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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR005994 | 5,994 | Guanosine monophosphate reductase, type2 | GuaC_type_2 | Family | 2,772 | false | false | Guanosine monophosphate reductase ( ) catalyses the irreversible and NADPH-dependent reductive deamination of GMP into IMP. NADPH + guanosine 5-phosphate = NADP+ + inosine 5-phosphate + NH3 It converts nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and maintains intracellular balance of A and ... | [
"GO:0003920",
"GO:0006163",
"GO:1902560"
] | [
"GMP reductase activity",
"purine nucleotide metabolic process",
"GMP reductase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM",
"PIRSF",
"NCBIFAM"
] | [
"MF_01511",
"NF003966",
"PIRSF036500",
"TIGR01306"
] | [
"GMP_reduct_type2",
"PRK05458.1",
"GMP_red_Firmic",
"GMP_reduct_2"
] | [
2737,
2772,
2751,
2689
] | 4 | [
"EC"
] | [
"1.7.1.7"
] | [
"EC:1.7.1.7"
] | 1 | [
"1ypf",
"2a1y"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
2743,
2,
17,
10
] | 4 | [] | [] | 0 | true | Family | Guanosine monophosphate reductase, type2 | Guanosine monophosphate reductase, type2 | GuaC_type_2 | 5 |
IPR005995 | 5,995 | Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent | Pgm_bpd_ind | Family | 19,842 | false | false | This 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM) is a metalloenzyme found particularly in eubacteria and higher plants. It is distantly related to archaeal iPGAM ( ) and distinct from the unrelated cofactor-dependent PGAM. Activity has been demonstrated for proteins from a variety of organisms, ... | [
"GO:0004619",
"GO:0006007"
] | [
"phosphoglycerate mutase activity",
"glucose catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PIRSF",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_01038",
"PIRSF001492",
"PTHR31637",
"TIGR01307",
"cd16010"
] | [
"GpmI",
"IPGAM",
"",
"pgm_bpd_ind",
"iPGM"
] | [
16549,
17938,
19839,
18293,
18412
] | 5 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.4.2.12",
"GenProp0691",
"GenProp1306",
"GenProp1344",
"GenProp1407",
"PWY-1042",
"PWY-2221",
"PWY-5484",
"PWY-5723",
"PWY-6142",
"PWY-6886",
"PWY-6901",
"PWY-7003",
"PWY-7124",
"PWY-7218",
"PWY-8362",
"PWY-8404"
] | [
"EC:5.4.2.12",
"GP:GenProp0691",
"GP:GenProp1306",
"GP:GenProp1344",
"GP:GenProp1407",
"METACYC:PWY-1042",
"METACYC:PWY-2221",
"METACYC:PWY-5484",
"METACYC:PWY-5723",
"METACYC:PWY-6142",
"METACYC:PWY-6886",
"METACYC:PWY-6901",
"METACYC:PWY-7003",
"METACYC:PWY-7124",
"METACYC:PWY-7218",
... | 17 | [
"1ejj",
"1eqj",
"1o98",
"1o99",
"2ify",
"3igy",
"3igz",
"3nvl",
"4my4",
"4nwj",
"4nwx",
"4qax",
"5kgl",
"5kgm",
"5kgn",
"5vpu",
"7knf",
"7kng",
"7tl7",
"7tl8"
] | 20 | [
"PUB00002717",
"PUB00014365",
"PUB00014367",
"PUB00014371",
"PUB00014401",
"PUB00014404",
"PUB00014416"
] | [
"1535626",
"10764795",
"8021172",
"8260624",
"10691985",
"10388626",
"7896694"
] | [
"Cloning and sequencing of a cDNA encoding 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from maize. Possible relationship to the alkaline phosphatase family.",
"Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the comp... | [
1992,
2000,
1994,
1993,
2000,
1999,
1995
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Hyperionvirus sp.",
"unclassified sequences"
] | [
483,
15350,
3684,
1,
324
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
5,
1,
1,
1,
8,
35
] | 6 | true | Family | Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent | Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent | Pgm_bpd_ind | 8 |
IPR005996 | 5,996 | Large ribosomal subunit protein uL30, bacteria | Ribosomal_uL30_bact | Family | 24,368 | false | false | Ribosomal protein uL30 is one of the proteins from the large ribosomal subunit. uL30 belongs to a family of ribosomal proteins which, on the basis of sequence similarities, groups bacteria and archaea uL30, yeast mitochondrial uL33m, and Drosophila, slime mould, fungal and mammalian L7 ribosomal proteins [ ]. uL30 from... | [
"GO:0003735",
"GO:0006412",
"GO:0015934"
] | [
"structural constituent of ribosome",
"translation",
"large ribosomal subunit"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PIRSF",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_01371_B",
"PIRSF002211",
"PTHR15892",
"TIGR01308",
"cd01658"
] | [
"Ribosomal_uL30_B",
"Ribosomal_L30_bac-type",
"",
"rpmD_bact",
"Ribosomal_L30"
] | [
21239,
20126,
22243,
22662,
22953
] | 5 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383",
"R-RNO-5389840",
"R-RNO-5419276",
"R-RNO-9937383"
] | [
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9937383",
"REACTOME:R-MMU-5389840",
"REACTOME:R-MMU-5419276",
"REACTOME:R-MMU-9937383",
"REACTOME:R-RNO-5389840",
"REACTOME:R-RNO-5419276",
"REACTOME:R-RNO-9937383"
] | 10 | [
"1bxy",
"1ml5",
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"2j28",
"2rdo",
"2zjp",
"2zjq",
"2zjr",
"3bbx",
"3cf5",
"3dll",
"3iy9",
"3j3v",
"3j5l",
"3j6b",
"3j7y",
"3j7z",
"3j8g",
"3j9m",
"3j9w",
"3j9y",
"3j9z",
"3ja1"... | 1,212 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00080279"
] | [
"11297922",
"11290319",
"11114498",
"24524803"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"A new system for naming ribosomal proteins."
] | [
2001,
2001,
2000,
2014
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
20254,
3774,
340
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
3,
1,
1,
2,
1,
2,
2,
1,
5,
6,
1,
1,
8
] | 13 | true | Family | Large ribosomal subunit protein uL30, bacteria | Large ribosomal subunit protein uL30, bacteria | Ribosomal_uL30_bact | 1 |
IPR005997 | 5,997 | Large ribosomal subunit protein uL30, archaea | Ribosomal_uL30_arc | Family | 910 | false | false | Ribosomal protein uL30 is one of the proteins from the large ribosomal subunit. This model describes archaeal 50S ribosomal protein uL30. These proteins share similarity to the longer eukaryotic 60S ribosomal protein, previously known as L7, and to the much shorter (~60 residue) bacterial 50S ribosomal protein uL30. Ri... | [
"GO:0003735",
"GO:0006412",
"GO:0015934"
] | [
"structural constituent of ribosome",
"translation",
"large ribosomal subunit"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01371_A",
"TIGR01309"
] | [
"Ribosomal_uL30_A",
"uL30_arch"
] | [
910,
840
] | 2 | [] | [] | [] | 0 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 92 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [
"IPR039699"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Desulfofervidus auxilii",
"ecological metagenomes"
] | [
885,
1,
24
] | 3 | [] | [] | 0 | true | Family | Large ribosomal subunit protein uL30, archaea | Large ribosomal subunit protein uL30, archaea | Ribosomal_uL30_arc | 4 |
IPR005998 | 5,998 | Large ribosomal subunit protein uL30, eukaryota | Ribosomal_uL30_euk | Family | 7,152 | false | false | This entry represents the large ribosomal subunit protein uL30 found in eukaryotes that was previously know as L7. The eukaryotic ribosomal protein uL30 contains an N-terminal bZIP DNA binding domain and a second, DNA-binding domain has been mapped to the 50 C-terminal amino acids of the protein [ ]. In addition to its... | [
"GO:0003723"
] | [
"RNA binding"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR01310"
] | [
"uL30_euk"
] | [
7152
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",
"R-DDI-97595... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-9759... | 69 | [
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j79",
"3j7o",
"3j7p",
"3j7q",
"3j7r",
"3j92",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jan",
"3jbn",
"3jbo",
"3jbp",
"3jcs",
"3jct",
"4d5y",
"4d67",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q",
"4u4r",
"4u4u",
"4u4y",
"4u4z"... | 566 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00007923"
] | [
"11297922",
"11290319",
"11114498",
"10329420"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Human ribosomal protein L7 carries two nucleic acid-binding domains with distinct specificities."
