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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR012135 | 12,135 | Dihydroorotate dehydrogenase, class 1/ 2 | Dihydroorotate_DH_1_2 | Family | 24,098 | false | false | Dihydroorotate dehydrogenase (DHOD), also known as dihydroorotate oxidase, catalyses the fourth step in de novo pyrimidine biosynthesis, the stereospecific oxidation of (S)-dihydroorotate to orotate, which is the only redox reaction in this pathway. DHODs can be divided into two mains classes: class 1 cytosolic enzymes... | [
"GO:0004152",
"GO:0006222"
] | [
"dihydroorotate dehydrogenase activity",
"UMP biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000164"
] | [
"DHO_oxidase"
] | [
24098
] | 1 | [
"EC",
"METACYC"
] | [
"1.3.5.2",
"PWY-5686"
] | [
"EC:1.3.5.2",
"METACYC:PWY-5686"
] | 2 | [
"1dor",
"1ep1",
"1ep2",
"1ep3",
"1f76",
"1jqv",
"1jqx",
"1jrb",
"1jrc",
"1jub",
"1jue",
"1ovd",
"2b4g",
"2bsl",
"2bx7",
"2djl",
"2djx",
"2dor",
"2e68",
"2e6a",
"2e6d",
"2e6f",
"3c3n",
"3c61",
"3gye",
"3gz3",
"3mhu",
"3mjy",
"3oix",
"3tjx",
"3tq0",
"3tro"... | 102 | [
"PUB00005052",
"PUB00024104",
"PUB00024613",
"PUB00033267",
"PUB00033268"
] | [
"9655329",
"10673429",
"11188687",
"9405053",
"12220493"
] | [
"The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function.",
"Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents.",
"Structure of dihydroorotate dehydrogenase B: electron tr... | [
1998,
2000,
2000,
1997,
2002
] | 5 | [] | [
"IPR005719",
"IPR024920"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
816,
22034,
708,
7,
533
] | 5 | [
"Escherichia coli (strain K12)",
"Mus musculus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
1,
1,
1,
1
] | 4 | true | Family | Dihydroorotate dehydrogenase, class 1/ 2 | Dihydroorotate dehydrogenase, class 1/ 2 | Dihydroorotate_DH_1_2 | 2 |
IPR012136 | 12,136 | NADP transhydrogenase, beta subunit | NADH_DH_b | Family | 13,041 | false | false | NAD(P) transhydrogenase catalyses the transfer of reducing equivalents between NAD(H) and NADP(H), coupled to the translocation of protons across a membrane [ ]. It is an integral membrane protein found in the inner membrane of animal mitochondria and in bacterial cytoplasmic membrane. Under most physiological conditio... | [
"GO:0008750",
"GO:0050661",
"GO:0016020"
] | [
"proton-translocating NAD(P)+ transhydrogenase activity",
"NADP binding",
"membrane"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"PIRSF"
] | [
"PIRSF000204"
] | [
"PNTB"
] | [
13041
] | 1 | [
"EC",
"GP"
] | [
"7.1.1.1",
"GenProp1305"
] | [
"EC:7.1.1.1",
"GP:GenProp1305"
] | 2 | [
"4o9u"
] | 1 | [
"PUB00022476",
"PUB00024417",
"PUB00024810",
"PUB00025858",
"PUB00033266",
"PUB00083188"
] | [
"12791694",
"11004437",
"10997900",
"11250201",
"12788487",
"12974635"
] | [
"Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation.",
"Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum... | [
2003,
2000,
2000,
2001,
2003,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
58,
12723,
40,
220
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | NADP transhydrogenase, beta subunit | NADP transhydrogenase, beta subunit | NADH_DH_b | 4 |
IPR012137 | 12,137 | Nitrate reductase NADH dependent | Nitr_rd_NADH | Family | 1,978 | false | false | This entry represents the NADH dependent nitrate reductase (NR) from plants and fungi, including NIA1 and NIA2 from Arabidopsis. They contain an N-terminal oxidoreductase molybdopterin binding domain and a C-terminal FAD-binding domain. In Arabidopsis, NR-mediated nitric oxide (NO) synthesis is required for ABA-induced... | [
"GO:0050464",
"GO:0006809",
"GO:0042128"
] | [
"nitrate reductase (NADPH) activity",
"nitric oxide biosynthetic process",
"nitrate assimilation"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF000233"
] | [
"Nitr_rd_NADH"
] | [
1978
] | 1 | [
"EC",
"METACYC"
] | [
"1.7.1.1",
"PWY-381"
] | [
"EC:1.7.1.1",
"METACYC:PWY-381"
] | 2 | [] | 0 | [
"PUB00074253",
"PUB00074254",
"PUB00074255"
] | [
"2905260",
"12446847",
"8510658"
] | [
"A new locus (NIA 1) in Arabidopsis thaliana encoding nitrate reductase.",
"A new role for an old enzyme: nitrate reductase-mediated nitric oxide generation is required for abscisic acid-induced stomatal closure in Arabidopsis thaliana.",
"Identification and characterization of a chlorate-resistant mutant of Ar... | [
1988,
2002,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1978
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
10,
6,
9
] | 3 | true | Family | Nitrate reductase NADH dependent | Nitrate reductase NADH dependent | Nitr_rd_NADH | 6 |
IPR012138 | 12,138 | Hydroxylamine oxidase | HAO | Family | 106 | false | false | Autotrophic ammonia oxidising bacteria, such as Nitrosomonas europaea, acquire energy from the oxidation of ammonia to nitrite, and fix carbon dioxide to obtain biomass [ ]. The respiratory chain in these organisms consists of ammonia monooxygenase (AMO), which oxidises ammonia to hyroxylamine, hydroxylamine oxidoreduc... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000242"
] | [
"HAO"
] | [
106
] | 1 | [] | [] | [] | 0 | [
"1fgj",
"4fas",
"4n4n",
"4n4o",
"6m0p",
"6m0q"
] | 6 | [
"PUB00016931",
"PUB00024877"
] | [
"14695127",
"9095195"
] | [
"Metabolism of inorganic N compounds by ammonia-oxidizing bacteria.",
"The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea."
] | [
2003,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"freshwater sediment metagenome"
] | [
105,
1
] | 2 | [] | [] | 0 | true | Family | Hydroxylamine oxidase | Hydroxylamine oxidase | HAO | 8 |
IPR012142 | 12,142 | Tryptophan 2-monooxygenase | Trp_2-mOase | Family | 67 | false | false | The FAD-containing tryptophan 2-monooxygenase enzyme catalyses the oxidation of tryptophan to indoleacetamide, carbon dioxide, and water [ ].The enzyme belongs to a group of flavoenzymes that catalyse the oxidative decarboxylation of amino acids. | [
"GO:0050361",
"GO:0009851"
] | [
"tryptophan 2-monooxygenase activity",
"auxin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000319"
] | [
"Trp_2-mono_O2ase"
] | [
67
] | 1 | [
"EC",
"METACYC"
] | [
"1.13.12.3",
"PWY-3161"
] | [
"EC:1.13.12.3",
"METACYC:PWY-3161"
] | 2 | [] | 0 | [
"PUB00016935"
] | [
"14636050"
] | [
"Identification of Tyr413 as an active site residue in the flavoprotein tryptophan 2-monooxygenase and analysis of its contribution to catalysis."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Rhizobium/Agrobacterium group"
] | [
67
] | 1 | [] | [] | 0 | true | Family | Tryptophan 2-monooxygenase | Tryptophan 2-monooxygenase | Trp_2-mOase | 7 |
IPR012144 | 12,144 | Nitric-oxide synthase, eukaryote | NOS_euk | Family | 3,952 | false | false | Nitric oxide synthase ( ) (NOS) enzymes produce nitric oxide (NO) by catalyzing a five-electron oxidation of a guanidino nitrogen of L-arginine (L-Arg). Oxidation of L-Arg to L-citrulline occurs via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine as an intermediate. 2 mol of O(2) and 1.5 ... | [
"GO:0004517",
"GO:0005516",
"GO:0010181",
"GO:0020037",
"GO:0050660",
"GO:0050661",
"GO:0006809"
] | [
"nitric-oxide synthase activity",
"calmodulin binding",
"FMN binding",
"heme binding",
"flavin adenine dinucleotide binding",
"NADP binding",
"nitric oxide biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 7 | [
"PIRSF"
] | [
"PIRSF000333"
] | [
"NOS"
] | [
3952
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"1.14.13.39",
"PWY-4983",
"R-DME-1222556",
"R-DME-1474151",
"R-DME-203615",
"R-DME-203754",
"R-DME-392154",
"R-DME-5218920",
"R-DME-5578775",
"R-DME-9009391",
"R-DME-9033241",
"R-DME-9856530",
"R-HSA-1222556",
"R-HSA-1474151",
"R-HSA-203615",
"R-HSA-203641",
"R-HSA-203754",
"R-HSA-... | [
"EC:1.14.13.39",
"METACYC:PWY-4983",
"REACTOME:R-DME-1222556",
"REACTOME:R-DME-1474151",
"REACTOME:R-DME-203615",
"REACTOME:R-DME-203754",
"REACTOME:R-DME-392154",
"REACTOME:R-DME-5218920",
"REACTOME:R-DME-5578775",
"REACTOME:R-DME-9009391",
"REACTOME:R-DME-9033241",
"REACTOME:R-DME-9856530",
... | 50 | [
"8t1j",
"8t1k"
] | 2 | [
"PUB00007289",
"PUB00007290",
"PUB00007291",
"PUB00007292",
"PUB00018125",
"PUB00021600",
"PUB00022275",
"PUB00031493"
] | [
"8782597",
"7510950",
"9199168",
"7535955",
"10331866",
"11695891",
"10409685",
"15208315"
] | [
"Binding sites of nitric oxide synthases.",
"Nitric oxide synthases in mammals.",
"The first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the Golgi region of cells: a green fluorescent protein study.",
"DHR domains in syntrophins, neurona... | [
1996,
1994,
1997,
1995,
1999,
2001,
1999,
2004
] | 8 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3952
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
1,
10,
8,
19
] | 5 | true | Family | Nitric-oxide synthase, eukaryote | Nitric-oxide synthase, eukaryote | NOS_euk | 2 |
IPR012147 | 12,147 | Phosphate acetyl/butyryltransferase | P_Ac_Bu_trans | Family | 11,920 | false | false | This group represents phosphate acetyltransferase and phosphate butyryltransferase. | [
"GO:0016746"
] | [
"acyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000428"
] | [
"P_Ac_trans"
] | [
11920
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.1.8",
"PWY-1281",
"PWY-5482",
"PWY-5485",
"PWY-5497",
"PWY-6637",
"PWY-8086",
"PWY-8377"
] | [
"EC:2.3.1.8",
"METACYC:PWY-1281",
"METACYC:PWY-5482",
"METACYC:PWY-5485",
"METACYC:PWY-5497",
"METACYC:PWY-6637",
"METACYC:PWY-8086",
"METACYC:PWY-8377"
] | 8 | [
"1qzt",
"1r5j",
"1td9",
"1vmi",
"1xco",
"1yco",
"2af3",
"2af4",
"3tng",
"3u9e",
"3uf6",
"4e4r",
"6iow",
"6iox",
"6zn9",
"6zne",
"6znk",
"6znr",
"6znt",
"6znu",
"7t88",
"7vg9",
"8fir"
] | 23 | [] | [] | [] | [] | 0 | [] | [
"IPR014079",
"IPR014081"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
50,
11710,
19,
141
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phosphate acetyl/butyryltransferase | Phosphate acetyl/butyryltransferase | P_Ac_Bu_trans | 8 |
IPR012148 | 12,148 | Aromatic prenyltransferase DMATS-type, fungi | ABBA_DMATS-like | Family | 1,661 | false | false | This family of fungal proteins includes tryptophan dimethylallyltransferase, cyclic dipeptide N-prenyltransferase (CdpNPT), fumigaclavine C synthase (FgaPT1), dimethylallyltryptophan synthase (DMATS), indole diterpene prenyltransferase anaPT and related proteins. CdpNPT accepts a variety of tryptophan-containing cyclic... | [
"GO:0016765",
"GO:0009820"
] | [
"transferase activity, transferring alkyl or aryl (other than methyl) groups",
"alkaloid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000509"
] | [
"Trp_DMAT"
] | [
1661
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"... | [
"2.5.1",
"2.5.1.-",
"PWY-4502",
"PWY-4681",
"PWY-5802",
"PWY-5815",
"PWY-5816",
"PWY-5817",
"PWY-5893",
"PWY-5979",
"PWY-6262",
"PWY-6403",
"PWY-6659",
"PWY-6681",
"PWY-6936",
"PWY-7372",
"PWY-7405",
"PWY-7407",
"PWY-7493",
"PWY-7520",
"PWY-7529",
"PWY-7532",
"PWY-7540",
... | [
"EC:2.5.1",
"EC:2.5.1.-",
"METACYC:PWY-4502",
"METACYC:PWY-4681",
"METACYC:PWY-5802",
"METACYC:PWY-5815",
"METACYC:PWY-5816",
"METACYC:PWY-5817",
"METACYC:PWY-5893",
"METACYC:PWY-5979",
"METACYC:PWY-6262",
"METACYC:PWY-6403",
"METACYC:PWY-6659",
"METACYC:PWY-6681",
"METACYC:PWY-6936",
... | 44 | [
"3i4x",
"3i4z",
"3o24",
"3o2k",
"4e0t",
"4e0u",
"4ld7",
"5kcg",
"5kcl",
"5kcq",
"5kcy",
"5kd0",
"5kd6",
"5kda",
"6vy9",
"6vya",
"7xvj",
"7y3v",
"8day",
"8daz",
"8db0",
"8db1",
"8y9d",
"8y9e",
"8y9g",
"9iia",
"9jhx"
] | 27 | [
"PUB00042956",
"PUB00080703",
"PUB00080704",
"PUB00083133"
] | [
"7488077",
"16397874",
"17525915",
"19001367"
] | [
"The Claviceps purpurea gene encoding dimethylallyltryptophan synthase, the committed step for ergot alkaloid biosynthesis.",
"Reverse prenyltransferase in the biosynthesis of fumigaclavine C in Aspergillus fumigatus: gene expression, purification, and characterization of fumigaclavine C synthase FGAPT1.",
"Cdp... | [
1995,
2006,
2007,
2009
] | 4 | [
"IPR017795"
] | [
"IPR017796"
] | 1 | 1 | 0 | [
"Dikarya"
] | [
1661
] | 1 | [] | [] | 0 | true | Family | Aromatic prenyltransferase DMATS-type, fungi | Aromatic prenyltransferase DMATS-type, fungi | ABBA_DMATS-like | 5 |
IPR012151 | 12,151 | Protein-tyrosine phosphatase, non-receptor type-3, -4 | Tyr_Pase_non-rcpt_typ-3/4 | Family | 2,145 | false | false | Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is ... | [
"GO:0004725",
"GO:0008092",
"GO:0006470"
] | [
"protein tyrosine phosphatase activity",
"cytoskeletal protein binding",
"protein dephosphorylation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF000927"
] | [
"Tyr-Ptase_nr3"
] | [
2145
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3.48",
"R-CEL-182971",
"R-CEL-5675221",
"R-HSA-166016",
"R-HSA-182971",
"R-HSA-5675221",
"R-HSA-9008059",
"R-HSA-9022699",
"R-MMU-166016",
"R-MMU-182971",
"R-MMU-5675221"
] | [
"EC:3.1.3.48",
"REACTOME:R-CEL-182971",
"REACTOME:R-CEL-5675221",
"REACTOME:R-HSA-166016",
"REACTOME:R-HSA-182971",
"REACTOME:R-HSA-5675221",
"REACTOME:R-HSA-9008059",
"REACTOME:R-HSA-9022699",
"REACTOME:R-MMU-166016",
"REACTOME:R-MMU-182971",
"REACTOME:R-MMU-5675221"
] | 11 | [
"6t36"
] | 1 | [
"PUB00035793",
"PUB00035794",
"PUB00035795",
"PUB00035796",
"PUB00035797",
"PUB00035798"
] | [
"9818190",
"14625689",
"12678841",
"16672235",
"8948575",
"9646865"
] | [
"Protein tyrosine phosphatases: mechanisms of catalysis and regulation.",
"Receptor and nonreceptor protein tyrosine phosphatases in the nervous system.",
"An overview of the protein tyrosine phosphatase superfamily.",
"The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase dom... | [
1998,
2003,
2003,
2006,
1996,
1998
] | 6 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
2145
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
11,
3,
6,
2,
15
] | 6 | true | Family | Protein-tyrosine phosphatase, non-receptor type-3, -4 | Protein-tyrosine phosphatase, non-receptor type-3, -4 | Tyr_Pase_non-rcpt_typ-3/4 | 2 |
IPR012152 | 12,152 | Protein-tyrosine phosphatase, non-receptor type-6, -11 | Tyr_Pase_non-rcpt_typ-6/11 | Family | 3,404 | false | false | Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is ... | [
"GO:0004725",
"GO:0006470"
] | [
"protein tyrosine phosphatase activity",
"protein dephosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000929"
] | [
"Tyr-Ptase_nr_6"
] | [
3404
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.3.48",
"R-CEL-6798695",
"R-GGA-1059683",
"R-GGA-109704",
"R-GGA-1257604",
"R-GGA-1433557",
"R-GGA-180292",
"R-GGA-186763",
"R-GGA-210990",
"R-GGA-210993",
"R-GGA-389513",
"R-GGA-389948",
"R-GGA-432142",
"R-GGA-512988",
"R-GGA-5654689",
"R-GGA-5654693",
"R-GGA-5654695",
"R-GGA-... | [
"EC:3.1.3.48",
"REACTOME:R-CEL-6798695",
"REACTOME:R-GGA-1059683",
"REACTOME:R-GGA-109704",
"REACTOME:R-GGA-1257604",
"REACTOME:R-GGA-1433557",
"REACTOME:R-GGA-180292",
"REACTOME:R-GGA-186763",
"REACTOME:R-GGA-210990",
"REACTOME:R-GGA-210993",
"REACTOME:R-GGA-389513",
"REACTOME:R-GGA-389948",
... | 183 | [
"2b3o",
"3ps5",
"4dgp",
"4dgx",
"4gwf",
"4h1o",
"4h34",
"4nwf",
"4nwg",
"4ohd",
"4ohe",
"4ohh",
"4ohi",
"4ohl",
"5bk8",
"5xzr",
"6cmp",
"6cmr",
"6cms",
"6wu8",
"7emn",
"7r75",
"7r7d",
"7r7i",
"7r7l",
"8rzw",
"8rzy",
"8s01",
"8s04",
"8s06",
"8s07",
"8s0h"... | 42 | [
"PUB00005794",
"PUB00020570",
"PUB00033259",
"PUB00035793",
"PUB00035794",
"PUB00035795",
"PUB00035796",
"PUB00035797",
"PUB00035798"
] | [
"9244303",
"9491886",
"7531337",
"9818190",
"14625689",
"12678841",
"16672235",
"8948575",
"9646865"
] | [
"Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling.",
"Crystal structure of the tyrosine phosphatase SHP-2.",
"Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling.",
"Protein tyrosine phosphatases: mechanisms of catalysis and regu... | [
1997,
1998,
1995,
1998,
2003,
2003,
2006,
1996,
1998
] | 9 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
3404
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
7,
10,
5,
10
] | 5 | true | Family | Protein-tyrosine phosphatase, non-receptor type-6, -11 | Protein-tyrosine phosphatase, non-receptor type-6, -11 | Tyr_Pase_non-rcpt_typ-6/11 | 7 |
IPR012153 | 12,153 | Tyrosine-protein phosphatase non-receptor type 13 | PTPN13 | Family | 1,473 | false | false | This entry represents non-receptor PTPase type 13 (also known as PTPL1, FAP-1 and PTP-BL). Studies indicate that this PTPase is involved in multiple regulatory functions including: negative regulation of FAS-induced apoptosis and NGFR-mediated pro-apoptotic signalling, regulation of the phophorylation status of ephrinB... | [
"GO:0004725",
"GO:0006470"
] | [
"protein tyrosine phosphatase activity",
"protein dephosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000933"
] | [
"Tyr-Ptase_nr13"
] | [
1473
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1660499",
"R-HSA-9008059",
"R-HSA-9696264",
"R-HSA-9696270",
"R-HSA-9696273",
"R-MMU-1660499",
"R-MMU-9696264",
"R-MMU-9696270",
"R-MMU-9696273"
] | [
"REACTOME:R-HSA-1660499",
"REACTOME:R-HSA-9008059",
"REACTOME:R-HSA-9696264",
"REACTOME:R-HSA-9696270",
"REACTOME:R-HSA-9696273",
"REACTOME:R-MMU-1660499",
"REACTOME:R-MMU-9696264",
"REACTOME:R-MMU-9696270",
"REACTOME:R-MMU-9696273"
] | 9 | [] | 0 | [
"PUB00033254",
"PUB00033255",
"PUB00033256",
"PUB00033257",
"PUB00033258"
] | [
"10544233",
"11983165",
"12529439",
"9544992",
"10951583"
] | [
"Functional interaction of Fas-associated phosphatase-1 (FAP-1) with p75(NTR) and their effect on NF-kappaB activation.",
"EphrinB phosphorylation and reverse signaling: regulation by Src kinases and PTP-BL phosphatase.",
"The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in th... | [
1999,
2002,
2003,
1998,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1473
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
18,
3,
3,
6
] | 4 | true | Family | Tyrosine-protein phosphatase non-receptor type 13 | Tyrosine-protein phosphatase non-receptor type 13 | PTPN13 | 7 |
IPR012156 | 12,156 | Cold shock, CspA | Cold_shock_CspA | Family | 66,633 | false | false | Temperature downshift produces a number of changes in cellular physiology including decreased membrane fluidity, reduced mRNA transcription and translation due to the stabilisation of secondary structures, inefficient folding of some proteins, and reduced enzyme activity [ ]. In response to this, bacteria produce a set... | [
"GO:0003676"
] | [
"nucleic acid binding"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF002599"
] | [
"Cold_shock_A"
] | [
66633
] | 1 | [] | [] | [] | 0 | [
"1c9o",
"1csp",
"1csq",
"1g6p",
"1h95",
"1hz9",
"1hza",
"1hzb",
"1hzc",
"1i5f",
"1mjc",
"1nmf",
"1nmg",
"2es2",
"2f52",
"2hax",
"2i5l",
"2i5m",
"2k5n",
"2l15",
"2lss",
"2lxj",
"2lxk",
"2mo0",
"2mo1",
"2n49",
"3a0j",
"3cam",
"3i2z",
"3mef",
"3pf4",
"3pf5"... | 52 | [
"PUB00023876",
"PUB00025145",
"PUB00029131",
"PUB00032978",
"PUB00033244"
] | [
"10736231",
"11322871",
"8321289",
"9692981",
"12530521"
] | [
"Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein.",
"Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.",
"Structure in solution of the major cold-shock protein from Bacillus subtilis.",
"Solution... | [
2000,
2001,
1993,
1998,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1578,
64032,
229,
21,
773
] | 5 | [
"Escherichia coli (strain K12)"
] | [
9
] | 1 | true | Family | Cold shock, CspA | Cold shock, CspA | Cold_shock_CspA | 7 |
IPR012159 | 12,159 | Inner membrane protein YejM-like | YejM-like | Family | 2,947 | false | false | This entry represents the inner membrane protein YejMfrom Escherichia coli. YejM (also known as LapC, PbgA) belongs to a regulatory system that controls the activity of LpxC, the enzyme that catalyses the first committed step in the LPS synthesis [ , , ]. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF004950"
] | [
"Mmb_sulf_HI0842"
] | [
2947
] | 1 | [] | [] | [] | 0 | [
"5i5d",
"5i5f",
"5i5h",
"6v8q",
"6xlp",
"7t6d"
] | 6 | [
"PUB00105698",
"PUB00105699",
"PUB00105700"
] | [
"33082366",
"33260377",
"33323515"
] | [
"The essential inner membrane protein YejM is a metalloenzyme.",
"Regulation of the First Committed Step in Lipopolysaccharide Biosynthesis Catalyzed by LpxC Requires the Essential Protein LapC (YejM) and HslVU Protease.",
"Restoring Balance to the Outer Membrane: YejM's Role in LPS Regulation."
