRAM_NEG_PORIN"
] | [
7188
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00498",
"R-HSA-1236974",
"R-HSA-166058",
"R-HSA-168179",
"R-HSA-3000484",
"R-HSA-5602498",
"R-HSA-5603041"
] | [
"PROSITEDOC:PDOC00498",
"REACTOME:R-HSA-1236974",
"REACTOME:R-HSA-166058",
"REACTOME:R-HSA-168179",
"REACTOME:R-HSA-3000484",
"REACTOME:R-HSA-5602498",
"REACTOME:R-HSA-5603041"
] | 7 | [
"1bt9",
"1gfm",
"1gfn",
"1gfo",
"1gfp",
"1gfq",
"1hxt",
"1hxu",
"1hxx",
"1mpf",
"1opf",
"1osm",
"1pho",
"2j1n",
"2j4u",
"2omf",
"2xe1",
"2xe2",
"2xe3",
"2xe5",
"2xg6",
"2zfg",
"2zld",
"2zle",
"3a2s",
"3fyx",
"3hw9",
"3hwb",
"3k19",
"3k1b",
"3nb3",
"3nsg"... | 99 | [
"PUB00001604",
"PUB00003334",
"PUB00003475",
"PUB00003829",
"PUB00005073"
] | [
"1707373",
"7525973",
"1725488",
"1373213",
"2178269"
] | [
"The structure of porin from Rhodobacter capsulatus at 1.8 A resolution.",
"Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus.",
"A common channel-forming motif in evolutionarily distant porins.",
"Porins and specific channels of bacterial out... | [
1991,
1994,
1991,
1992,
1990
] | 5 | [] | [] | 0 | 0 | null | [
"Acidiplasma",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
2,
7165,
9,
8,
4
] | 5 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Conserved_site | Porin, Gram-negative type, conserved site | Porin, Gram-negative type, conserved site | Porin_Gram-ve_CS | 9 |
IPR013795 | 13,795 | DNA/RNA-binding protein Alba | DNA/RNA-bd_Alba | Family | 732 | false | false | The DNA/RNA-binding protein Alba binds double-stranded DNA tightly but without sequence specificity. It binds rRNA and mRNA in vivo, and may play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes. It is distributed uniformly and abundantly on the chromosome. Alba has been sho... | [
"GO:0003677",
"GO:0003723"
] | [
"DNA binding",
"RNA binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"HAMAP",
"PIRSF",
"NCBIFAM"
] | [
"MF_01122",
"PIRSF028732",
"TIGR00285"
] | [
"AlbA",
"Alba",
""
] | [
721,
639,
535
] | 3 | [] | [] | [] | 0 | [
"1h0x",
"1h0y",
"1nfh",
"1nfj",
"1nh9",
"1udv",
"1y9x",
"2a2y",
"2bky",
"2h9u",
"2z7c",
"3toe",
"3u6y",
"3wbm",
"4z9e",
"8xao",
"8xap",
"8xaq"
] | 18 | [
"PUB00015328",
"PUB00028062"
] | [
"10869069",
"16256418"
] | [
"An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion.",
"Archaeal chromatin proteins: different structures but common function?"
] | [
2000,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Geodia barretti",
"candidate division WOR-3 bacterium",
"unclassified sequences"
] | [
679,
1,
1,
51
] | 4 | [] | [] | 0 | true | Family | DNA/RNA-binding protein Alba | DNA/RNA-binding protein Alba | DNA/RNA-bd_Alba | 4 |
IPR013797 | 13,797 | Maltooligosyl trehalose synthase, domain 4 | Maltooligo_trehalose_synth_4 | Homologous_superfamily | 6,359 | false | false | Maltooligosyl trehalose synthase ( ) is one of two enzymes in the coupled trehalose biosynthesis system in the archaea Sulfolobus acidocaldarius [ , ]. This enzyme catalyses the conversion of maltopentaose to maltotriosyltrehalose, which is further hydrolysed by maltooligosyl trehalose trehalohydrolase to produce treha... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.10.470"
] | [
""
] | [
6359
] | 1 | [
"EC",
"METACYC",
"REACTOME"
] | [
"5.4.99.15",
"PWY-2661",
"R-MTU-868688"
] | [
"EC:5.4.99.15",
"METACYC:PWY-2661",
"REACTOME:R-MTU-868688"
] | 3 | [
"1iv8",
"6lcu",
"6lcv"
] | 3 | [
"PUB00035953",
"PUB00035954",
"PUB00097586"
] | [
"10089339",
"11164309",
"30387780"
] | [
"Crystallization and improvement of crystal quality for x-ray diffraction of maltooligosyl trehalose synthase by reductive methylation of lysine residues.",
"Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius.",
"Crystal structure of glycosyltrehalo... | [
1999,
2001,
2018
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
26,
6315,
10,
8
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Maltooligosyl trehalose synthase, domain 4 | Maltooligosyl trehalose synthase, domain 4 | Maltooligo_trehalose_synth_4 | 1 |
IPR013798 | 13,798 | Indole-3-glycerol phosphate synthase domain | Indole-3-glycerol_P_synth_dom | Domain | 29,898 | false | false | Indole-3-glycerol phosphate synthase ( ) (IGPS) catalyses the fourth step in the biosynthesis of tryptophan, the ring closure of 1-(2-carboxy-phenylamino)-1-deoxyribulose into indol-3-glycerol-phosphate. In some bacteria, IGPS is a single chain enzyme. In others, such as Escherichia coli, it is the N-terminal domain of... | [
"GO:0004425"
] | [
"indole-3-glycerol-phosphate synthase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"HAMAP",
"PFAM",
"CDD"
] | [
"MF_00134_A",
"MF_00134_B",
"PF00218",
"cd00331"
] | [
"IGPS_A",
"IGPS_B",
"IGPS",
"IGPS"
] | [
3984,
21986,
29896,
28734
] | 4 | [
"EC",
"GP",
"GP"
] | [
"4.1.1.48",
"GenProp0037",
"GenProp1450"
] | [
"EC:4.1.1.48",
"GP:GenProp0037",
"GP:GenProp1450"
] | 3 | [
"1a53",
"1i4n",
"1igs",
"1j5t",
"1jcm",
"1juk",
"1jul",
"1lbf",
"1lbl",
"1pii",
"1vc4",
"2c3z",
"3hoj",
"3nxf",
"3nyz",
"3nz1",
"3o6y",
"3qja",
"3t40",
"3t44",
"3t55",
"3t78",
"3tc6",
"3tc7",
"3tsm",
"3ud6",
"3uxa",
"3uxd",
"3uy7",
"3uy8",
"3uyc",
"3uz5"... | 66 | [
"PUB00007146"
] | [
"8747452"
] | [
"How to make my blood boil."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
784,
24813,
3735,
566
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
11,
1,
1,
12,
1,
1,
17
] | 7 | true | Domain | Indole-3-glycerol phosphate synthase domain | Indole-3-glycerol phosphate synthase domain | Indole-3-glycerol_P_synth_dom | 4 |
IPR013799 | 13,799 | STAT transcription factor, protein interaction | STAT_TF_prot_interaction | Domain | 9,880 | false | false | The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus ... | [
"GO:0006355",
"GO:0007165"
] | [
"regulation of DNA-templated transcription",
"signal transduction"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF02865",
"SM00964"
] | [
"STAT_int",
"STAT_int"
] | [
9759,
9728
] | 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-1251985",
"R-BTA-1266695",
"R-BTA-1433557",
"R-BTA-186763",
"R-BTA-512988",
"R-BTA-8854691",
"R-BTA-8983432",
"R-BTA-8985947",
"R-BTA-9020558",
"R-BTA-9020958",
"R-DME-1059683",
"R-DME-1169408",
"R-DME-1251985",
"R-DME-1433557",
"R-DME-186763",
"R-DME-201556",
"R-DME-209228",
... | [
"REACTOME:R-BTA-1251985",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-186763",
"REACTOME:R-BTA-512988",
"REACTOME:R-BTA-8854691",
"REACTOME:R-BTA-8983432",
"REACTOME:R-BTA-8985947",
"REACTOME:R-BTA-9020558",
"REACTOME:R-BTA-9020958",
"REACTOME:R-DME-1059683",
"REACTOME:... | 193 | [
"1bgf",
"1yvl",
"3wwt",
"4zia",
"6ux2",
"6wcz",
"7zn7",
"7znn",
"8t12",
"8t13",
"8yyu",
"8yyv"
] | 12 | [
"PUB00007134",
"PUB00011807",
"PUB00032712",
"PUB00051157"
] | [
"12039028",
"9630226",
"15780933",
"18433722"
] | [
"Signaling through the JAK/STAT pathway, recent advances and future challenges.",
"Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.",
"Structural bases of unphosphorylated STAT1 association and receptor binding.",
"Crystal structure of unphosphorylated STAT3 core fragment."