] | [
2001,
2001,
2000,
1999
] | 4 | [
"IPR039699"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Kangiella spongicola"
] | [
7151,
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... | [
11,
1,
2,
4,
4,
7,
1,
10,
9,
2,
3,
13
] | 12 | true | Family | Large ribosomal subunit protein uL30, eukaryota | Large ribosomal subunit protein uL30, eukaryota | Ribosomal_uL30_euk | 4 |
IPR005999 | 5,999 | Glycerol kinase | Glycerol_kin | Family | 29,655 | false | false | Glycerol kinase ( ) is a bacterial sugar kinase which catalyses the Mg-ATP-dependent phosphorylation of glycerol to yield glycerol 3-phosphate. The enzyme from Escherichia coli is an allosteric regulatory enzyme whose activity is inhibited by fructose 1,6-bisphosphate (FBP) and the glucose-specific phosphocarrier of th... | [
"GO:0004370",
"GO:0006072"
] | [
"glycerol kinase activity",
"glycerol-3-phosphate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00186",
"TIGR01311"
] | [
"Glycerol_kin",
"glycerol_kin"
] | [
21777,
29648
] | 2 | [
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.30",
"GenProp1567",
"PWY-4261",
"R-BTA-75109",
"R-CEL-75109",
"R-HSA-75109",
"R-MMU-75109",
"R-RNO-75109",
"R-SCE-75109"
] | [
"EC:2.7.1.30",
"GP:GenProp1567",
"METACYC:PWY-4261",
"REACTOME:R-BTA-75109",
"REACTOME:R-CEL-75109",
"REACTOME:R-HSA-75109",
"REACTOME:R-MMU-75109",
"REACTOME:R-RNO-75109",
"REACTOME:R-SCE-75109"
] | 9 | [
"1bo5",
"1bot",
"1bu6",
"1bwf",
"1gla",
"1glb",
"1glc",
"1gld",
"1gle",
"1glf",
"1glj",
"1gll",
"1r59",
"1xup",
"2d4w",
"2dpn",
"2w40",
"2w41",
"2zf5",
"3d7e",
"3ezw",
"3flc",
"3g25",
"3ge1",
"3h3n",
"3h3o",
"3h45",
"3h46",
"3wxi",
"3wxj",
"3wxk",
"3wxl"... | 53 | [
"PUB00007924"
] | [
"10364471"
] | [
"X-Ray structure of glycerol kinase complexed with an ATP analog implies a novel mechanism for the ATP-dependent glycerol phosphorylation by glycerol kinase."
] | [
1999
] | 1 | [
"IPR000577"
] | [
"IPR042018"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
423,
22566,
6432,
234
] | 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",... | [
3,
1,
13,
5,
1,
6,
9,
1,
3,
14,
1,
2
] | 12 | true | Family | Glycerol kinase | Glycerol kinase | Glycerol_kin | 4 |
IPR006000 | 6,000 | Xylulokinase | Xylulokinase | Family | 13,531 | false | false | The ability to metabolise xylose, one of the most abundant sugars in nature, is dependent on its conversion to xylulose-5-phosphate, which then enters the non-oxidative pentose phosphate pathway [ ]. Xylulose-5-phosphate is produced from xylose by the sequential action of two enzymes; xylose isomerase, which converts x... | [
"GO:0004856",
"GO:0005997"
] | [
"D-xylulokinase activity",
"xylulose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_02220",
"TIGR01312"
] | [
"XylB",
"XylB"
] | [
12260,
12734
] | 2 | [
"EC",
"GP"
] | [
"2.7.1.17",
"GenProp1656"
] | [
"EC:2.7.1.17",
"GP:GenProp1656"
] | 2 | [
"2itm",
"2nlx",
"3i8b",
"5vm1"
] | 4 | [
"PUB00034670",
"PUB00034671"
] | [
"17123542",
"11168365"
] | [
"Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli.",
"Phosphorylation of 1-deoxy-D-xylulose by D-xylulokinase of Escherichia coli."
] | [
2007,
2001
] | 2 | [
"IPR000577"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
9,
13295,
102,
125
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Xylulokinase | Xylulokinase | Xylulokinase | 1 |
IPR006001 | 6,001 | Carbohydrate kinase, thermoresistant glucokinase | Therm_gnt_kin | Family | 16,646 | false | false | This family of proteins includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to glu... | [
"GO:0016301",
"GO:0005975"
] | [
"kinase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"PTHR43442",
"TIGR01313",
"cd02021"
] | [
"",
"therm_gnt_kin",
"GntK"
] | [
15654,
15359,
16434
] | 3 | [
"EC",
"GP",
"METACYC"
] | [
"2.7.1.12",
"GenProp1228",
"PWY-5530"
] | [
"EC:2.7.1.12",
"GP:GenProp1228",
"METACYC:PWY-5530"
] | 3 | [
"1knq",
"1ko1",
"1ko4",
"1ko5",
"1ko8",
"1kof",
"2bdt",
"3t61",
"4eun"
] | 9 | [
"PUB00007925",
"PUB00076697",
"PUB00080681"
] | [
"12054802",
"11468405",
"8925917"
] | [
"Conformational changes during the catalytic cycle of gluconate kinase as revealed by X-ray crystallography.",
"Crystallization and preliminary X-ray crystallographic studies of recombinant thermoresistant gluconate kinase GntK from Escherichia coli.",
"Purification and characterization of the Escherichia coli ... | [
2002,
2001,
1996
] | 3 | [
"IPR031322"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
12159,
4439,
48
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 2045... | [
9,
1,
2,
3,
3,
2,
3,
8,
1,
1,
3
] | 11 | true | Family | Carbohydrate kinase, thermoresistant glucokinase | Carbohydrate kinase, thermoresistant glucokinase | Therm_gnt_kin | 9 |
IPR006002 | 6,002 | Gluconate kinase | Gluconate_kinase | Family | 2,000 | false | false | Gluconate kinase ( ) has an α/β structure consisting of a twisted parallel β-sheet surrounded by α-helices with overall topology similar to nucleoside monophosphate (NMP) kinases, such as adenylate kinase. Significant conformational changes are induced upon binding of ATP to the enzyme. The largest changes involve a hi... | [
"GO:0046316",
"GO:0019521"
] | [
"gluconokinase activity",
"D-gluconate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01314"
] | [
"gntK_FGGY"
] | [
2000
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007925"
] | [
"12054802"
] | [
"Conformational changes during the catalytic cycle of gluconate kinase as revealed by X-ray crystallography."
] | [
2002
] | 1 | [
"IPR000577"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
1998,
2
] | 2 | [
"Arabidopsis thaliana"
] | [
1
] | 1 | true | Family | Gluconate kinase | Gluconate kinase | Gluconate_kinase | 6 |
IPR006003 | 6,003 | FGGY carbohydrate kinase, pentulose kinase | FGGY_RbtK-like | Family | 6,548 | false | false | This entry represents a subfamily of the FGGY family of carbohydrate kinases, including FGGY carbohydrate kinase domain-containing proteins from mammals and D-ribulokinase YDR109C from S. cerevisiae, which catalyse ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate [ ]. These proteins may... | [
"GO:0016773",
"GO:0005975"
] | [
"phosphotransferase activity, alcohol group as acceptor",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM",
"CDD"
] | [
"TIGR01315",
"cd07782"
] | [
"5C_CHO_kinase",
"ASKHA_NBD_FGGY_D-RBK"
] | [
6342,
6463
] | 2 | [
"EC",
"METACYC"
] | [
"2.7.1.47",
"PWY-8334"
] | [
"EC:2.7.1.47",
"METACYC:PWY-8334"
] | 2 | [
"3gg4",
"3l0q"
] | 2 | [
"PUB00007926",
"PUB00099623"
] | [
"9639934",
"27909055"
] | [
"Genes for D-arabinitol and ribitol catabolism from Klebsiella pneumoniae.",
"Molecular Identification of d-Ribulokinase in Budding Yeast and Mammals."
] | [
1998,
2017
] | 2 | [
"IPR000577"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2154,
4391,
3
] | 3 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
12,
7,
2,
4,
3,
2,
2,
8,
1,
2
] | 10 | true | Family | FGGY carbohydrate kinase, pentulose kinase | FGGY carbohydrate kinase, pentulose kinase | FGGY_RbtK-like | 8 |
IPR006004 | 6,004 | Sulfide dehydrogenase subunit alpha-like | SudA-like | Family | 3,355 | false | false | This entry represents a group of prokaryotic dehydrogenases with a FAD/NAD(P)-binding domain, including Sulfide dehydrogenase subunit alpha (SudA) and Oxidoreductase ( ) from Pyrococcus furiosus. SudA is a bifunctional enzyme with four iron-sulfur centers that catalyses the reduction of elemental sulfur or polysulfide ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01316"
] | [
"gltA"
] | [
3355
] | 1 | [] | [] | [] | 0 | [
"4ylf",
"4yry",
"5jca",
"5jfc",
"5vj7"
] | 5 | [
"PUB00015574",
"PUB00150966",
"PUB00150967",
"PUB00150968"
] | [
"9202379",
"11398480",
"7961401",
"28705933"
] | [
"Gene cloning, sequencing and enzymatic properties of glutamate synthase from the hyperthermophilic archaeon Pyrococcus sp. KOD1.",
"Ferredoxin:NADP oxidoreductase from Pyrococcus furiosus.",
"Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in... | [
1997,
2001,
1994,
2017
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
244,
3033,
7,
71
] | 4 | [] | [] | 0 | true | Family | Sulfide dehydrogenase subunit alpha-like | Sulfide dehydrogenase subunit alpha-like | SudA-like | 4 |
IPR006005 | 6,005 | Glutamate synthase, NADH/NADPH, small subunit 1 | Glut_synth_ssu1 | Family | 17,400 | false | false | This family includes glutamate synthases from all cellular organisms. This enzyme, involved in the assimilation of ammonia and glutamate biosynthesis, transfers the amide group of glutamine to 2-oxoglutarate to yield two molecules of glutamate. 2 L-glutamate + NADP + = L-glutamine + 2-oxoglutarate + NADPH + H + Several... | [
"GO:0016639",
"GO:0006537"
] | [
"oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor",
"glutamate biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01317"
] | [
"GOGAT_sm_gam"
] | [
17400
] | 1 | [
"EC",
"GP",
"METACYC"
] | [
"1.4.1.14",
"GenProp1489",
"PWY-6963"
] | [
"EC:1.4.1.14",
"GP:GenProp1489",
"METACYC:PWY-6963"
] | 3 | [
"7mfm",
"7mft"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"CRESS virus sp. ctBnw2",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
13364,
1,
3696,
13,
326
] | 5 | [
"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... | [
5,
2,
4,
1,
6,
1,
1,
63
] | 8 | true | Family | Glutamate synthase, NADH/NADPH, small subunit 1 | Glutamate synthase, NADH/NADPH, small subunit 1 | Glut_synth_ssu1 | 9 |
IPR006007 | 6,007 | Inorganic carbon transporter | Inorganic_carbon_transpt | Family | 340 | false | false | Many photosynthetic organisms including cyanobacteria can concentrate CO2/HCO3- against a greater than ten-fold concentration gradient. This is the difference observed for dissolved CO2 at equilibrium in air and the Km for CO2 of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). In cyanobacteria, the CO2 conce... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00947"
] | [
"2A73"
] | [
340
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00044590"
] | [
"9688546"
] | [
"A putative HCO3- transporter in the cyanobacterium Synechococcus sp. strain PCC 7942."