] | [
2020,
2020,
2020
] | 3 | [] | [
"IPR047997"
] | 0 | 1 | 0 | [
"Bacteria",
"Knufia peltigerae",
"metagenomes"
] | [
2934,
1,
12
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Inner membrane protein YejM-like | Inner membrane protein YejM-like | YejM-like | 3 |
IPR012160 | 12,160 | Lipoteichoic acid synthase-like | LtaS-like | Family | 12,597 | false | false | This entry includes lipoteichoic acid synthase LtaS from Bacillus subtilis and some uncharacterised proteins, such as HI_1246 from Haemophilus influenzae. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF005091"
] | [
"Mmb_sulf_HI1246"
] | [
12597
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.8.-",
"PWY-6350",
"PWY-6580",
"PWY-6804",
"PWY-7815",
"PWY-7816",
"PWY-7817",
"PWY-7818",
"PWY-7819",
"PWY-7820",
"PWY-7981",
"PWY-8248"
] | [
"EC:2.7.8.-",
"METACYC:PWY-6350",
"METACYC:PWY-6580",
"METACYC:PWY-6804",
"METACYC:PWY-7815",
"METACYC:PWY-7816",
"METACYC:PWY-7817",
"METACYC:PWY-7818",
"METACYC:PWY-7819",
"METACYC:PWY-7820",
"METACYC:PWY-7981",
"METACYC:PWY-8248"
] | 12 | [] | 0 | [
"PUB00078041"
] | [
"17483484"
] | [
"Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus aureus."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Streptococcus phage 20617",
"metagenomes"
] | [
12509,
4,
1,
83
] | 4 | [] | [] | 0 | true | Family | Lipoteichoic acid synthase-like | Lipoteichoic acid synthase-like | LtaS-like | 9 |
IPR012163 | 12,163 | Sialyltransferase | Sialyl_trans | Family | 14,306 | false | false | The sialyltransferase family represents a group of enzymes that transfers sialic acid from its common nucleotide sugar donor, CMP-beta-N-acetylneuraminate, to the terminal carbohydrates group of various glycoproteins and glycolipids. Animal sialyltransferases have type II transmembrane topology, and are thought to loca... | [
"GO:0008373",
"GO:0009101"
] | [
"sialyltransferase activity",
"glycoprotein biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF005557"
] | [
"Sialyl_trans"
] | [
14306
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.4.3",
"R-BTA-2022854",
"R-BTA-4085001",
"R-BTA-9037629",
"R-GGA-2022854",
"R-GGA-4085001",
"R-GGA-977068",
"R-HSA-1912420",
"R-HSA-2022854",
"R-HSA-3656243",
"R-HSA-4085001",
"R-HSA-419037",
"R-HSA-9037629",
"R-HSA-9683673",
"R-HSA-9694548",
"R-HSA-9694719",
"R-HSA-975577",
"R-H... | [
"EC:2.4.3",
"REACTOME:R-BTA-2022854",
"REACTOME:R-BTA-4085001",
"REACTOME:R-BTA-9037629",
"REACTOME:R-GGA-2022854",
"REACTOME:R-GGA-4085001",
"REACTOME:R-GGA-977068",
"REACTOME:R-HSA-1912420",
"REACTOME:R-HSA-2022854",
"REACTOME:R-HSA-3656243",
"REACTOME:R-HSA-4085001",
"REACTOME:R-HSA-419037"... | 34 | [
"2wml",
"2wnb",
"2wnf",
"4js1",
"4js2",
"4mps",
"5bo6",
"5bo7",
"5bo8",
"5bo9",
"5cxy",
"6apj",
"6apl",
"6qvs",
"6qvt"
] | 15 | [
"PUB00070955",
"PUB00070956",
"PUB00070957"
] | [
"18460788",
"19822337",
"24825296"
] | [
"Characterization of mouse sialyltransferase genes: their evolution and diversity.",
"Analysis of CMP-sialic acid transporter-like proteins in plants.",
"The cell wall pectic polymer rhamnogalacturonan-II is required for proper pollen tube elongation: implications of a putative sialyltransferase-like protein."
... | [
2008,
2009,
2014
] | 3 | [
"IPR001675"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Viruses"
] | [
14292,
14
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
76,
50,
43,
42
] | 4 | true | Family | Sialyltransferase | Sialyltransferase | Sialyl_trans | 9 |
IPR012164 | 12,164 | DNA-directed RNA polymerase subunit/transcription factor S | Rpa12/Rpb9/Rpc10/TFS | Family | 13,034 | false | false | DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerase... | [
"GO:0003899",
"GO:0006351"
] | [
"DNA-directed RNA polymerase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF005586",
"PTHR11239"
] | [
"RNApol_RpoM",
""
] | [
10466,
12964
] | 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-5250924",
"R-BTA-73762",
"R-BTA-73772",
"R-BTA-73863",
"R-CEL-112382",
"R-CEL-113418",
"R-CEL-5578749",
"R-CEL-674695",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-6796648",
"R-CEL-6803529",
"R-CEL-6807505",
"R-CEL-72086",
"R-CEL-72163",
"R-CEL-72165",
"R-CEL-7... | [
"REACTOME:R-BTA-5250924",
"REACTOME:R-BTA-73762",
"REACTOME:R-BTA-73772",
"REACTOME:R-BTA-73863",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-113418",
"REACTOME:R-CEL-5578749",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6781823",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-6... | 189 | [
"1i3q",
"1i50",
"1i6h",
"1k83",
"1nik",
"1nt9",
"1pqv",
"1qyp",
"1r5u",
"1r9s",
"1r9t",
"1sfo",
"1twa",
"1twc",
"1twf",
"1twg",
"1twh",
"1wcm",
"1y1v",
"1y1w",
"1y1y",
"1y77",
"2b63",
"2b8k",
"2e2h",
"2e2i",
"2e2j",
"2ja5",
"2ja6",
"2ja7",
"2ja8",
"2nvq"... | 508 | [
"PUB00000061",
"PUB00008731",
"PUB00009536",
"PUB00018563",
"PUB00029086",
"PUB00033173",
"PUB00078615",
"PUB00099581"
] | [
"3052291",
"11313498",
"10777522",
"14963322",
"12782794",
"10499798",
"15130130",
"29203770"
] | [
"Structure and function of bacterial sigma factors.",
"Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.",
"Transcription factor S, a cleavage induction factor of the archaeal RNA polymerase.",
"Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angst... | [
1988,
2001,
2000,
2004,
2003,
1999,
2004,
2017
] | 8 | [] | [
"IPR006288"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1275,
6,
11588,
73,
92
] | 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... | [
19,
3,
4,
6,
6,
7,
3,
17,
11,
3,
3,
29
] | 12 | true | Family | DNA-directed RNA polymerase subunit/transcription factor S | DNA-directed RNA polymerase subunit/transcription factor S | Rpa12/Rpb9/Rpc10/TFS | 7 |
IPR012165 | 12,165 | Cytochrome-c3 hydrogenase, gamma subunit | Cyt_c3_hydrogenase_gsu | Family | 13,939 | false | false | This entry consists of electron transfer proteins found as components of oxidoreductase enzymes in bacteria and archaea. So far, these proteins have been shown to be components of sulphite reductase, which catalyses the production of hydrogen sulphide from sulphite, dihydroorotate dehydrogenase involved in pyrimidine b... | [
"GO:0050660",
"GO:0051537",
"GO:0006221"
] | [
"flavin adenine dinucleotide binding",
"2 iron, 2 sulfur cluster binding",
"pyrimidine nucleotide biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF006816"
] | [
"Cyc3_hyd_g"
] | [
13939
] | 1 | [] | [] | [] | 0 | [
"1ep1",
"1ep2",
"1ep3",
"2eix",
"4ylf",
"4yry",
"5jca",
"5jfc",
"5ksw",
"5ue9",
"5vj7",
"9nez",
"9nf0"
] | 13 | [
"PUB00002132",
"PUB00024613",
"PUB00033241",
"PUB00033242"
] | [
"1704886",
"11188687",
"8910599",
"7704275"
] | [
"Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite.",
"Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.",
"The B form of dihydroorotate dehydrogenase from Lact... | [
1991,
2000,
1996,
1995
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
907,
12565,
5,
462
] | 4 | [] | [] | 0 | true | Family | Cytochrome-c3 hydrogenase, gamma subunit | Cytochrome-c3 hydrogenase, gamma subunit | Cyt_c3_hydrogenase_gsu | 2 |
IPR012166 | 12,166 | Uncharacterised protein family RocB | Uncharacterised_RocB | Family | 1,907 | false | false | This group contains RocB of Bacillus subtilis and related proteins. RocB is one of the three genes found in the rocABC operon in B. subtilis, which is sigma L dependent and induced by arginine, suggesting it is involved in the arginine degradation pathway. The function of members of this family is unknown, though they ... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF010386"
] | [
"RocB"
] | [
1907
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR002933"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"bioreactor metagenome"
] | [
1902,
5
] | 2 | [] | [] | 0 | true | Family | Uncharacterised protein family RocB | Uncharacterised protein family RocB | Uncharacterised_RocB | 2 |
IPR012167 | 12,167 | Cyclin, epsilonretrovirus | Cyclin_epsilonretrovir | Family | 3 | false | false | Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [ ], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essenti... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF015200"
] | [
"Cyclin_WDSV"
] | [
3
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014101",
"PUB00014103"
] | [
"11056549",
"12910258"
] | [
"Cyclin' on the viral path to destruction.",
"Cell cycle regulation and neural differentiation."
] | [
2000,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Epsilonretrovirus"
] | [
3
] | 1 | [] | [] | 0 | true | Family | Cyclin, epsilonretrovirus | Cyclin, epsilonretrovirus | Cyclin_epsilonretrovir | 6 |
IPR012170 | 12,170 | TFIIH subunit Ssl1/p44 | TFIIH_SSL1/p44 | Family | 4,288 | false | false | This entry represents Ssl1/p44m (also known as GTF2H2), which is a component of the transcription factor TFIIH core (includes XPB, p62, p52, p44, p34) [ , ]. TFIIH complex is involved in nucleotide excision repair (NER) of damaged DNA and in RNA transcription by RNA polymerase II [ , ]. | [
"GO:0006289",
"GO:0006351",
"GO:0000439"
] | [
"nucleotide-excision repair",
"DNA-templated transcription",
"transcription factor TFIIH core complex"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF015919",
"TIGR00622"
] | [
"TFIIH_SSL1",
"ssl1"
] | [
3666,
4149
] | 2 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp2048",
"R-BTA-113418",
"R-BTA-5696395",
"R-BTA-5696400",
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-72086",
"R-BTA-73762",
"R-BTA-73772",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-73863",
"R-BTA-75953",
"R-BTA-75955",
"R-BTA-76042"... | [
"GP:GenProp2048",
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-5696395",
"REACTOME:R-BTA-5696400",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-72086",
"REACTOME:R-BTA-73762",
"REACTOME:R-BTA-73772"... | 145 | [
"1z60",
"5ivw",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5nus",
"5o85",
"5obz",
"5of4",
"5oqj",
"5oqm",
"6gym",
"6nmi",
"6o9l",
"6o9m",
"6ro4",
"7ad8",
"7egb",
"7egc",
"7ena",
"7enc",
"7k01",
"7k04",
"7lbm",
"7m2u",
"7ml0",
"7ml1",
"7ml2",
"7ml3",
"7ml4",
"7nvr"... | 73 | [
"PUB00056880",
"PUB00062838",
"PUB00151276"
] | [
"8631896",
"7961739",
"30798933"
] | [
"Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair.",
"RNA polymerase transcription factor IIH holoenzyme from yeast.",
"TFIIH: A multi-subunit complex at the cross-roads of transcription and DNA repair."
] | [
1996,
1994,
2019
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4288
] | 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... | [
6,
1,
2,
1,
3,
4,
1,
2,
2,
1,
1,
4
] | 12 | true | Family | TFIIH subunit Ssl1/p44 | TFIIH subunit Ssl1/p44 | TFIIH_SSL1/p44 | 2 |
IPR012171 | 12,171 | Fatty acid desaturase | Fatty_acid_desaturase | Family | 44,972 | false | false | This entry includes fatty acid desaturase family members from bacteria, fungi, plants and animals. Proteins in this family contain the fatty acid desaturase domain ( ). The eukaryotic members, including human FADS1 and FADS2, are fusion proteins containing an N-terminal cytochrome b5-like domain and a C-terminal multip... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"PANTHER",
"PANTHER"
] | [
"PIRSF015921",
"PTHR19353",
"PTHR32100"
] | [
"FA_sphinglp_des",
"",
""
] | [
14328,
32363,
12601
] | 3 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.19",
"R-BTA-2046105",
"R-BTA-2046106",
"R-CEL-2046105",
"R-CEL-2046106",
"R-DRE-2046105",
"R-DRE-2046106",
"R-HSA-1989781",
"R-HSA-2046105",
"R-HSA-2046106",
"R-MMU-2046105",
"R-MMU-2046106",
"R-RNO-2046105",
"R-RNO-2046106"
] | [
"EC:1.14.19",
"REACTOME:R-BTA-2046105",
"REACTOME:R-BTA-2046106",
"REACTOME:R-CEL-2046105",
"REACTOME:R-CEL-2046106",
"REACTOME:R-DRE-2046105",
"REACTOME:R-DRE-2046106",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-2046105",
"REACTOME:R-HSA-2046106",
"REACTOME:R-MMU-2046105",
"REACTOME:R-MMU-2046... | 14 | [
"8xks",
"8xqw",
"8xqx"
] | 3 | [
"PUB00074247",
"PUB00074248",
"PUB00095632"
] | [
"25123259",
"10860662",
"31916624"
] | [
"Fatty acid desaturase 1 gene polymorphisms control human hepatic lipid composition.",
"cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family.",
"Biosynthesis of the anti-lipid-microdomain sphingoid base 4,14-sphingadiene by the ceramide desatur... | [
2015,
2000,
2020
] | 3 | [] | [
"IPR039393",
"IPR054678"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
20559,
24117,
12,
284
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
36,
5,
3,
3,
36,
19,
3,
35,
22,
64
] | 10 | true | Family | Fatty acid desaturase | Fatty acid desaturase | Fatty_acid_desaturase | 1 |
IPR012173 | 12,173 | U3 small nucleolar ribonucleoprotein complex, subunit Mpp10 | Mpp10 | Family | 5,084 | false | false | Mpp10 (M phase phosphoprotein 10) is a component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP) required for three cleavage events that generate the mature 18S rRNA from the pre-rRNA [ , ]. | [
"GO:0006364",
"GO:0005634",
"GO:0005732",
"GO:0034457"
] | [
"rRNA processing",
"nucleus",
"sno(s)RNA-containing ribonucleoprotein complex",
"Mpp10 complex"
] | [
"biological_process",
"cellular_component",
"cellular_component",
"cellular_component"
] | 4 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF04006",
"PIRSF017300",
"PTHR17039"
] | [
"Mpp10",
"snoRNP_Mpp10",
""
] | [
5039,
3586,
4964
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6790901",
"R-HSA-6791226",
"R-MMU-6791226",
"R-SCE-6791226",
"R-SPO-6791226"
] | [
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-6791226",
"REACTOME:R-SCE-6791226",
"REACTOME:R-SPO-6791226"
] | 5 | [
"5o9e",
"5oql",
"5wlc",
"5wxm",
"5wyj",
"5wyk",
"6ke6",
"6lqp",
"6lqq",
"6lqr",
"6lqs",
"6lqt",
"6lqu",
"6lqv",
"6nd4",
"6rxt",
"6rxu",
"6rxv",
"6rxx",
"6rxy",
"6rxz",
"6zqa",
"6zqb",
"6zqc",
"6zqd",
"6zqe",
"6zqf",
"6zqg",
"7ajt",
"7aju",
"7d4i",
"7d5s"... | 56 | [
"PUB00009804",
"PUB00019879"
] | [
"9391061",
"9450966"
] | [
"Functional separation of pre-rRNA processing steps revealed by truncation of the U3 small nucleolar ribonucleoprotein component, Mpp10.",
"M phase phosphoprotein 10 is a human U3 small nucleolar ribonucleoprotein component."
] | [
1997,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5084
] | 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... | [
5,
1,
3,
1,
5,
5,
1,
7,
5,
1,
1,
6
] | 12 | true | Family | U3 small nucleolar ribonucleoprotein complex, subunit Mpp10 | U3 small nucleolar ribonucleoprotein complex, subunit Mpp10 | Mpp10 | 5 |
IPR012175 | 12,175 | Xanthine dehydrogenase, small subunit, bacteria | Xanth_DH_ssu_bac | Family | 5,689 | false | false | Xanthine dehydrogenase is a complex metallo-flavoprotein catalysing the oxidation of hypoxanthine to xanthine followed by oxidation of xanthine to uric acid, linked to the reduction of NAD(+). Additionally, this enzyme can catalyse the oxidative hydroxylation of purines, pyrimidines, pterins, and aldehyde substrates. T... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036557"
] | [
"XdhA_RC"
] | [
5689
] | 1 | [] | [] | [] | 0 | [
"1jro",
"1jrp",
"2w3r",
"2w3s",
"2w54",
"2w55"
] | 6 | [
"PUB00026513",
"PUB00033237"
] | [
"11796116",
"9515710"
] | [
"Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus.",
"Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes."
] | [
2002,
1998
] | 2 | [
"IPR016208"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5642,
6,
41
] | 3 | [] | [] | 0 | true | Family | Xanthine dehydrogenase, small subunit, bacteria | Xanthine dehydrogenase, small subunit, bacteria | Xanth_DH_ssu_bac | 9 |
IPR012176 | 12,176 | Bifunctional nitroreductase/nicotinate-nucleotide-dimethylbenzimidazole, phosphoribosyltransferase | NRdtase/NN_dMeBzImd_PRibTrfase | Family | 4 | false | false | Nicotinate mononucleotide (NaMN):5,6-dimethylbenzimidazole (DMB) phosphoribosyltransferase (CobT) plays a central role in the synthesis of alpha-ribazole-5'-phosphate, an intermediate for the lower ligand of cobalamin [ ]. It is one of the enzymes of the anaerobic pathway of cobalamin biosynthesis, and one of the four ... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036558"
] | [
"Ntrrd_NNDBI_PRT"
] | [
4
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009745",
"PUB00014667",
"PUB00014670",
"PUB00014672",
"PUB00015874",
"PUB00015996"
] | [
"7592411",
"12196148",
"8550510",
"11153269",
"12101181",
"8206834"
] | [
"The cobalamin (coenzyme B12) biosynthetic genes of Escherichia coli.",
"Biosynthesis of cobalamin (vitamin B(12)).",
"Salmonella typhimurium cobalamin (vitamin B12) biosynthetic genes: functional studies in S. typhimurium and Escherichia coli.",
"Multiple biosynthetic pathways for vitamin B12: variations on ... | [
1995,
2002,
1996,
2001,
2002,
1994
] | 6 | [
"IPR017846"
] | [] | 1 | 0 | 1 | [
"Streptomyces"
] | [
4
] | 1 | [] | [] | 0 | true | Family | Bifunctional nitroreductase/nicotinate-nucleotide-dimethylbenzimidazole, phosphoribosyltransferase | Bifunctional nitroreductase/nicotinate-nucleotide-dimethylbenzimidazole, phosphoribosyltransferase | NRdtase/NN_dMeBzImd_PRibTrfase | 1 |
IPR012177 | 12,177 | Thiamine triphosphatase, eukaryotes | ThTPase_euk | Family | 642 | false | false | Thiamine triphosphate (ThTP), the triphosphorylated form of vitamin B1, is found in most organisms including bacteria, fungi, plants and animals. In mammals, cytosolic ThTP concentration is kept low by a highly specific soluble phosphohydrolase, the 25kDa thiamine triphosphatase (ThTPase) [ ]. This entry includes the 2... | [
"GO:0050333",
"GO:0006772"
] | [
"thiamine triphosphate phosphatase activity",
"thiamine metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"CDD"
] | [
"PIRSF036561",
"cd07758"
] | [
"ThTPase",
"ThTPase"
] | [
228,
640
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.1.28",
"PWY-7369",
"R-BTA-196819",
"R-HSA-196819",
"R-MMU-196819",
"R-RNO-196819"
] | [
"EC:3.6.1.28",
"METACYC:PWY-7369",
"REACTOME:R-BTA-196819",
"REACTOME:R-HSA-196819",
"REACTOME:R-MMU-196819",
"REACTOME:R-RNO-196819"
] | 6 | [
"2jmu",
"3bhd",
"3tvl",
"5a64",
"5a65"
] | 5 | [
"PUB00072561"
] | [
"23707715"
] | [
"Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase."
] | [
2013
] | 1 | [
"IPR039582"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
642
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
1,
1,
5
] | 4 | true | Family | Thiamine triphosphatase, eukaryotes | Thiamine triphosphatase, eukaryotes | ThTPase_euk | 2 |
IPR012178 | 12,178 | Replication factor C subunit 1 | RFC1 | Family | 4,624 | false | false | This entry represents replication factor C subunit 1 (RFC1), which is the large subunit of replication factor C (RF-C), a five subunit DNA polymerase accessory protein. RF-C is a DNA binding protein complex and ATPase that acts as a clamp loader of the proliferating cell nuclear antigen (PCNA) processivity factor for D... | [
"GO:0003689",
"GO:0005524",
"GO:0006260",
"GO:0006281",
"GO:0005663"
] | [
"DNA clamp loader activity",
"ATP binding",
"DNA replication",
"DNA repair",
"DNA replication factor C complex"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PIRSF"
] | [
"PIRSF036578"
] | [
"RFC1"
] | [
4624
] | 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-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",
"R-DME-6782135",
"R-DME-6782210",
"R-DME-69091",
"R-HSA-110312",
"R-HSA-110314",
"R-HSA-110320",
"R-HSA-174411",
"R-HSA-5651801",
"R... | [
"REACTOME:R-DME-110312",
"REACTOME:R-DME-110314",
"REACTOME:R-DME-110320",
"REACTOME:R-DME-5651801",
"REACTOME:R-DME-5655862",
"REACTOME:R-DME-5656121",
"REACTOME:R-DME-5656169",
"REACTOME:R-DME-5696397",
"REACTOME:R-DME-5696400",
"REACTOME:R-DME-6782135",
"REACTOME:R-DME-6782210",
"REACTOME:R... | 61 | [
"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 | [
"PUB00073556",
"PUB00073557"
] | [
"14530260",
"8954124"
] | [
"Replication factor C clamp loader subunit arrangement within the circular pentamer and its attachment points to proliferating cell nuclear antigen.",
"Replication factor C recognizes 5'-phosphate ends of telomeres."