] | [
2002,
1998,
2005,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9880
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
29,
4,
115,
35,
30
] | 5 | true | Domain | STAT transcription factor, protein interaction | STAT transcription factor, protein interaction | STAT_TF_prot_interaction | 6 |
IPR013800 | 13,800 | STAT transcription factor, all-alpha domain | STAT_TF_alpha | Domain | 10,491 | false | false | This entry represents the all-α helical domain of animal STAT transcription factors, which consists of four long helices arranged in a bundle with a left-handed twist (coiled-coil), which in turn forms a right-handed superhelix. The STAT protein (Signal Transducers and Activators of Transcription) family contains trans... | [
"GO:0006355",
"GO:0007165"
] | [
"regulation of DNA-templated transcription",
"signal transduction"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01017"
] | [
"STAT_alpha"
] | [
10491
] | 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-1251985",
"R-BTA-1266695",
"R-BTA-1433557",
"R-BTA-186763",
"R-BTA-512988",
"R-BTA-8854691",
"R-BTA-8983432",
"R-BTA-8985947",
"R-BTA-9020558",
"R-BTA-9020958",
"R-CEL-1059683",
"R-CEL-1169408",
"R-CEL-1251985",
"R-CEL-186763",
"R-CEL-201556",
"R-CEL-3249367",
"R-CEL-6783783",... | [
"REACTOME:R-BTA-1251985",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-186763",
"REACTOME:R-BTA-512988",
"REACTOME:R-BTA-8854691",
"REACTOME:R-BTA-8983432",
"REACTOME:R-BTA-8985947",
"REACTOME:R-BTA-9020558",
"REACTOME:R-BTA-9020958",
"REACTOME:R-CEL-1059683",
"REACTOME:... | 216 | [
"1bf5",
"1bg1",
"1y1u",
"1yvl",
"3cwg",
"4e68",
"4y5u",
"4y5w",
"5d39",
"5oen",
"6mbw",
"6mbz",
"6njs",
"6nuq",
"6qhd",
"6tlc",
"6ux2",
"6wcz",
"7nuf",
"7tva",
"7tvb",
"7ubt",
"7uc6",
"7uc7",
"7zn7",
"7znn",
"8d3f",
"8t12",
"8t13",
"8yyu",
"8yyv",
"9big"... | 32 | [
"PUB00007134",
"PUB00011807",
"PUB00032712",
"PUB00051157"
] | [
"12039028",
"9630226",
"15780933",
"18433722"
] | [
"Signaling through the JAK/STAT pathway, recent advances and future challenges.",
"Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.",
"Structural bases of unphosphorylated STAT1 association and receptor binding.",
"Crystal structure of unphosphorylated STAT3 core fragment."
] | [
2002,
1998,
2005,
2008
] | 4 | [] | [
"IPR046991",
"IPR046994"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
2,
10488,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
29,
6,
108,
32,
31
] | 6 | true | Domain | STAT transcription factor, all-alpha domain | STAT transcription factor, all-alpha domain | STAT_TF_alpha | 3 |
IPR013801 | 13,801 | STAT transcription factor, DNA-binding | STAT_TF_DNA-bd | Domain | 10,584 | false | false | The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus ... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02864"
] | [
"STAT_bind"
] | [
10584
] | 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-1251985",
"R-BTA-1266695",
"R-BTA-1433557",
"R-BTA-186763",
"R-BTA-512988",
"R-BTA-8854691",
"R-BTA-8983432",
"R-BTA-8985947",
"R-BTA-9020558",
"R-BTA-9020958",
"R-CEL-1059683",
"R-CEL-1169408",
"R-CEL-1251985",
"R-CEL-186763",
"R-CEL-201556",
"R-CEL-3249367",
"R-CEL-6783783",... | [
"REACTOME:R-BTA-1251985",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-186763",
"REACTOME:R-BTA-512988",
"REACTOME:R-BTA-8854691",
"REACTOME:R-BTA-8983432",
"REACTOME:R-BTA-8985947",
"REACTOME:R-BTA-9020558",
"REACTOME:R-BTA-9020958",
"REACTOME:R-CEL-1059683",
"REACTOME:... | 216 | [
"1bf5",
"1bg1",
"1y1u",
"1yvl",
"3cwg",
"4e68",
"4y5u",
"4y5w",
"5d39",
"6mbw",
"6mbz",
"6njs",
"6nuq",
"6qhd",
"6tlc",
"6ux2",
"6wcz",
"7nuf",
"7tva",
"7tvb",
"7ubt",
"7uc6",
"7uc7",
"7zn7",
"7znn",
"8d3f",
"8t12",
"8t13",
"8yyu",
"8yyv",
"9big"
] | 31 | [
"PUB00007134",
"PUB00011807",
"PUB00032712",
"PUB00051157"
] | [
"12039028",
"9630226",
"15780933",
"18433722"
] | [
"Signaling through the JAK/STAT pathway, recent advances and future challenges.",
"Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.",
"Structural bases of unphosphorylated STAT1 association and receptor binding.",
"Crystal structure of unphosphorylated STAT3 core fragment."
] | [
2002,
1998,
2005,
2008
] | 4 | [] | [
"IPR029839"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
10584
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
29,
6,
101,
33,
30
] | 6 | true | Domain | STAT transcription factor, DNA-binding | STAT transcription factor, DNA-binding | STAT_TF_DNA-bd | 7 |
IPR013802 | 13,802 | Formiminotransferase, C-terminal subdomain | Formiminotransferase_C | Domain | 3,999 | false | false | The formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD) forms a homodimer, with each protomer being comprised of two subdomains. The formiminotransferase domain has an N-terminal subdomain that is made up of a six-stranded mixed β-pleated sheet and five α-helices, which are arranged on the ex... | [
"GO:0005542",
"GO:0016740"
] | [
"folic acid binding",
"transferase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF02971",
"SM01221"
] | [
"FTCD",
"FTCD"
] | [
3255,
3981
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.2.5",
"4.3.1.4",
"PWY-5030",
"PWY-5497",
"R-DDI-70921",
"R-HSA-70921",
"R-MMU-70921",
"R-RNO-70921"
] | [
"EC:2.1.2.5",
"EC:4.3.1.4",
"METACYC:PWY-5030",
"METACYC:PWY-5497",
"REACTOME:R-DDI-70921",
"REACTOME:R-HSA-70921",
"REACTOME:R-MMU-70921",
"REACTOME:R-RNO-70921"
] | 8 | [
"1qd1",
"1tt9",
"2pfd"
] | 3 | [
"PUB00007432",
"PUB00015609"
] | [
"10673422",
"12815595"
] | [
"The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.",
"The molecular basis of glutamate formiminotransferase deficiency."
] | [
2000,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
38,
1739,
2067,
155
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
8,
1,
3,
1,
3,
2,
10
] | 7 | true | Domain | Formiminotransferase, C-terminal subdomain | Formiminotransferase, C-terminal subdomain | Formiminotransferase_C | 3 |
IPR013803 | 13,803 | Amyloidogenic glycoprotein, amyloid-beta peptide | Amyloid_glyco_Abeta | Domain | 2,727 | false | false | Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [ , , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with D... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF03494",
"PR00204"
] | [
"Beta-APP",
"BETAAMYLOID"
] | [
2727,
2700
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-HSA-114608",
"R-HSA-3000178",
"R-HSA-381426",
"R-HSA-416476",
"R-HSA-418594",
"R-HSA-432720",
"R-HSA-444473",
"R-HSA-445989",
"R-HSA-844456",
"R-HSA-879415",
"R-HSA-8862803",
"R-HSA-8957275",
"R-HSA-933542",
"R-HSA-9609523",
"R-HSA-9660826",
"R-HSA-977225",
"R-HSA-9837999",
"R-M... | [
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-3000178",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-432720",
"REACTOME:R-HSA-444473",
"REACTOME:R-HSA-445989",
"REACTOME:R-HSA-844456",
"REACTOME:R-HSA-879415",
"REACTOME:R-HSA-8862803",
"REACTOME:R-HSA-8... | 54 | [
"1amb",
"1amc",
"1aml",
"1ba4",
"1ba6",
"1bjb",
"1bjc",
"1hz3",
"1iyt",
"1nmj",
"1z0q",
"2beg",
"2g47",
"2lfm",
"2llm",
"2lmn",
"2lmo",
"2lmp",
"2lmq",
"2lnq",
"2loh",
"2lp1",
"2lz3",
"2lz4",
"2m4j",
"2m9r",
"2m9s",
"2mj1",
"2mpz",
"2mvx",
"2mxu",
"2nao"... | 150 | [
"PUB00029624",
"PUB00033916",
"PUB00033917",
"PUB00033918",
"PUB00099232",
"PUB00099233"
] | [