] | [
1998
] | 1 | [
"IPR051533"
] | [] | 1 | 0 | 1 | [
"Cyanobacteriota",
"Paulinella"
] | [
338,
2
] | 2 | [] | [] | 0 | true | Family | Inorganic carbon transporter | Inorganic carbon transporter | Inorganic_carbon_transpt | 8 |
IPR006008 | 6,008 | Inner membrane-spanning protein YciB | YciB | Family | 8,478 | false | false | Inner membrane-spanning protein YciB (also known as intracellular septation protein A) is a family of proteins which are essential for both normal cell division and bacterial virulence and are believed to play a role in the septation process [ , ]. These proteins play a role in cell envelope biogenesis, maintenance of ... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00189",
"PF04279",
"PTHR36917",
"TIGR00997"
] | [
"YciB",
"IspA",
"",
"ispZ"
] | [
7833,
8478,
8224,
5620
] | 4 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007927",
"PUB00099567",
"PUB00099568",
"PUB00099621",
"PUB00099622"
] | [
"9746567",
"30368949",
"33431434",
"26391555",
"26454142"
] | [
"Identification of two Shigella flexneri chromosomal loci involved in intercellular spreading.",
"A synergistic role for two predicted inner membrane proteins of Escherichia coli in cell envelope integrity.",
"Defects in The First Step of Lipoprotein Maturation Underlie The Synthetic Lethality of <i>Escherichia... | [
1998,
2019,
2021,
2015,
2015
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcina",
"metagenomes"
] | [
8342,
18,
2,
116
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Inner membrane-spanning protein YciB | Inner membrane-spanning protein YciB | YciB | 1 |
IPR006009 | 6,009 | N-acetylglucosaminyltransferase, MurG | GlcNAc_MurG | Family | 27,196 | false | false | The murG gene of Escherichia coli encodes the N-acetylglucosaminyltransferase, UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase, responsible for the final step in the formation of the lipid-linked disaccharide-pentapeptide subunit of peptidoglycan [ ]. ... | [
"GO:0050511"
] | [
"undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00033",
"TIGR01133"
] | [
"MurG",
"murG"
] | [
27172,
21881
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.4.1.227",
"GenProp1480",
"PWY-5265",
"PWY-6385",
"PWY-6470",
"PWY-6471"
] | [
"EC:2.4.1.227",
"GP:GenProp1480",
"METACYC:PWY-5265",
"METACYC:PWY-6385",
"METACYC:PWY-6470",
"METACYC:PWY-6471"
] | 6 | [
"1f0k",
"1nlm",
"3s2u",
"7d1i"
] | 4 | [
"PUB00024731",
"PUB00033163",
"PUB00080974"
] | [
"10892798",
"8449890",
"12455415"
] | [
"The 1.9 A crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis.",
"The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm.",
"E. Coli MurG: a paradigm for a superfamily of glycosyltransferases."
] | [
2000,
1993,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
26381,
381,
434
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
1,
2,
2
] | 4 | true | Family | N-acetylglucosaminyltransferase, MurG | N-acetylglucosaminyltransferase, MurG | GlcNAc_MurG | 5 |
IPR006011 | 6,011 | Syntaxin, N-terminal domain | Syntaxin_N | Domain | 28,976 | false | false | Syntaxins are the prototype family of SNARE proteins. They usually consist of three main regions - a C-terminal transmembrane region, a central SNARE domain which is characteristic of and conserved in all syntaxins , and an N-terminal domain that is featured in this entry. This domain varies between syntaxin isoforms; ... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PFAM",
"SMART",
"CDD"
] | [
"PF00804",
"PF14523",
"SM00503",
"cd00179"
] | [
"Syntaxin",
"Syntaxin_2",
"SynN",
"SynN"
] | [
18765,
9087,
23341,
15238
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-181429",
"R-BTA-181430",
"R-BTA-210500",
"R-BTA-212676",
"R-BTA-264642",
"R-BTA-449836",
"R-BTA-5682910",
"R-BTA-888590",
"R-BTA-9609523",
"R-CEL-114516",
"R-CEL-181429",
"R-CEL-181430",
"R-CEL-199992",
"R-CEL-210500",
"R-CEL-212676",
"R-CEL-264642",
"R-CEL-449836",
"R-CEL-8... | [
"REACTOME:R-BTA-181429",
"REACTOME:R-BTA-181430",
"REACTOME:R-BTA-210500",
"REACTOME:R-BTA-212676",
"REACTOME:R-BTA-264642",
"REACTOME:R-BTA-449836",
"REACTOME:R-BTA-5682910",
"REACTOME:R-BTA-888590",
"REACTOME:R-BTA-9609523",
"REACTOME:R-CEL-114516",
"REACTOME:R-CEL-181429",
"REACTOME:R-CEL-1... | 79 | [
"1br0",
"1ez3",
"1fio",
"1hs7",
"1s94",
"2dnx",
"2xhe",
"3c98",
"3lg7",
"4jeh",
"4jeu",
"5lg4",
"5m4y",
"6ip1",
"6mdm",
"6mdn",
"7q83",
"7udb",
"7udc",
"7xsj",
"9cru",
"9crx",
"9n22",
"9ng2",
"9nlu",
"9nlw",
"9nly",
"9nlz",
"9nm1",
"9ojz",
"9ok3",
"9olo"... | 44 | [
"PUB00020397"
] | [
"11737951"
] | [
"The syntaxins."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"organismal metagenomes"
] | [
4,
28970,
2
] | 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... | [
64,
5,
36,
6,
41,
30,
4,
29,
58,
4,
2,
79
] | 12 | true | Domain | Syntaxin, N-terminal domain | Syntaxin, N-terminal domain | Syntaxin_N | 5 |
IPR006012 | 6,012 | Syntaxin/epimorphin, conserved site | Syntaxin/epimorphin_CS | Conserved_site | 29,933 | false | false | Syntaxins A and B are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. Syntaxins are a family of receptors for intracellular transport vesicles. Each target membrane may be identified by a specific member of the syntaxin family [ ]. Members of the syn... | [
"GO:0005484",
"GO:0006886",
"GO:0016020"
] | [
"SNAP receptor activity",
"intracellular protein transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS00914"
] | [
"SYNTAXIN"
] | [
29933
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00709",
"R-BTA-181429",
"R-BTA-181430",
"R-BTA-204005",
"R-BTA-210500",
"R-BTA-212676",
"R-BTA-264642",
"R-BTA-449836",
"R-BTA-5682910",
"R-BTA-5694530",
"R-BTA-6807878",
"R-BTA-6811438",
"R-BTA-888590",
"R-BTA-8980692",
"R-BTA-9013106",
"R-BTA-9013408",
"R-BTA-9609523",
"R-CE... | [
"PROSITEDOC:PDOC00709",
"REACTOME:R-BTA-181429",
"REACTOME:R-BTA-181430",
"REACTOME:R-BTA-204005",
"REACTOME:R-BTA-210500",
"REACTOME:R-BTA-212676",
"REACTOME:R-BTA-264642",
"REACTOME:R-BTA-449836",
"REACTOME:R-BTA-5682910",
"REACTOME:R-BTA-5694530",
"REACTOME:R-BTA-6807878",
"REACTOME:R-BTA-6... | 128 | [
"1gl2",
"1hvv",
"1jth",
"1kil",
"1l4a",
"1n7s",
"1sfc",
"1urq",
"2m8r",
"2n1t",
"2nps",
"2xhe",
"3b5n",
"3c98",
"3hd7",
"3ipd",
"3j96",
"3j97",
"3j98",
"3j99",
"3rk2",
"3rk3",
"3rl0",
"4jeh",
"4jeu",
"5buz",
"5ccg",
"5cch",
"5cci",
"5kj7",
"5kj8",
"5w5c"... | 69 | [
"PUB00000891",
"PUB00000897",
"PUB00005397",
"PUB00014194"
] | [
"8490959",
"7690687",
"8493722",
"14570579"
] | [
"Is epimorphin involved in vesicular transport?",
"The syntaxin family of vesicular transport receptors.",
"Epimorphin is related to a new class of neuronal and yeast vesicle targeting proteins.",
"SNARE protein structure and function."