] | [
2003,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Medusavirus",
"viral metagenome"
] | [
4621,
2,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
1,
2,
1,
1,
5,
1,
3,
6,
1,
1,
14
] | 12 | true | Family | Replication factor C subunit 1 | Replication factor C subunit 1 | RFC1 | 8 |
IPR012179 | 12,179 | [NiFe]-hydrogenase-3-type complex Ech, subunit EchD | NiFe-hyd_3_EchD | Family | 151 | false | false | [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions [NiFe] hydrogenases consist of two subunits, hydrogenase large and hydrogenase small. The large subunit contains the binuclear [NiFe] active sit... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036585"
] | [
"EchD"
] | [
151
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00035516",
"PUB00035517",
"PUB00035518",
"PUB00096941"
] | [
"15168611",
"16645307",
"15119826",
"22872868"
] | [
"Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I.",
"Energy-converting [NiFe] hydrogenases: more than just H2 activation.",
"Molecular biology of microbial hydrogenases.",
"Essential anaplerotic role for the energy-converting hydrogenase Eha in hydrogenotrophic met... | [
2004,
2005,
2004,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanomicrobia",
"ecological metagenomes"
] | [
122,
25,
4
] | 3 | [] | [] | 0 | true | Family | [NiFe]-hydrogenase-3-type complex Ech, subunit EchD | [NiFe]-hydrogenase-3-type complex Ech, subunit EchD | NiFe-hyd_3_EchD | 7 |
IPR012180 | 12,180 | Predicted bifunctional ATPase/phosphotransferase | Bifunc_ATPase/PTrfase | Family | 907 | false | false | This entry represents a predicted bifunctional ATPase/phosphotransferase involved in cell wall biosynthesis. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036599"
] | [
"AtpPhos"
] | [
907
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Alphaproteobacteria",
"Effrenium voratum",
"ecological metagenomes"
] | [
903,
1,
3
] | 3 | [] | [] | 0 | true | Family | Predicted bifunctional ATPase/phosphotransferase | Predicted bifunctional ATPase/phosphotransferase | Bifunc_ATPase/PTrfase | 1 |
IPR012182 | 12,182 | Bifunctional molybdenum cofactor biosynthesis MobB/MoeA | MobB_MoeA | Family | 528 | false | false | The majority of molybdenum-containing enzymes utilise a molybdenum cofactor (MoCF or Moco) consisting of a Mo atom coordinated via a cis-dithiolene moiety to molybdopterin (MPT). MoCF is ubiquitous in nature, and the pathway for MoCF biosynthesis is conserved in all three domains of life. MoCF-containing enzymes functi... | [] | [] | [] | 0 | [
"NCBIFAM",
"PIRSF"
] | [
"NF011060",
"PIRSF036618"
] | [
"PRK14491.1",
"MobB_MoeA"
] | [
528,
361
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015635",
"PUB00015921",
"PUB00034757",
"PUB00034758",
"PUB00034759"
] | [
"12372836",
"8528286",
"12114025",
"17198377",
"16784786"
] | [
"In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli.",
"Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamo... | [
2002,
1995,
2002,
2007,
2006
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome"
] | [
526,
2
] | 2 | [] | [] | 0 | true | Family | Bifunctional molybdenum cofactor biosynthesis MobB/MoeA | Bifunctional molybdenum cofactor biosynthesis MobB/MoeA | MobB_MoeA | 6 |
IPR012183 | 12,183 | Bifunctional FAD diphosphatase/FAD synthase | FLAD1 | Family | 681 | false | false | This entry represents Bifunctional FAD diphosphatase/FAD synthase (FLAD1) found in metazoans. FLAD1 is a bifunctional protein possessing both FAD diphosphatase and FAD synthase activities [ , , , , , , , , ]. The FAD diphosphatase activity hydrolyses FAD and NADH to produce FMN and NMNH, respectively [ , , ]. The FAD s... | [
"GO:0003919",
"GO:0006747"
] | [
"FMN adenylyltransferase activity",
"FAD biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF036620"
] | [
"MPTbdFAD"
] | [
681
] | 1 | [
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.2",
"3.6.1.18",
"3.6.1.22",
"PWY-5381",
"PWY-6167",
"PWY-6168",
"PWY-7761",
"R-CEL-196843",
"R-DRE-196843",
"R-HSA-196843",
"R-MMU-196843"
] | [
"EC:2.7.7.2",
"EC:3.6.1.18",
"EC:3.6.1.22",
"METACYC:PWY-5381",
"METACYC:PWY-6167",
"METACYC:PWY-6168",
"METACYC:PWY-7761",
"REACTOME:R-CEL-196843",
"REACTOME:R-DRE-196843",
"REACTOME:R-HSA-196843",
"REACTOME:R-MMU-196843"
] | 11 | [
"8ron"
] | 1 | [
"PUB00010127",
"PUB00030175",
"PUB00035657",
"PUB00043603",
"PUB00043604",
"PUB00159016",
"PUB00163247",
"PUB00163248",
"PUB00163249",
"PUB00163250",
"PUB00163251",
"PUB00163252",
"PUB00163253",
"PUB00163254"
] | [
"12517446",
"14580199",
"17049878",
"16643857",
"16183635",
"27259049",
"21924249",
"21951714",
"23443125",
"25135855",
"25954742",
"26277395",
"31351152",
"38688286"
] | [
"A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer.",
"Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism.",
"Over-expression in Escherichia coli, purification and characterization of isoform 2 ... | [
2003,
2003,
2007,
2006,
2005,
2016,
2011,
2011,
2012,
2014,
2015,
2015,
2019,
2024
] | 14 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
681
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
1,
1,
3
] | 5 | true | Family | Bifunctional FAD diphosphatase/FAD synthase | Bifunctional FAD diphosphatase/FAD synthase | FLAD1 | 2 |
IPR012184 | 12,184 | Bifunctional molybdopterin binding protein /nucleotidyl transferase, putative | Bifunc_Mopterin-bd | Family | 854 | false | false | This group represents a predicted bifunctional molybdopterin binding protein /nucleotidyl transferase. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036626"
] | [
"MPTBd_MobAlike"
] | [
854
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
849,
5
] | 2 | [] | [] | 0 | true | Family | Bifunctional molybdopterin binding protein /nucleotidyl transferase, putative | Bifunctional molybdopterin binding protein /nucleotidyl transferase, putative | Bifunc_Mopterin-bd | 6 |
IPR012186 | 12,186 | Adenine modification methylase, M.StsI-type | Ade-mod_methylase_MStsI | Family | 190 | false | false | In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. Adenine modification methylases are a large group of enzymes, most of which form so-called 'restriction-modification systems'. Methylation of specific adenine residues is required for both restriction an... | [
"GO:0009007",
"GO:0009307"
] | [
"site-specific DNA-methyltransferase (adenine-specific) activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF036638"
] | [
"M_m6A_StsI"
] | [
190
] | 1 | [
"EC"
] | [
"2.1.1.72"
] | [
"EC:2.1.1.72"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR012327"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Siphoviridae sp. ctcfw7",
"bioreactor metagenome",
"uncultured marine group II/III euryarchaeote KM3_74_C08"
] | [
187,
1,
1,
1
] | 4 | [] | [] | 0 | true | Family | Adenine modification methylase, M.StsI-type | Adenine modification methylase, M.StsI-type | Ade-mod_methylase_MStsI | 8 |
IPR012187 | 12,187 | Disulphide bond formation protein BdbC | Disulphide_bond_form_BdbC | Family | 3,274 | false | false | Disulphide bonds contribute to folding, maturation, stability, and regulation of proteins, in particular those localized out of the cytosol. Oxidation of selected pairs of cysteines to disulphide in vivo requires cellular factors present in the bacterial periplasmic space or in the endoplasmic reticulum of eukaryotic c... | [] | [] | [] | 0 | [
"HAMAP",
"PIRSF",
"PANTHER"
] | [
"MF_00287",
"PIRSF036659",
"PTHR43469"
] | [
"BdbC",
"BdbC",
""
] | [
1992,
2852,
3274
] | 3 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014003",
"PUB00053944",
"PUB00054232"
] | [
"12524212",
"11844773",
"12415301"
] | [
"Protein disulfide bond formation in prokaryotes.",
"Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells.",
"Formation and transfer of disulphide bonds in living cells."
] | [
2003,
2002,
2002
] | 3 | [
"IPR003752"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacillus phage SPbeta",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
180,
1,
3034,
6,
53
] | 5 | [] | [] | 0 | true | Family | Disulphide bond formation protein BdbC | Disulphide bond formation protein BdbC | Disulphide_bond_form_BdbC | 1 |
IPR012188 | 12,188 | NAD(P)-dependent malic enzyme | ME_PTA | Family | 12,596 | false | false | Malic enzymes, or malate oxidoreductases, catalyze the oxidative decarboxylation of malate into pyruvate important for a wide range of metabolic pathways [ , ]. | [
"GO:0004470",
"GO:0046872",
"GO:0006108"
] | [
"malic enzyme activity",
"metal ion binding",
"malate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF036684"
] | [
"ME_PTA"
] | [
12596
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.1.1.40",
"PWY-241",
"PWY-7117"
] | [
"EC:1.1.1.40",
"METACYC:PWY-241",
"METACYC:PWY-7117"
] | 3 | [
"6zng",
"6znj",
"8jzo"
] | 3 | [
"PUB00002681",
"PUB00002876"
] | [
"1993674",
"8300616"
] | [
"Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli.",
"Cloning and analysis of the C4 photosynthetic NAD-dependent malic enzyme of amaranth mitochondria."
] | [
1991,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Siphoviridae sp. ctYaH2",
"unclassified sequences"
] | [
12039,
7,
471,
1,
78
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | NAD(P)-dependent malic enzyme | NAD(P)-dependent malic enzyme | ME_PTA | 5 |
IPR012189 | 12,189 | Peptidase M28E, aminopeptidase AP1 | Pept_M28E_Ap1 | Family | 531 | false | false | Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036685"
] | [
"BacLeuNPeptidase"
] | [
531
] | 1 | [] | [] | [] | 0 | [
"1amp",
"1cp6",
"1ft7",
"1igb",
"1lok",
"1rtq",
"1txr",
"1xry",
"2anp",
"2dea",
"2iq6",
"2nyq",
"2prq",
"3b35",
"3b3c",
"3b3s",
"3b3t",
"3b3v",
"3b3w",
"3b7i",
"3fh4",
"3vh9"
] | 22 | [
"PUB00003579",
"PUB00016219",
"PUB00016220"
] | [
"7674922",
"11302179",
"8087555"
] | [
"Evolutionary families of metallopeptidases.",
"Characterization of the pro-aminopeptidase from Aeromonas caviae T-64.",
"Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family."
] | [
1995,
2001,
1994
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
531
] | 1 | [] | [] | 0 | true | Family | Peptidase M28E, aminopeptidase AP1 | Peptidase M28E, aminopeptidase AP1 | Pept_M28E_Ap1 | 4 |
IPR012190 | 12,190 | Uncharacterised conserved protein UCP036698, YpmA | UCP036698 | Family | 837 | false | false | This group represents an uncharacterised conserved protein, Bacillus YpmA type. | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF14084",
"PIRSF036698"
] | [
"DUF4264",
"UCP036698"
] | [
837,
685
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillati",
"ecological metagenomes"
] | [
834,
3
] | 2 | [] | [] | 0 | true | Family | Uncharacterised conserved protein UCP036698, YpmA | Uncharacterised conserved protein UCP036698, YpmA | UCP036698 | 1 |
IPR012198 | 12,198 | cAMP-dependent protein kinase regulatory subunit | cAMP_dep_PK_reg_su | Family | 7,342 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0008603",
"GO:0001932",
"GO:0005952"
] | [
"cAMP-dependent protein kinase regulator activity",
"regulation of protein phosphorylation",
"cAMP-dependent protein kinase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF"
] | [
"PIRSF000548"
] | [
"PK_regulatory"
] | [
7342
] | 1 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp2095",
"R-BTA-163615",
"R-BTA-164378",
"R-BTA-180024",
"R-BTA-432040",
"R-BTA-442720",
"R-BTA-5610787",
"R-BTA-9634597",
"R-BTA-983231",
"R-BTA-9856530",
"R-CEL-163615",
"R-CEL-164378",
"R-CEL-180024",
"R-CEL-432040",
"R-CEL-442720",
"R-CEL-5610787",
"R-CEL-9634597",
"R-CEL... | [
"GP:GenProp2095",
"REACTOME:R-BTA-163615",
"REACTOME:R-BTA-164378",
"REACTOME:R-BTA-180024",
"REACTOME:R-BTA-432040",
"REACTOME:R-BTA-442720",
"REACTOME:R-BTA-5610787",
"REACTOME:R-BTA-9634597",
"REACTOME:R-BTA-983231",
"REACTOME:R-BTA-9856530",
"REACTOME:R-CEL-163615",
"REACTOME:R-CEL-164378"... | 111 | [
"1cx4",
"1ne4",
"1ne6",
"1rgs",
"1rl3",
"2qcs",
"2qvs",
"3j4q",
"3j4r",
"3shr",
"3tnp",
"3tnq",
"4din",
"4jv4",
"4jva",
"4mx3",
"4wbb",
"4x6q",
"4x6r",
"4z07",
"5j3u",
"5jr7",
"5kbf",
"6byr",
"6bys",
"6flo",
"6ftf",
"6h4g",
"6hyi",
"6hyq",
"6no7",
"6rsx"... | 39 | [
"PUB00005115",
"PUB00007194",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899"
] | [
"3291115",
"11734894",
"12368087",
"12471243",
"15078142",
"15320712"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Classification and phylogenetic analysis of the cAMP-dependent protein kinase regulatory subunit family.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human g... | [
1988,
2002,
2002,
2002,
2004,
2004
] | 6 | [
"IPR050503"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
7342
] | 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... | [
1,
9,
6,
13,
12,
1,
8,
1,
1
] | 9 | true | Family | cAMP-dependent protein kinase regulatory subunit | cAMP-dependent protein kinase regulatory subunit | cAMP_dep_PK_reg_su | 2 |
IPR012206 | 12,206 | Ferredoxin-like, FixX | Fd_FixX | Family | 3,082 | false | false | Rhizobium meliloti (Sinorhizobium meliloti) FixX protein contains a cluster of cysteine residues characteristic of bacterial ferredoxins [ ]. The gene product from Escherichia coli could be a 3Fe-4S cluster-containing protein. These are highly homologous to an Azotobacter ferredoxin which has been shown to donate elect... | [
"GO:0005506"
] | [
"iron ion binding"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF036548",
"PTHR43082"
] | [
"Fdx_FixX",
""
] | [
3014,
3082
] | 2 | [] | [] | [] | 0 | [
"7koe"
] | 1 | [
"PUB00015760",
"PUB00015841"
] | [
"3031010",
"3029021"
] | [
"Rhizobium meliloti insertion element ISRm2 and its use for identification of the fixX gene.",
"Genetic and structural analysis of the Rhizobium meliloti fixA, fixB, fixC, and fixX genes."
] | [
1987,
1987
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"unclassified sequences"
] | [
200,
2829,
53
] | 3 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Family | Ferredoxin-like, FixX | Ferredoxin-like, FixX | Fd_FixX | 8 |
IPR012210 | 12,210 | Insulin-like growth factor binding protein 2 | IGFBP-2 | Family | 1,060 | false | false | Insulin is found in many animals, and is involved in the regulation of normal glucose homeostasis. It also has other specific physiological effects, such as increasing the permeability of cells to monosaccharides, amino acids and fatty acids, and accelerating glycolysis and glycogen synthesis in the liver [ ]. Insulin ... | [
"GO:0005520",
"GO:0005576"
] | [
"insulin-like growth factor binding",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR01978"
] | [
"IGFBPFAMILY2"
] | [
1060
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-381426",
"R-DRE-381426",
"R-HSA-381426",
"R-MMU-381426",
"R-RNO-381426",
"R-SSC-381426",
"R-XTR-381426"
] | [
"REACTOME:R-BTA-381426",
"REACTOME:R-DRE-381426",
"REACTOME:R-HSA-381426",
"REACTOME:R-MMU-381426",
"REACTOME:R-RNO-381426",
"REACTOME:R-SSC-381426",
"REACTOME:R-XTR-381426"
] | 7 | [
"2h7t"
] | 1 | [
"PUB00003970",
"PUB00003972",
"PUB00003973",
"PUB00013535",
"PUB00013536",
"PUB00013537",
"PUB00013538",
"PUB00013539",
"PUB00013540",
"PUB00013541",
"PUB00013542",
"PUB00015691",
"PUB00015700",
"PUB00015800",
"PUB00023078",
"PUB00037375",
"PUB00053639",
"PUB00053640",
"PUB000536... | [
"503234",
"6243748",
"6107857",
"11874691",
"9822601",
"9725901",
"7519375",
"9660801",
"12379487",
"12379489",
"7504269",
"11751371",
"12672024",
"9348216",
"2036417",
"9141131",
"10601981",
"8735594",
"8683595",
"1319992"
] | [
"Nucleotide sequence of a cDNA clone encoding human preproinsulin.",
"Sequence of the human insulin gene.",
"Hormone families: pancreatic hormones and homologous growth factors.",
"IGF-binding protein-5: flexible player in the IGF system and effector on its own.",
"Structure of the IGF-binding domain of the... | [
1979,
1980,
1980,
2002,
1998,
1998,
1994,
1998,
2002,
2002,
1993,
2001,
2003,
1997,
1991,
1997,
1999,
1996,
1996,
1992
] | 20 | [
"IPR022321"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
1060
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
2,
5
] | 4 | true | Family | Insulin-like growth factor binding protein 2 | Insulin-like growth factor binding protein 2 | IGFBP-2 | 8 |
IPR012211 | 12,211 | Insulin-like growth factor binding protein 3 | IGFBP-3 | Family | 932 | false | false | Insulin is found in many animals, and is involved in the regulation of normal glucose homeostasis. It also has other specific physiological effects, such as increasing the permeability of cells to monosaccharides, amino acids and fatty acids, and accelerating glycolysis and glycogen synthesis in the liver [ ]. Insulin ... | [
"GO:0005520",
"GO:0005576"
] | [
"insulin-like growth factor binding",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR01979"
] | [
"IGFBPFAMILY3"
] | [
932
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-381426",
"R-BTA-6803211",
"R-BTA-8957275",
"R-HSA-381426",
"R-HSA-6803211",
"R-HSA-8957275",
"R-MMU-381426",
"R-MMU-6803211",
"R-MMU-8957275",
"R-RNO-381426",
"R-RNO-6803211",
"R-RNO-8957275"
] | [
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-6803211",
"REACTOME:R-BTA-8957275",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-6803211",
"REACTOME:R-HSA-8957275",
"REACTOME:R-MMU-381426",
"REACTOME:R-MMU-6803211",
"REACTOME:R-MMU-8957275",
"REACTOME:R-RNO-381426",
"REACTOME:R-RNO-6803211",
"REACTOME:R-... | 12 | [
"7wrq"
] | 1 | [
"PUB00003970",
"PUB00003972",
"PUB00003973",
"PUB00013535",
"PUB00013536",
"PUB00013537",
"PUB00013538",
"PUB00013539",
"PUB00013540",
"PUB00013541",
"PUB00013542",
"PUB00015724",
"PUB00015755",
"PUB00015765",
"PUB00015818",
"PUB00023078",
"PUB00037375",
"PUB00053639",
"PUB000536... | [
"503234",
"6243748",
"6107857",
"11874691",
"9822601",
"9725901",
"7519375",
"9660801",
"12379487",
"12379489",
"7504269",
"12466191",
"10723094",
"9075742",
"1384805",
"2036417",
"9141131",
"10601981",
"8735594",
"8683595",
"1319992"
] | [
"Nucleotide sequence of a cDNA clone encoding human preproinsulin.",
"Sequence of the human insulin gene.",
"Hormone families: pancreatic hormones and homologous growth factors.",
"IGF-binding protein-5: flexible player in the IGF system and effector on its own.",
"Structure of the IGF-binding domain of the... | [
1979,
1980,
1980,
2002,
1998,
1998,
1994,
1998,
2002,
2002,
1993,
2002,
2000,
1997,
1992,
1991,
1997,
1999,
1996,
1996,
1992
] | 21 | [
"IPR022321"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
932
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
16,
3,
3
] | 4 | true | Family | Insulin-like growth factor binding protein 3 | Insulin-like growth factor binding protein 3 | IGFBP-3 | 5 |
IPR012218 | 12,218 | Cytochrome c, Bacillus subtilis c550-type | Cyt_c_BACSU-c550-type | Family | 2,464 | false | false | These Class I cytochromes from Gram-positive bacteria are membrane anchored via a lipid anchor in the N-terminal region. Properties of the Bacillus subtilis protein are described in [ ]. | [
"GO:0005506",
"GO:0009055",
"GO:0020037",
"GO:0016020"
] | [
"iron ion binding",
"electron transfer activity",
"heme binding",
"membrane"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"cellular_component"
] | 4 | [
"PIRSF"
] | [
"PIRSF000025"
] | [
"Cytc_Bsub_c550"
] | [
2464
] | 1 | [] | [] | [] | 0 | [
"1b7v",
"1c75",
"1k3g",
"1k3h",
"1n9c"
] | 5 | [
"PUB00015758"
] | [
"8383048"
] | [
"Physico-chemical characterisation of membrane-bound and water-soluble forms of Bacillus subtilis cytochrome c-550."