"12611883",
"16301322",
"16406235",
"16364896",
"28713158",
"33302541"
] | [
"Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis.",
"Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging.",
"The amyloid precursor protein and postnatal neurogenesis/... | [
2003,
2006,
2006,
2005,
2017,
2020
] | 6 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
2727
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
13,
9,
6
] | 4 | true | Domain | Amyloidogenic glycoprotein, amyloid-beta peptide | Amyloidogenic glycoprotein, amyloid-beta peptide | Amyloid_glyco_Abeta | 4 |
IPR013805 | 13,805 | GrpE nucleotide exchange factor, coiled-coil | GrpE_CC | Homologous_superfamily | 35,152 | false | false | In prokaryotes, the nucleotide exchange factor GrpE and the chaperone DnaJ are required for nucleotide binding of the molecular chaperone DnaK [ ]. The DnaK reaction cycle involves rapid peptide binding and release, which is dependent upon nucleotide binding. DnaJ accelerates the hydrolysis of ATP by DnaK, which enable... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.90.20.20",
"SSF58014"
] | [
"",
""
] | [
34954,
35127
] | 2 | [
"REACTOME"
] | [
"R-HSA-1268020"
] | [
"REACTOME:R-HSA-1268020"
] | 1 | [
"1dkg",
"3a6m",
"4ani",
"8gb3",
"9bls",
"9blt",
"9blu"
] | 7 | [
"PUB00005226"
] | [
"9103205"
] | [
"Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
706,
26501,
7353,
6,
586
] | 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,
9,
11,
1,
1,
20
] | 13 | true | Homologous_superfamily | GrpE nucleotide exchange factor, coiled-coil | GrpE nucleotide exchange factor, coiled-coil | GrpE_CC | 9 |
IPR013806 | 13,806 | Kringle-like fold | Kringle-like | Homologous_superfamily | 36,468 | false | false | This entry represents proteins displaying a Kringle-like structure, which consists of a nearly all-beta, disulphide-rich fold. Proteins displaying this fold include both Kringle modules as well as fibronectin type II modules, the latter displaying a shorter two-disulphide version of the Kringle module. Kringle modules ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF57440"
] | [
""
] | [
36468
] | 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-1433557",
"R-BTA-1442490",
"R-BTA-1474228",
"R-BTA-1592389",
"R-BTA-3928665",
"R-BTA-6798695",
"R-BTA-75205",
"R-BTA-9009391",
"R-CEL-5140745",
"R-CFA-114608",
"R-CFA-1257604",
"R-CFA-5673001",
"R-CFA-6806942",
"R-CFA-6807004",
"R-CFA-6811558",
"R-CFA-8851805",
"R-CFA-8851907"... | [
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1592389",
"REACTOME:R-BTA-3928665",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-75205",
"REACTOME:R-BTA-9009391",
"REACTOME:R-CEL-5140745",
"REACTOME:R-CFA-114608",
"REACTOME:R-CFA-1257604",
"REACTOME:R... | 243 | [
"1a0h",
"1b2i",
"1bht",
"1cea",
"1ceb",
"1ck7",
"1cxw",
"1e88",
"1e8b",
"1eak",
"1gmn",
"1gmo",
"1gp9",
"1gxd",
"1h8p",
"1hpj",
"1hpk",
"1i5k",
"1i71",
"1j7m",
"1jfn",
"1kdu",
"1ki0",
"1kiv",
"1krn",
"1ks0",
"1l6j",
"1nk1",
"1nl1",
"1nl2",
"1pdc",
"1pk2"... | 174 | [
"PUB00001346",
"PUB00001541",
"PUB00003257",
"PUB00028079",
"PUB00028080"
] | [
"3780752",
"6373375",
"2157850",
"16019990",
"16085117"
] | [
"Complete primary structure of bovine plasma fibronectin.",
"Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases.",
"Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance sp... | [
1986,
1984,
1990,
2005,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mimiviridae sp. ChoanoV1",
"Pseudomonadota",
"metagenomes"
] | [
36407,
3,
49,
9
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
58,
3,
119,
86,
111
] | 6 | true | Homologous_superfamily | Kringle-like fold | Kringle-like fold | Kringle-like | 9 |
IPR013808 | 13,808 | Transglutaminase, active site | Transglutaminase_AS | Active_site | 6,675 | false | false | Transglutaminases (EC 2.3.2.13) (TGase) [ , ] are calcium-dependent enzymes that catalyze the cross-linking of proteins by promoting the formation of isopeptide bonds between the γ-carboxyl group of a glutamine in one polypeptide chain and the ε-amino group of a lysine in a second polypeptide chain. TGases also catalyz... | [
"GO:0018149"
] | [
"peptide cross-linking"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS00547"
] | [
"TRANSGLUTAMINASES"
] | [
6675
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.2.13",
"PDOC00473",
"R-HSA-114608",
"R-HSA-140875",
"R-HSA-6785807",
"R-HSA-6809371",
"R-MMU-114608",
"R-MMU-140875",
"R-MMU-6809371",
"R-RNO-114608",
"R-RNO-140875",
"R-RNO-6809371"
] | [
"EC:2.3.2.13",
"PROSITEDOC:PDOC00473",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-140875",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6809371",
"REACTOME:R-MMU-114608",
"REACTOME:R-MMU-140875",
"REACTOME:R-MMU-6809371",
"REACTOME:R-RNO-114608",
"REACTOME:R-RNO-140875",
"REACTOME:R-RNO-6809371"
] | 12 | [
"1evu",
"1ex0",
"1f13",
"1fie",
"1g0d",
"1ggt",
"1ggu",
"1ggy",
"1kv3",
"1l9m",
"1l9n",
"1nud",
"1nuf",
"1nug",
"1qrk",
"2q3z",
"3ly6",
"3s3j",
"3s3p",
"3s3s",
"4kty",
"4pyg",
"5mhl",
"5mhm",
"5mhn",
"5mho",
"6a8p",
"6kzb",
"7tvz",
"7tw0",
"7tw1",
"7tw3"... | 53 | [
"PUB00001513",
"PUB00002570",
"PUB00095165"
] | [
"1683845",
"1974250",
"19269200"
] | [
"Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues.",
"Structure of transglutaminases.",
"Protein 4.2: a complex linker."
] | [
1991,
1990,
2009
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
6675
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
34,
23,
22
] | 4 | true | Active_site | Transglutaminase, active site | Transglutaminase, active site | Transglutaminase_AS | 8 |
IPR013809 | 13,809 | ENTH domain | ENTH | Domain | 43,893 | false | false | The ENTH (Epsin N-terminal homology) domain is approximately 150 amino acids in length and is always found located at the N-termini of proteins. The domain forms a compact globular structure, composed of 9 α-helices connected by loops of varying length. The general topology is determined by three helical hairpins that ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01417",
"PS50942",
"SM00273"
] | [
"ENTH",
"ENTH",
"ENTH"
] | [
17804,
41937,
39908
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50942",
"R-CEL-432722",
"R-CEL-8856825",
"R-CEL-8856828",
"R-DDI-8856825",
"R-DME-432722",
"R-DME-8856825",
"R-DME-8856828",
"R-HSA-182971",
"R-HSA-432722",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-9696264",
"R-HSA-9700645",
"R-HSA-9725370",
"R-MMU-182971",
"R-MMU-432722",
"R-... | [
"PROSITEDOC:PDOC50942",
"REACTOME:R-CEL-432722",
"REACTOME:R-CEL-8856825",
"REACTOME:R-CEL-8856828",
"REACTOME:R-DDI-8856825",
"REACTOME:R-DME-432722",
"REACTOME:R-DME-8856825",
"REACTOME:R-DME-8856828",
"REACTOME:R-HSA-182971",
"REACTOME:R-HSA-432722",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HS... | 28 | [
"1edu",
"1eyh",
"1h0a",
"1hf8",
"1hfa",
"1hg2",
"1hg5",
"1hx8",
"1inz",
"1k4w",
"1kv6",
"1n4h",
"1pzl",
"1tfc",
"1vdy",
"1xgw",
"1xiu",
"2a4j",
"2dcp",
"2ggm",
"2hbh",
"2hc4",
"2hcd",
"2obh",
"2qy7",
"2v8s",
"3cwd",
"3dr1",
"3lmp",
"3onk",
"3onl",
"3qt0"... | 123 | [
"PUB00005059",
"PUB00007107",
"PUB00007108"
] | [
"10048338",
"11911874",
"12353027"
] | [
"Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery.",
"The ENTH domain.",
"Curvature of clathrin-coated pits driven by epsin."