] | [
1993,
1993,
1993,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadati",
"Viruses",
"organismal metagenomes"
] | [
29819,
108,
4,
2
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
102,
7,
41,
10,
43,
41,
2,
27,
76,
7,
1,
67
] | 12 | true | Conserved_site | Syntaxin/epimorphin, conserved site | Syntaxin/epimorphin, conserved site | Syntaxin/epimorphin_CS | 1 |
IPR006013 | 6,013 | Antifreeze, type III | Antifreeze_III | Family | 556 | false | false | Marine teleosts from polar oceans can be protected from freezing in icy sea-water by serum antifreeze proteins (AFPs) or glycoproteins (AFGPs) [ , ]: these function by binding to, and preventing the growth of, ice crystals within the fish. Despite functional similarity, the proteins are structurally diverse and include... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00357"
] | [
"ANTIFREEZIII"
] | [
556
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-4085001",
"R-MMU-4085001"
] | [
"REACTOME:R-HSA-4085001",
"REACTOME:R-MMU-4085001"
] | 2 | [
"1ame",
"1b7i",
"1b7j",
"1b7k",
"1c89",
"1c8a",
"1ekl",
"1gzi",
"1hg7",
"1jab",
"1kde",
"1kdf",
"1msi",
"1msj",
"1ops",
"1ucs",
"1wvo",
"2ame",
"2jia",
"2lx2",
"2lx3",
"2msi",
"2msj",
"2spg",
"3ame",
"3msi",
"3nla",
"3qf6",
"3rdn",
"4ame",
"4msi",
"4ny6"... | 51 | [
"PUB00005271",
"PUB00007091",
"PUB00032842",
"PUB00070658",
"PUB00158953"
] | [
"8939756",
"12171656",
"9466928",
"10749855",
"27213289"
] | [
"Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction.",
"Structure and function of antifreeze proteins.",
"The effects of steric mutations on the structure of type III antifreeze protein and its interaction with ice.",
... | [
1996,
2002,
1998,
2000,
2016
] | 5 | [] | [] | 0 | 0 | null | [
"Aerococcus mictus",
"Eukaryota"
] | [
1,
555
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus"
] | [
3,
1,
1
] | 3 | true | Family | Antifreeze, type III | Antifreeze, type III | Antifreeze_III | 5 |
IPR006015 | 6,015 | Universal stress protein A family | Universal_stress_UspA | Family | 110,685 | false | false | Transcriptional induction of the uspA gene of Escherichia coli occurs when conditions cause growth arrest; cells deficient in UspA survive poorly in stationary phase [ ]. The product of uspA has been shown to be a cytoplasmic serine and threonine phosphoprotein. Members of the Usp family are predicted to be related to ... | [] | [] | [] | 0 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF006276",
"PR01438"
] | [
"UspA",
"UNVRSLSTRESS"
] | [
15875,
107542
] | 2 | [] | [] | [] | 0 | [
"1jmv",
"1mjh",
"1tq8",
"1wjg",
"2dum",
"2gm3",
"2jax",
"2pfs",
"2z08",
"2z09",
"2z3v",
"3ab7",
"3ab8",
"3cis",
"3fdx",
"3fg9",
"3fh0",
"3hgm",
"3idf",
"3loq",
"3qtb",
"3s3t",
"3tnj",
"4r2l",
"4r2m",
"4wny",
"5ahw",
"6hcd"
] | 28 | [
"PUB00006689",
"PUB00007929",
"PUB00092650"
] | [
"9405142",
"9860944",
"12732303"
] | [
"The universal stress protein, UspA, of Escherichia coli is phosphorylated in response to stasis.",
"Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics.",
"The bacterial universal stress protein: function and regulation."
] | [
1997,
1998,
2003
] | 3 | [] | [
"IPR044162",
"IPR044187"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
10123,
86188,
2,
13624,
1,
747
] | 6 | [
"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",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
50,
5,
3,
54,
1,
70
] | 6 | true | Family | Universal stress protein A family | Universal stress protein A family | Universal_stress_UspA | 4 |
IPR006016 | 6,016 | UspA | UspA | Domain | 159,151 | false | false | This entry represents a domain found in the universal stress protein UspA [ ], which is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress en... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00582"
] | [
"Usp"
] | [
159151
] | 1 | [] | [] | [] | 0 | [
"1jmv",
"1mjh",
"1q77",
"1tq8",
"1wjg",
"2dum",
"2gm3",
"2jax",
"2pfs",
"2z08",
"2z09",
"2z3v",
"3ab7",
"3ab8",
"3cis",
"3fdx",
"3fg9",
"3fh0",
"3hgm",
"3idf",
"3loq",
"3mt0",
"3olq",
"3qtb",
"3s3t",
"3tnj",
"4r2j",
"4r2k",
"4r2l",
"4r2m",
"4wny",
"4wy2"... | 36 | [
"PUB00003858",
"PUB00007929",
"PUB00009389",
"PUB00067935"
] | [
"8152377",
"9860944",
"11738040",
"20113006"
] | [
"Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest.",
"Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics.",
"Structure of the universal stress protein of Haemophilus influenzae.",
"Structure an... | [
1994,
1998,
2001,
2010
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
14764,
117216,
2,
26128,
1,
1040
] | 6 | [
"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",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
175,
6,
4,
114,
2,
229
] | 6 | true | Domain | UspA | UspA | UspA | 2 |
IPR006017 | 6,017 | Caldesmon | Caldesmon | Family | 2,079 | false | false | null | [
"GO:0003779",
"GO:0005516",
"GO:0017022",
"GO:0006936"
] | [
"actin binding",
"calmodulin binding",
"myosin binding",
"muscle contraction"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PRINTS"
] | [
"PR01076"
] | [
"CALDESMON"
] | [
2079
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-445355",
"R-RNO-445355"
] | [
"REACTOME:R-HSA-445355",
"REACTOME:R-RNO-445355"
] | 2 | [] | 0 | [
"PUB00001815",
"PUB00003449"
] | [
"1555769",
"1939602"
] | [
"Cloning of cDNAs encoding human caldesmons.",
"Sequence of an avian non-muscle caldesmon."
] | [
1992,
1991
] | 2 | [
"IPR006018"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
2079
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
12,
8,
9
] | 4 | true | Family | Caldesmon | Caldesmon | Caldesmon | 3 |
IPR006018 | 6,018 | Caldesmon/lymphocyte specific protein | Caldesmon_LSP | Family | 3,490 | false | false | This group of proteins includes two protein families: caldesmon and lymphocyte specific protein. Caldesmon (CDM) is an actin-and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and non-muscle cells, possibly acting as a bridge between myosin and actin filaments [ ]. CDM i... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02029"
] | [
"Caldesmon"
] | [
3490
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-445355",
"R-RNO-445355"
] | [
"REACTOME:R-HSA-445355",
"REACTOME:R-RNO-445355"
] | 2 | [] | 0 | [
"PUB00001815"
] | [
"1555769"
] | [
"Cloning of cDNAs encoding human caldesmons."
] | [
1992
] | 1 | [] | [
"IPR002211",
"IPR006017"
] | 0 | 2 | 0 | [
"Chordata"
] | [
3490
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
21,
18,
19
] | 4 | true | Family | Caldesmon/lymphocyte specific protein | Caldesmon/lymphocyte specific protein | Caldesmon_LSP | 1 |
IPR006019 | 6,019 | Phosphotyrosine interaction domain, Shc-like | PID_Shc-like | Domain | 4,678 | false | false | null | [
"GO:0035556"
] | [
"intracellular signal transduction"
] | [
"biological_process"
] | 1 | [
"PRINTS",
"CDD"
] | [
"PR00629",
"cd01209"
] | [
"SHCPIDOMAIN",
"PTB_Shc"
] | [
4633,
4413
] | 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-1250196",
"R-BTA-1250347",
"R-BTA-167044",
"R-BTA-180336",
"R-BTA-201556",
"R-BTA-210993",
"R-BTA-2424491",
"R-BTA-2428933",
"R-BTA-2730905",
"R-BTA-2871796",
"R-BTA-2871809",
"R-BTA-354192",
"R-BTA-512988",
"R-BTA-5654688",
"R-BTA-5654699",
"R-BTA-5654704",
"R-BTA-5654719",
... | [
"REACTOME:R-BTA-1250196",
"REACTOME:R-BTA-1250347",
"REACTOME:R-BTA-167044",
"REACTOME:R-BTA-180336",
"REACTOME:R-BTA-201556",
"REACTOME:R-BTA-210993",
"REACTOME:R-BTA-2424491",
"REACTOME:R-BTA-2428933",
"REACTOME:R-BTA-2730905",
"REACTOME:R-BTA-2871796",
"REACTOME:R-BTA-2871809",
"REACTOME:R-... | 133 | [
"1n3h",
"1oy2",
"1shc",
"2l1c",
"4xwx"
] | 5 | [
"PUB00000936",
"PUB00002911",
"PUB00003928"
] | [
"8646778",
"7541035",
"8599766"
] | [
"Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor.",
"Shc binding to nerve growth factor receptor is mediated by the phosphotyrosine interaction domain.",
"Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain."