] | [
1993
] | 1 | [
"IPR051811"
] | [
"IPR054780",
"IPR054782"
] | 1 | 2 | 0 | [
"Bacillota"
] | [
2464
] | 1 | [] | [] | 0 | true | Family | Cytochrome c, Bacillus subtilis c550-type | Cytochrome c, Bacillus subtilis c550-type | Cyt_c_BACSU-c550-type | 3 |
IPR012220 | 12,220 | Glutamate synthase, eukaryotic | Glu_synth_euk | Family | 2,778 | false | false | This group represents the eukaryotic type of glutamate synthase (NADH-GOGAT, ). This pyridine-linked form is found in both photosynthetic and nonphotosynthetic eukaryotes. It displays a single-subunit structure corresponding to the fusion of the small and the large bacterial subunits. Glutamate synthase (GOGAT, GltS) i... | [
"GO:0005506",
"GO:0010181",
"GO:0016040",
"GO:0050660",
"GO:0006537"
] | [
"iron ion binding",
"FMN binding",
"glutamate synthase (NADH) activity",
"flavin adenine dinucleotide binding",
"glutamate biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 5 | [
"PIRSF"
] | [
"PIRSF000187"
] | [
"GOGAT"
] | [
2778
] | 1 | [
"EC",
"METACYC"
] | [
"1.4.1.14",
"PWY-6963"
] | [
"EC:1.4.1.14",
"METACYC:PWY-6963"
] | 2 | [] | 0 | [
"PUB00008698",
"PUB00009386",
"PUB00013982",
"PUB00015710",
"PUB00015727",
"PUB00015747",
"PUB00015837"
] | [
"11967268",
"10357231",
"11188694",
"11230537",
"7836314",
"12455964",
"12069605"
] | [
"Structural studies on the synchronization of catalytic centers in glutamate synthase.",
"Glutamate synthase: a complex iron-sulfur flavoprotein.",
"Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase.",
"Phylogenetic analyses of two \"archaeal\"... | [
2002,
1999,
2000,
2001,
1995,
2002,
2002
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
2,
2776
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Drosophila melanogaster",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 248... | [
3,
2,
2,
1,
4,
1,
1,
17
] | 8 | true | Family | Glutamate synthase, eukaryotic | Glutamate synthase, eukaryotic | Glu_synth_euk | 3 |
IPR012223 | 12,223 | Thioesterase type II, NRPS/PKS/S-FAS | TEII | Family | 15,488 | false | false | This family contains thioesterases involved in non-ribosomal peptide biosynthesis or polyketide biosynthesis, as well as those involved in vertebrate fatty acid biosynthesis (medium-chain S-acyl fatty acid synthase thioesterases, ). Based on domain architecture, they belong to type II (stand-alone, non-integrated) thio... | [
"GO:0009058"
] | [
"biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PANTHER"
] | [
"PTHR11487"
] | [
""
] | [
15488
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"3.1.2.-",
"PWY-3602",
"PWY-5109",
"PWY-6322",
"PWY-6585",
"PWY-6917",
"PWY-6948",
"PWY-6995",
"PWY-6997",
"PWY-7007",
"PWY-7216",
"PWY-7292",
"PWY-7401",
"PWY-7402",
"PWY-7471",
"PWY-7690",
"PWY-7706",
"PWY-7733",
"PWY-7734",
"PWY-7738",
"PWY-7740",
"PWY-7741",
"PWY-7742... | [
"EC:3.1.2.-",
"METACYC:PWY-3602",
"METACYC:PWY-5109",
"METACYC:PWY-6322",
"METACYC:PWY-6585",
"METACYC:PWY-6917",
"METACYC:PWY-6948",
"METACYC:PWY-6995",
"METACYC:PWY-6997",
"METACYC:PWY-7007",
"METACYC:PWY-7216",
"METACYC:PWY-7292",
"METACYC:PWY-7401",
"METACYC:PWY-7402",
"METACYC:PWY-7... | 35 | [
"1mn6",
"1mna",
"1mnq",
"2h7x",
"2h7y",
"2hfj",
"2k2q",
"2ron",
"3fla",
"3flb",
"3lcr",
"3qmv",
"3qmw",
"4xjv",
"5ugz",
"6ba8",
"6ba9",
"6ecb",
"6ecc",
"6fvj",
"6fw5",
"6vap",
"7e3z",
"9cbd",
"9cgl"
] | 25 | [
"PUB00000169",
"PUB00005275",
"PUB00015705",
"PUB00015719",
"PUB00015726",
"PUB00015734",
"PUB00015766",
"PUB00015784",
"PUB00015814",
"PUB00015842",
"PUB00015860"
] | [
"9560421",
"8805534",
"11080636",
"12384573",
"3968077",
"2318831",
"12005429",
"12416979",
"11001063",
"10508662",
"11401555"
] | [
"Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis.",
"Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one ac... | [
1998,
1996,
2000,
2002,
1985,
1990,
2002,
2002,
2000,
1999,
2001
] | 11 | [] | [
"IPR011412"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
14250,
1206,
32
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
5,
1,
3
] | 4 | true | Family | Thioesterase type II, NRPS/PKS/S-FAS | Thioesterase type II, NRPS/PKS/S-FAS | TEII | 4 |
IPR012224 | 12,224 | Peptidase S1A, coagulation factor VII/IX/X/C/Z | Pept_S1A_FX | Family | 5,733 | false | false | This group of plasma glycoproteins includes coagulation factors VII, IX, and X, and proteins C and Z, which belong to MEROPS peptidase family S1, subfamily S1A (chymotrypsin, clan PA(S)). All but protein Z are peptidases and are involved in blood coagulation. The precursors contain a signal sequence, propeptide, Gla do... | [
"GO:0004252",
"GO:0005509",
"GO:0007596"
] | [
"serine-type endopeptidase activity",
"calcium ion binding",
"blood coagulation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF001143"
] | [
"Factor_X"
] | [
5733
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.21",
"R-BTA-140834",
"R-BTA-159740",
"R-BTA-159763",
"R-BTA-159782",
"R-CFA-140875",
"R-CFA-159740",
"R-CFA-159763",
"R-CFA-159782",
"R-CFA-202733",
"R-CFA-381426",
"R-CFA-8957275",
"R-GGA-140834",
"R-GGA-140837",
"R-GGA-140875",
"R-GGA-159763",
"R-GGA-159782",
"R-HSA-1368108"... | [
"EC:3.4.21",
"REACTOME:R-BTA-140834",
"REACTOME:R-BTA-159740",
"REACTOME:R-BTA-159763",
"REACTOME:R-BTA-159782",
"REACTOME:R-CFA-140875",
"REACTOME:R-CFA-159740",
"REACTOME:R-CFA-159763",
"REACTOME:R-CFA-159782",
"REACTOME:R-CFA-202733",
"REACTOME:R-CFA-381426",
"REACTOME:R-CFA-8957275",
"RE... | 52 | [
"4bxs",
"4bxw",
"9cli",
"9cm2",
"9cm9",
"9l6q",
"9l6r",
"9l6s"
] | 8 | [
"PUB00015412",
"PUB00015647",
"PUB00015685",
"PUB00015698"
] | [
"8663165",
"6630196",
"6688526",
"10358041"
] | [
"Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX.",
"Beta-hydroxyaspartic acid in vitamin K-dependent proteins.",
"The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens.",
"The propeptides of the vitamin... | [
1996,
1983,
1983,
1999
] | 4 | [
"IPR001314"
] | [] | 1 | 0 | 1 | [
"Eumetazoa"
] | [
5733
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
17,
16,
13,
23
] | 4 | true | Family | Peptidase S1A, coagulation factor VII/IX/X/C/Z | Peptidase S1A, coagulation factor VII/IX/X/C/Z | Pept_S1A_FX | 9 |
IPR012226 | 12,226 | Diguanylate cyclase/phosphodiesterase | Diguanyl_cyclase/Pdiesterase | Family | 3,059 | false | false | Members of this group are signal transduction proteins that are direct oxygen sensors and are involved in regulation of cellular processes via the effector molecule cyclic diguanylate (c-di-GMP, bis(3',5')-cyclic diguanylic acid). They contain PAS/PAC, GGDEF, and EAL domains and have diguanylate cyclase and phosphodies... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF005925"
] | [
"Dos"
] | [
3059
] | 1 | [] | [] | [] | 0 | [
"9bgv",
"9bkv",
"9cdr",
"9ce0",
"9clo",
"9cmf"
] | 6 | [
"PUB00007061",
"PUB00007150",
"PUB00007364",
"PUB00015641",
"PUB00015649",
"PUB00015676",
"PUB00015695",
"PUB00015697",
"PUB00015702",
"PUB00015783",
"PUB00015791",
"PUB00015810",
"PUB00015830"
] | [
"11119645",
"11557134",
"11292341",
"11682196",
"9721278",
"10844669",
"10704219",
"12198316",
"11297407",
"2172238",
"10357859",
"12271121",
"11970957"
] | [
"GGDEF domain is homologous to adenylyl cyclase.",
"Novel domains of the prokaryotic two-component signal transduction systems.",
"Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains.",
"Genetic data indicate that proteins containing the GGDEF dom... | [
2001,
2001,
2001,
2001,
1998,
2000,
2000,
2002,
2001,
1990,
1999,
2002,
2002
] | 13 | [
"IPR052155"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Sar",
"unclassified sequences"
] | [
3012,
2,
45
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Diguanylate cyclase/phosphodiesterase | Diguanylate cyclase/phosphodiesterase | Diguanyl_cyclase/Pdiesterase | 2 |
IPR012227 | 12,227 | TNF receptor-associated factor TRAF, metazoa | TNF_rcpt-assoc_TRAF_met | Family | 8,258 | false | false | This entry represents the TNF receptor associated factors found in metazoa. The tumour necrosis factor (TNF) receptor associated factors (TRAFs) are major signal transducers for the TNF receptor (TNFR) superfamily and the interleukin-1 receptor/Toll-like receptor superfamily in mammals [ ]. TRAFs constitute a family of... | [
"GO:0008270",
"GO:0007165",
"GO:0042981"
] | [
"zinc ion binding",
"signal transduction",
"regulation of apoptotic process"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF015614"
] | [
"TRAF"
] | [
8258
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"2.3.2.27",
"PWY-7511",
"R-BTA-1257604",
"R-BTA-166058",
"R-BTA-193692",
"R-BTA-202424",
"R-BTA-205043",
"R-BTA-209543",
"R-BTA-209560",
"R-BTA-2871837",
"R-BTA-450302",
"R-BTA-450321",
"R-BTA-5607764",
"R-BTA-5689880",
"R-BTA-5689896",
"R-BTA-6811558",
"R-BTA-9020702",
"R-BTA-9370... | [
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-166058",
"REACTOME:R-BTA-193692",
"REACTOME:R-BTA-202424",
"REACTOME:R-BTA-205043",
"REACTOME:R-BTA-209543",
"REACTOME:R-BTA-209560",
"REACTOME:R-BTA-2871837",
"REACTOME:R-BTA-450302",
"REACTOME:R-BTA-450321",
"REAC... | 184 | [
"8zuk"
] | 1 | [
"PUB00011814",
"PUB00011816",
"PUB00011818",
"PUB00015663",
"PUB00015701",
"PUB00015834",
"PUB00015838",
"PUB00015846"
] | [
"8069916",
"10206649",
"11865024",
"11098060",
"9847406",
"9744859",
"11607847",
"10021364"
] | [
"A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.",
"Structural basis for self-association and receptor recognition of human TRAF2.",
"All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated sign... | [
1994,
1999,
2002,
2001,
1998,
1998,
2001,
1999
] | 8 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
8258
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
22,
3,
11,
15,
15
] | 6 | true | Family | TNF receptor-associated factor TRAF, metazoa | TNF receptor-associated factor TRAF, metazoa | TNF_rcpt-assoc_TRAF_met | 8 |
IPR012233 | 12,233 | Protein kinase C | PKC | Family | 2,638 | false | false | This group represents protein kinase C (PKC), including zeta/iota types from mammals, protein kinase C-like 3 from round worms [ ] and atypical protein kinase C (aPKC) from fruit flies [ ]. | [
"GO:0004674",
"GO:0005524"
] | [
"protein serine/threonine kinase activity",
"ATP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PIRSF"
] | [
"PIRSF000554"
] | [
"PKC_zeta"
] | [
2638
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11.13",
"R-CEL-1912408",
"R-CEL-2173791",
"R-CEL-5218921",
"R-CEL-9634635",
"R-CEL-9755511",
"R-DME-2173791",
"R-DME-5218921",
"R-DME-9634635",
"R-DME-9755511",
"R-DRE-209543",
"R-DRE-420029",
"R-DRE-9755511",
"R-HSA-114604",
"R-HSA-1912408",
"R-HSA-209543",
"R-HSA-2173791",
"... | [
"EC:2.7.11.13",
"REACTOME:R-CEL-1912408",
"REACTOME:R-CEL-2173791",
"REACTOME:R-CEL-5218921",
"REACTOME:R-CEL-9634635",
"REACTOME:R-CEL-9755511",
"REACTOME:R-DME-2173791",
"REACTOME:R-DME-5218921",
"REACTOME:R-DME-9634635",
"REACTOME:R-DME-9755511",
"REACTOME:R-DRE-209543",
"REACTOME:R-DRE-420... | 38 | [
"9ejk",
"9ejl",
"9ejm"
] | 3 | [
"PUB00069225",
"PUB00069226",
"PUB00069543",
"PUB00069545",
"PUB00069546",
"PUB00069693",
"PUB00070184",
"PUB00072939",
"PUB00072940"
] | [
"10467349",
"11257119",
"20686607",
"19738040",
"22349825",
"11544035",
"11035106",
"10995441",
"9422779"
] | [
"Overexpression of atypical PKC in PC12 cells enhances NGF-responsiveness and survival through an NF-kappaB dependent pathway.",
"Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures.",
"The i... | [
1999,
2001,
2010,
2009,
2013,
2001,
2000,
2000,
1998
] | 9 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
2638
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
2,
4,
6,
4
] | 6 | true | Family | Protein kinase C | Protein kinase C | PKC | 3 |
IPR012234 | 12,234 | Tyrosine-protein kinase, non-receptor SYK/ZAP-70 | Tyr_kinase_non-rcpt_SYK/ZAP70 | Family | 1,881 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004715",
"GO:0005524",
"GO:0006468",
"GO:0035556",
"GO:0005737"
] | [
"non-membrane spanning protein tyrosine kinase activity",
"ATP binding",
"protein phosphorylation",
"intracellular signal transduction",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PIRSF"
] | [
"PIRSF000604"
] | [
"TyrPK_SYK"
] | [
1881
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.2",
"R-GGA-114604",
"R-GGA-2029481",
"R-GGA-2029482",
"R-GGA-2029485",
"R-GGA-2424491",
"R-GGA-354192",
"R-GGA-912631",
"R-GGA-9674555",
"R-GGA-9705462",
"R-GGA-983695",
"R-HSA-114604",
"R-HSA-202430",
"R-HSA-202433",
"R-HSA-2029481",
"R-HSA-2029482",
"R-HSA-2029485",
"R-HS... | [
"EC:2.7.10.2",
"REACTOME:R-GGA-114604",
"REACTOME:R-GGA-2029481",
"REACTOME:R-GGA-2029482",
"REACTOME:R-GGA-2029485",
"REACTOME:R-GGA-2424491",
"REACTOME:R-GGA-354192",
"REACTOME:R-GGA-912631",
"REACTOME:R-GGA-9674555",
"REACTOME:R-GGA-9705462",
"REACTOME:R-GGA-983695",
"REACTOME:R-HSA-114604"... | 72 | [
"2ozo",
"4fl2",
"4fl3",
"4k2r"
] | 4 | [
"PUB00005115",
"PUB00015362",
"PUB00015714",
"PUB00015759",
"PUB00015771",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412",
"PUB00052529",
"PUB00052530",
"PUB00052531"
] | [
"3291115",
"12368087",
"1423621",
"8163536",
"1874735",
"12471243",
"15078142",
"15320712",
"19275641",
"16700535",
"15845350",
"19592646",
"19670961",
"8124727"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain.",
"Molecular cloning of human Syk. A B cell protein-tyrosine kinase ass... | [
1988,
2002,
1992,
1994,
1991,
2002,
2004,
2004,
2009,
2006,
2005,
2009,
2009,
1994
] | 14 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
1881
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
3,
5,
8
] | 4 | true | Family | Tyrosine-protein kinase, non-receptor SYK/ZAP-70 | Tyrosine-protein kinase, non-receptor SYK/ZAP-70 | Tyr_kinase_non-rcpt_SYK/ZAP70 | 1 |
IPR012235 | 12,235 | 3-isopropylmalate dehydratase, fused small/large subunit | 3-IsopropMal_deHydtase_ssu/lsu | Family | 1,419 | false | false | 3-isopropylmalate dehydratase (or isopropylmalate isomerase; ) catalyses the stereo-specific isomerisation of 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. This enzyme performs the second step in the biosynthesis of leucine, and is present in most prokaryotes and many fungal species.... | [
"GO:0003861",
"GO:0009098"
] | [
"3-isopropylmalate dehydratase activity",
"L-leucine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF001418"
] | [
"ACN"
] | [
1419
] | 1 | [
"EC"
] | [
"4.2.1.33"
] | [
"EC:4.2.1.33"
] | 1 | [] | 0 | [
"PUB00005471",
"PUB00015742",
"PUB00016210",
"PUB00032014",
"PUB00033924",
"PUB00036023",
"PUB00082326"
] | [
"9020582",
"8706708",
"9813279",
"15522288",
"1400210",
"16524361",
"20663849"
] | [
"The aconitase family: three structural variations on a common theme.",
"Conservation of aconitase residues revealed by multiple sequence analysis. Implications for structure/function relationships.",
"The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus.",
"Crysta... | [
1997,
1996,
1998,
2004,
1992,
2006,
2010
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1419
] | 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 | 3-isopropylmalate dehydratase, fused small/large subunit | 3-isopropylmalate dehydratase, fused small/large subunit | 3-IsopropMal_deHydtase_ssu/lsu | 3 |
IPR012245 | 12,245 | Molybdenum cofactor biosynthesis protein MoaB | MoaB | Family | 10,012 | false | false | This entry represents the MoaB family of predicted molybdenum cofactor biosynthesis proteins and related sequences [ , ]. | [
"GO:0006777"
] | [
"Mo-molybdopterin cofactor biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF006443",
"PTHR43232"
] | [
"MoaB",
""
] | [
9539,
9815
] | 2 | [] | [] | [] | 0 | [
"1mkz",
"1r2k",
"1y5e",
"3iwt",
"4lhb"
] | 5 | [
"PUB00015718",
"PUB00015825"
] | [
"15159566",
"15269205"
] | [
"Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli.",
"The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis."
] | [
2004,
2004
] | 2 | [] | [
"IPR013484"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
936,
8913,
9,
154
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Molybdenum cofactor biosynthesis protein MoaB | Molybdenum cofactor biosynthesis protein MoaB | MoaB | 2 |
IPR012247 | 12,247 | Bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA | MoaC_MogA | Family | 1,441 | false | false | This entry includes a group of molybdenum cofactor biosynthesis bifunctional proteins. The proteins are composed of 2 domains: a molybdenum cofactor biosynthesis protein C-like domain and a molybdenum cofactor biosynthesis protein B-like domain. Together with MoaA, they are involved in the conversion of 5'-GTP to cycli... | [
"GO:0006777"
] | [
"Mo-molybdopterin cofactor biosynthetic process"
] | [
"biological_process"
] | 1 | [
"NCBIFAM",
"PIRSF"
] | [
"NF002947",
"PIRSF036594"
] | [
"PRK03604.1",
"MoaC_MogA"
] | [
1436,
1375
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nitrosocosmicus",
"Eukaryota",
"ecological metagenomes"
] | [
1414,
2,
4,
21
] | 4 | [] | [] | 0 | true | Family | Bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA | Bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA | MoaC_MogA | 9 |
IPR012251 | 12,251 | N-acetylglucosamine-6-sulfatase | GlcNAc_6-SO4ase | Family | 2,653 | false | false | N-acetylglucosamine-6-sulfatase catalyses the hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate [ ]. This enzyme is deficient in Sanfilippo Syndrome type IIID [ ]. Mucopolysaccharidosis type III (MPS-III), or Sanfilippo syndrome, is a group of lysoso... | [
"GO:0008449",
"GO:0030203"
] | [
"N-acetylglucosamine-6-sulfatase activity",
"glycosaminoglycan metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF036666"
] | [
"G6S"
] | [
2653
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.6.14",
"R-HSA-2022857",
"R-HSA-2206305",
"R-HSA-432720",
"R-HSA-6798695",
"R-MMU-2022857",
"R-MMU-432720",
"R-MMU-6798695"
] | [
"EC:3.1.6.14",
"REACTOME:R-HSA-2022857",
"REACTOME:R-HSA-2206305",
"REACTOME:R-HSA-432720",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-2022857",
"REACTOME:R-MMU-432720",
"REACTOME:R-MMU-6798695"
] | 8 | [] | 0 | [
"PUB00070289",
"PUB00070290"
] | [
"2500866",
"3689315"
] | [
"Sanfilippo D syndrome: estimation of N-acetylglucosamine-6-sulfatase activity with a radiolabeled monosulfated disaccharide substrate.",
"Human liver N-acetylglucosamine-6-sulphate sulphatase. Catalytic properties."
] | [
1989,
1987
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"metagenomes"
] | [
482,
2,
2156,
13
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
3,
8,
3,
4
] | 5 | true | Family | N-acetylglucosamine-6-sulfatase | N-acetylglucosamine-6-sulfatase | GlcNAc_6-SO4ase | 5 |
IPR012255 | 12,255 | Electron transfer flavoprotein, beta subunit | ETF_b | Family | 33,497 | false | false | Electron transfer flavoproteins (ETFs) serve as specific electron acceptors for primary dehydrogenases, transferring the electrons to terminal respiratory systems. They can be functionally classified into constitutive, "housekeeping" ETFs, mainly involved in the oxidation of fatty acids (Group I), and ETFs produced by ... | [
"GO:0009055"
] | [
"electron transfer activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF000090",
"PTHR21294"
] | [
"Beta-ETF",
""
] | [
29479,
33497
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-611105",
"R-HSA-611105",
"R-HSA-8876725",
"R-MMU-611105",
"R-MMU-8876725",
"R-RNO-611105",
"R-RNO-8876725",
"R-SCE-611105",
"R-SPO-611105",
"R-SSC-611105",
"R-SSC-8876725"
] | [
"REACTOME:R-DDI-611105",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-8876725",
"REACTOME:R-MMU-611105",
"REACTOME:R-MMU-8876725",
"REACTOME:R-RNO-611105",
"REACTOME:R-RNO-8876725",
"REACTOME:R-SCE-611105",
"REACTOME:R-SPO-611105",
"REACTOME:R-SSC-611105",
"REACTOME:R-SSC-8876725"
] | 11 | [
"1efp",
"1efv",
"1o94",
"1o95",
"1o96",
"1o97",
"1t9g",
"2a1t",
"2a1u",
"3clr",
"3cls",
"3clt",
"3clu",
"4kpu",
"4l2i",
"5ol2",
"5ow0",
"6fah",
"7koe",
"7qh2"
] | 20 | [
"PUB00004879",
"PUB00024527",
"PUB00033231",
"PUB00033232"
] | [
"8962055",
"10026281",
"8599534",
"12567183"
] | [
"Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.",
"Crystal structure of Paracoccus denitrificans electron transfer flavoprotein: structural and electrostatic analysis of a conserved flavin binding domain.",
"Bradyrhizobium japonicum possesses two discrete sets of electr... | [
1996,
1999,
1996,
2003
] | 4 | [] | [
"IPR023463",
"IPR030982",
"IPR050044"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
959,
27741,
4097,
700
] | 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,
2,
1,
2,
3,
2,
7,
1,
1,
3,
1,
1,
6
] | 13 | true | Family | Electron transfer flavoprotein, beta subunit | Electron transfer flavoprotein, beta subunit | ETF_b | 5 |
IPR012256 | 12,256 | D-lactate dehydrogenase | D_lactate_DH | Family | 3,301 | false | false | D-lactate dehydrogenases catalyse the reversible oxidation of D-lactate to pyruvate. This entry represents the NADH-independent D-lactate dehydrogenases found in many bacterial species. These are membrane-associated respiratory enzymes which contain an FAD cofactor and transfer electrons derived from susbstrate oxidati... | [
"GO:0016901",
"GO:0050660",
"GO:0006089",
"GO:0022904",
"GO:0005886"
] | [
"oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor",
"flavin adenine dinucleotide binding",
"lactate metabolic process",
"respiratory electron transport chain",
"plasma membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"HAMAP",
"NCBIFAM",
"PIRSF"
] | [
"MF_02092",
"NF008387",
"PIRSF000101"
] | [
"DLDH_Dld",
"PRK11183.1",
"D-lactate_dh"
] | [
3088,
3298,
3178
] | 3 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.1.5.12",
"PWY-5386",
"PWY-7425"
] | [
"EC:1.1.5.12",
"METACYC:PWY-5386",
"METACYC:PWY-7425"
] | 3 | [
"1f0x"
] | 1 | [
"PUB00024738",
"PUB00086655"
] | [
"10944213",
"21159175"
] | [
"The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme.",
"Quinone-dependent D-lactate dehydrogenase Dld (Cg1027) is essential for growth of Corynebacterium glutamicum on D-lactate."