] | [
1999,
2002,
2002
] | 3 | [] | [
"IPR048050"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"ecological metagenomes"
] | [
34,
43855,
2,
2
] | 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... | [
107,
6,
207,
27,
56,
46,
4,
54,
59,
8,
4,
124
] | 12 | true | Domain | ENTH domain | ENTH domain | ENTH | 6 |
IPR013810 | 13,810 | Small ribosomal subunit protein uS5, N-terminal | Ribosomal_uS5_N | Domain | 39,796 | false | false | Small ribosomal subunit protein uS5 is one of the proteins from the small ribosomal subunit, and is a protein of 166 to 254 amino acid residues. In Escherichia coli, uS5 is known to be important in the assembly and function of the 30S ribosomal subunit. Mutations in uS5 have been shown to increase translational error f... | [
"GO:0003723",
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"RNA binding",
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"PROFILE"
] | [
"PF00333",
"PS50881"
] | [
"Ribosomal_S5",
"S5_DSRBD"
] | [
39651,
39532
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00505",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-6791226",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-CEL-9937383",
"R-DDI-156... | [
"PROSITEDOC:PDOC00505",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-5389840",
"REACTOME:R-CEL-5419276",
"REACTOME:R-CEL-6791226",
"REACTOME:R-CEL-72649",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL... | 116 | [
"1dv4",
"1eg0",
"1fjg",
"1fka",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1pkp",
"1qd7",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xmo"... | 1,858 | [
"PUB00003665",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"2247072",
"11297922",
"11290319",
"11114498"
] | [
"Sequence and functional similarity between a yeast ribosomal protein and the Escherichia coli S5 ram protein.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1990,
2001,
2001,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
947,
23661,
14695,
493
] | 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",... | [
28,
2,
2,
3,
1,
17,
15,
2,
13,
32,
2,
2,
23
] | 13 | true | Domain | Small ribosomal subunit protein uS5, N-terminal | Small ribosomal subunit protein uS5, N-terminal | Ribosomal_uS5_N | 1 |
IPR013813 | 13,813 | Endoribonuclease L-PSP/chorismate mutase-like | Endoribo_LPSP/chorism_mut-like | Domain | 15,404 | false | false | This entry represents the β-α-β-α-β(2) domains common both to bacterial chorismate mutase and to members of the YjgF/Yer057p/UK114 family. These proteins form trimers with a three-fold symmetry with three closely-packed β-sheets. The conserved domain is similar in structure to chorismate mutase but there is no sequence... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER",
"CDD"
] | [
"PF14588",
"PTHR43760",
"cd02199"
] | [
"YjgF_endoribonc",
"",
"YjgF_YER057c_UK114_like_1"
] | [
13827,
15372,
15330
] | 3 | [] | [] | [] | 0 | [
"2otm",
"3d01",
"9bk9",
"9bkb",
"9bki"
] | 5 | [
"PUB00006517",
"PUB00007949",
"PUB00011078",
"PUB00027819",
"PUB00028112",
"PUB00028113",
"PUB00028737",
"PUB00038220",
"PUB00049511",
"PUB00054810",
"PUB00056792",
"PUB00064878",
"PUB00074576",
"PUB00080805"
] | [
"10557275",
"10400702",
"10818343",
"12777779",
"10595546",
"11442631",
"12112709",
"16323205",
"17506874",
"19899170",
"20400551",
"22094463",
"18296521",
"14624641"
] | [
"Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family.",
"Ribonuclease activity of rat liver perchloric acid-soluble protein, a potent inhibitor of protein synthesis.",
"The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase ... | [
1999,
1999,
2000,
2003,
1999,
2001,
2002,
2006,
2007,
2010,
2010,
2012,
2008,
2003
] | 14 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermoproteati",
"unclassified sequences"
] | [
14623,
442,
42,
297
] | 4 | [] | [] | 0 | true | Domain | Endoribonuclease L-PSP/chorismate mutase-like | Endoribonuclease L-PSP/chorismate mutase-like | Endoribo_LPSP/chorism_mut-like | 7 |
IPR013815 | 13,815 | ATP-grasp fold, subdomain 1 | ATP_grasp_subdomain_1 | Homologous_superfamily | 320,532 | false | false | This entry represents subdomain 1 found at the N-terminal end of the ATP-grasp domain. The ATP-grasp fold is one of several distinct ATP-binding folds, and is found in enzymes that catalyse the formation of amide bonds, catalysing the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol grou... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.1490.20"
] | [
""
] | [
320532
] | 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-71403",
"R-BTA-73817",
"R-BTA-8955332",
"R-BTA-8964539",
"R-BTA-9837999",
"R-CEL-196780",
"R-CEL-500753",
"R-CEL-71032",
"R-CEL-71403",
"R-CEL-9837999",
"R-DDI-196780",
"R-DDI-200425",
"R-DDI-500753",
"R-DDI-70895",
"R-DDI-71403",
"R-DDI-73817",
"R-DDI-75105",
"R-DME-181429"... | [
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-73817",
"REACTOME:R-BTA-8955332",
"REACTOME:R-BTA-8964539",
"REACTOME:R-BTA-9837999",
"REACTOME:R-CEL-196780",
"REACTOME:R-CEL-500753",
"REACTOME:R-CEL-71032",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-196780",
"REACTOME:R-DDI-200... | 78 | [
"1auv",
"1aux",
"1b6r",
"1b6s",
"1bnc",
"1cqi",
"1cqj",
"1dik",
"1dv1",
"1dv2",
"1e4e",
"1ehi",
"1euc",
"1eud",
"1eyz",
"1ez1",
"1ggo",
"1glv",
"1gsa",
"1gsh",
"1gso",
"1i7l",
"1i7n",
"1iov",
"1iow",
"1jde",
"1jkj",
"1jll",
"1kbl",
"1kc7",
"1kj8",
"1kj9"... | 328 | [
"PUB00015342",
"PUB00020972",
"PUB00028114"
] | [
"7862655",
"9416615",
"12392708"
] | [
"A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli.",
"A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity.",
"Mutational analysis of ATP-grasp residues in the two ATP sites of Saccharomyce... | [
1995,
1997,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
8562,
255406,
51643,
1,
37,
4883
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
81,
14,
74,
20,
12,
66,
34,
8,
29,
89,
8,
6,
195
] | 13 | true | Homologous_superfamily | ATP-grasp fold, subdomain 1 | ATP-grasp fold, subdomain 1 | ATP_grasp_subdomain_1 | 5 |
IPR013818 | 13,818 | Lipase | Lipase | Domain | 23,799 | 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 | [
"PFAM"
] | [
"PF00151"
] | [
"Lipase"
] | [
23799
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"3.1.1",
"GenProp1703",
"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-... | [
"EC:3.1.1",
"GP:GenProp1703",
"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",
"REA... | 39 | [
"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 | [] | [
"IPR033906"
] | 0 | 1 | 0 | [
"Adenoviridae",
"Bacteria",
"Eukaryota"
] | [
41,
80,
23678
] | 3 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
66,
53,
39,
37
] | 5 | true | Domain | Lipase | Lipase | Lipase | 1 |
IPR013819 | 13,819 | Lipoxygenase, C-terminal | LipOase_C | Domain | 19,472 | false | false | Lipoxygenases ([ec:1.13.11.-]) are a class of iron-containing dioxygenases which catalyses the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure. They are common in plants where they may be involved in a number of diverse aspects of plant physiology including growth and development, pest resist... | [
"GO:0016702",
"GO:0046872"
] | [
"oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF00305",
"PR00087",
"PS51393"
] | [
"Lipoxygenase",
"LIPOXYGENASE",
"LIPOXYGENASE_3"
] | [
18674,
14132,
19370
] | 3 | [
"EC",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"1.13.11",
"GenProp1588",
"GenProp1653",
"PDOC00077",
"R-BTA-2142691",
"R-BTA-2142712",
"R-BTA-2142770",
"R-BTA-9018677",
"R-BTA-9018681",
"R-BTA-9018896",
"R-BTA-9023661",
"R-BTA-9025106",
"R-BTA-9026286",
"R-HSA-2142688",
"R-HSA-2142691",
"R-HSA-2142696",
"R-HSA-2142700",
"R-HSA-... | [
"EC:1.13.11",
"GP:GenProp1588",
"GP:GenProp1653",
"PROSITEDOC:PDOC00077",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-2142712",
"REACTOME:R-BTA-2142770",
"REACTOME:R-BTA-9018677",
"REACTOME:R-BTA-9018681",
"REACTOME:R-BTA-9018896",
"REACTOME:R-BTA-9023661",
"REACTOME:R-BTA-9025106",
"REACTOME:... | 81 | [
"1f8n",
"1fgm",
"1fgo",
"1fgq",
"1fgr",
"1fgt",
"1hu9",
"1ik3",
"1jnq",
"1lnh",
"1lox",
"1n8q",
"1no3",
"1rov",
"1rrh",
"1rrl",
"1y4k",
"1yge",
"2fnq",
"2iuj",
"2iuk",
"2p0m",
"2sbl",
"3bnb",
"3bnc",
"3bnd",
"3bne",
"3d3l",
"3dy5",
"3fg1",
"3fg3",
"3fg4"... | 84 | [
"PUB00000045",
"PUB00000363",
"PUB00002887",
"PUB00005162"
] | [
"3017195",
"1567851",
"7508918",
"8502991"
] | [
"Arachidonic acid metabolism.",
"Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement.",
"A novel lipoxygenase from rice. Primary structure and specific expression upon incompatible infection with rice blast fungus.",
"The three-dimensional structure of an arachid... | [
1986,
1992,
1994,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"Viruses",
"ecological metagenomes"
] | [
591,
18873,
3,
3,
2
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
29,
44,
25,
25,
1,
66,
30,
179
] | 8 | true | Domain | Lipoxygenase, C-terminal | Lipoxygenase, C-terminal | LipOase_C | 5 |
IPR013821 | 13,821 | Potassium channel, voltage dependent, KCNQ, C-terminal | K_chnl_volt-dep_KCNQ_C | Domain | 9,919 | false | false | Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03520"
] | [
"KCNQ_channel"
] | [
9919
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-1296072",
"R-HSA-1296072",
"R-HSA-445095",