] | [
1996,
1995,
1996
] | 3 | [
"IPR006020"
] | [] | 1 | 0 | 1 | [
"Opisthokonta"
] | [
4678
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
25,
3,
14,
12,
19
] | 5 | true | Domain | Phosphotyrosine interaction domain, Shc-like | Phosphotyrosine interaction domain, Shc-like | PID_Shc-like | 7 |
IPR006020 | 6,020 | PTB/PI domain | PTB/PI_dom | Domain | 73,223 | false | false | Proteins encoding phosphotyrosine binding (PTB) domains function as adaptors or scaffolds to organise the signaling complexes involved in wide-ranging physiological processes including neural development, immunity, tissue homeostasis and cell growth. Due to structural differences, PTB domains are divided into three gro... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00640",
"PF14719",
"PS01179",
"SM00462"
] | [
"PID",
"PID_2",
"PID",
"PTB"
] | [
49959,
3864,
56503,
66518
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00907",
"R-BTA-1250196",
"R-BTA-1250347",
"R-BTA-167044",
"R-BTA-180336",
"R-BTA-201556",
"R-BTA-210993",
"R-BTA-2424491",
"R-BTA-2428933",
"R-BTA-2730905",
"R-BTA-2871796",
"R-BTA-2871809",
"R-BTA-354192",
"R-BTA-512988",
"R-BTA-5654688",
"R-BTA-5654699",
"R-BTA-5654704",
"R-... | [
"PROSITEDOC:PDOC00907",
"REACTOME:R-BTA-1250196",
"REACTOME:R-BTA-1250347",
"REACTOME:R-BTA-167044",
"REACTOME:R-BTA-180336",
"REACTOME:R-BTA-201556",
"REACTOME:R-BTA-210993",
"REACTOME:R-BTA-2424491",
"REACTOME:R-BTA-2428933",
"REACTOME:R-BTA-2730905",
"REACTOME:R-BTA-2871796",
"REACTOME:R-BT... | 197 | [
"1aqc",
"1ddm",
"1m7e",
"1n3h",
"1ntv",
"1nu2",
"1oqn",
"1oy2",
"1p3r",
"1shc",
"1wgu",
"1wj1",
"1wvh",
"1x11",
"2cy4",
"2cy5",
"2dkq",
"2dyq",
"2ej8",
"2ela",
"2gjy",
"2l1c",
"2loz",
"2m38",
"2nmb",
"2roz",
"2ysz",
"2yt0",
"2yt1",
"3d8d",
"3d8e",
"3d8f"... | 55 | [
"PUB00000914",
"PUB00002884",
"PUB00005190",
"PUB00018031",
"PUB00018032"
] | [
"7534213",
"7798194",
"7527937",
"15567406",
"12737822"
] | [
"A phosphotyrosine interaction domain.",
"A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors.",
"An alternative to SH2 domains for binding tyrosine-phosphorylated proteins.",
"Structural and evolutionary division of phosphotyrosine binding (PTB) domains.",
... | [
1995,
1994,
1994,
2005,
2003
] | 5 | [] | [
"IPR006019",
"IPR033930",
"IPR039114",
"IPR047237",
"IPR048561"
] | 0 | 5 | 0 | [
"Bacteria",
"Eukaryota",
"Microbacterium phage Percival"
] | [
68,
73154,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
42,
507,
56,
207,
170,
218
] | 6 | true | Domain | PTB/PI domain | PTB/PI domain | PTB/PI_dom | 6 |
IPR006024 | 6,024 | Opioid neuropeptide precursor | Opioid_neupept | Family | 2,983 | false | false | Vertebrate endogenous opioid neuropeptides are released by post-translational proteolytic cleavage of precursor proteins. The precursors consist of the following components: a signal sequence that precedes a conserved region of about 50 residues; a variable-length region; and the sequence of the neuropeptide itself. Th... | [
"GO:0007218"
] | [
"neuropeptide signaling pathway"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PRINTS",
"PROSITE",
"PANTHER"
] | [
"PF01160",
"PR01028",
"PS01252",
"PTHR11438"
] | [
"Opiods_neuropep",
"OPIOIDPRCRSR",
"OPIOIDS_PRECURSOR",
""
] | [
2368,
2202,
647,
2958
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00964",
"R-BTA-375276",
"R-BTA-381426",
"R-BTA-418594",
"R-BTA-8957275",
"R-HSA-111885",
"R-HSA-202040",
"R-HSA-375276",
"R-HSA-381426",
"R-HSA-418594",
"R-HSA-8957275",
"R-MMU-111885",
"R-MMU-202040",
"R-MMU-375276",
"R-MMU-381426",
"R-MMU-418594",
"R-MMU-8957275",
"R-RNO-111... | [
"PROSITEDOC:PDOC00964",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-8957275",
"REACTOME:R-HSA-111885",
"REACTOME:R-HSA-202040",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-8957275",
"REACTOME:R-MMU-11... | 23 | [] | 0 | [
"PUB00004901"
] | [
"8710928"
] | [
"Structure, tissue distribution, and chromosomal localization of the prepronociceptin gene."
] | [
1996
] | 1 | [] | [
"IPR000703",
"IPR000750",
"IPR002367"
] | 0 | 3 | 0 | [
"Deuterostomia",
"marine sediment metagenome"
] | [
2982,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
21,
11,
9
] | 4 | true | Family | Opioid neuropeptide precursor | Opioid neuropeptide precursor | Opioid_neupept | 7 |
IPR006027 | 6,027 | NusB/RsmB/TIM44 | NusB_RsmB_TIM44 | Domain | 47,182 | false | false | This domain is found in a number of functionally different proteins: NusB a prokaryotic transcription factor involved in antitermination TIM44, the mitochondrial inner membrane translocase subunit RsmB, the 16S rRNA m5C967 methyltransferase NusB is a prokaryotic transcription factor involved in antitermination processe... | [
"GO:0003723",
"GO:0006355"
] | [
"RNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01029"
] | [
"NusB"
] | [
47182
] | 1 | [] | [] | [] | 0 | [
"1ey1",
"1eyv",
"1sqf",
"1sqg",
"1tzt",
"1tzu",
"1tzv",
"1tzw",
"1tzx",
"2jr0",
"3d3b",
"3d3c",
"3imq",
"3r2c",
"3r2d",
"4eya",
"5lm7",
"5ms0",
"6ckq",
"6gov",
"6tqn",
"6tqo"
] | 22 | [
"PUB00001316",
"PUB00017040"
] | [
"9670024",
"15279620"
] | [
"Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein.",
"Crystal structures of the antitermination factor NusB from Thermotoga maritima and implications for RNA binding."
] | [
1998,
2004
] | 2 | [] | [
"IPR048019"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
44837,
1294,
72,
979
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
2,
6,
19
] | 4 | true | Domain | NusB/RsmB/TIM44 | NusB/RsmB/TIM44 | NusB_RsmB_TIM44 | 3 |
IPR006031 | 6,031 | XYPPX repeat | XYPPX | Repeat | 582 | false | false | This repeat is found in a wide variety of proteins and generally consists of the motif XYPPX where X can be any amino acid. The family includes annexin VII ANX7_DICDI, the carboxy tail of certain rhodopsins OPSD_LOLSU. This family also includes plaque matrix proteins, however this motif is embedded in a ten residue rep... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02162"
] | [
"XYPPX"
] | [
582
] | 1 | [] | [] | [] | 0 | [
"2z73",
"3aym",
"3ayn"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Eukaryota",
"viral metagenome"
] | [
4,
577,
1
] | 3 | [
"Zea mays"
] | [
6
] | 1 | true | Repeat | XYPPX repeat | XYPPX repeat | XYPPX | 8 |
IPR006032 | 6,032 | Small ribosomal subunit protein uS12 | Ribosomal_uS12 | Family | 51,521 | false | false | Ribosomal protein uS12 is one of the proteins from the small ribosomal subunit. In Escherichia coli, uS12 is known to be involved in the translation initiation step. It is a very basic protein of 120 to 150 amino-acid residues. uS12 belongs to a family of ribosomal proteins which are grouped on the basis of sequence si... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PIRSF",
"PROSITE",
"PANTHER"
] | [
"PF00164",
"PIRSF002133",
"PS00055",
"PTHR11652"
] | [
"Ribosom_S12_S23",
"Ribosomal_S12/S23",
"RIBOSOMAL_S12",
""
] | [
51457,
43277,
48536,
51065
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00054",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-9629569",
"R-BTA-975956",
"R-BTA-975957",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-7264... | [
"PROSITEDOC:PDOC00054",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-96295... | 114 | [
"1fjg",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1mj1",
"1ml5",
"1mvr",
"1n32",
"1n33",
"1n34",
"1n36",
"1pn7",
"1pn8",
"1qzc",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xmo"... | 1,929 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [] | [
"IPR005679",
"IPR005680"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
894,
23232,
26925,
470
] | 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",... | [
16,
2,
2,
5,
1,
6,
7,
2,
22,
8,
3,
3,
33
] | 13 | true | Family | Small ribosomal subunit protein uS12 | Small ribosomal subunit protein uS12 | Ribosomal_uS12 | 5 |
IPR006033 | 6,033 | Type I L-asparaginase family | AsnA_fam | Family | 8,901 | false | false | Two related families of asparaginase are designated type I and type II according to the terminology in Escherichia coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This family ... | [
"GO:0004067",
"GO:0006520"
] | [
"asparaginase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR00519"
] | [
"asnASE_I"
] | [
8901
] | 1 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.5.-",
"GenProp1365",
"GenProp1404",
"PWY-5297",
"PWY-7811",
"PWY-8229",
"R-HSA-8963693",
"R-MMU-8963693",
"R-RNO-8963693"
] | [
"EC:6.3.5.-",
"GP:GenProp1365",
"GP:GenProp1404",
"METACYC:PWY-5297",
"METACYC:PWY-7811",
"METACYC:PWY-8229",
"REACTOME:R-HSA-8963693",
"REACTOME:R-MMU-8963693",
"REACTOME:R-RNO-8963693"
] | 9 | [
"1wls",
"1wnf",
"1zq1",
"2d6f",
"2him",
"2ocd",
"2p2d",
"2p2n",
"3ntx",
"4q0m",
"5ot0",
"6nxc",
"6nxd",
"7r69",
"7r6a",
"7r6b",
"9ufq",
"9ufr"
] | 18 | [
"PUB00040197"
] | [
"16809540"
] | [
"Structural basis of RNA-dependent recruitment of glutamine to the genetic code."