] | [
2000,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3282,
6,
13
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | D-lactate dehydrogenase | D-lactate dehydrogenase | D_lactate_DH | 4 |
IPR012257 | 12,257 | Glycolate oxidase, iron-sulphur subunit | Glc_ox_4Fe-4S | Family | 9,242 | false | false | This group represents a glycolate oxidase, iron-sulphur subunit [ ]. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000139"
] | [
"Glc_ox_4Fe-4S"
] | [
9242
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007282"
] | [
"8606183"
] | [
"glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Geodia barretti",
"Sym plasmid",
"unclassified sequences"
] | [
10,
9065,
4,
1,
162
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glycolate oxidase, iron-sulphur subunit | Glycolate oxidase, iron-sulphur subunit | Glc_ox_4Fe-4S | 7 |
IPR012258 | 12,258 | Acyl-CoA oxidase | Acyl-CoA_oxidase | Family | 20,664 | false | false | Acyl-CoA oxidase (ACO) acts on CoA derivatives of fatty acids with chain lengths from 8 to 18. It catalyses the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids and a major producer of hydrogen peroxide (H2O2) [ , ]. Acyl-CoA oxidase is a homodimer and the polypeptide chain of the subuni... | [
"GO:0003997",
"GO:0071949",
"GO:0006631",
"GO:0005777"
] | [
"acyl-CoA oxidase activity",
"FAD binding",
"fatty acid metabolic process",
"peroxisome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF000168",
"PTHR10909"
] | [
"Acyl-CoA_oxidase",
""
] | [
14666,
20663
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"1.3.3.6",
"PWY-5136",
"PWY-6837",
"PWY-6920",
"PWY-7007",
"PWY-7288",
"PWY-7291",
"PWY-7337",
"PWY-7338",
"PWY-7340",
"PWY-735",
"PWY-7574",
"PWY-7606",
"PWY-7726",
"PWY-7854",
"PWY-7858",
"R-BTA-2046106",
"R-BTA-390247",
"R-BTA-9033241",
"R-CEL-193368",
"R-CEL-2046106",
"... | [
"EC:1.3.3.6",
"METACYC:PWY-5136",
"METACYC:PWY-6837",
"METACYC:PWY-6920",
"METACYC:PWY-7007",
"METACYC:PWY-7288",
"METACYC:PWY-7291",
"METACYC:PWY-7337",
"METACYC:PWY-7338",
"METACYC:PWY-7340",
"METACYC:PWY-735",
"METACYC:PWY-7574",
"METACYC:PWY-7606",
"METACYC:PWY-7726",
"METACYC:PWY-78... | 53 | [
"1is2",
"1w07",
"2ddh",
"2fon",
"5k3g",
"5k3h",
"5k3i",
"5k3j",
"5y9d",
"5ys9",
"7q84",
"7q86"
] | 12 | [
"PUB00003040",
"PUB00026133",
"PUB00032141",
"PUB00097235"
] | [
"9525937",
"11872165",
"15581893",
"32169171"
] | [
"Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin.",
"Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase.",
"Acyl-CoA ... | [
1998,
2002,
2005,
2020
] | 4 | [] | [
"IPR034171"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
3708,
16929,
7,
20
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
29,
7,
10,
11,
21,
13,
9,
29,
1,
46
] | 10 | true | Family | Acyl-CoA oxidase | Acyl-CoA oxidase | Acyl-CoA_oxidase | 8 |
IPR012259 | 12,259 | Dihydrofolate reductase | DHFR | Family | 27,626 | false | false | Dihydrofolate reductase (DHFR) ( ) catalyses the NADPH-dependent reduction of dihydrofolate to tetrahydrofolate, an essential step in de novo synthesis both of glycine and of purines and deoxythymidine phosphate (the precursors of DNA synthesis) [ ], and important also in the conversion of deoxyuridine monophosphate to... | [
"GO:0004146",
"GO:0050661",
"GO:0046654"
] | [
"dihydrofolate reductase activity",
"NADP binding",
"tetrahydrofolate biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF000194",
"PTHR48069"
] | [
"DHFR",
""
] | [
18736,
27626
] | 2 | [
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.5.1.3",
"PWY-3841",
"PWY-6614",
"R-CEL-196757",
"R-DME-196757",
"R-HSA-1474151",
"R-HSA-196757",
"R-HSA-69205",
"R-MMU-196757",
"R-RNO-196757",
"R-SCE-196757",
"R-SPO-196757"
] | [
"EC:1.5.1.3",
"METACYC:PWY-3841",
"METACYC:PWY-6614",
"REACTOME:R-CEL-196757",
"REACTOME:R-DME-196757",
"REACTOME:R-HSA-1474151",
"REACTOME:R-HSA-196757",
"REACTOME:R-HSA-69205",
"REACTOME:R-MMU-196757",
"REACTOME:R-RNO-196757",
"REACTOME:R-SCE-196757",
"REACTOME:R-SPO-196757"
] | 12 | [
"1ai9",
"1ao8",
"1aoe",
"1boz",
"1bzf",
"1cd2",
"1cz3",
"1d1g",
"1daj",
"1ddr",
"1dds",
"1df7",
"1dg5",
"1dg7",
"1dg8",
"1dhf",
"1dhi",
"1dhj",
"1dis",
"1diu",
"1dlr",
"1dls",
"1dr1",
"1dr2",
"1dr3",
"1dr4",
"1dr5",
"1dr6",
"1dr7",
"1dra",
"1drb",
"1dre"... | 581 | [
"PUB00001361",
"PUB00002379",
"PUB00002387",
"PUB00003657",
"PUB00005107"
] | [
"3383852",
"500653",
"6815178",
"2601715",
"2830673"
] | [
"Crystal structure of human dihydrofolate reductase complexed with folate.",
"Porcine liver dihydrofolate reductase. Purification, properties, and amino acid sequence.",
"Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and b... | [
1988,
1979,
1982,
1989,
1988
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid R483",
"Viruses",
"unclassified sequences"
] | [
456,
21511,
4782,
1,
577,
299
] | 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)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (stra... | [
1,
1,
3,
2,
1,
6,
2,
1,
4,
1,
1,
2
] | 12 | true | Family | Dihydrofolate reductase | Dihydrofolate reductase | DHFR | 9 |
IPR012262 | 12,262 | Bifunctional dihydrofolate reductase/thymidylate synthase | DHFR-TS | Family | 1,585 | false | false | This group represents a bifunctional dihydrofolate reductase/thymidylate synthase found in some plant species and protozoal parasites including malarial species and trypanosomes. In other species dihydrofolate reductase and thymidilate synthase are encoded on separate polypeptides. Thymidylate synthase ( ) [ ] catalyse... | [
"GO:0004146",
"GO:0004799",
"GO:0006730"
] | [
"dihydrofolate reductase activity",
"thymidylate synthase activity",
"one-carbon metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF000389"
] | [
"DHFR-TS"
] | [
1585
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.5.1.3",
"2.1.1.45",
"PWY-3841",
"PWY-6614",
"PWY-7184",
"PWY-7187",
"PWY-7198",
"PWY-7199",
"PWY-7210"
] | [
"EC:1.5.1.3",
"EC:2.1.1.45",
"METACYC:PWY-3841",
"METACYC:PWY-6614",
"METACYC:PWY-7184",
"METACYC:PWY-7187",
"METACYC:PWY-7198",
"METACYC:PWY-7199",
"METACYC:PWY-7210"
] | 9 | [
"1qzf",
"1sej",
"2h2q",
"2oip",
"3cl9",
"3clb",
"3dl5",
"3dl6",
"3hbb",
"3hj3",
"3i3r",
"3inv",
"3irm",
"3irn",
"3iro",
"3jsu",
"3k2h",
"3kjr",
"3kjs",
"3nrr",
"3qg2",
"3qgt",
"3um5",
"3um6",
"3um8",
"4dp3",
"4dpd",
"4dph",
"4eck",
"4eil",
"4ky4",
"4ky8"... | 87 | [
"PUB00000031",
"PUB00001361",
"PUB00005100",
"PUB00005107",
"PUB00021881"
] | [
"6996564",
"3383852",
"3099389",
"2830673",
"12704428"
] | [
"On the mechanism of action of folate- and biopterin-requiring enzymes.",
"Crystal structure of human dihydrofolate reductase complexed with folate.",
"Atomic structure of thymidylate synthase: target for rational drug design.",
"A gene for dihydrofolate reductase in a herpesvirus.",
"Insights into antifola... | [
1980,
1988,
1987,
1988,
2003
] | 5 | [
"IPR045097"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
1568,
6,
11
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
16,
6,
13
] | 3 | true | Family | Bifunctional dihydrofolate reductase/thymidylate synthase | Bifunctional dihydrofolate reductase/thymidylate synthase | DHFR-TS | 2 |
IPR012265 | 12,265 | Protein-tyrosine phosphatase, non-receptor type-1/2 | Ptpn1/Ptpn2 | Family | 2,216 | false | false | Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is ... | [
"GO:0004725",
"GO:0006470"
] | [
"protein tyrosine phosphatase activity",
"protein dephosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000926"
] | [
"Tyr-Ptase_nr1"
] | [
2216
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.3.48",
"R-HSA-354192",
"R-HSA-6807004",
"R-HSA-77387",
"R-HSA-877312",
"R-HSA-8849472",
"R-HSA-9008059",
"R-HSA-9022699",
"R-HSA-912694",
"R-HSA-982772",
"R-HSA-9833482",
"R-HSA-9860927",
"R-MMU-354192",
"R-MMU-6807004",
"R-MMU-77387",
"R-MMU-877312",
"R-MMU-8849472",
"R-MMU-9... | [
"EC:3.1.3.48",
"REACTOME:R-HSA-354192",
"REACTOME:R-HSA-6807004",
"REACTOME:R-HSA-77387",
"REACTOME:R-HSA-877312",
"REACTOME:R-HSA-8849472",
"REACTOME:R-HSA-9008059",
"REACTOME:R-HSA-9022699",
"REACTOME:R-HSA-912694",
"REACTOME:R-HSA-982772",
"REACTOME:R-HSA-9833482",
"REACTOME:R-HSA-9860927",... | 30 | [
"1a5y",
"2cma",
"3a5j",
"3eu0",
"3zmp",
"3zmq",
"4bjo",
"4i8n",
"6cwu",
"6cwv",
"6w30",
"7ken",
"7lfo",
"8u1e"
] | 14 | [
"PUB00021105",
"PUB00026962",
"PUB00033227",
"PUB00033228",
"PUB00035793",
"PUB00035794",
"PUB00035795",
"PUB00035796",
"PUB00035797",
"PUB00035798"
] | [
"9553104",
"11907034",
"10066179",
"9271584",
"9818190",
"14625689",
"12678841",
"16672235",
"8948575",
"9646865"
] | [
"Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography.",
"Structure determination of T cell protein-tyrosine phosphatase.",
"Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene.",
"Impaired bo... | [
1998,
2002,
1999,
1997,
1998,
2003,
2003,
2006,
1996,
1998
] | 10 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
2216
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
7,
5,
8
] | 4 | true | Family | Protein-tyrosine phosphatase, non-receptor type-1/2 | Protein-tyrosine phosphatase, non-receptor type-1/2 | Ptpn1/Ptpn2 | 5 |
IPR012266 | 12,266 | Tyrosine-protein phosphatase non-receptor type 12 | PTN12 | Family | 875 | false | false | This entry represents Tyrosine-protein phosphatase non-receptor type 12 (PTN12). Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Conse... | [
"GO:0004725",
"GO:0006470"
] | [
"protein tyrosine phosphatase activity",
"protein dephosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000932"
] | [
"Tyr-Ptase_nr12"
] | [
875
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1250196",
"R-HSA-182971",
"R-HSA-186797",
"R-HSA-8863795",
"R-HSA-9008059",
"R-HSA-9634285",
"R-MMU-1250196",
"R-MMU-182971",
"R-MMU-186797",
"R-MMU-8863795"
] | [
"REACTOME:R-HSA-1250196",
"REACTOME:R-HSA-182971",
"REACTOME:R-HSA-186797",
"REACTOME:R-HSA-8863795",
"REACTOME:R-HSA-9008059",
"REACTOME:R-HSA-9634285",
"REACTOME:R-MMU-1250196",
"REACTOME:R-MMU-182971",
"REACTOME:R-MMU-186797",
"REACTOME:R-MMU-8863795"
] | 10 | [] | 0 | [
"PUB00035793",
"PUB00035794",
"PUB00035795",
"PUB00035796",
"PUB00035797",
"PUB00035798"
] | [
"9818190",
"14625689",
"12678841",
"16672235",
"8948575",
"9646865"
] | [
"Protein tyrosine phosphatases: mechanisms of catalysis and regulation.",
"Receptor and nonreceptor protein tyrosine phosphatases in the nervous system.",
"An overview of the protein tyrosine phosphatase superfamily.",
"The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase dom... | [
1998,
2003,
2003,
2006,
1996,
1998
] | 6 | [
"IPR047170"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
875
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
2,
1,
7
] | 4 | true | Family | Tyrosine-protein phosphatase non-receptor type 12 | Tyrosine-protein phosphatase non-receptor type 12 | PTN12 | 3 |
IPR012267 | 12,267 | Peptidase S1A, acrosin | Pept_S1A_acrosin | Family | 133 | false | false | This group of proteins are serine peptidases belonging to MEROPS peptidase family S1, subfamily S1A (chymotrypsin, clan PA(S)). Members of this family are found specifically within the acrosomal vesicle of all mammalian spermatozoa. Acrosin is thought to be involved in the recognition and binding of the sperm to the zo... | [
"GO:0004252",
"GO:0001669"
] | [
"serine-type endopeptidase activity",
"acrosomal vesicle"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PIRSF"
] | [
"PIRSF001141"
] | [
"Acrosin"
] | [
133
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.21.10",
"R-HSA-1300645",
"R-MMU-1300645",
"R-RNO-1300645"
] | [
"EC:3.4.21.10",
"REACTOME:R-HSA-1300645",
"REACTOME:R-MMU-1300645",
"REACTOME:R-RNO-1300645"
] | 4 | [] | 0 | [
"PUB00016218"
] | [
"9041140"
] | [
"Spermatozoa lacking acrosin protein show delayed fertilization."
] | [
1997
] | 1 | [
"IPR001314"
] | [] | 1 | 0 | 1 | [
"Eutheria"
] | [
133
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
2
] | 3 | true | Family | Peptidase S1A, acrosin | Peptidase S1A, acrosin | Pept_S1A_acrosin | 1 |
IPR012270 | 12,270 | CCR4-NOT complex, subunit 3/ 5 | CCR4-NOT_su3/5 | Family | 5,879 | false | false | The Ccr4-Not complex is a global regulator of gene expression that is conserved from yeast to human. It affects genes positively and negatively and is thought to regulate transcription factor IID function. In Saccharomyces cerevisiae, it exists in two prominent forms and consists of at least nine core subunits: the fiv... | [
"GO:0006355",
"GO:0030015"
] | [
"regulation of DNA-templated transcription",
"CCR4-NOT core complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PIRSF"
] | [
"PIRSF005290"
] | [
"NOT_su_3_5"
] | [
5879
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-429947",
"R-HSA-6804115",
"R-HSA-9820841",
"R-MMU-429947",
"R-MMU-6804115"
] | [
"REACTOME:R-HSA-429947",
"REACTOME:R-HSA-6804115",
"REACTOME:R-HSA-9820841",
"REACTOME:R-MMU-429947",
"REACTOME:R-MMU-6804115"
] | 5 | [
"8k82",
"9c3h",
"9c3i"
] | 3 | [
"PUB00010586",
"PUB00044101",
"PUB00044102",
"PUB00044103"
] | [
"11696541",
"10637334",
"12957374",
"18430587"
] | [
"Interaction between Not1p, a component of the Ccr4-not complex, a global regulator of transcription, and Dhh1p, a putative RNA helicase.",
"Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits.",
"Global control of gene expression in yeast by the Ccr4-Not complex.",
"Biophysic... | [
2002,
2000,
2003,
2008
] | 4 | [
"IPR040168"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"bird metagenome"
] | [
5878,
1
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
10,
1,
7,
1,
6,
3,
1,
4,
2,
2,
1,
32
] | 12 | true | Family | CCR4-NOT complex, subunit 3/ 5 | CCR4-NOT complex, subunit 3/ 5 | CCR4-NOT_su3/5 | 6 |
IPR012280 | 12,280 | Semialdehyde dehydrogenase, dimerisation domain | Semialdhyde_DH_dimer_dom | Domain | 33,899 | false | false | This domain contains N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase [ ], an enzyme involved in the biosynthesis of various amino acids from aspartate. It also contains the yeast and fungal Arg5,6 protein, which is cleaved into t... | [
"GO:0016620",
"GO:0046983",
"GO:0008652"
] | [
"oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor",
"protein dimerization activity",
"amino acid biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF02774"
] | [
"Semialdhyde_dhC"
] | [
33899
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.2.1.11",
"PWY-2941",
"PWY-2942",
"PWY-5097",
"PWY-6160",
"PWY-6559",
"PWY-6562",
"PWY-7153",
"PWY-7977",
"PWY-8088",
"PWY-8179",
"PWY-8296"
] | [
"EC:1.2.1.11",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097",
"METACYC:PWY-6160",
"METACYC:PWY-6559",
"METACYC:PWY-6562",
"METACYC:PWY-7153",
"METACYC:PWY-7977",
"METACYC:PWY-8088",
"METACYC:PWY-8179",
"METACYC:PWY-8296"
] | 12 | [
"1brm",
"1gl3",
"1mb4",
"1mc4",
"1nwc",
"1nwh",
"1nx6",
"1oza",
"1pqp",
"1pqu",
"1pr3",
"1ps8",
"1pu2",
"1q2x",
"1t4b",
"1t4d",
"1ta4",
"1tb4",
"1ys4",
"2ep5",
"2gyy",
"2gz1",
"2gz2",
"2gz3",
"2hjs",
"2qz9",
"2r00",
"2yv3",
"3hsk",
"3pwk",
"3pws",
"3pyl"... | 65 | [
"PUB00016262"
] | [
"10369777"
] | [
"Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"unclassified sequences"
] | [
883,
29548,
2867,
1,
600
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
2,
1,
3,
1,
1,
6
] | 7 | true | Domain | Semialdehyde dehydrogenase, dimerisation domain | Semialdehyde dehydrogenase, dimerisation domain | Semialdhyde_DH_dimer_dom | 7 |
IPR012281 | 12,281 | Phospholipid biosynthesis protein, PlsX-like | Phospholipid_synth_PlsX-like | Family | 18,260 | false | false | The proteins in this group are phospholipid biosynthesis proteins of unknown function. Escherichia coli PlsX protein has been shown to be required for phospholipid biosynthesis, but its exact function is not yet known [ , ]. It has been suggested to be an enzyme. | [
"GO:0006633"
] | [
"fatty acid biosynthetic process"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"MF_00019",
"PIRSF002465",
"PTHR30100",
"TIGR00182"
] | [
"PlsX",
"Phsphlp_syn_PlsX",
"",
"plsX"
] | [
17982,
17584,
18251,
17349
] | 4 | [
"EC",
"GP",
"METACYC"
] | [
"2.3.1.274",
"GenProp0837",
"PWY-5981"
] | [
"EC:2.3.1.274",
"GP:GenProp0837",
"METACYC:PWY-5981"
] | 3 | [
"1u7n",
"1vi1",
"6a1k"
] | 3 | [
"PUB00008132",
"PUB00014592"
] | [
"10464226",
"6094487"
] | [
"Characterization of a Pseudomonas aeruginosa fatty acid biosynthetic gene cluster: purification of acyl carrier protein (ACP) and malonyl-coenzyme A:ACP transacylase (FabD).",
"sn-Glycerol-3-phosphate auxotrophy of plsB strains of Escherichia coli: evidence that a second mutation, plsX, is required."
] | [
1999,
1984
] | 2 | [
"IPR003664"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
17761,
54,
445
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phospholipid biosynthesis protein, PlsX-like | Phospholipid biosynthesis protein, PlsX-like | Phospholipid_synth_PlsX-like | 7 |
IPR012286 | 12,286 | Tetraheme cytochrome domain | Tetraheme_cytochrome | Domain | 2,259 | false | false | Flavocytochrome C3 (Fcc3) enzymes from a number of Shewanella species, including Shewanella frigidimarina (strain NCIMB 400), have respiratory fumarate reductase activity, which enables the bacteria to respire anaerobically with fumarate as a terminal electron acceptor. Flavocytochrome C3 in S. frigidimarina is a solub... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF14537"
] | [
"Cytochrom_c3_2"
] | [
2259
] | 1 | [] | [] | [] | 0 | [
"1d4c",
"1d4d",
"1d4e",
"1e39",
"1jrx",
"1jry",
"1jrz",
"1kss",
"1ksu",
"1lj1",
"1m1p",
"1m1q",
"1m1r",
"1m64",
"1p2e",
"1p2h",
"1q9i",
"1qjd",
"1qo8",
"1y0p",
"2b7r",
"2b7s",
"2k3v",
"6ee7",
"6hr0"
] | 25 | [
"PUB00016225",
"PUB00016226"
] | [
"12080059",
"15581639"
] | [
"Crystal structures at atomic resolution reveal the novel concept of \"electron-harvesting\" as a role for the small tetraheme cytochrome c.",
"Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR."