"R-HSA-5576890",
"R-HSA-5576893",
"R-HSA-9662360",
"R-HSA-9662361",
"R-MMU-1296072",
"R-MMU-5576890",
"R-MMU-5576893",
"R-RNO-1296072",
"R-RNO-5576890",
"R-RNO-5576893"
] | [
"REACTOME:R-BTA-1296072",
"REACTOME:R-HSA-1296072",
"REACTOME:R-HSA-445095",
"REACTOME:R-HSA-5576890",
"REACTOME:R-HSA-5576893",
"REACTOME:R-HSA-9662360",
"REACTOME:R-HSA-9662361",
"REACTOME:R-MMU-1296072",
"REACTOME:R-MMU-5576890",
"REACTOME:R-MMU-5576893",
"REACTOME:R-RNO-1296072",
"REACTOME... | 13 | [
"2ovc",
"4gow",
"5j03",
"5vms",
"6b8l",
"6b8m",
"6b8n",
"6b8p",
"6b8q",
"6feg",
"6feh",
"6n5w",
"6uzz",
"6v00",
"6v01",
"7byl",
"7bym",
"7byn",
"7cr0",
"7cr1",
"7cr2",
"7cr3",
"7cr4",
"7cr7",
"7tci",
"7tcp",
"7vnp",
"7vnq",
"7vnr",
"7xni",
"7xnk",
"7xnl"... | 62 | [
"PUB00001055",
"PUB00001622",
"PUB00002771",
"PUB00004011",
"PUB00004020",
"PUB00006577",
"PUB00008295",
"PUB00008296",
"PUB00008297",
"PUB00009378"
] | [
"1772658",
"1879548",
"1373731",
"2448635",
"2451788",
"2555158",
"10838601",
"8528244",
"9430594",
"11178249"
] | [
"The molecular biology of K+ channels.",
"Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.",
"Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.",
"Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Droso... | [
1991,
1991,
1992,
1988,
1988,
1989,
2000,
1996,
1998,
2000
] | 10 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
9919
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
84,
12,
37,
25,
32
] | 6 | true | Domain | Potassium channel, voltage dependent, KCNQ, C-terminal | Potassium channel, voltage dependent, KCNQ, C-terminal | K_chnl_volt-dep_KCNQ_C | 6 |
IPR013822 | 13,822 | Signal recognition particle SRP54, helical bundle | Signal_recog_particl_SRP54_hlx | Domain | 62,760 | false | false | This entry represents the N-terminal helical bundle domain of the 54kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M... | [
"GO:0005525",
"GO:0006614"
] | [
"GTP binding",
"SRP-dependent cotranslational protein targeting to membrane"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF02881",
"SM00963"
] | [
"SRP54_N",
"SRP54_N"
] | [
62601,
61396
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.5.4",
"R-BTA-1799339",
"R-CFA-1799339",
"R-DDI-1799339",
"R-DRE-1799339",
"R-HSA-1799339",
"R-HSA-381038",
"R-MMU-1799339",
"R-RNO-1799339",
"R-SCE-1799339",
"R-SPO-1799339"
] | [
"EC:3.6.5.4",
"REACTOME:R-BTA-1799339",
"REACTOME:R-CFA-1799339",
"REACTOME:R-DDI-1799339",
"REACTOME:R-DRE-1799339",
"REACTOME:R-HSA-1799339",
"REACTOME:R-HSA-381038",
"REACTOME:R-MMU-1799339",
"REACTOME:R-RNO-1799339",
"REACTOME:R-SCE-1799339",
"REACTOME:R-SPO-1799339"
] | 11 | [
"1ffh",
"1fts",
"1j8m",
"1j8y",
"1jpj",
"1jpn",
"1ls1",
"1ng1",
"1o87",
"1okk",
"1qzw",
"1qzx",
"1rj9",
"1ry1",
"1vma",
"1wgw",
"1zu4",
"1zu5",
"2c03",
"2c04",
"2cnw",
"2ffh",
"2iy3",
"2iyl",
"2j28",
"2j37",
"2j45",
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"2q9a"... | 96 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
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1829,
48132,
2,
11765,
1032
] | 5 | [
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"Drosophila melanogaster",
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2,
2,
4,
2,
11,
7,
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19,
4,
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2,
36
] | 13 | true | Domain | Signal recognition particle SRP54, helical bundle | Signal recognition particle SRP54, helical bundle | Signal_recog_particl_SRP54_hlx | 1 |
IPR013824 | 13,824 | DNA topoisomerase, type IA, central region, subdomain 1 | Topo_IA_cen_sub1 | Homologous_superfamily | 60,255 | false | false | Type IA topoisomerases are comprised of four domains that together form a toroidal structure with a central hole large enough to accommodate single- and double-stranded DNA: an N-terminal alpha α/β Toprim domain, domain 2 and the C-terminal domain 4 are winged-helix domains, and domain 3 is a β-barrel. Domains 1 (Topri... | [] | [] | [] | 0 | [
"CATHGENE3D"
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"G3DSA:1.10.460.10"
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""
] | [
60255
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"REACTOME:R-HSA-912446... | 26 | [
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"The mechanisms of DNA topoisomerases.",
"DNA topoisomerases: structure, function, and mechanism.",
"Phylogenomics of type II DNA topoisomerases.",
"Cellular roles of DNA topoisomerases: a molecular perspective.",... | [
1998,
1995,
2001,
2003,
2002,
2003,
1999,
2010,
2010,
2007,
2007
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
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] | [
1292,
47737,
10018,
60,
10,
1138
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
19,
4,
3,
6,
2,
10,
14,
1,
11,
3,
1,
1,
73
] | 13 | true | Homologous_superfamily | DNA topoisomerase, type IA, central region, subdomain 1 | DNA topoisomerase, type IA, central region, subdomain 1 | Topo_IA_cen_sub1 | 6 |
IPR013825 | 13,825 | DNA topoisomerase, type IA, central region, subdomain 2 | Topo_IA_cen_sub2 | Homologous_superfamily | 57,380 | false | false | DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single-or double-strand breaks, crossing the strands through one another, then resealing the breaks [ ]. These enzymes have several functions: to remove DNA supercoi... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.70.20.10"
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""
] | [
57380
] | 1 | [
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"REACTOME:R-HSA-912446... | 26 | [
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"6cq2"... | 55 | [
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"Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA.",
"The mechanisms of DNA topoisomerases.",
"DNA topoisomerases: structure, function, and mechanism.",
"Phylogenomics of type II DNA topoisomerases.",
"Cellular roles of DNA topoisomerases: a molecular perspective.",... | [
1998,
1995,
2001,
2003,
2002,
2003,
1999,
2010,
2010,
2007,
2007
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
934,
46576,
8847,
56,
9,
958
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
19,
3,
3,
3,
2,
9,
11,
1,
7,
3,
1,
1,
53
] | 13 | true | Homologous_superfamily | DNA topoisomerase, type IA, central region, subdomain 2 | DNA topoisomerase, type IA, central region, subdomain 2 | Topo_IA_cen_sub2 | 5 |
IPR013826 | 13,826 | DNA topoisomerase, type IA, central region, subdomain 3 | Topo_IA_cen_sub3 | Homologous_superfamily | 58,382 | false | false | DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single-or double-strand breaks, crossing the strands through one another, then resealing the breaks [ ]. These enzymes have several functions: to remove DNA supercoi... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.290.10"
] | [
""
] | [
58382
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"REACTOME:R-HSA-912446... | 26 | [
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"4ddv",
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"DNA topoisomerases: structure, function, and mechanism.",
"Phylogenomics of type II DNA topoisomerases.",
"Cellular roles of DNA topoisomerases: a molecular perspective.",... | [
1998,
1995,
2001,
2003,
2002,
2003,
1999,
2010,
2010,
2007,
2007
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
1260,
46769,
9337,
57,
10,
949
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
19,
3,
3,
5,
2,
6,
12,
1,
9,
3,
1,
1,
59
] | 13 | true | Homologous_superfamily | DNA topoisomerase, type IA, central region, subdomain 3 | DNA topoisomerase, type IA, central region, subdomain 3 | Topo_IA_cen_sub3 | 7 |
IPR013828 | 13,828 | Haemagglutinin, HA1 chain, alpha/beta domain superfamily | Hemagglutn_HA1_a/b_dom_sf | Homologous_superfamily | 153,874 | false | false | Haemagglutinin (HA) is one of two main surface fusion glycoproteins embedded in the envelope of influenza viruses, the other being neuraminidase (NA). There are sixteen known HA subtypes (H1-H16) and nine NA subtypes (N1-N9), which together are used to classify influenza viruses (e.g. H5N1). The antigenic variations in... | [
"GO:0046789",
"GO:0019064"
] | [
"host cell surface receptor binding",
"fusion of virus membrane with host plasma membrane"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.209.20"
] | [
""
] | [
153874
] | 1 | [
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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] | [
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"R-HSA-168303",
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"R-HSA-168336",
"R-HSA-168874",
"R-HSA-192823",
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"REACTOME:R-HSA-168874",
"REACTOME:R-HSA-192823",
"REACTOME:R-HSA-198933"
] | 11 | [
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"1hgf",
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"1ruz",
"1rv0",
"1rvt",
"1rvx",
"1rvz",
"1ti8",
"2fk0",
"2hmg",
"2ibx"... | 791 | [
"PUB00033162",
"PUB00033164",
"PUB00033165"
] | [
"16543414",
"15475582",
"16178512"
] | [
"Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus.",
"Plasticity of influenza haemagglutinin fusion peptides and their interaction with lipid bilayers.",
"The factors of virulence of influenza a virus."