] | [
2006
] | 1 | [
"IPR006034"
] | [
"IPR011878",
"IPR041725"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"metagenomes"
] | [
948,
6018,
1887,
1,
47
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
8,
2,
1,
2,
1,
3
] | 7 | true | Family | Type I L-asparaginase family | Type I L-asparaginase family | AsnA_fam | 5 |
IPR006034 | 6,034 | Asparaginase/glutaminase-like | Asparaginase/glutaminase-like | Family | 31,752 | false | false | L-Asparaginases ( ) hydrolyse L-asparagine to L-aspartate and ammonia. Enzymes with asparaginase activity play an important role in the metabolism of all living organisms [ , ]. Enzymes capable of converting L-asparagine to L-aspartate can be classified as bacterial-type or plant-type L-asparaginase. Bacterial-type L-a... | [] | [] | [] | 0 | [
"PIRSF",
"PRINTS",
"PROFILE",
"PANTHER",
"SMART"
] | [
"PIRSF001220",
"PR00139",
"PS51732",
"PTHR11707",
"SM00870"
] | [
"L-ASNase_gatD",
"ASNGLNASE",
"ASN_GLN_ASE_3",
"",
"Asparaginase"
] | [
31597,
29555,
31143,
30158,
28958
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00132",
"R-HSA-8963693",
"R-MMU-8963693",
"R-RNO-8963693"
] | [
"PROSITEDOC:PDOC00132",
"REACTOME:R-HSA-8963693",
"REACTOME:R-MMU-8963693",
"REACTOME:R-RNO-8963693"
] | 4 | [
"1agx",
"1djo",
"1djp",
"1hfj",
"1hfk",
"1hfw",
"1hg0",
"1hg1",
"1ho3",
"1ihd",
"1jaz",
"1jja",
"1jsl",
"1jsr",
"1nns",
"1o7j",
"1wls",
"1wnf",
"1wsa",
"1zcf",
"1zq1",
"2d6f",
"2gvn",
"2him",
"2hln",
"2jk0",
"2ocd",
"2p2d",
"2p2n",
"2wlt",
"2wt4",
"3eca"... | 154 | [
"PUB00040197",
"PUB00085037",
"PUB00085038",
"PUB00085039",
"PUB00085040"
] | [
"16809540",
"11996000",
"17143335",
"9575212",
"12610720"
] | [
"Structural basis of RNA-dependent recruitment of glutamine to the genetic code.",
"Sequence analysis of enzymes with asparaginase activity.",
"Structural aspects of L-asparaginases, their friends and relations.",
"Cloning and expression of cDNA encoding rat liver 60-kDa lysophospholipase containing an aspara... | [
2006,
2001,
2006,
1998,
2003
] | 5 | [] | [
"IPR004550",
"IPR006033"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
1242,
23682,
21,
6506,
301
] | 5 | [
"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 (strain ATCC 204508 / S288c)",
... | [
4,
10,
3,
2,
3,
4,
2,
3,
7,
4
] | 10 | true | Family | Asparaginase/glutaminase-like | Asparaginase/glutaminase-like | Asparaginase/glutaminase-like | 3 |
IPR006035 | 6,035 | Ureohydrolase | Ureohydrolase | Family | 52,733 | false | false | The ureohydrolase superfamily includes arginase ( ), agmatinase ( ), formiminoglutamase ( ) and proclavaminate amidinohydrolase ( ) [ ]. These enzymes show trimeric or hexameric structures and share a 3-layer α-β-α structure [ , , , ], playing important roles in arginine/agmatine metabolism, the urea cycle, histidine d... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PIRSF",
"PRINTS",
"PROFILE",
"PANTHER",
"PANTHER"
] | [
"PF00491",
"PIRSF036979",
"PR00116",
"PS51409",
"PTHR11358",
"PTHR43782"
] | [
"Arginase",
"Arginase",
"ARGINASE",
"ARGINASE_2",
"",
""
] | [
52615,
34328,
29128,
51741,
35428,
15402
] | 6 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"3.5.3",
"GenProp1279",
"GenProp1282",
"GenProp1300",
"GenProp1428",
"GenProp1596",
"GenProp1619",
"PDOC00135",
"R-BTA-6798695",
"R-BTA-70635",
"R-HSA-351143",
"R-HSA-6798695",
"R-HSA-70635",
"R-HSA-9837999",
"R-MMU-351143",
"R-MMU-6798695",
"R-MMU-70635",
"R-MMU-9837999",
"R-PFA... | [
"EC:3.5.3",
"GP:GenProp1279",
"GP:GenProp1282",
"GP:GenProp1300",
"GP:GenProp1428",
"GP:GenProp1596",
"GP:GenProp1619",
"PROSITEDOC:PDOC00135",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70635",
"REACTOME:R-HSA-351143",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-70635",
"REACTOME:R-HSA-98379... | 32 | [
"1cev",
"1d3v",
"1gq6",
"1gq7",
"1hq5",
"1hqf",
"1hqg",
"1hqh",
"1hqx",
"1p8m",
"1p8n",
"1p8o",
"1p8p",
"1p8q",
"1p8r",
"1p8s",
"1pq3",
"1r1o",
"1rla",
"1t4p",
"1t4r",
"1t4s",
"1t4t",
"1t5f",
"1t5g",
"1ta1",
"1tbh",
"1tbj",
"1tbl",
"1wog",
"1woh",
"1woi"... | 200 | [
"PUB00001437",
"PUB00025337",
"PUB00028086",
"PUB00028087",
"PUB00052609"
] | [
"7916684",
"12020346",
"15355972",
"16141327",
"18360740"
] | [
"Developmental and hormonal regulation of the Xenopus liver-type arginase gene.",
"Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis.",
"Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ur... | [
1993,
2002,
2004,
2005,
2008
] | 5 | [] | [
"IPR005923",
"IPR005925",
"IPR014033"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1770,
38328,
11849,
12,
774
] | 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",... | [
8,
1,
3,
4,
2,
5,
5,
5,
2,
13,
1,
5,
6
] | 13 | true | Family | Ureohydrolase | Ureohydrolase | Ureohydrolase | 7 |
IPR006036 | 6,036 | Potassium uptake protein TrkA | K_uptake_TrkA | Family | 22,569 | false | false | The Trk system is a low to medium affinity potassium uptake system, widely found in both in bacteria and archaea, where the uptake of K(+) is believed to be linked to H(+) symport [ ]. The core Trk system consists of two proteins, the integral membrane K(+)-translocating protein TrkH (or TrkG), and the regulatory NAD-b... | [
"GO:0015079",
"GO:0006813",
"GO:0005886"
] | [
"potassium ion transmembrane transporter activity",
"potassium ion transport",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00335"
] | [
"KUPTAKETRKA"
] | [
22569
] | 1 | [] | [] | [] | 0 | [
"1lss",
"2g1u",
"3eyw",
"3l4b",
"3l9w",
"3l9x",
"4g65",
"4j9u",
"4j9v",
"5nc8",
"6v4j",
"6v4k",
"6v4l",
"8bxg",
"8by2",
"9emb"
] | 16 | [
"PUB00001263",
"PUB00003817",
"PUB00042655",
"PUB00042656",
"PUB00042657",
"PUB00061657",
"PUB00099198",
"PUB00099201"
] | [
"8076592",
"2046548",
"10423425",
"15205426",
"9720051",
"22316140",
"31992706",
"27803167"
] | [
"A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium.",
"The cloning and DNA sequence of the gene for the glutathione-regulated potassium-efflux system KefC of Escherichia coli.",
"Evolutionary relationship between K(+) channels and symporters.",
"Multiple... | [
1994,
1991,
1999,
2004,
1998,
2012,
2020,
2016
] | 8 | [] | [
"IPR023941"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2409,
19578,
16,
566
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | Potassium uptake protein TrkA | Potassium uptake protein TrkA | K_uptake_TrkA | 6 |
IPR006037 | 6,037 | Regulator of K+ conductance, C-terminal | RCK_C | Domain | 83,264 | false | false | The regulator of K+ conductance (RCK) domain is found in many ligand-gated K+ channels, most often attached to the intracellular carboxy terminus. The domain is prevalent among prokaryotic K+ channels, and also found in eukaryotic, high-conductance Ca2+-activated K+ channels (BK channels) [ , , ]. Largely involved in r... | [
"GO:0008324",
"GO:0006813"
] | [
"monoatomic cation transmembrane transporter activity",
"potassium ion transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF02080",
"PS51202"
] | [
"TrkA_C",
"RCK_C"
] | [
76318,
82648
] | 2 | [
"PROSITEDOC"
] | [
"PDOC51201"
] | [
"PROSITEDOC:PDOC51201"
] | 1 | [
"1lnq",
"1vct",
"2aef",
"2aej",
"2aem",
"2bkn",
"2bko",
"2bkp",
"2fy8",
"2ogu",
"3jxo",
"3kxd",
"3l4b",
"3rbx",
"3rbz",
"4ei2",
"4g65",
"4gvl",
"4gx0",
"4gx1",
"4gx2",
"4gx5",
"4j7c",
"4j90",
"4j91",
"4j9u",
"4j9v",
"4l73",
"4l74",
"4l75",
"4l76",
"4ro0"... | 84 | [
"PUB00003847",
"PUB00007364",
"PUB00025981",
"PUB00027068",
"PUB00033755",
"PUB00099198"
] | [
"8412700",
"11292341",
"11301020",
"12037559",
"16227203",
"31992706"
] | [
"NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA and sequence similarity between TrkA and domains of a family of dehydrogenases suggest a role for NAD+ in bacterial transport.",
"Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains.",
"... | [
1993,
2001,
2001,
2002,
2005,
2020
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Gordonia phage Pupper",
"unclassified sequences"
] | [
5943,
75453,
437,
1,
1430
] | 5 | [
"Escherichia coli (strain K12)"
] | [
5
] | 1 | true | Domain | Regulator of K+ conductance, C-terminal | Regulator of K+ conductance, C-terminal | RCK_C | 7 |
IPR006040 | 6,040 | Allergen Ole e 1, conserved site | Allergen_Ole_e_I_CS | Conserved_site | 1,249 | false | false | Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS All... | [
"GO:0005615"
] | [
"extracellular space"
] | [
"cellular_component"
] | 1 | [
"PROSITE"
] | [
"PS00925"
] | [
"OLEEI"
] | [
1249
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00715"
] | [
"PROSITEDOC:PDOC00715"
] | 1 | [
"6yoa"
] | 1 | [
"PUB00001444"
] | [
"8404906"
] | [
"The amino acid sequence of Ole e I, the major allergen from olive tree (Olea europaea) pollen."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1249
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
11,
12,
15
] | 3 | true | Conserved_site | Allergen Ole e 1, conserved site | Allergen Ole e 1, conserved site | Allergen_Ole_e_I_CS | 4 |
IPR006041 | 6,041 | Pollen allergen Ole e 1 family | Pollen_Ole_e1_allergen | Family | 2,989 | false | false | Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS All... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR31614"
] | [
""
] | [
2989
] | 1 | [] | [] | [] | 0 | [
"4z8w",
"6yoa"
] | 2 | [
"PUB00001444"
] | [
"8404906"
] | [
"The amino acid sequence of Ole e I, the major allergen from olive tree (Olea europaea) pollen."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2989
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
24,
17,
23
] | 3 | true | Family | Pollen allergen Ole e 1 family | Pollen allergen Ole e 1 family | Pollen_Ole_e1_allergen | 9 |
IPR006042 | 6,042 | Xanthine/uracil permease | Xan_ur_permease | Family | 35,499 | false | false | A number of transport proteins which are involved in the uptake of xanthine or uracil are evolutionary related [ ]. They are proteins of from 430 to 595 residues that seem to contain 12 transmembrane domains. | [
"GO:0022857",
"GO:0055085",
"GO:0016020"
] | [
"transmembrane transporter activity",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE",
"NCBIFAM"
] | [
"PS01116",
"TIGR00801"
] | [
"XANTH_URACIL_PERMASE",
"ncs2"
] | [
29356,
31220
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00860",
"R-HSA-196836",
"R-MMU-196836",
"R-RNO-196836",
"R-XTR-196836"
] | [
"PROSITEDOC:PDOC00860",
"REACTOME:R-HSA-196836",
"REACTOME:R-MMU-196836",
"REACTOME:R-RNO-196836",
"REACTOME:R-XTR-196836"
] | 5 | [
"3qe7",
"5i6c",
"5xls",
"8omz",
"8oo1"
] | 5 | [
"PUB00002949"
] | [
"7721763"
] | [
"Genetic and molecular characterization of a gene encoding a wide specificity purine permease of Aspergillus nidulans reveals a novel family of transporters conserved in prokaryotes and eukaryotes."
] | [
1995
] | 1 | [
"IPR006043"
] | [
"IPR017588",
"IPR019918"
] | 1 | 2 | 0 | [
"Bacteria",
"Enterobacteria phage VT2-Sa",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
29833,
1,
5222,
277,
166
] | 5 | [
"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",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
13,
1,
5,
4,
3,
1,
6,
1
] | 8 | true | Family | Xanthine/uracil permease | Xanthine/uracil permease | Xan_ur_permease | 9 |
IPR006043 | 6,043 | Nucleobase cation symporter 2 family | NCS2 | Family | 85,666 | false | false | The nucleobase cation symporter 2 (NCS2) family, also known as the nucleobase ascorbate transporter(NAT) family, are a large family found in bacteria, fungi (except Saccharomyces cerevisiae), plants and mammals. Nucleobase transporter families have solute transport preferences among purines and pyrimidines. Members of ... | [
"GO:0022857",
"GO:0055085",
"GO:0016020"
] | [
"transmembrane transporter activity",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF00860"
] | [
"Xan_ur_permease"
] | [
85666
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196836",
"R-MMU-196836",
"R-RNO-196836",
"R-XTR-196836"
] | [
"REACTOME:R-HSA-196836",
"REACTOME:R-MMU-196836",
"REACTOME:R-RNO-196836",
"REACTOME:R-XTR-196836"
] | 4 | [
"3qe7",
"5i6c",
"5xls",
"7tak",
"7ytw",
"7yty",
"8irl",
"8irm",
"8irn",
"8iro",
"8irp",
"8jew",
"8jez",
"8jf0",
"8jf1",
"8omz",
"8oo1",
"8wmq",
"8wo7",
"9j12",
"9j13",
"9j14",
"9j15",
"9j16",
"9j17",
"9j18"
] | 26 | [
"PUB00092449"
] | [
"29385571"
] | [
"The solute transport profile of two Aza-guanine transporters from the Honey bee pathogen Paenibacillus larvae."
] | [
2018
] | 1 | [] | [
"IPR006042",
"IPR045018"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
1090,
63351,
4,
20733,
488
] | 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",... | [
66,
8,
18,
1,
10,
17,
10,
4,
44,
12,
2,
123
] | 12 | true | Family | Nucleobase cation symporter 2 family | Nucleobase cation symporter 2 family | NCS2 | 6 |
IPR006045 | 6,045 | Cupin 1 | Cupin_1 | Domain | 39,758 | false | false | This entry represents the conserved β-barrel fold of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant [ , , ]. This domain can also be fo... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00190",
"SM00835"
] | [
"Cupin_1",
"Cupin_1"
] | [
38756,
35716
] | 2 | [] | [] | [] | 0 | [
"1cau",
"1cav",
"1caw",
"1cax",
"1dgr",
"1dgw",
"1fi2",
"1fxz",
"1ipj",
"1ipk",
"1j58",
"1l3j",
"1od5",
"1phs",
"1ucx",
"1ud1",
"1uij",
"1uik",
"1uw8",
"2b8m",
"2cau",
"2cav",
"2cv6",
"2d5f",
"2d5h",
"2e9q",
"2ea7",
"2eaa",
"2et1",
"2et7",
"2ete",
"2evx"... | 83 | [
"PUB00005817",
"PUB00007277",
"PUB00095171",
"PUB00095173"
] | [
"9573603",
"10704478",
"21954589",
"28000570"
] | [
"Cupins: a new superfamily of functionally diverse proteins that include germins and plant storage proteins.",
"Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily.",
"[Evolution of seed storage gl... | [
1998,
2000,
2011,
2017
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
217,
5091,
34421,
4,
25
] | 5 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
183,
1,
146,
257
] | 4 | true | Domain | Cupin 1 | Cupin 1 | Cupin_1 | 6 |
IPR006046 | 6,046 | Alpha amylase | Alpha_amylase | Family | 16,877 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004556",
"GO:0043169",
"GO:0005975"
] | [
"alpha-amylase activity",
"cation binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS"
] | [
"PR00110"
] | [
"ALPHAAMYLASE"
] | [
16877
] | 1 | [
"CAZY",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH13",
"3.2.1.1",
"R-DME-189085",
"R-HSA-189085",
"R-HSA-9925561",
"R-MMU-189085"
] | [
"CAZY:GH13",
"EC:3.2.1.1",
"REACTOME:R-DME-189085",
"REACTOME:R-HSA-189085",
"REACTOME:R-HSA-9925561",
"REACTOME:R-MMU-189085"
] | 6 | [
"1a47",
"1amy",
"1aqh",
"1aqm",
"1ava",
"1b0i",
"1b2y",
"1bag",
"1bg9",
"1bsi",
"1bvn",
"1c8q",
"1cdg",
"1cgt",
"1cgu",
"1cgv",
"1cgw",
"1cgx",
"1cgy",
"1ciu",
"1clv",
"1cpu",
"1cxe",
"1cxf",
"1cxh",
"1cxi",
"1cxk",
"1cxl",
"1cyg",
"1d3c",
"1d7f",
"1ded"... | 219 | [
"PUB00004870",
"PUB00005266"
] | [
"7624375",
"8535779"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1995,
1995
] | 2 | [] | [
"IPR013775",
"IPR013776"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Terrestrivirus sp.",
"unclassified sequences"
] | [
148,
8679,
8004,
1,
45
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
1,
13,
23,
10,
8,
26,
11,
14
] | 9 | true | Family | Alpha amylase | Alpha amylase | Alpha_amylase | 2 |