] | [
2002,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Cyprideis torosa",
"ecological metagenomes"
] | [
38,
2166,
1,
54
] | 4 | [] | [] | 0 | true | Domain | Tetraheme cytochrome domain | Tetraheme cytochrome domain | Tetraheme_cytochrome | 5 |
IPR012289 | 12,289 | Lytic transglycosylase, superhelical linker | Lytic_TGlycosylase_superhlx_L | Domain | 5,916 | false | false | Bacterial lytic transglycosylases degrade murein via cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine, with the concomitant formation of a 1,6-anhydrobond in the muramic acid residue. There are both soluble (Slt enzymes) and membrane-bound (Mlt enzymes) lytic transglycosylas... | [
"GO:0004553",
"GO:0042597"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"periplasmic space"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF14718"
] | [
"SLT_L"
] | [
5916
] | 1 | [] | [] | [] | 0 | [
"1qsa",
"1qte",
"1sly",
"5mpq",
"5o1j",
"5o24",
"5o29",
"5o2n",
"5o2o",
"5ohu",
"6fbt",
"6fc4",
"6fcq",
"6fcr",
"6fcs",
"6fcu",
"6fpn",
"6h5f"
] | 18 | [
"PUB00011783"
] | [
"10452894"
] | [
"High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5848,
11,
57
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Lytic transglycosylase, superhelical linker | Lytic transglycosylase, superhelical linker | Lytic_TGlycosylase_superhlx_L | 2 |
IPR012290 | 12,290 | Fibrinogen, alpha/beta/gamma chain, coiled coil domain | Fibrinogen_a/b/g_coil_dom | Domain | 3,024 | false | false | Fibrinogen plays key roles in both blood clotting and platelet aggregation. During blood clot formation, the conversion of soluble fibrinogen to insoluble fibrin is triggered by thrombin, resulting in the polymerisation of fibrin, which forms a soft clot; this is then converted to a hard clot by factor XIIIA, which cro... | [
"GO:0005102",
"GO:0030168",
"GO:0051258",
"GO:0005577"
] | [
"signaling receptor binding",
"platelet activation",
"protein polymerization",
"fibrinogen complex"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"SMART"
] | [
"PF08702",
"SM01212"
] | [
"Fib_alpha",
"Fib_alpha"
] | [
3010,
2983
] | 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-1236974",
"R-HSA-140875",
"R-HSA-166058",
"R-HSA-216083",
"R-HSA-354192",
"R-HSA-354194",
"R-HSA-372708",
"R-HSA-381426",
"R-HSA-5602498",
"R-HSA-5603041",
"R-HSA-5674135",
"R-HSA-5686938",
"R-HSA-6802946",
"R-HSA-6802948",
"R-HSA-6802952",
"R-HSA-6802955",
"... | [
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-1236974",
"REACTOME:R-HSA-140875",
"REACTOME:R-HSA-166058",
"REACTOME:R-HSA-216083",
"REACTOME:R-HSA-354192",
"REACTOME:R-HSA-354194",
"REACTOME:R-HSA-372708",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-5602498",
"REACTOME:R-HSA-5603041",
"REACTOME:R-HSA-... | 41 | [
"1deq",
"1ei3",
"1fza",
"1fzb",
"1fzc",
"1fze",
"1fzf",
"1fzg",
"1jy2",
"1jy3",
"1lt9",
"1ltj",
"1lwu",
"1m1j",
"1n73",
"1n86",
"1n8e",
"1re3",
"1re4",
"1rf0",
"1rf1",
"2a45",
"2ffd",
"2h43",
"2hlo",
"2hod",
"2hpc",
"2oyh",
"2oyi",
"2q9i",
"2xnx",
"2xny"... | 38 | [
"PUB00016231",
"PUB00016232",
"PUB00016233",
"PUB00017188"
] | [
"12799374",
"11460466",
"11593005",
"15837518"
] | [
"Identification of a novel binding site for platelet integrins alpha IIb beta 3 (GPIIbIIIa) and alpha 5 beta 1 in the gamma C-domain of fibrinogen.",
"The structure and biological features of fibrinogen and fibrin.",
"Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution... | [
2003,
2001,
2001,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3024
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
18,
6,
14
] | 4 | true | Domain | Fibrinogen, alpha/beta/gamma chain, coiled coil domain | Fibrinogen, alpha/beta/gamma chain, coiled coil domain | Fibrinogen_a/b/g_coil_dom | 7 |
IPR012291 | 12,291 | CBM2, carbohydrate-binding domain superfamily | CBM2_carb-bd_dom_sf | Homologous_superfamily | 30,770 | false | false | The microbial degradation of cellulose and xylans requires several types of enzyme such as endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91) (exoglucanases), or xylanases (EC 3.2.1.8) [ ]. Structurally, cellulases and xylanases generally consist of a catalytic domain and a conserved region of ~100 amino aci... | [
"GO:0004553",
"GO:0030247"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"polysaccharide binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.40.290"
] | [
""
] | [
30770
] | 1 | [
"EC"
] | [
"3.2.1"
] | [
"EC:3.2.1"
] | 1 | [
"1c7s",
"1c7t",
"1e5b",
"1e5c",
"1exg",
"1exh",
"1heh",
"1hej",
"1qba",
"1qbb",
"1xbd",
"2cwr",
"2czn",
"2rtt",
"2xbd",
"3ndy",
"3ndz",
"5dhd",
"5dhe",
"6bt9",
"6f7e",
"6qfs",
"8ose",
"8otb",
"8owf",
"8oye"
] | 26 | [
"PUB00000421",
"PUB00003608",
"PUB00005068",
"PUB00032378",
"PUB00033740"
] | [
"7766609",
"1886523",
"1812490",
"10425686",
"9662439"
] | [
"Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy.",
"Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.",
"Bacterial cellulose-binding domain-like sequences in eucaryotic polypeptides.",
"A family ... | [
1995,
1991,
1991,
1999,
1998
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Megaviricetes",
"Methanobacteriota",
"unclassified sequences"
] | [
29610,
1079,
21,
11,
49
] | 5 | [] | [] | 0 | true | Homologous_superfamily | CBM2, carbohydrate-binding domain superfamily | CBM2, carbohydrate-binding domain superfamily | CBM2_carb-bd_dom_sf | 1 |
IPR012292 | 12,292 | Globin/Protoglobin | Globin/Proto | Homologous_superfamily | 79,827 | false | false | Globins are haem-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family that is widely distributed in many organisms [ ]. Globins have evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric gl... | [
"GO:0019825",
"GO:0020037"
] | [
"oxygen binding",
"heme binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.490.10"
] | [
""
] | [
79827
] | 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-1237044",
"R-BTA-1247673",
"R-BTA-2168880",
"R-BTA-6798695",
"R-BTA-8981607",
"R-BTA-9707564",
"R-BTA-9707616",
"R-CFA-8981607",
"R-DRE-1237044",
"R-DRE-1247673",
"R-DRE-203615",
"R-DRE-2168880",
"R-DRE-6798695",
"R-DRE-8981607",
"R-DRE-9707564",
"R-DRE-9707616",
"R-GGA-123704... | [
"REACTOME:R-BTA-1237044",
"REACTOME:R-BTA-1247673",
"REACTOME:R-BTA-2168880",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8981607",
"REACTOME:R-BTA-9707564",
"REACTOME:R-BTA-9707616",
"REACTOME:R-CFA-8981607",
"REACTOME:R-DRE-1237044",
"REACTOME:R-DRE-1247673",
"REACTOME:R-DRE-203615",
"REACTOME... | 57 | [
"1a00",
"1a01",
"1a0u",
"1a0z",
"1a3n",
"1a3o",
"1a4f",
"1a9w",
"1abw",
"1aby",
"1aj9",
"1ash",
"1b0b",
"1b86",
"1bab",
"1bbb",
"1bij",
"1bin",
"1buw",
"1bz0",
"1bz1",
"1bzz",
"1c40",
"1c7b",
"1c7c",
"1c7d",
"1cbl",
"1cbm",
"1cg5",
"1cg8",
"1ch4",
"1cls"... | 996 | [
"PUB00016016",
"PUB00016265",
"PUB00029465",
"PUB00035865",
"PUB00035866",
"PUB00035867",
"PUB00035868",
"PUB00035869",
"PUB00035870",
"PUB00035871",
"PUB00035872",
"PUB00035873",
"PUB00035877",
"PUB00055462",
"PUB00055463",
"PUB00153677"
] | [
"15096613",
"14560666",
"12962627",
"16600051",
"17540514",
"11092893",
"11481493",
"15598488",
"16888280",
"15598493",
"15339940",
"15804833",
"17084861",
"17540516",
"17701548",
"21495624"
] | [
"Ancestral hemoglobins in Archaea.",
"Microbial globins.",
"Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity.",
"A phylogenomic profile of globins.",
"A model of globin evolution.",
"Flavohemoglobin, a globin with a peroxidase-like catalytic site.",
"Globin-couple... | [
2004,
2003,
2003,
2006,
2007,
2001,
2001,
2005,
2006,
2005,
2004,
2004,
2007,
2007,
2007,
2011
] | 16 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
717,
45450,
33090,
8,
562
] | 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",... | [
13,
61,
45,
6,
2,
148,
66,
3,
9,
60,
2,
1,
17
] | 13 | true | Homologous_superfamily | Globin/Protoglobin | Globin/Protoglobin | Globin/Proto | 7 |
IPR012295 | 12,295 | TBP domain superfamily | TBP_dom_sf | Homologous_superfamily | 36,746 | false | false | The TATA-box binding protein (TBP) is required for the initiation of transcription by RNA polymerases I, II and III, from promoters with or without a TATA box [ , ]. The core of TBP (~180 residues) is highly conserved and contains two 77-amino acid repeats that produce a saddle-shaped structure that straddles the DNA; ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.310.10"
] | [
""
] | [
36746
] | 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-177504",
"R-BTA-2132295",
"R-BTA-416993",
"R-BTA-437239",
"R-BTA-5099900",
"R-BTA-5140745",
"R-BTA-5250924",
"R-BTA-674695",
"R-BTA-6798695",
"R-BTA-6804756",
"R-BTA-6807505",
"R-BTA-6807878",
"R-BTA-6811434",
"R-BTA-73762",
"R-BTA-73772",
"R-BTA-73776",
"R-BTA-73779",
"R-BT... | [
"REACTOME:R-BTA-177504",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-416993",
"REACTOME:R-BTA-437239",
"REACTOME:R-BTA-5099900",
"REACTOME:R-BTA-5140745",
"REACTOME:R-BTA-5250924",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6804756",
"REACTOME:R-BTA-6807505",
"REACTOME:R-... | 222 | [
"1ais",
"1b9k",
"1c9b",
"1cdw",
"1d3u",
"1e42",
"1jfi",
"1ky6",
"1ky7",
"1kyd",
"1kyf",
"1kyu",
"1mp9",
"1ngm",
"1nh2",
"1nvp",
"1pcz",
"1pzd",
"1qn3",
"1qn4",
"1qn5",
"1qn6",
"1qn7",
"1qn8",
"1qn9",
"1qna",
"1qnb",
"1qnc",
"1qne",
"1qtp",
"1qts",
"1r4x"... | 214 | [
"PUB00004136",
"PUB00017042",
"PUB00017043",
"PUB00088137"
] | [
"1436073",
"10974559",
"12782648",
"21664908"
] | [
"Crystal structure of TFIID TATA-box binding protein.",
"Control of gene expression through regulation of the TATA-binding protein.",
"Diversified transcription initiation complexes expand promoter selectivity and tissue-specific gene expression.",
"Identification of the substrate binding site in the N-termin... | [
1992,
2000,
2003,
2011
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1722,
2497,
32059,
91,
377
] | 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... | [
37,
8,
34,
23,
51,
40,
3,
26,
60,
3,
3,
142
] | 12 | true | Homologous_superfamily | TBP domain superfamily | TBP domain superfamily | TBP_dom_sf | 4 |
IPR012296 | 12,296 | Nuclease, putative, TT1808 | Nuclease_put_TT1808 | Homologous_superfamily | 44,043 | false | false | This superfamily represents a structural motif found in the putative nuclease, hypothetical protein TT1808 (or TTHA1514), an AT-rich DNA-binding protein from Thermus thermophilus. This domain has a 3-layer α/β/α topology similar to that found in restriction endonucleases [ ]. The nuclease domain is ubiquitously found i... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.1570.10"
] | [
""
] | [
44043
] | 1 | [] | [] | [] | 0 | [
"1wdj",
"3ot2",
"6okh",
"9y1l"
] | 4 | [
"PUB00035698",
"PUB00035699"
] | [
"17154156",
"15720711"
] | [
"Crystal structure of TTHA1657 (AT-rich DNA-binding protein; p25) from Thermus thermophilus HB8 at 2.16 A resolution.",
"Identification of a new family of putative PD-(D/E)XK nucleases with unusual phylogenomic distribution and a new type of the active site."
] | [
2007,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
2,
43068,
861,
3,
109
] | 5 | [] | [] | 0 | true | Homologous_superfamily | Nuclease, putative, TT1808 | Nuclease, putative, TT1808 | Nuclease_put_TT1808 | 2 |
IPR012297 | 12,297 | Restriction endonuclease EcoO109IR, catalytic domain superfamily | EcoO109IR_cat_dom_sf | Homologous_superfamily | 139 | false | false | There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.1560.10"
] | [
""
] | [
139
] | 1 | [] | [] | [] | 0 | [
"1wtd",
"1wte"
] | 2 | [
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035700",
"PUB00035705",
"PUB00035707"
] | [
"15770420",
"14576294",
"11827971",
"11557805",
"15590682",
"15121719",
"12665693"
] | [
"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship between different subgroups of restriction endonucleases.",
"Structure and function of type II restriction endonucleases.",
"Cry... | [
2005,
2003,
2002,
2001,
2005,
2004,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanofollis tationis",
"Tilletia caries",
"ecological metagenomes"
] | [
134,
1,
1,
3
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Restriction endonuclease EcoO109IR, catalytic domain superfamily | Restriction endonuclease EcoO109IR, catalytic domain superfamily | EcoO109IR_cat_dom_sf | 7 |
IPR012300 | 12,300 | Peptidase M6, InhA | Pept_M6_InhA | Family | 2,853 | false | false | Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF007519"
] | [
"Protease_InhA"
] | [
2853
] | 1 | [
"EC",
"METACYC"
] | [
"3.4.24.-",
"PWY-8119"
] | [
"EC:3.4.24.-",
"METACYC:PWY-8119"
] | 2 | [
"4yu5",
"4yu6"
] | 2 | [
"PUB00000112",
"PUB00003579",
"PUB00011416",
"PUB00014362",
"PUB00014369",
"PUB00014396",
"PUB00014398",
"PUB00014400",
"PUB00014414",
"PUB00015264"
] | [
"3318666",
"7674922",
"9371455",
"6421577",
"2089225",
"992874",
"11429458",
"12029046",
"10475957",
"7140755"
] | [
"Cell-free immunity in insects.",
"Evolutionary families of metallopeptidases.",
"Characterization of the Vibrio cholerae El Tor lipase operon lipAB and a protease gene downstream of the hly region.",
"Characterization of inhibitor A, a protease from Bacillus thuringiensis which degrades attacins and cecropin... | [
1987,
1995,
1997,
1984,
1990,
1976,
2001,
2002,
1999,
1982
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Rhynchospora breviuscula"
] | [
2852,
1
] | 2 | [] | [] | 0 | true | Family | Peptidase M6, InhA | Peptidase M6, InhA | Pept_M6_InhA | 3 |
IPR012301 | 12,301 | Malic enzyme, N-terminal domain | Malic_N_dom | Domain | 51,823 | false | false | This entry represents the N-terminal domain of the NAD(P)-dependent malic enzyme and related proteins from bacteria, eukaryotes and archaea. Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate, a reaction important in a number of metabolic pathways - e.g. carbon diox... | [
"GO:0004470",
"GO:0016616"
] | [
"malic enzyme activity",
"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF00390",
"SM01274"
] | [
"malic",
"malic"
] | [
51735,
51203
] | 2 | [
"EC",
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"1.1.1.38",
"GenProp1344",
"GenProp1722",
"PWY-3641",
"PWY-7115",
"PWY-7118",
"PWY-7384",
"PWY-7686",
"R-HSA-1989781",
"R-HSA-70268",
"R-HSA-9818025",
"R-HSA-9837999",
"R-HSA-9861718",
"R-MMU-70268",
"R-MMU-9837999",
"R-MMU-9861718",
"R-RNO-70268",
"R-RNO-9861718"
] | [
"EC:1.1.1",
"EC:1.1.1.38",
"GP:GenProp1344",
"GP:GenProp1722",
"METACYC:PWY-3641",
"METACYC:PWY-7115",
"METACYC:PWY-7118",
"METACYC:PWY-7384",
"METACYC:PWY-7686",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-70268",
"REACTOME:R-HSA-9818025",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9861718",... | 19 | [
"1do8",
"1efk",
"1efl",
"1gq2",
"1gz3",
"1gz4",
"1llq",
"1o0s",
"1pj2",
"1pj3",
"1pj4",
"1pjl",
"1qr6",
"1vl6",
"1ww8",
"2a9f",
"2aw5",
"2dvm",
"2hae",
"3nv9",
"3wja",
"5cee",
"5ou5",
"6ags",
"6c7n",
"6urf",
"6w29",
"6w2n",
"6w49",
"6w53",
"6w56",
"6w57"... | 55 | [
"PUB00000616",
"PUB00002681",
"PUB00002876",
"PUB00004541",
"PUB00022087",
"PUB00099681",
"PUB00099683"
] | [
"1911848",
"1993674",
"8300616",
"2103472",
"12033925",
"10477256",
"1640469"
] | [
"Duck liver malic enzyme: sequence of a tryptic peptide containing the cysteine residue labeled by the substrate analog bromopyruvate.",
"Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli.",
"Cloning and analysis of the C4 photosynthetic NAD-d... | [
1991,
1991,
1994,
1990,
2002,
1999,
1992
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctYaH2",
"unclassified sequences"
] | [
822,
34717,
15809,
1,
474
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
25,
1,
6,
25,
2,
20,
11,
2,
31,
14,
1,
1,
91
] | 13 | true | Domain | Malic enzyme, N-terminal domain | Malic enzyme, N-terminal domain | Malic_N_dom | 4 |
IPR012302 | 12,302 | Malic enzyme, NAD-binding | Malic_NAD-bd | Domain | 52,515 | false | false | This entry represents the NAD-binding domain of malic enzymes. Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate, a reaction important in a number of metabolic pathways - e.g. carbon dioxide released from the reaction may be used in sugar production during the Calv... | [
"GO:0051287"
] | [
"NAD binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF03949",
"SM00919"
] | [
"Malic_M",
"Malic_M"
] | [
52352,
51671
] | 2 | [
"EC",
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"1.1.1.38",
"GenProp1344",
"GenProp1722",
"PWY-3641",
"PWY-7115",
"PWY-7118",
"PWY-7384",
"PWY-7686",
"R-HSA-1989781",
"R-HSA-70268",
"R-HSA-9818025",
"R-HSA-9837999",
"R-HSA-9861718",
"R-MMU-70268",
"R-MMU-9837999",
"R-MMU-9861718",
"R-RNO-70268",
"R-RNO-9861718"
] | [
"EC:1.1.1",
"EC:1.1.1.38",
"GP:GenProp1344",
"GP:GenProp1722",
"METACYC:PWY-3641",
"METACYC:PWY-7115",
"METACYC:PWY-7118",
"METACYC:PWY-7384",
"METACYC:PWY-7686",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-70268",
"REACTOME:R-HSA-9818025",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9861718",... | 19 | [
"1do8",
"1efk",
"1efl",
"1gq2",
"1gz3",
"1gz4",
"1llq",
"1o0s",
"1pj2",
"1pj3",
"1pj4",
"1pjl",
"1qr6",
"1vl6",
"1ww8",
"2a9f",
"2aw5",
"2dvm",
"2hae",
"3nv9",
"3wja",
"5cee",
"5ou5",
"6ags",
"6c7n",
"6urf",
"6w29",
"6w2n",
"6w49",
"6w53",
"6w56",
"6w57"... | 55 | [
"PUB00000616",
"PUB00002681",
"PUB00002876",
"PUB00004541",
"PUB00022087",
"PUB00099681",
"PUB00099683"
] | [
"1911848",
"1993674",
"8300616",
"2103472",
"12033925",
"10477256",
"1640469"
] | [
"Duck liver malic enzyme: sequence of a tryptic peptide containing the cysteine residue labeled by the substrate analog bromopyruvate.",
"Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli.",
"Cloning and analysis of the C4 photosynthetic NAD-d... | [
1991,
1991,
1994,
1990,
2002,
1999,
1992
] | 7 | [] | [
"IPR045213"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctYaH2",
"unclassified sequences"
] | [
820,
34884,
16288,
1,
522
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
25,
1,
6,
25,
2,
14,
9,
2,
29,
14,
1,
2,
81
] | 13 | true | Domain | Malic enzyme, NAD-binding | Malic enzyme, NAD-binding | Malic_NAD-bd | 2 |
IPR012308 | 12,308 | DNA ligase, ATP-dependent, N-terminal | DNA_ligase_ATP-dep_N | Domain | 23,744 | false | false | DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalysing 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:0003677",
"GO:0003910",
"GO:0006281",
"GO:0006310"
] | [
"DNA binding",
"DNA ligase (ATP) activity",
"DNA repair",
"DNA recombination"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF04675"
] | [
"DNA_ligase_A_N"
] | [
23744
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"6.5.1",
"6.5.1.1",
"R-CEL-5358565",
"R-CEL-5358606",
"R-CEL-5651801",
"R-CEL-6782210",
"R-CEL-69183",
"R-DDI-110362",
"R-DDI-110381",
"R-DDI-5358565",
"R-DDI-5358606",
"R-DDI-5649702",
"R-DDI-5651801",
"R-DDI-5693571",
"R-DDI-6782210",
"R-DDI-69183",
"R-DME-5358565",
"R-DME-535860... | [
"EC:6.5.1",
"EC:6.5.1.1",
"REACTOME:R-CEL-5358565",
"REACTOME:R-CEL-5358606",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-69183",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-110381",
"REACTOME:R-DDI-5358565",
"REACTOME:R-DDI-5358606",
"REACTOME:R-DDI-5649702",
"REACTOME:... | 65 | [
"1x9n",
"2cfm",
"2hiv",
"2hix",
"3gde",
"3l2p",
"3rr5",
"3w1b",
"3w1g",
"3w5o",
"4eq5",
"4hto",
"4htp",
"6bkf",
"6bkg",
"6p09",
"6p0a",
"6p0b",
"6p0c",
"6p0d",
"6p0e",
"6q1v",
"6wbo",
"7d9k",
"7d9y",
"7kr3",
"7kr4",
"7l34",
"7l35",
"7lsy",
"7lt3",
"7nfc"... | 65 | [
"PUB00000083",
"PUB00004409",
"PUB00004738",
"PUB00010654",
"PUB00016293"
] | [
"1497311",
"1437556",
"1988940",
"11983065",
"9016621"
] | [
"Mammalian DNA ligases.",
"Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases.",
"Location of the active site for enzyme-adenylate formation in DNA ligases.",
"ATP-dependent DNA ligases.",... | [
1992,
1992,
1991,
2002,
1997
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1003,
6954,
15530,
192,
65
] | 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... | [
20,
4,
6,
5,
24,
12,
4,
8,
16,
2,
3,
27
] | 12 | true | Domain | DNA ligase, ATP-dependent, N-terminal | DNA ligase, ATP-dependent, N-terminal | DNA_ligase_ATP-dep_N | 6 |
IPR012309 | 12,309 | DNA ligase, ATP-dependent, C-terminal | DNA_ligase_ATP-dep_C | Domain | 37,710 | false | false | This region is found in many but not all ATP-dependent DNA ligase enzymes ( ). It is thought to constitute part of the catalytic core of ATP dependent DNA ligase [ ]. DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalysing the formation of an internucleotide ester bond bet... | [
"GO:0003910",
"GO:0006281",
"GO:0006310"
] | [
"DNA ligase (ATP) activity",
"DNA repair",
"DNA recombination"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF04679"
] | [
"DNA_ligase_A_C"
] | [
37710
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"6.5.1",
"6.5.1.1",
"R-CEL-5358565",
"R-CEL-5358606",
"R-CEL-5651801",
"R-CEL-6782210",
"R-CEL-69183",
"R-DDI-110362",
"R-DDI-110381",
"R-DDI-5358565",
"R-DDI-5358606",
"R-DDI-5649702",
"R-DDI-5651801",
"R-DDI-5693571",
"R-DDI-6782210",
"R-DDI-69183",
"R-DME-5358565",
"R-DME-535860... | [
"EC:6.5.1",
"EC:6.5.1.1",
"REACTOME:R-CEL-5358565",
"REACTOME:R-CEL-5358606",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-69183",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-110381",
"REACTOME:R-DDI-5358565",
"REACTOME:R-DDI-5358606",
"REACTOME:R-DDI-5649702",
"REACTOME:... | 65 | [
"1vs0",
"1x9n",
"2cfm",
"2hiv",
"2hix",
"3gde",
"3l2p",
"3rr5",
"3w1b",
"3w1g",
"3w5o",
"4eq5",
"6bkf",
"6bkg",
"6nhx",
"6nhz",
"6p09",
"6p0a",
"6p0b",
"6p0c",
"6p0d",
"6p0e",
"6q1v",
"6wbo",
"7kr3",
"7kr4",
"7l34",
"7l35",
"7lsy",
"7lt3",
"7nfc",
"7nfe"... | 63 | [
"PUB00000083",
"PUB00004409",
"PUB00004738",
"PUB00010654",
"PUB00016293"
] | [
"1497311",
"1437556",
"1988940",
"11983065",
"9016621"
] | [
"Mammalian DNA ligases.",
"Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases.",
"Location of the active site for enzyme-adenylate formation in DNA ligases.",
"ATP-dependent DNA ligases.",... | [
1992,
1992,
1991,
2002,
1997
] | 5 | [] | [
"IPR044117"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1012,
23512,
12857,
181,
148
] | 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... | [
20,
1,
6,
3,
14,
12,
3,
8,
15,
1,
3,
22
] | 12 | true | Domain | DNA ligase, ATP-dependent, C-terminal | DNA ligase, ATP-dependent, C-terminal | DNA_ligase_ATP-dep_C | 8 |
IPR012310 | 12,310 | DNA ligase, ATP-dependent, central | DNA_ligase_ATP-dep_cent | Domain | 50,275 | false | false | DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalysing 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:0003910",
"GO:0005524",
"GO:0006281",
"GO:0006310"
] | [
"DNA ligase (ATP) activity",
"ATP binding",
"DNA repair",
"DNA recombination"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PFAM",
"PROFILE"
] | [
"PF01068",
"PS50160"
] | [
"DNA_ligase_A_M",
"DNA_LIGASE_A3"
] | [
49052,
44810
] | 2 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"6.5.1",
"6.5.1.1",
"PDOC00295",
"R-CEL-5358565",
"R-CEL-5358606",
"R-CEL-5651801",
"R-CEL-6782210",
"R-CEL-69183",
"R-DDI-110362",
"R-DDI-110381",
"R-DDI-5358565",
"R-DDI-5358606",
"R-DDI-5649702",
"R-DDI-5651801",
"R-DDI-5693571",
"R-DDI-6782210",
"R-DDI-69183",
"R-DME-5358565",
... | [
"EC:6.5.1",
"EC:6.5.1.1",
"PROSITEDOC:PDOC00295",
"REACTOME:R-CEL-5358565",
"REACTOME:R-CEL-5358606",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-69183",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-110381",
"REACTOME:R-DDI-5358565",
"REACTOME:R-DDI-5358606",
"REACTOME:R-... | 66 | [
"1a0i",
"1fvi",
"1p8l",
"1vs0",
"1x9n",
"2cfm",
"2hiv",
"2hix",
"2q2t",
"2q2u",
"3gde",
"3l2p",
"3rr5",
"3vnn",
"3w1b",
"3w1g",
"3w5o",
"4d05",
"4eq5",
"6bkf",
"6bkg",
"6dt1",
"6gdr",
"6imj",
"6imk",
"6iml",
"6imn",
"6nhx",
"6nhz",
"6p09",
"6p0a",
"6p0b"... | 83 | [
"PUB00000083",
"PUB00000934",
"PUB00004409",
"PUB00004738",
"PUB00010654"
] | [
"1497311",
"8653795",
"1437556",
"1988940",
"11983065"
] | [
"Mammalian DNA ligases.",
"Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7.",
"Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases.",
"Location of the active site for... | [
1992,
1996,
1992,
1991,
2002
] | 5 | [] | [
"IPR044119",
"IPR044125"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1058,
28911,
17800,
2125,
381
] | 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... | [
25,
3,
6,
5,
19,
12,
4,
10,
15,
2,
3,
27
] | 12 | true | Domain | DNA ligase, ATP-dependent, central | DNA ligase, ATP-dependent, central | DNA_ligase_ATP-dep_cent | 6 |
IPR012312 | 12,312 | Hemerythrin-like | Hemerythrin-like | Domain | 51,172 | false | false | This entry represents a hemerythrin cation-binding domain that occurs [ ] in hemerythrins, myohemerythrin and related proteins. This domain binds iron in hemerythrin, but can bind other metals in related proteins, such as cadmium in a Nereis diversicolor protein ( ) [ ]. This domain is also found in Repair of iron cent... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01814"
] | [
"Hemerythrin"
] | [
51172
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8951664",
"R-BTA-917937",
"R-BTA-983168",
"R-DRE-8951664",
"R-DRE-917937",
"R-DRE-983168",
"R-HSA-390471",
"R-HSA-8951664",
"R-HSA-917937",
"R-HSA-983168",
"R-MMU-8951664",
"R-MMU-917937",
"R-MMU-983168"
] | [
"REACTOME:R-BTA-8951664",
"REACTOME:R-BTA-917937",
"REACTOME:R-BTA-983168",
"REACTOME:R-DRE-8951664",
"REACTOME:R-DRE-917937",
"REACTOME:R-DRE-983168",
"REACTOME:R-HSA-390471",
"REACTOME:R-HSA-8951664",
"REACTOME:R-HSA-917937",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-8951664",
"REACTOME:R-MMU... | 13 | [
"1a7d",
"1a7e",
"1hmd",
"1hmo",
"1hrb",
"1i4y",
"1i4z",
"2avk",
"2awc",
"2awy",
"2hmq",
"2hmz",
"2mhr",
"2p0n",
"3agt",
"3agu",
"3cax",
"3u9j",
"3u9m",
"3v5x",
"3v5y",
"3v5z",
"3waq",
"3whn",
"4xpw",
"4xpx",
"4xpy",
"4xq1",
"5fnn",
"5fnp",
"5fny",
"6q09"... | 42 | [
"PUB00016669",
"PUB00057272",
"PUB00075456"
] | [
"12625841",
"12743530",
"19140014"
] | [
"New knowledge from old: in silico discovery of novel protein domains in Streptomyces coelicolor.",
"Antibacterial properties of hemerythrin of the sand worm Nereis diversicolor.",
"Di-iron proteins of the Ric family are involved in iron-sulfur cluster repair."