] | [
2006,
2005,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Negarnaviricota"
] | [
19,
6,
153849
] | 3 | [] | [] | 0 | true | Homologous_superfamily | Haemagglutinin, HA1 chain, alpha/beta domain superfamily | Haemagglutinin, HA1 chain, alpha/beta domain superfamily | Hemagglutn_HA1_a/b_dom_sf | 9 |
IPR013830 | 13,830 | SGNH hydrolase-type esterase domain | SGNH_hydro | Domain | 118,424 | false | false | This entry represents the SGNH hydrolase-type esterase domain, which has a similar fold to flavoproteins, namely a three-layer α/β/α structure, where the β-sheets are composed of five parallel strands. Enzymes containing this domain act as esterases and lipases, but have little sequence homology to true lipases [ , ]. ... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF13472",
"PF14606"
] | [
"Lipase_GDSL_2",
"Lipase_GDSL_3"
] | [
116462,
2235
] | 2 | [
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"REACTOME",
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"REACTOME:R-MMU-6811436",
"REACTOME:R-RNO-6798695",
"REACTOME:R-RNO-681143... | 12 | [
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"3dci",
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"3hp4"... | 114 | [
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"Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus.",
"Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases.",
"Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-a... | [
1998,
2000,
2001,
2003,
2002,
1995,
2004
] | 7 | [] | [
"IPR037461"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
248,
97207,
19603,
418,
948
] | 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",... | [
2,
1,
291,
1,
1,
8,
8,
8,
3,
8,
11
] | 11 | true | Domain | SGNH hydrolase-type esterase domain | SGNH hydrolase-type esterase domain | SGNH_hydro | 7 |
IPR013834 | 13,834 | Bacteriophage, G3P, N2-domain superfamily | Phage_G3P_N2_sf | Homologous_superfamily | 17 | false | false | The G3P protein (also known as attachment protein or coat protein A) of filamentous phage such as M13, phage fd and phage f1, is an essential coat protein for the infection of Escherichia coli. The G3P protein consists of three domains: two N-terminal domains (N1 and N2) with a similar β-barrel fold, and a C-terminal d... | [
"GO:0019028"
] | [
"viral capsid"
] | [
"cellular_component"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.450.1"
] | [
""
] | [
17
] | 1 | [] | [] | [] | 0 | [
"1g3p",
"2g3p",
"3dgs",
"3knq",
"8b3o",
"8ixk",
"8jwx",
"9g8e"
] | 8 | [
"PUB00033212",
"PUB00033213"
] | [
"9461080",
"12767837"
] | [
"The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p.",
"The folding mechanism of a two-domain protein: folding kinetics and domain docking of the gene-3 protein of phage fd."
] | [
1998,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Arsenophonus nasoniae",
"Enterobacteria phage M13"
] | [
2,
15
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Bacteriophage, G3P, N2-domain superfamily | Bacteriophage, G3P, N2-domain superfamily | Phage_G3P_N2_sf | 8 |
IPR013836 | 13,836 | CD34/Podocalyxin | CD34/Podocalyxin | Family | 2,987 | false | false | This family consists of several mammalian CD34 antigen proteins. The CD34 antigen is a human leukocyte membrane protein expressed specifically by lymphohematopoietic progenitor cells. CD34 is a phosphoprotein. Activation of protein kinase C (PKC) has been found to enhance CD34 phosphorylation [ , ]. This family contain... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06365"
] | [
"CD34_antigen"
] | [
2987
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CFA-198933",
"R-HSA-156584",
"R-HSA-198933",
"R-MMU-156584",
"R-MMU-198933"
] | [
"REACTOME:R-CFA-198933",
"REACTOME:R-HSA-156584",
"REACTOME:R-HSA-198933",
"REACTOME:R-MMU-156584",
"REACTOME:R-MMU-198933"
] | 5 | [] | 0 | [
"PUB00010258",
"PUB00011425",
"PUB00019271"
] | [
"1694174",
"10982412",
"10722749"
] | [
"Activated protein kinase C directly phosphorylates the CD34 antigen on hematopoietic cells.",
"Expression of podocalyxin inhibits cell-cell adhesion and modifies junctional properties in Madin-Darby canine kidney cells.",
"Identification of endoglycan, a member of the CD34/podocalyxin family of sialomucins."
] | [
1990,
2000,
2000
] | 3 | [] | [
"IPR008083",
"IPR017403",
"IPR042397"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota"
] | [
5,
2982
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
13,
12,
9
] | 4 | true | Family | CD34/Podocalyxin | CD34/Podocalyxin | CD34/Podocalyxin | 1 |
IPR013837 | 13,837 | ATP synthase, F0 complex, subunit B | ATP_synth_F0_suB | Family | 4,058 | 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:0015078",
"GO:0015986"
] | [
"proton transmembrane transporter activity",
"proton motive force-driven ATP synthesis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER"
] | [
"PTHR12733"
] | [
""
] | [
4058
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-163210",
"R-BTA-8949613",
"R-CEL-163210",
"R-CEL-8949613",
"R-DME-163210",
"R-DME-8949613",
"R-HSA-163210",
"R-HSA-8949613",
"R-MMU-163210",
"R-MMU-8949613",
"R-RNO-163210",
"R-RNO-8949613"
] | [
"REACTOME:R-BTA-163210",
"REACTOME:R-BTA-8949613",
"REACTOME:R-CEL-163210",
"REACTOME:R-CEL-8949613",
"REACTOME:R-DME-163210",
"REACTOME:R-DME-8949613",
"REACTOME:R-HSA-163210",
"REACTOME:R-HSA-8949613",
"REACTOME:R-MMU-163210",
"REACTOME:R-MMU-8949613",
"REACTOME:R-RNO-163210",
"REACTOME:R-RN... | 12 | [
"2cly",
"2wss",
"4b2q",
"5ara",
"5are",
"5arh",
"5ari",
"5fij",
"5fik",
"5fil",
"5lqx",
"5lqy",
"5lqz",
"6b2z",
"6b8h",
"6cp3",
"6cp5",
"6cp6",
"6cp7",
"6j54",
"6j5a",
"6j5i",
"6j5j",
"6j5k",
"6tt7",
"6wtd",
"6yy0",
"6z1r",
"6z1u",
"6za9",
"6zbb",
"6ziq"... | 102 | [
"PUB00009752",
"PUB00020603",
"PUB00020604",
"PUB00020607",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"11309608",
"15473999",
"15078220",
"16045926",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Structure of the F1-binding... | [
2001,
2004,
2004,
2005,
2010,
2008,
1992,
1998
] | 8 | [
"IPR008688"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
4058
] | 1 | [
"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... | [
2,
1,
4,
5,
7,
1,
7,
1,
1
] | 9 | true | Family | ATP synthase, F0 complex, subunit B | ATP synthase, F0 complex, subunit B | ATP_synth_F0_suB | 1 |
IPR013838 | 13,838 | Beta tubulin, autoregulation binding site | Beta-tubulin_BS | Binding_site | 21,244 | false | false | The stability of beta-tubulin mRNAs are autoregulated by their own translation product [ ]. Unpolymerised tubulin subunits bind directly (or activate a factor(s) which binds co-translationally) to the nascent N terminus of beta-tubulin. This binding is transduced through the adjacent ribosomes to activate an RNAse that... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00228"
] | [
"TUBULIN_B_AUTOREG"
] | [
21244
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00200",
"R-BTA-190840",
"R-BTA-2132295",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-2565942",
"R-BTA-3371497",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-5610787",
"R-BTA-5617833",
"R-BTA-5620912",
"R-BTA-5620924",
"R-BTA-5626467",
"R-BTA-5663220",
"R... | [
"PROSITEDOC:PDOC00200",
"REACTOME:R-BTA-190840",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-380259",
"REACTOME:R-BTA-380270",
"REACTOME:R-BTA-380284",
"REACTOME:R-BTA-380320",
"REACTOME:R-BTA... | 187 | [
"1ffx",
"1ia0",
"1jff",
"1sa0",
"1sa1",
"1tub",
"1tvk",
"1z2b",
"2hxf",
"2hxh",
"2p4n",
"2wbe",
"2xrp",
"3dco",
"3du7",
"3e22",
"3edl",
"3hkb",
"3hkc",
"3hkd",
"3hke",
"3iz0",
"3j1t",
"3j1u",
"3j2u",
"3j6e",
"3j6f",
"3j6g",
"3j6p",
"3j7i",
"3j8x",
"3j8y"... | 704 | [
"PUB00005335"
] | [
"3072712"
] | [
"Autoregulated instability of tubulin mRNAs: a novel eukaryotic regulatory mechanism."