] | [
2003,
2003,
2009
] | 3 | [] | [
"IPR012827",
"IPR045808"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
605,
40895,
9113,
7,
552
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",... | [
18,
3,
1,
2,
5,
3,
12,
6,
1,
39
] | 10 | true | Domain | Hemerythrin-like | Hemerythrin-like | Hemerythrin-like | 2 |
IPR012313 | 12,313 | Zinc finger, FCS-type | Znf_FCS | Domain | 8,375 | false | false | Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b... | [
"GO:0008270",
"GO:0005634"
] | [
"zinc ion binding",
"nucleus"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROFILE"
] | [
"PS51024"
] | [
"ZF_FCS"
] | [
8375
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51024",
"R-DME-2559580",
"R-DME-3108214",
"R-DME-3899300",
"R-DME-4551638",
"R-DME-4570464",
"R-DME-8939243",
"R-DME-8943724",
"R-DME-8953750",
"R-DRE-2559580",
"R-DRE-3899300",
"R-DRE-4570464",
"R-HSA-2559580",
"R-HSA-3108214",
"R-HSA-3899300",
"R-HSA-4551638",
"R-HSA-4570464",... | [
"PROSITEDOC:PDOC51024",
"REACTOME:R-DME-2559580",
"REACTOME:R-DME-3108214",
"REACTOME:R-DME-3899300",
"REACTOME:R-DME-4551638",
"REACTOME:R-DME-4570464",
"REACTOME:R-DME-8939243",
"REACTOME:R-DME-8943724",
"REACTOME:R-DME-8953750",
"REACTOME:R-DRE-2559580",
"REACTOME:R-DRE-3899300",
"REACTOME:... | 29 | [
"2l8e",
"2w0t"
] | 2 | [
"PUB00014077",
"PUB00016642",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"12665246",
"15200961",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"Zinc fingers--folds for many occasions.",
"The C. elegans Polycomb gene SOP-2 encodes an RNA binding protein.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
"Zinc finger proteins: getting a grip on RNA.",
"Zinc finger peptide... | [
2002,
2004,
2007,
2005,
2005,
1999,
2001
] | 7 | [] | [] | 0 | 0 | null | [
"Actinomycetes",
"Eukaryota"
] | [
5,
8370
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
79,
10,
23,
21,
25
] | 5 | true | Domain | Zinc finger, FCS-type | Zinc finger, FCS-type | Znf_FCS | 5 |
IPR012314 | 12,314 | Peptidase M12B, GON-ADAMTSs | Pept_M12B_GON-ADAMTSs | Domain | 3,469 | false | false | Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase... | [
"GO:0004222",
"GO:0008270"
] | [
"metalloendopeptidase activity",
"zinc ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF08685",
"PS51046"
] | [
"GON",
"GON"
] | [
3312,
3344
] | 2 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.24.-",
"PWY-8119",
"PDOC51046",
"R-CEL-5173214",
"R-HSA-1474228",
"R-HSA-5083635",
"R-HSA-5173214",
"R-MMU-5173214"
] | [
"EC:3.4.24.-",
"METACYC:PWY-8119",
"PROSITEDOC:PDOC51046",
"REACTOME:R-CEL-5173214",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-5083635",
"REACTOME:R-HSA-5173214",
"REACTOME:R-MMU-5173214"
] | 8 | [] | 0 | [
"PUB00003579",
"PUB00016664",
"PUB00016666"
] | [
"7674922",
"12514189",
"12562771"
] | [
"Evolutionary families of metallopeptidases.",
"Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1.",
"Identification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases-disintegrins with multiple thrombospondin-1 repea... | [
1995,
2003,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcina",
"ecological metagenomes"
] | [
106,
3348,
9,
6
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
3,
6,
5,
6
] | 6 | true | Domain | Peptidase M12B, GON-ADAMTSs | Peptidase M12B, GON-ADAMTSs | Pept_M12B_GON-ADAMTSs | 3 |
IPR012316 | 12,316 | ITAM motif, hantavirus type | ITAM_motif_hantavir-typ | Domain | 941 | false | false | Signal transduction by T and B cell antigen receptors and certain receptors for Ig Fc regions involves a conserved sequence motif, termed an immunoreceptor tyrosine-based activation motif (ITAM). It is also found in the cytoplasmic domain of the apoptosis receptor. Phosphorylation of the two ITAM tyrosines is a critica... | [
"GO:0007165"
] | [
"signal transduction"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF10538",
"PS51056"
] | [
"ITAM_Cys-rich",
"ITAM_2"
] | [
471,
890
] | 2 | [
"PROSITEDOC"
] | [
"PDOC51055"
] | [
"PROSITEDOC:PDOC51055"
] | 1 | [
"9p3i",
"9p3l",
"9p3m",
"9p3x",
"9p3y"
] | 5 | [
"PUB00008053",
"PUB00016636",
"PUB00016637"
] | [
"7594458",
"14552840",
"12502882"
] | [
"Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate Lyn and Syk tyrosine kinases.",
"T-cell receptor signal transmission: who gives an ITAM?",
"Hantavirus pulmonary syndrome-associated hantaviruses contain conserved and functional ITAM signaling elements."
] | [
1995,
2003,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Hantaviridae"
] | [
941
] | 1 | [] | [] | 0 | true | Domain | ITAM motif, hantavirus type | ITAM motif, hantavirus type | ITAM_motif_hantavir-typ | 6 |
IPR012317 | 12,317 | Poly(ADP-ribose) polymerase, catalytic domain | Poly(ADP-ribose)pol_cat_dom | Domain | 41,572 | false | false | Poly(ADP-ribose) polymerases (PARP) are a family of enzymes present in eukaryotes, which catalyse the poly(ADP-ribosyl)ation of a limited number of proteins involved in chromatin architecture, DNA repair, or in DNA metabolism, including PARP itself. PARP, also known as poly(ADP-ribose) synthetase and poly(ADP-ribose) t... | [
"GO:0003950"
] | [
"NAD+ poly-ADP-ribosyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF00644",
"PS51059"
] | [
"PARP",
"PARP_CATALYTIC"
] | [
36638,
36620
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTO... | [
"2.4.2.-",
"PWY-5381",
"PWY-5800",
"PWY-6148",
"PWY-6720",
"PWY-7018",
"PWY-7025",
"PWY-7450",
"PWY-7817",
"PWY-7981",
"PDOC51059",
"R-CEL-5696394",
"R-CEL-5696395",
"R-CEL-5696400",
"R-DME-110362",
"R-DME-2173795",
"R-DME-3108214",
"R-DME-5685939",
"R-DME-5696394",
"R-DME-5696... | [
"EC:2.4.2.-",
"METACYC:PWY-5381",
"METACYC:PWY-5800",
"METACYC:PWY-6148",
"METACYC:PWY-6720",
"METACYC:PWY-7018",
"METACYC:PWY-7025",
"METACYC:PWY-7450",
"METACYC:PWY-7817",
"METACYC:PWY-7981",
"PROSITEDOC:PDOC51059",
"REACTOME:R-CEL-5696394",
"REACTOME:R-CEL-5696395",
"REACTOME:R-CEL-5696... | 61 | [
"1a26",
"1efy",
"1gs0",
"1pax",
"1uk0",
"1uk1",
"1wok",
"2paw",
"2pax",
"2pqf",
"2rcw",
"2rd6",
"2rf5",
"2x5y",
"3blj",
"3c49",
"3c4h",
"3ce0",
"3fhb",
"3gey",
"3gjw",
"3gn7",
"3goy",
"3hkv",
"3kcz",
"3kjd",
"3kr7",
"3kr8",
"3l3l",
"3l3m",
"3mhj",
"3mhk"... | 433 | [
"PUB00004898",
"PUB00005417",
"PUB00016633",
"PUB00016634",
"PUB00016672"
] | [
"8755499",
"8016868",
"15273990",
"15561303",
"14739238"
] | [
"Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.",
"Poly(ADP-ribose) polymerase: a molecular nick-sensor.",
"The PARP superfamily.",
"Poly(ADP-ribose) polymerases: homology, structural domains and functions. Novel therapeutical applications.",
"Crystal structure of the cataly... | [
1996,
1994,
2004,
2005,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
2,
186,
41302,
49,
33
] | 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"
] | [
60,
6,
76,
3,
69,
45,
1,
33,
49,
81
] | 10 | true | Domain | Poly(ADP-ribose) polymerase, catalytic domain | Poly(ADP-ribose) polymerase, catalytic domain | Poly(ADP-ribose)pol_cat_dom | 3 |
IPR012318 | 12,318 | Crp-type HTH domain | HTH_CRP | Domain | 87,051 | false | false | The Crp-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 70-75 amino acids present in transcription regulators of the crp-fnr family, involved in the control of virulence factors, enzymes of aromatic ring degradation, nitrogen fixation, photosynthesis, and various types of respiration. T... | [
"GO:0003677",
"GO:0006355"
] | [
"DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00325",
"PF13545",
"PR00034",
"PS51063",
"SM00419"
] | [
"Crp",
"HTH_Crp_2",
"HTHCRP",
"HTH_CRP_2",
"HTH_CRP"
] | [
1343,
79197,
29336,
74179,
67443
] | 5 | [
"PROSITEDOC"
] | [
"PDOC00041"
] | [
"PROSITEDOC:PDOC00041"
] | 1 | [
"1cgp",
"1ft9",
"1g6n",
"1hw5",
"1i5z",
"1i6x",
"1j59",
"1lb2",
"1o3q",
"1o3r",
"1o3s",
"1o3t",
"1o5l",
"1omi",
"1run",
"1ruo",
"1zrc",
"1zrd",
"1zre",
"1zrf",
"1zyb",
"2beo",
"2bgc",
"2cgp",
"2fmy",
"2gau",
"2gzw",
"2h6b",
"2h6c",
"2hkx",
"2oz6",
"2wc2"... | 149 | [
"PUB00004442",
"PUB00013967"
] | [
"8441692",
"14638413"
] | [
"Lactobacillus casei contains a member of the CRP-FNR family.",
"Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs."
] | [
1993,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
917,
84800,
221,
17,
1096
] | 5 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | Crp-type HTH domain | Crp-type HTH domain | HTH_CRP | 6 |
IPR012319 | 12,319 | Formamidopyrimidine-DNA glycosylase, catalytic domain | FPG_cat | Domain | 42,631 | false | false | This entry represents the catalytic domain of DNA glycosylase/AP lyase enzymes including formamidopyrimidine-DNA glycosylases (Fpg; MutM) and endonuclease VIII (Nei). Formamidopyrimidine-DNA glycosylases (Fpg, MutM) are trifunctional DNA base excision repair enzymes that remove a wide range of oxidation-damaged bases (... | [
"GO:0003906",
"GO:0008270",
"GO:0019104",
"GO:0006284"
] | [
"DNA-(apurinic or apyrimidinic site) endonuclease activity",
"zinc ion binding",
"DNA N-glycosylase activity",
"base-excision repair"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01149",
"PS51068",
"SM00898"
] | [
"Fapy_DNA_glyco",
"FPG_CAT",
"Fapy_DNA_glyco"
] | [
40865,
40959,
41053
] | 3 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.2.2.23",
"4.2.99.18",
"PDOC00956",
"R-BTA-110329",
"R-BTA-5649702",
"R-HSA-110328",
"R-HSA-110329",
"R-HSA-110330",
"R-HSA-110331",
"R-HSA-5649702",
"R-HSA-9616334",
"R-HSA-9629232",
"R-HSA-9636003",
"R-MMU-110328",
"R-MMU-110329",
"R-MMU-110330",
"R-MMU-110331",
"R-MMU-5649702"... | [
"EC:3.2.2.23",
"EC:4.2.99.18",
"PROSITEDOC:PDOC00956",
"REACTOME:R-BTA-110329",
"REACTOME:R-BTA-5649702",
"REACTOME:R-HSA-110328",
"REACTOME:R-HSA-110329",
"REACTOME:R-HSA-110330",
"REACTOME:R-HSA-110331",
"REACTOME:R-HSA-5649702",
"REACTOME:R-HSA-9616334",
"REACTOME:R-HSA-9629232",
"REACTOM... | 18 | [
"1ee8",
"1k3w",
"1k3x",
"1k82",
"1kfv",
"1l1t",
"1l1z",
"1l2b",
"1l2c",
"1l2d",
"1nnj",
"1pji",
"1pjj",
"1pm5",
"1q39",
"1q3b",
"1q3c",
"1r2y",
"1r2z",
"1tdh",
"1tdz",
"1xc8",
"2ea0",
"2f5n",
"2f5o",
"2f5p",
"2f5q",
"2f5s",
"2opf",
"2oq4",
"2xzf",
"2xzu"... | 121 | [
"PUB00002832",
"PUB00003593",
"PUB00012853",
"PUB00014010",
"PUB00018046",
"PUB00018047",
"PUB00031419"
] | [
"8473347",
"7704272",
"11912217",
"10921868",
"15588838",
"12055620",
"15232006"
] | [
"Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role.",
"Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein.",
"Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA.",
"Cryst... | [
1993,
1995,
2002,
2000,
2004,
2002,
2004
] | 7 | [] | [
"IPR044090",
"IPR044091"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
58,
36766,
5144,
61,
602
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
8,
4,
2,
10,
6,
1,
7,
8,
9
] | 9 | true | Domain | Formamidopyrimidine-DNA glycosylase, catalytic domain | Formamidopyrimidine-DNA glycosylase, catalytic domain | FPG_cat | 2 |
IPR012320 | 12,320 | Stonin homology | SHD_dom | Domain | 2,876 | false | false | Human stonins, like their Drosophila homologue stoned B, are supposed to be endocytotic proteins involved in clathrin-mediated endocytosis at synapses. The two human stonins, as well as their Drosophila melanogaster (Fruit fly) and Caenorhabditis elegans homologues, exhibit a modular structure consisting of an N-termin... | [
"GO:0006897"
] | [
"endocytosis"
] | [
"biological_process"
] | 1 | [
"PROFILE"
] | [
"PS51070"
] | [
"SHD"
] | [
2876
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC51070",
"R-CEL-8856825",
"R-CEL-8856828",
"R-DME-8856825",
"R-DME-8856828",
"R-HSA-8856825",
"R-HSA-8856828",
"R-MMU-8856825",
"R-MMU-8856828",
"R-RNO-8856825",
"R-RNO-8856828"
] | [
"PROSITEDOC:PDOC51070",
"REACTOME:R-CEL-8856825",
"REACTOME:R-CEL-8856828",
"REACTOME:R-DME-8856825",
"REACTOME:R-DME-8856828",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-MMU-8856825",
"REACTOME:R-MMU-8856828",
"REACTOME:R-RNO-8856825",
"REACTOME:R-RNO-8856828"
] | 11 | [] | 0 | [
"PUB00016632",
"PUB00016661"
] | [
"11381094",
"14726597"
] | [
"Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery.",
"Functional dissection of the interactions of stonin 2 with the adaptor complex AP-2 and synaptotagmin."
] | [
2001,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
6,
2870
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
4,
3,
14,
4,
7
] | 6 | true | Domain | Stonin homology | Stonin homology | SHD_dom | 4 |
IPR012321 | 12,321 | Conotoxin, omega-type, conserved site | Conotoxin_omega-typ_CS | Conserved_site | 190 | false | false | Cone snail toxins, conotoxins, are small neurotoxic peptides with disulphide connectivity that target ion-channels or G-protein coupled receptors. Based on the number and pattern of disulphide bonds and biological activities, conotoxins can be classified into several families [ ]. Omega, delta and kappa families of con... | [
"GO:0008200",
"GO:0005576"
] | [
"ion channel inhibitor activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS60004"
] | [
"OMEGA_CONOTOXIN"
] | [
190
] | 1 | [
"PROSITEDOC"
] | [
"PDOC60004"
] | [
"PROSITEDOC:PDOC60004"
] | 1 | [
"1cnn",
"1dw4",
"1dw5",
"1f3k",
"1feo",
"1fyg",
"1mvi",
"1mvj",
"1omc",
"1omg",
"1omn",
"1tr6",
"1tt3",
"1ttk",
"1ttl",
"2cco",
"2km9",
"5znu",
"6ceg",
"7mix",
"7vfu",
"8x91"
] | 22 | [
"PUB00016617",
"PUB00016620",
"PUB00016622",
"PUB00016662"
] | [
"11478951",
"15225557",
"10988292",
"10903392"
] | [
"Cone venom--from accidental stings to deliberate injection.",
"Toxins in anti-nociception and anti-inflammation.",
"lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus.",
"Conotoxins - new vistas for... | [
2001,
2004,
2000,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Polyangia",
"Protostomia"
] | [
2,
188
] | 2 | [] | [] | 0 | true | Conserved_site | Conotoxin, omega-type, conserved site | Conotoxin, omega-type, conserved site | Conotoxin_omega-typ_CS | 8 |
IPR012322 | 12,322 | Conotoxin, delta-type, conserved site | Conotoxin_d-typ_CS | Conserved_site | 35 | false | false | null | [
"GO:0019871",
"GO:0005576"
] | [
"sodium channel inhibitor activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS60005"
] | [
"DELTA_CONOTOXIN"
] | [
35
] | 1 | [
"PROSITEDOC"
] | [
"PDOC60004"
] | [
"PROSITEDOC:PDOC60004"
] | 1 | [
"1fu3",
"1g1p",
"1g1z",
"1yz2"
] | 4 | [
"PUB00016617",
"PUB00016620",
"PUB00016622",
"PUB00016662"
] | [
"11478951",
"15225557",
"10988292",
"10903392"
] | [
"Cone venom--from accidental stings to deliberate injection.",
"Toxins in anti-nociception and anti-inflammation.",
"lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus.",
"Conotoxins - new vistas for... | [
2001,
2004,
2000,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Conus"
] | [
35
] | 1 | [] | [] | 0 | true | Conserved_site | Conotoxin, delta-type, conserved site | Conotoxin, delta-type, conserved site | Conotoxin_d-typ_CS | 7 |
IPR012323 | 12,323 | Cyclotide, bracelet, conserved site | Cyclotide_bracelet_CS | Conserved_site | 238 | false | false | Cyclotides (cyclo peptides) are plant peptides of ~30 amino acids with a head to-tail cyclic backbone and six cysteine residues involved in three disulphide bonds. The cyclotides are extremely resistant to proteolysis and are remarkably stable. Cyclotides display a diverse range of biological activities, including uter... | [
"GO:0006952"
] | [
"defense response"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS60008"
] | [
"CYCLOTIDE_BRACELET"
] | [
238
] | 1 | [
"PROSITEDOC"
] | [
"PDOC51052"
] | [
"PROSITEDOC:PDOC51052"
] | 1 | [
"1bh4",
"1nbj",
"1vb8",
"1za8",
"2eri",
"2kcg",
"2knm",
"2kux",
"7kpd",
"7rih",
"7rmq",
"7rn3",
"7s55"
] | 13 | [
"PUB00008429",
"PUB00016616",
"PUB00016663",
"PUB00016667",
"PUB00080270"
] | [
"10600388",
"12946412",
"12482868",
"12482862",
"21596752"
] | [
"Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.",
"Primary and 3-D modelled structures of two cyclotides from Viola odorata.",
"Twists, knots, and rings in proteins. Structural definition of the cyclotide framework.",
"Disulfide folding ... | [
1999,
2003,
2003,
2003,
2011
] | 5 | [] | [] | 0 | 0 | null | [
"Mesangiospermae"
] | [
238
] | 1 | [
"Zea mays"
] | [
1
] | 1 | true | Conserved_site | Cyclotide, bracelet, conserved site | Cyclotide, bracelet, conserved site | Cyclotide_bracelet_CS | 4 |
IPR012324 | 12,324 | Cyclotide, moebius, conserved site | Cyclotide_moebius_CS | Conserved_site | 102 | false | false | Cyclotides (cyclo peptides) are plant peptides of ~30 amino acids with a head to-tail cyclic backbone and six cysteine residues involved in three disulphide bonds. The cyclotides are extremely resistant to proteolysis and are remarkably stable. Cyclotides display a diverse range of biological activities, including uter... | [
"GO:0006952"
] | [
"defense response"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS60009"
] | [
"CYCLOTIDE_MOEBIUS"
] | [
102
] | 1 | [
"PROSITEDOC"
] | [
"PDOC51052"
] | [
"PROSITEDOC:PDOC51052"
] | 1 | [
"1jjz",
"1k48",
"1kal",
"1nb1",
"1orx",
"1pt4",
"1yp8",
"1znu",
"2f2i",
"2f2j",
"2jue",
"2jwm",
"2k7g",
"2kch",
"2khb",
"2kuk",
"2lam",
"2lur",
"2m9o",
"2mh1",
"2mn1",
"2mw0",
"3e4h",
"4ttm",
"4ttn",
"4tto",
"7k7x",
"7lhc",
"7rfa",
"8tyi"
] | 30 | [
"PUB00008429",
"PUB00016616",
"PUB00016663",
"PUB00016667",
"PUB00080270"
] | [
"10600388",
"12946412",
"12482868",
"12482862",
"21596752"
] | [
"Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.",
"Primary and 3-D modelled structures of two cyclotides from Viola odorata.",
"Twists, knots, and rings in proteins. Structural definition of the cyclotide framework.",
"Disulfide folding ... | [
1999,
2003,
2003,
2003,
2011
] | 5 | [] | [] | 0 | 0 | null | [
"Mesangiospermae"
] | [
102
] | 1 | [] | [] | 0 | true | Conserved_site | Cyclotide, moebius, conserved site | Cyclotide, moebius, conserved site | Cyclotide_moebius_CS | 3 |
IPR012325 | 12,325 | Assassin bug toxin-like | Assassin_bug_toxin-like | Family | 13 | false | false | Assassin bugs (Arthropoda:Insecta:Hemiptera:Reduviidae), sometimes known as conenose or kissing bugs, are one of the largest and morphologically diverse families of true bugs feeding on crickets, caterpillars and other insects. Some assassin bug species are bloodsucking parasites of mammals, even of human. They can be ... | [
"GO:0019855",
"GO:0005576"
] | [
"calcium channel inhibitor activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PROSITE"
] | [
"PF08117",
"PS60010"
] | [
"Toxin_30",
"ASSASSIN_BUG_TOXIN"
] | [
13,
7
] | 2 | [
"PROSITEDOC"
] | [
"PDOC60010"
] | [
"PROSITEDOC:PDOC60010"
] | 1 | [
"1i26",
"1lmr"
] | 2 | [
"PUB00016409",
"PUB00016615",
"PUB00099566"
] | [
"11669615",
"11423127",
"33893140"
] | [
"Solution structure of Ptu1, a toxin from the assassin bug Peirates turpis that blocks the voltage-sensitive calcium channel N-type.",
"Novel peptides from assassin bugs (Hemiptera: Reduviidae): isolation, chemical and biological characterization.",
"Production, composition, and mode of action of the painful de... | [
2001,
2001,
2021
] | 3 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
13
] | 1 | [] | [] | 0 | true | Family | Assassin bug toxin-like | Assassin bug toxin-like | Assassin_bug_toxin-like | 1 |
IPR012327 | 12,327 | D12 class N6 adenine-specific DNA methyltransferase | MeTrfase_D12 | Family | 19,619 | false | false | In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. There are 2 major classes of DNA methyltransferase that differ in the nature of the modifications they effect. The members of one class (C-MTases) methylate a ring carbon and form C5-methylcytosine (see ... | [
"GO:0009007",
"GO:0009307"
] | [
"site-specific DNA-methyltransferase (adenine-specific) activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"PF02086",
"PR00505",
"PTHR30481",
"TIGR00571"
] | [
"MethyltransfD12",
"D12N6MTFRASE",
"",
"dam"
] | [
19132,
16548,
16450,
9218
] | 4 | [
"EC"
] | [
"2.1.1.72"
] | [
"EC:2.1.1.72"
] | 1 | [
"1q0s",
"1q0t",
"1yf3",
"1yfj",
"1yfl",
"2dpm",
"2g1p",
"2ore",
"4gbe",
"4gol",
"4gom",
"4gon",
"4goo",
"4rtj",
"4rtk",
"4rtl",
"4rtm",
"4rtn",
"4rto",
"4rtp",
"4rtq",
"4rtr",
"4rts",
"7m6b"
] | 24 | [
"PUB00000092",
"PUB00001770",
"PUB00001857",
"PUB00003225",
"PUB00003245",
"PUB00004831"
] | [
"7663118",
"3248728",
"7607512",
"3323532",
"2541254",
"7971991"
] | [
"Structure and function of DNA methyltransferases.",
"The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases.",
"Sequence motifs characteristic for DNA [cytosine-N4] ... | [
1995,
1988,
1995,
1987,
1989,
1994
] | 6 | [] | [
"IPR012186",
"IPR012263"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
479,
17688,
100,
3,
792,
557
] | 6 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | D12 class N6 adenine-specific DNA methyltransferase | D12 class N6 adenine-specific DNA methyltransferase | MeTrfase_D12 | 5 |
IPR012328 | 12,328 | Chalcone/stilbene synthase, C-terminal | Chalcone/stilbene_synt_C | Domain | 19,430 | false | false | Chalcone synthases (CHS) ( ) and stilbene synthases (STS) (formerly known as resveratrol synthases) are related plant enzymes. CHS is an important enzyme in flavanoid biosynthesis and STS is a key enzyme in stilbene-type phyloalexin biosynthesis. Both enzymes catalyse the addition of three molecules of malonyl-CoA to a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02797"
] | [
"Chal_sti_synt_C"
] | [
19430
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME"
] | [
"2.3.1",
"2.3.1.74",
"PWY-5135",
"PWY-6316",
"PWY-6515",
"PWY-6787",
"PWY-7397",
"PWY-7897",
"R-DDI-199220",
"R-DDI-75105"
] | [
"EC:2.3.1",
"EC:2.3.1.74",
"METACYC:PWY-5135",
"METACYC:PWY-6316",
"METACYC:PWY-6515",
"METACYC:PWY-6787",
"METACYC:PWY-7397",
"METACYC:PWY-7897",
"REACTOME:R-DDI-199220",
"REACTOME:R-DDI-75105"
] | 10 | [
"1bi5",
"1bq6",
"1cgk",
"1cgz",
"1chw",
"1cml",
"1d6f",
"1d6h",
"1d6i",
"1ee0",
"1i86",
"1i88",
"1i89",
"1i8b",
"1jwx",
"1qlv",
"1ted",
"1tee",
"1u0m",
"1u0u",
"1u0v",
"1u0w",
"1xes",
"1xet",
"1z1e",
"1z1f",
"2d3m",
"2d51",
"2d52",
"2h84",
"2p0u",
"3a5q"... | 133 | [
"PUB00002705",
"PUB00014376",
"PUB00072442",
"PUB00095149"
] | [
"2033084",
"10426957",
"2184816",
"21909286"
] | [
"The role of cysteines in polyketide synthases. Site-directed mutagenesis of resveratrol and chalcone synthases, two key enzymes in different plant-specific pathways.",
"Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis.",
"Stilbene and chalcone synthases: related enzymes w... | [
1991,
1999,
1990,
2011
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Marine Group I thaumarchaeote",
"Yasminevirus sp. GU-2018",
"unclassified sequences"
] | [
8030,
11359,
1,
1,
39
] | 5 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
53,
1,
76,
60
] | 4 | true | Domain | Chalcone/stilbene synthase, C-terminal | Chalcone/stilbene synthase, C-terminal | Chalcone/stilbene_synt_C | 4 |
IPR012331 | 12,331 | Clathrin, heavy chain, linker | Clathrin_H-chain_linker | Homologous_superfamily | 1,959 | false | false | Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.25.40.30"
] | [
""
] | [
1959
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000964",
"PUB00035753",
"PUB00035765",
"PUB00035769",
"PUB00035906",
"PUB00035907",
"PUB00035908",
"PUB00035909"
] | [
"9827808",
"17449236",
"11598180",
"15261670",
"15752139",
"16806884",
"16734666",
"16699812"
] | [
"Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker.",
"Do different endocytic pathways make different synaptic vesicles?",
"Adaptins: the final recount.",
"COP and clathrin-coated vesicle budding: different pathways, common approaches.",
"New faces of the familiar c... | [
1998,
2007,
2001,
2004,
2005,
2006,
2006,
2006
] | 8 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1959
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
5,
2,
1,
5,
18
] | 5 | true | Homologous_superfamily | Clathrin, heavy chain, linker | Clathrin, heavy chain, linker | Clathrin_H-chain_linker | 6 |
IPR012332 | 12,332 | Autotransporter, pectate lyase C-like domain superfamily | Autotransporter_pectin_lyase_C | Homologous_superfamily | 25,379 | false | false | Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type V pathway was first described for the IgA1 protease [ ]. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the protein... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.160.20.20"
] | [
""
] | [
25379
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-9760173",
"R-HSA-9927020"
] | [
"REACTOME:R-HSA-9760173",
"REACTOME:R-HSA-9927020"
] | 2 | [
"1clw",
"1dab",
"1qa1",
"1qa2",
"1qa3",
"1qq1",
"1qrb",
"1qrc",
"1tsp",
"1tyu",
"1tyv",
"1tyw",
"1tyx",
"1wxr",
"2iou",
"2v5i",
"2vfm",
"2vfn",
"2vfo",
"2vfp",
"2vfq",
"2xc1",
"3ak5",
"3h09",
"3ml3",
"3riq",
"3syj",
"3sze",
"3th0",
"4kh3",
"4mee",
"4om9"... | 59 | [
"PUB00008434",
"PUB00019185",
"PUB00061585"
] | [
"3027577",
"15014442",
"20060837"
] | [
"Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease.",
"Structure of the translocator domain of a bacterial autotransporter.",
"Crystal structure of a full-length autotransporter."
] | [
1987,
2004,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
158,
24172,
734,
238,
77
] | 5 | [
"Escherichia coli (strain K12)"
] | [
9
] | 1 | true | Homologous_superfamily | Autotransporter, pectate lyase C-like domain superfamily | Autotransporter, pectate lyase C-like domain superfamily | Autotransporter_pectin_lyase_C | 5 |
IPR012334 | 12,334 | Pectin lyase fold | Pectin_lyas_fold | Homologous_superfamily | 263,586 | false | false | This entry covers proteins that are closely related to the pectolytic enzyme, pectin lyase, which act as virulence factors. These proteins include pectate lyase, iota-carrageenase, and glycoside hydrolases from family 28 (such as galacturonases). Pectin lyases, pectate lyases and galacturonases all act on forms of pect... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.160.20.10"
] | [
""
] | [
263586
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-8951664",
"R-CEL-983168",
"R-DDI-418594",
"R-DDI-420499",
"R-DDI-977444",
"R-HSA-8951664",
"R-HSA-983168",
"R-MMU-8951664",
"R-MMU-983168",
"R-RNO-8951664",
"R-RNO-983168"
] | [
"REACTOME:R-CEL-8951664",
"REACTOME:R-CEL-983168",
"REACTOME:R-DDI-418594",
"REACTOME:R-DDI-420499",
"REACTOME:R-DDI-977444",
"REACTOME:R-HSA-8951664",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-8951664",
"REACTOME:R-MMU-983168",
"REACTOME:R-RNO-8951664",
"REACTOME:R-RNO-983168"
] | 11 | [
"1air",
"1bhe",
"1bn8",
"1czf",
"1dbg",
"1dbo",
"1ee6",
"1gq8",
"1h80",
"1hg8",
"1ia5",
"1ib4",
"1idj",
"1idk",
"1jrg",
"1jta",
"1k5c",
"1kcc",
"1kcd",
"1ktw",
"1nhc",
"1o88",
"1o8d",
"1o8e",
"1o8f",
"1o8g",
"1o8h",
"1o8i",
"1o8j",
"1o8k",
"1o8l",
"1o8m"... | 326 | [
"PUB00014172",
"PUB00016281",
"PUB00016282",
"PUB00016283"
] | [
"9195887",
"11518536",
"12324535",
"11493601"
] | [
"Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases.",
"The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturo... | [
1997,
2001,
2002,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5754,
122843,
130122,
1543,
3324
] | 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",... | [
780,
6,
16,
3,
2,
16,
15,
12,
330,
19,
1,
606
] | 12 | true | Homologous_superfamily | Pectin lyase fold | Pectin lyase fold | Pectin_lyas_fold | 7 |
IPR012336 | 12,336 | Thioredoxin-like fold | Thioredoxin-like_fold | Domain | 121,411 | false | false | Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2), where a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system, the NADP/thioredoxin system, and the glutathione/glutare... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM"
] | [
"PF13098",
"PF13192",
"PF13462",
"PF13899",
"PF13905",
"PF17172"
] | [
"Thioredoxin_2",
"Thioredoxin_3",
"Thioredoxin_4",
"Thioredoxin_7",
"Thioredoxin_8",
"GST_N_4"
] | [
27886,
14697,
31638,
22144,
18122,
7028
] | 6 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-114608",
"R-DDI-8951664",
"R-DDI-9755511",
"R-HSA-114608",
"R-HSA-8951664",
"R-HSA-9755511",
"R-MMU-114608",
"R-MMU-8951664",
"R-MMU-9755511",
"R-SCE-8951664",
"R-SCE-9755511",
"R-SPO-8951664",
"R-SPO-9755511"
] | [
"REACTOME:R-BTA-114608",
"REACTOME:R-DDI-8951664",
"REACTOME:R-DDI-9755511",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-8951664",
"REACTOME:R-HSA-9755511",
"REACTOME:R-MMU-114608",
"REACTOME:R-MMU-8951664",
"REACTOME:R-MMU-9755511",
"REACTOME:R-SCE-8951664",
"REACTOME:R-SCE-9755511",
"REACTOME:R... | 13 | [
"1a8l",
"1eej",
"1ewx",
"1ezk",
"1fg4",
"1fo5",
"1g0t",
"1hyu",
"1i5g",
"1ilo",
"1j08",
"1jzd",
"1jzo",
"1nho",
"1o6j",
"1o73",
"1o7u",
"1o81",
"1o85",
"1o8w",
"1o8x",
"1oc8",
"1oc9",
"1okd",
"1qk8",
"1sen",
"1t3b",
"1tjd",
"1uc7",
"1v57",
"1v58",
"1vrs"... | 146 | [
"PUB00016292"
] | [
"15862094"
] | [
"Redox regulation: a broadening horizon."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2052,
91854,
25905,
91,
1509
] | 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",... | [
49,
29,
13,
21,
4,
26,
14,
3,
33,
31,
1,
2,
65
] | 13 | true | Domain | Thioredoxin-like fold | Thioredoxin-like fold | Thioredoxin-like_fold | 8 |
IPR012337 | 12,337 | Ribonuclease H-like superfamily | RNaseH-like_sf | Homologous_superfamily | 1,297,464 | false | false | The catalytic domain of several polynucleotidyl transferases share a similar structure, consisting of a 3-layer α/β/α fold that contains mixed β-sheets, suggesting that they share a similar mechanism of catalysis. Polynucleotidyl transferases containing this domain include ribonuclease H class I (RNase HI) and class II... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF53098"
] | [
""
] | [
1297464
] | 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-429947",
"R-BTA-6791226",
"R-BTA-6804115",
"R-CEL-110314",
"R-CEL-112382",
"R-CEL-203927",
"R-CEL-426486",
"R-CEL-5578749",
"R-CEL-5651801",
"R-CEL-5656169",
"R-CEL-5696397",
"R-CEL-5696400",
"R-CEL-674695",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-6791226",
"R-CEL-69091",
"... | [
"REACTOME:R-BTA-429947",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-6804115",
"REACTOME:R-CEL-110314",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-203927",
"REACTOME:R-CEL-426486",
"REACTOME:R-CEL-5578749",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-5656169",
"REACTOME:R-CEL-5696397",
"REACTOME:R-C... | 289 | [
"1a5v",
"1a5w",
"1a5x",
"1asu",
"1asv",
"1asw",
"1b7e",
"1b92",
"1b9d",
"1b9f",
"1bcm",
"1bco",
"1bgx",
"1bhl",
"1bi4",
"1bis",
"1biu",
"1biz",
"1bl3",
"1bqm",
"1bqn",
"1c0m",
"1c0t",
"1c0u",
"1c1a",
"1c1b",
"1c1c",
"1c6v",
"1clq",
"1cxq",
"1cxu",
"1cz9"... | 2,862 | [
"PUB00009701",
"PUB00016296",
"PUB00016297",
"PUB00016298",
"PUB00029612"
] | [
"10982859",
"15299518",
"8696976",
"12823554",
"14512736"
] | [
"SURVEY AND SUMMARY: holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories.",
"Crystallographic analyses of an active HIV-1 ribonuclease H domain show structural features that distinguish it from the inactive form.",
"Retroviral i... | [
2000,
1993,
1996,
2003,
2003
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"other sequences",
"unclassified sequences"
] | [
8471,
480361,
715121,
81561,
25,
11925
] | 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",... | [
1052,
101,
428,
166,
49,
296,
215,
32,
3447,
224,
70,
34,
1225
] | 13 | true | Homologous_superfamily | Ribonuclease H-like superfamily | Ribonuclease H-like superfamily | RNaseH-like_sf | 5 |
IPR012338 | 12,338 | Beta-lactamase/transpeptidase-like | Beta-lactam/transpept-like | Homologous_superfamily | 435,282 | false | false | This superfamily represents a beta-lactamase structural motif, which contains a cluster of α-helices and an α/β sandwich. In addition to beta-lactamases, this domain is also found in D-ala carboxypeptidase/transpeptidase, esterase (EstB) [ ], the penicillin receptor BlaR (C-terminal domain), D-aminopeptidase (N-termina... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.40.710.10",
"SSF56601"
] | [
"",
""
] | [
433500,
434359
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-210500",
"R-CEL-5628897",
"R-CEL-8964539",
"R-HSA-210500",
"R-HSA-5628897",
"R-HSA-8964539",
"R-HSA-9638771",
"R-HSA-9913143",
"R-MMU-210500",
"R-MMU-5628897",
"R-MMU-8964539",
"R-RNO-210500",
"R-RNO-5628897",
"R-RNO-8964539"
] | [
"REACTOME:R-CEL-210500",
"REACTOME:R-CEL-5628897",
"REACTOME:R-CEL-8964539",
"REACTOME:R-HSA-210500",
"REACTOME:R-HSA-5628897",
"REACTOME:R-HSA-8964539",
"REACTOME:R-HSA-9638771",
"REACTOME:R-HSA-9913143",
"REACTOME:R-MMU-210500",
"REACTOME:R-MMU-5628897",
"REACTOME:R-MMU-8964539",
"REACTOME:R... | 14 | [
"1alq",
"1axb",
"1blc",
"1blh",
"1blp",
"1bls",
"1bsg",
"1bt5",
"1btl",
"1bue",
"1bul",
"1bza",
"1c3b",
"1cef",
"1ceg",
"1ci8",
"1ci9",
"1ck3",
"1dja",
"1djb",
"1djc",
"1dy6",
"1e25",
"1e3u",
"1e4d",
"1ei5",
"1erm",
"1ero",
"1erq",
"1es2",
"1es3",
"1es4"... | 1,922 | [
"PUB00013322",
"PUB00016300",
"PUB00016301"
] | [
"10986464",
"12945052",
"11847270"
] | [
"Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family.",
"Understanding the acylation mechanisms of active-site serine penicillin-recognizing proteins: a molecular dynamics simulation study.",
"EstB from Burkholderia gladioli: a novel est... | [
2000,
2003,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"other sequences",
"unclassified sequences"
] | [
670,
396772,
31600,
340,
11,
5889
] | 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",... | [
9,
23,
33,
12,
16,
23,
16,
6,
4,
25,
11
] | 11 | true | Homologous_superfamily | Beta-lactamase/transpeptidase-like | Beta-lactamase/transpeptidase-like | Beta-lactam/transpept-like | 5 |
IPR012339 | 12,339 | Bacteriophage T4, Gp32, single-stranded DNA-binding domain | Phage_T4_Gp32_ssDNA-bd | Domain | 859 | false | false | This entry represents the Bacteriophage T4, Gp32, single-stranded DNA-binding domain. The characteristics of the protein distribution suggest prophage matches in addition to the phage matches. Single-stranded DNA-binding protein (also known as Gp32 or SSB) is essential for bacteriophage T4 DNA replication, recombinatio... | [
"GO:0003697"
] | [
"single-stranded DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08804"
] | [
"gp32"
] | [
859
] | 1 | [] | [] | [] | 0 | [
"1gpc",
"2a1k",
"2atq",
"8gme"
] | 4 | [
"PUB00016302",
"PUB00100562",
"PUB00100567",
"PUB00100568"
] | [
"7630406",
"9079662",
"14871889",
"11459967"
] | [
"Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA.",
"Role of the bacteriophage T7 and T4 single-stranded DNA-binding proteins in the formation of joint molecules and DNA helicase-catalyzed polar branch migration.",
"Dual functions of single-stranded DNA-bin... | [
1995,
1997,
2004,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Viruses",
"Wuchereria bancrofti",
"metagenomes"
] | [
3,
138,
651,
1,
66
] | 5 | [] | [] | 0 | true | Domain | Bacteriophage T4, Gp32, single-stranded DNA-binding domain | Bacteriophage T4, Gp32, single-stranded DNA-binding domain | Phage_T4_Gp32_ssDNA-bd | 7 |
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