] | [
1988
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
47,
21197
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
34,
6,
9,
10,
57,
11,
2,
19,
20,
1,
2,
62
] | 12 | true | Binding_site | Beta tubulin, autoregulation binding site | Beta tubulin, autoregulation binding site | Beta-tubulin_BS | 9 |
IPR013839 | 13,839 | NAD-dependent DNA ligase, adenylation | DNAligase_adenylation | Domain | 32,858 | false | false | DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalyzing the formation of an internucleotide ester bond between phosphate and deoxyribose. It is active during DNA replication, DNA repair and DNA recombination. There are two forms of DNA ligase: one requires ATP ( ), the oth... | [
"GO:0003911"
] | [
"DNA ligase (NAD+) activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"CDD"
] | [
"PF01653",
"cd00114"
] | [
"DNA_ligase_aden",
"LIGANc"
] | [
32858,
27052
] | 2 | [
"EC"
] | [
"6.5.1.2"
] | [
"EC:6.5.1.2"
] | 1 | [
"1b04",
"1dgs",
"1ta8",
"1tae",
"1v9p",
"1zau",
"2owo",
"3ba8",
"3ba9",
"3baa",
"3bab",
"3bac",
"3jsl",
"3jsn",
"3pn1",
"3sgi",
"3uq8",
"4cc5",
"4cc6",
"4eeq",
"4efb",
"4efe",
"4glw",
"4glx",
"4lh6",
"4lh7",
"4uco",
"4ucr",
"4ucs",
"4uct",
"4ucu",
"4ucv"... | 46 | [
"PUB00001728",
"PUB00002786",
"PUB00007386",
"PUB00019427"
] | [
"1526462",
"8390989",
"10698952",
"10368271"
] | [
"Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis.",
"Guanylate kinase of Escherichia coli K-12.",
"Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and functional implications.",
"Structure of the adenylation domain of an NAD+-dependent DNA liga... | [
1992,
1993,
2000,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
352,
30974,
305,
412,
815
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Homo sapiens"
] | [
1,
2,
1
] | 3 | true | Domain | NAD-dependent DNA ligase, adenylation | NAD-dependent DNA ligase, adenylation | DNAligase_adenylation | 8 |
IPR013840 | 13,840 | NAD-dependent DNA ligase, N-terminal | DNAligase_N | Domain | 32,893 | false | false | DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalyzing the formation of an internucleotide ester bond between phosphate and deoxyribose. It is active during DNA replication, DNA repair and DNA recombination. There are two forms of DNA ligase: one requires ATP ( ), the oth... | [
"GO:0003911"
] | [
"DNA ligase (NAD+) activity"
] | [
"molecular_function"
] | 1 | [
"SMART"
] | [
"SM00532"
] | [
"LIGANc"
] | [
32893
] | 1 | [
"EC"
] | [
"6.5.1.2"
] | [
"EC:6.5.1.2"
] | 1 | [
"1b04",
"1dgs",
"1ta8",
"1tae",
"1v9p",
"1zau",
"2owo",
"3ba8",
"3ba9",
"3baa",
"3bab",
"3bac",
"3jsl",
"3jsn",
"3pn1",
"3sgi",
"3uq8",
"4cc5",
"4cc6",
"4eeq",
"4efb",
"4efe",
"4glw",
"4glx",
"4lh6",
"4lh7",
"4uco",
"4ucr",
"4ucs",
"4uct",
"4ucu",
"4ucv"... | 46 | [
"PUB00001728",
"PUB00002786",
"PUB00007386",
"PUB00019427"
] | [
"1526462",
"8390989",
"10698952",
"10368271"
] | [
"Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis.",
"Guanylate kinase of Escherichia coli K-12.",
"Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and functional implications.",
"Structure of the adenylation domain of an NAD+-dependent DNA liga... | [
1992,
1993,
2000,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
354,
30991,
296,
421,
831
] | 5 | [
"Escherichia coli (strain K12)",
"Homo sapiens"
] | [
2,
1
] | 2 | true | Domain | NAD-dependent DNA ligase, N-terminal | NAD-dependent DNA ligase, N-terminal | DNAligase_N | 8 |
IPR013842 | 13,842 | GTP-binding protein LepA, C-terminal | LepA_CTD | Domain | 31,293 | false | false | The elongation factor 4 (LepA or GUF1 in Saccaromyces) is a GTP-binding membrane protein related to EF-G and EF-Tu. LepA is a noncanonical GTPase that has an unknown function. It is highly conserved and present in bacteria, mitochondria, and chloroplasts [ ]. LepA contains domains that are homologous to EF-G domain I, ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06421"
] | [
"LepA_C"
] | [
31293
] | 1 | [] | [] | [] | 0 | [
"2ywe",
"2ywf",
"2ywg",
"2ywh",
"3cb4",
"3deg",
"3jcd",
"3jce",
"4w2e",
"5imq",
"5imr",
"5j8b"
] | 12 | [
"PUB00050954",
"PUB00085883"
] | [
"18362332",
"28320876"
] | [
"The structure of LepA, the ribosomal back translocase.",
"Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function."
] | [
2008,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences",
"virus sp. ct1Uu26"
] | [
25381,
5339,
572,
1
] | 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",... | [
7,
1,
5,
3,
1,
1,
2,
1,
2,
3,
1,
1,
9
] | 13 | true | Domain | GTP-binding protein LepA, C-terminal | GTP-binding protein LepA, C-terminal | LepA_CTD | 8 |
IPR013843 | 13,843 | Small ribosomal subunit protein eS4, N-terminal | Ribosomal_eS4_N | Domain | 7,162 | false | false | A number of eukaryotic and archaeal ribosomal proteins can be grouped on the basis of sequence similarities. One of them consists of the small ribosomal subunit protein eS4 from archaea and eukaryotes. Small ribosomal subunit protein eS4A from yeast is also known as S7/YS6; archaeal members are also known as S4e; and m... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08071"
] | [
"RS4NT"
] | [
7162
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00457",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R... | [
"PROSITEDOC:PDOC00457",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827"... | 116 | [
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7a",
"3j7p",
"3j7r",
"3j80",
"3j81",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jam",
"3jan",
"3jap",
"3jbn",
"3jbo",
"3jbp",
"4bts",
"4d5l",
"4d61",
"4kzx",
"4kzy",
"4kzz",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q",
"4u4r"... | 617 | [
"PUB00000844",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00080279"
] | [
"2124517",
"11297922",
"11290319",
"11114498",
"24524803"
] | [
"Homologous ribosomal protein genes on the human X and Y chromosomes: escape from X inactivation and possible implications for Turner syndrome.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"A new system... | [
1990,
2001,
2001,
2000,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Pseudomonadota",
"unclassified sequences"
] | [
886,
6247,
2,
27
] | 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... | [
13,
1,
1,
2,
10,
5,
1,
9,
7,
2,
3,
24
] | 12 | true | Domain | Small ribosomal subunit protein eS4, N-terminal | Small ribosomal subunit protein eS4, N-terminal | Ribosomal_eS4_N | 7 |
IPR013845 | 13,845 | Small ribosomal subunit protein eS4, central region | Ribosomal_eS4_central_region | Domain | 7,982 | false | false | A number of eukaryotic and archaeal ribosomal proteins can be grouped on the basis of sequence similarities. One of them consists of the small ribosomal subunit protein eS4 from archaea and eukaryotes. Small ribosomal subunit protein eS4A from yeast is also known as S7/YS6; archaeal members are also known as S4e; and m... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00900"
] | [
"Ribosomal_S4e"
] | [
7982
] | 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-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R-CEL-975956",
... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-179933... | 115 | [
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7a",
"3j7p",
"3j7r",
"3j80",
"3j81",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jam",
"3jan",
"3jap",
"3jbn",
"3jbo",
"3jbp",
"3kbg",
"4bts",
"4d5l",
"4d61",
"4kzx",
"4kzy",
"4kzz",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q"... | 630 | [
"PUB00000844",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00080279"
] | [
"2124517",
"11297922",
"11290319",
"11114498",
"24524803"
] | [
"Homologous ribosomal protein genes on the human X and Y chromosomes: escape from X inactivation and possible implications for Turner syndrome.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"A new system... | [
1990,
2001,
2001,
2000,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Pseudomonadati",
"unclassified sequences"
] | [
940,
7000,
4,
38
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
14,
1,
1,
2,
11,
5,
1,
9,
7,
2,
3,
134
] | 12 | true | Domain | Small ribosomal subunit protein eS4, central region | Small ribosomal subunit protein eS4, central region | Ribosomal_eS4_central_region | 7 |
IPR013846 | 13,846 | mRNA capping enzyme, C-terminal domain | mRNA_cap_enzyme_C | Domain | 5,402 | false | false | This domain is found at the C-terminal in mRNA-capping enzyme subunit alpha. The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase [ ]. Binding of the enzyme to nucleotides is specific to the GMP moiety of GTP. The viral mRNA capp... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03919"
] | [
"mRNA_cap_C"
] | [
5402
] | 1 | [
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.50",
"GenProp1354",
"PWY-7375",
"R-CEL-72086",
"R-CEL-77075",
"R-DRE-72086",
"R-DRE-77075",
"R-HSA-167160",
"R-HSA-72086",
"R-HSA-77075",
"R-MMU-72086",
"R-MMU-77075",
"R-SCE-72086",
"R-SCE-77075",
"R-SPO-72086",
"R-SPO-77075"
] | [
"EC:2.7.7.50",
"GP:GenProp1354",
"METACYC:PWY-7375",
"REACTOME:R-CEL-72086",
"REACTOME:R-CEL-77075",
"REACTOME:R-DRE-72086",
"REACTOME:R-DRE-77075",
"REACTOME:R-HSA-167160",
"REACTOME:R-HSA-72086",
"REACTOME:R-HSA-77075",
"REACTOME:R-MMU-72086",
"REACTOME:R-MMU-77075",
"REACTOME:R-SCE-72086"... | 16 | [
"1ckm",
"1ckn",
"1cko",
"1p16",
"3kyh",
"3rtx",
"3s24",
"4pz6",
"4pz7",
"4pz8",
"8p4a",
"8p4b",
"8p4c",
"8p4d",
"8p4e",
"8w8e",
"8w8f"
] | 17 | [
"PUB00000947",
"PUB00029683",
"PUB00079683"
] | [
"9160746",
"12820968",
"11051760"
] | [
"X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes.",
"Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II.",
"Structure, mechanism, and evolution of the mRNA capping apparatus."
] | [
1997,
2003,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"metagenomes"
] | [
5287,
60,
55
] | 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... | [
9,
2,
1,
1,
5,
4,
2,
6,
5,
1,
1,
14
] | 12 | true | Domain | mRNA capping enzyme, C-terminal domain | mRNA capping enzyme, C-terminal domain | mRNA_cap_enzyme_C | 3 |
IPR013847 | 13,847 | POU domain | POU | Domain | 16,974 | false | false | POU proteins are eukaryotic transcription factors containing a bipartite DNA binding domain referred to as the POU domain. The acronym POU (pronounced 'pow') is derived from the names of three mammalian transcription factors, the pituitary-specific Pit-1, the octamer-binding proteins Oct-1 and Oct-2, and the neural Unc... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00028"
] | [
"POUDOMAIN"
] | [
16974
] | 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-373752",
"R-CEL-418885",
"R-CEL-418886",
"R-DME-373752",
"R-DME-418885",
"R-DME-418886",
"R-DME-6804759",
"R-DME-6807505",
"R-DME-9018519",
"R-DRE-373752",
"R-DRE-418885",
"R-DRE-418886",
"R-HSA-2892245",
"R-HSA-2892247",
"R-HSA-452723",
"R-HSA-6785807",
"R-HSA-6804759",
"R-... | [
"REACTOME:R-CEL-373752",
"REACTOME:R-CEL-418885",
"REACTOME:R-CEL-418886",
"REACTOME:R-DME-373752",
"REACTOME:R-DME-418885",
"REACTOME:R-DME-418886",
"REACTOME:R-DME-6804759",
"REACTOME:R-DME-6807505",
"REACTOME:R-DME-9018519",
"REACTOME:R-DRE-373752",
"REACTOME:R-DRE-418885",
"REACTOME:R-DRE-... | 41 | [
"1au7",
"1cqt",
"1e3o",
"1gt0",
"1hf0",
"1o4x",
"1ocp",
"1oct",
"1pog",
"1pou",
"2xsd",
"3d1n",
"3l1p",
"5wc9",
"6ht5",
"6t90",
"6yov",
"7u0g",
"7u0i",
"7xrc",
"8bx1",
"8bx2",
"8g87",
"8g88",
"8g8b",
"8g8e",
"8g8g",
"8ots",
"8sps",
"8spu",
"9dzm",
"9pfn"... | 34 | [
"PUB00000905",
"PUB00007263",
"PUB00007264",
"PUB00007265"
] | [
"8156594",
"11159814",
"11183772",
"9009203"
] | [
"Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules.",
"POU domain factors in the neuroendocrine system: lessons from developmental biology provide insights into human disease.",
"The virtuoso of versatility: POU proteins that flex to fit.",
"... | [
1994,
2001,
2000,
1997
] | 4 | [] | [] | 0 | 0 | null | [
"Atopococcus tabaci",
"Eukaryota"
] | [
1,
16973
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
116,
28,
97,
47,
66
] | 6 | true | Domain | POU domain | POU domain | POU | 7 |
IPR013848 | 13,848 | Methylthiotransferase, N-terminal | Methylthiotransferase_N | Domain | 58,496 | false | false | The methylthiotransferase (MTTase) or miaB-like family is named after the (dimethylallyl)adenosine tRNA MTTase miaB protein, which catalyses a C-H to C-S bond conversion in the methylthiolation of tRNA. A related bacterial enzyme rimO performs a similar methylthiolation, but on a protein substrate. RimO acts on the rib... | [
"GO:0035596",
"GO:0051539"
] | [
"methylthiotransferase activity",
"4 iron, 4 sulfur cluster binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF00919",
"PS51449"
] | [
"UPF0004",
"MTTASE_N"
] | [
57838,
58460
] | 2 | [
"EC",
"REACTOME"
] | [
"2.8.4",
"R-HSA-6782315"
] | [
"EC:2.8.4",
"REACTOME:R-HSA-6782315"
] | 2 | [
"4jc0",
"7mjv",
"7mjw",
"7mjx",
"7mjy",
"7mjz"
] | 6 | [
"PUB00009728",
"PUB00010539",
"PUB00046148",
"PUB00052321"
] | [
"11882645",
"11222759",
"18252828",
"15289575"
] | [
"Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein.",
"Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods.",
"RimO, a MiaB-like enzyme, met... | [
2002,
2001,
2008,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
903,
50081,
6271,
3,
1238
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
8,
2,
4,
2,
2,
7,
5,
6,
14,
18
] | 10 | true | Domain | Methylthiotransferase, N-terminal | Methylthiotransferase, N-terminal | Methylthiotransferase_N | 5 |
IPR013849 | 13,849 | DNA helicase, Holliday junction RuvA type, domain I, bacterial | DNA_helicase_Holl-junc_RuvA_I | Domain | 25,085 | false | false | In prokaryotes, RuvA, RuvB, and RuvC process the universal DNA intermediate of homologous recombination, termed Holliday junction. The tetrameric DNA helicase RuvA specifically binds to the Holliday junction and facilitates the isomerization of the junction from the stacked folded configuration to the square-planar str... | [
"GO:0005524",
"GO:0009378",
"GO:0006281",
"GO:0006310"
] | [
"ATP binding",
"four-way junction helicase activity",
"DNA repair",
"DNA recombination"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF01330"
] | [
"RuvA_N"
] | [
25085
] | 1 | [] | [] | [] | 0 | [
"1bdx",
"1c7y",
"1cuk",
"1d8l",
"1hjp",
"1ixr",
"2h5x",
"2ztc",
"2ztd",
"2zte",
"7oa5",
"7pbu",
"7x5a",
"7x7q",
"8gh8"
] | 15 | [
"PUB00005222",
"PUB00013198"
] | [
"8832889",
"12408833"
] | [
"Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction.",
"Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery."
] | [
1996,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
24471,
29,
40,
2,
543
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | DNA helicase, Holliday junction RuvA type, domain I, bacterial | DNA helicase, Holliday junction RuvA type, domain I, bacterial | DNA_helicase_Holl-junc_RuvA_I | 6 |
IPR013851 | 13,851 | Transcription factor Otx, C-terminal | Otx_TF_C | Domain | 3,050 | false | false | Otx proteins constitute a class of vertebrate homeodomain-containing transcription factors that have been shown to be essential for anterior head formation, including brain morphogenesis. They are orthologous to the product of the Drosophila head gap gene, orthodenticle (Otd), and appear to play similar roles in both, ... | [
"GO:0003700",
"GO:0007275",
"GO:0005634"
] | [
"DNA-binding transcription factor activity",
"multicellular organism development",
"nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF03529"
] | [
"TF_Otx"
] | [
3050
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-9823739",
"R-HSA-9832991"
] | [
"REACTOME:R-HSA-9823739",
"REACTOME:R-HSA-9832991"
] | 2 | [] | 0 | [
"PUB00006144",
"PUB00006146",
"PUB00006147"
] | [
"10199636",
"10375352",
"10440864"
] | [
"The TINS Lecture. Understanding the roles of Otx1 and Otx2 in the control of brain morphogenesis.",
"Function and evolution of Otx proteins.",
"Conserved genetic programs in insect and mammalian brain development."
] | [
1999,
1999,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Bilateria",
"bird metagenome"
] | [
3049,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
25,
9,
11,
12
] | 4 | true | Domain | Transcription factor Otx, C-terminal | Transcription factor Otx, C-terminal | Otx_TF_C | 3 |
IPR013852 | 13,852 | Translation elongation factor P/YeiP, conserved site | Transl_elong_P/YeiP_CS | Conserved_site | 24,764 | false | false | Elongation factor P (EF-P) is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet [ ]. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01275"
] | [
"EFP"
] | [
24764
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00981"
] | [
"PROSITEDOC:PDOC00981"
] | 1 | [
"1ueb",
"1yby",
"3a5z",
"3tre",
"4v6a",
"6enj",
"6enu",
"6rji",
"6rk3",
"6s8z",
"8s8u",
"8vwq",
"8w2n"
] | 13 | [
"PUB00000702"
] | [
"9195040"
] | [
"Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
23116,
1159,
1,
488
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
11,
2,
8,
4
] | 4 | true | Conserved_site | Translation elongation factor P/YeiP, conserved site | Translation elongation factor P/YeiP, conserved site | Transl_elong_P/YeiP_CS | 3 |
IPR013853 | 13,853 | Galactitol permease IIC component | EIIC-GAT | Family | 5,683 | false | false | The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active-transport system, catalyses the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This family represents the IIC component of the PTS galactitol-specific family.... | [
"GO:0015577",
"GO:0015796"
] | [
"galactitol transmembrane transporter activity",
"galactitol transmembrane transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"PIRSF006304",
"PTHR37324",
"TIGR00827"
] | [
"GatC",
"",
"EIIC-GAT"
] | [
5148,
5683,
1462
] | 3 | [
"GP"
] | [
"GenProp0119"
] | [
"GP:GenProp0119"
] | 1 | [
"9u82",
"9u84",
"9u8e",
"9u8h"
] | 4 | [
"PUB00014684"
] | [
"8955298"
] | [
"Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism."
] | [
1996
] | 1 | [
"IPR004703"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Halobacteriales",
"metagenomes"
] | [
5646,
16,
21
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | Galactitol permease IIC component | Galactitol permease IIC component | EIIC-GAT | 9 |
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