IPR006047 | 6,047 | Glycosyl hydrolase family 13, catalytic domain | GH13_cat_dom | Domain | 195,771 | false | false | Enzymes containing this domain, such as alpha-amylase, belong to family 13 ( ) of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme that catalyses the hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the c... | [
"GO:0005975"
] | [
"carbohydrate metabolic process"
] | [
"biological_process"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF00128",
"SM00642"
] | [
"Alpha-amylase",
"Aamy"
] | [
179461,
191037
] | 2 | [
"CAZY",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"GH13",
"GenProp1412",
"GenProp1483",
"GenProp1726",
"R-DDI-3322077",
"R-DME-189085",
"R-DME-352230",
"R-HSA-189085",
"R-HSA-210991",
"R-HSA-3322077",
"R-HSA-352230",
"R-HSA-3878781",
"R-HSA-5619113",
"R-HSA-5660862",
"R-HSA-5660883",
"R-HSA-71240",
"R-HSA-9925561",
"R-MMU-189085",... | [
"CAZY:GH13",
"GP:GenProp1412",
"GP:GenProp1483",
"GP:GenProp1726",
"REACTOME:R-DDI-3322077",
"REACTOME:R-DME-189085",
"REACTOME:R-DME-352230",
"REACTOME:R-HSA-189085",
"REACTOME:R-HSA-210991",
"REACTOME:R-HSA-3322077",
"REACTOME:R-HSA-352230",
"REACTOME:R-HSA-3878781",
"REACTOME:R-HSA-561911... | 28 | [
"1a47",
"1amy",
"1aqh",
"1aqm",
"1ava",
"1b0i",
"1b2y",
"1bag",
"1bf2",
"1bg9",
"1bli",
"1bpl",
"1bsi",
"1bvn",
"1bvz",
"1c8q",
"1cdg",
"1cgt",
"1cgu",
"1cgv",
"1cgw",
"1cgx",
"1cgy",
"1ciu",
"1clv",
"1cpu",
"1cxe",
"1cxf",
"1cxh",
"1cxi",
"1cxk",
"1cxl"... | 696 | [
"PUB00004870",
"PUB00005266",
"PUB00027665",
"PUB00047252",
"PUB00060751",
"PUB00080589",
"PUB00119822",
"PUB00128908"
] | [
"7624375",
"8535779",
"16302977",
"17724034",
"9302327",
"17085431",
"18838391",
"19878315"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for reco... | [
1995,
1995,
2005,
2007,
1997,
2006,
2009,
2009
] | 8 | [] | [
"IPR044077",
"IPR044096"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1324,
155883,
37254,
6,
1304
] | 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",... | [
37,
7,
22,
53,
8,
39,
20,
9,
55,
25,
8,
12,
114
] | 13 | true | Domain | Glycosyl hydrolase family 13, catalytic domain | Glycosyl hydrolase family 13, catalytic domain | GH13_cat_dom | 4 |
IPR006048 | 6,048 | Alpha-amylase/branching enzyme, C-terminal all beta | A-amylase/branching_C | Domain | 36,472 | false | false | This entry represents the all-β C-terminal domain that is found in members of the glycosyl hydrolase 13 family, such as alpha-amylases and 1,4-alpha-glucan branching enzyme. This domain forms a Greek key β-barrel fold in these enzymes [ ]. Alpha-amylase is classified as family 13 ( ) of the glycosyl hydrolases and is p... | [
"GO:0003824",
"GO:0043169",
"GO:0005975"
] | [
"catalytic activity",
"cation binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF02806"
] | [
"Alpha-amylase_C"
] | [
36472
] | 1 | [
"CAZY",
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH13",
"2.4.1.18",
"GenProp1483",
"PWY-5067",
"PWY-622",
"PWY-7900",
"R-DDI-3322077",
"R-DME-189085",
"R-HSA-189085",
"R-HSA-3322077",
"R-HSA-3878781",
"R-HSA-9925561",
"R-MMU-189085",
"R-MMU-3322077",
"R-SCE-3322077"
] | [
"CAZY:GH13",
"EC:2.4.1.18",
"GP:GenProp1483",
"METACYC:PWY-5067",
"METACYC:PWY-622",
"METACYC:PWY-7900",
"REACTOME:R-DDI-3322077",
"REACTOME:R-DME-189085",
"REACTOME:R-HSA-189085",
"REACTOME:R-HSA-3322077",
"REACTOME:R-HSA-3878781",
"REACTOME:R-HSA-9925561",
"REACTOME:R-MMU-189085",
"REACT... | 15 | [
"1a47",
"1aqh",
"1aqm",
"1b0i",
"1b2y",
"1bag",
"1bsi",
"1bvn",
"1c8q",
"1cdg",
"1cgt",
"1cgu",
"1cgv",
"1cgw",
"1cgx",
"1cgy",
"1ciu",
"1clv",
"1cpu",
"1cxe",
"1cxf",
"1cxh",
"1cxi",
"1cxk",
"1cxl",
"1cyg",
"1d3c",
"1d7f",
"1ded",
"1dhk",
"1dtu",
"1eo5"... | 191 | [
"PUB00023681",
"PUB00027252",
"PUB00027666"
] | [
"7877175",
"12196524",
"11141191"
] | [
"Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution.",
"The X-ray crystallographic structure of Escherichia coli branching enzyme.",
"Evolution of alpha-amylases: architectural features and key residues in the stabilization of the (beta/alpha)(8) scaffold."
] | [
1995,
2002,
2001
] | 3 | [] | [
"IPR031319"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
89,
24755,
11338,
290
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
14,
3,
16,
27,
2,
13,
8,
1,
23,
19,
1,
53
] | 12 | true | Domain | Alpha-amylase/branching enzyme, C-terminal all beta | Alpha-amylase/branching enzyme, C-terminal all beta | A-amylase/branching_C | 5 |
IPR006050 | 6,050 | DNA photolyase, N-terminal | DNA_photolyase_N | Domain | 39,930 | false | false | The photolyase/cryptochrome family consists of flavoproteins that perform various functions using blue-light photons as an energie source. It is present in all three domains of life, that is, archaea, eubacteria, and eukaryotes, and hence has arisen very early during evolution to protect genomes against the genotoxic e... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00875",
"PS51645"
] | [
"DNA_photolyase",
"PHR_CRY_ALPHA_BETA"
] | [
39384,
39639
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-432395",
"R-DME-432553",
"R-DME-538864",
"R-HSA-9931510",
"R-HSA-9931521",
"R-HSA-9931530",
"R-HSA-9932298"
] | [
"REACTOME:R-DME-432395",
"REACTOME:R-DME-432553",
"REACTOME:R-DME-538864",
"REACTOME:R-HSA-9931510",
"REACTOME:R-HSA-9931521",
"REACTOME:R-HSA-9931530",
"REACTOME:R-HSA-9932298"
] | 7 | [
"1dnp",
"1iqr",
"1iqu",
"1np7",
"1owl",
"1owm",
"1own",
"1owo",
"1owp",
"1qnf",
"1tez",
"1u3c",
"1u3d",
"2e0i",
"2ijg",
"2j07",
"2j08",
"2j09",
"2j4d",
"2vtb",
"2wb2",
"2wq6",
"2wq7",
"2xry",
"2xrz",
"3cvu",
"3cvv",
"3cvw",
"3cvx",
"3cvy",
"3fy4",
"3umv"... | 174 | [
"PUB00029173",
"PUB00049892",
"PUB00052826",
"PUB00059547",
"PUB00063938",
"PUB00063939",
"PUB00063940"
] | [
"12535521",
"19074258",
"19570997",
"22170053",
"9487120",
"21892138",
"22325881"
] | [
"Identification of a new cryptochrome class. Structure, function, and evolution.",
"Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome.",
"The archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes.",
"Eukaryotic class II cyclobutane pyrimidin... | [
2003,
2008,
2009,
2012,
1998,
2011,
2012
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
822,
20309,
18349,
81,
369
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae... | [
40,
35,
8,
1,
6,
2,
2,
29,
6,
1,
52
] | 11 | true | Domain | DNA photolyase, N-terminal | DNA photolyase, N-terminal | DNA_photolyase_N | 3 |
IPR006052 | 6,052 | Tumour necrosis factor domain | TNF_dom | Domain | 14,469 | false | false | The following cytokines can be grouped into a family on the basis of sequence, functional, and structural similarities [ , , ]: Tumor Necrosis Factor (TNF) (also known as cachectin or TNF-alpha) [ , ] is a cytokine which has a wide variety of functions. It can cause cytolysis of certain tumor cell lines; it is involved... | [
"GO:0005164",
"GO:0006955",
"GO:0016020"
] | [
"tumor necrosis factor receptor binding",
"immune response",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00229",
"PS50049",
"SM00207",
"cd00184"
] | [
"TNF",
"THD_2",
"TNF",
"TNF"
] | [
13498,
13647,
9588,
8117
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00224",
"R-BTA-5668541",
"R-BTA-5669034",
"R-BTA-5676594",
"R-CFA-198933",
"R-CFA-5357786",
"R-CFA-5357905",
"R-CFA-5357956",
"R-CFA-5626978",
"R-CFA-5668541",
"R-CFA-5669034",
"R-CFA-5676594",
"R-CFA-75893",
"R-DME-450520",
"R-GGA-198933",
"R-GGA-5668541",
"R-GGA-5676594",
"R... | [
"PROSITEDOC:PDOC00224",
"REACTOME:R-BTA-5668541",
"REACTOME:R-BTA-5669034",
"REACTOME:R-BTA-5676594",
"REACTOME:R-CFA-198933",
"REACTOME:R-CFA-5357786",
"REACTOME:R-CFA-5357905",
"REACTOME:R-CFA-5357956",
"REACTOME:R-CFA-5626978",
"REACTOME:R-CFA-5668541",
"REACTOME:R-CFA-5669034",
"REACTOME:R... | 78 | [
"1a8m",
"1aly",
"1d0g",
"1d2q",
"1d4v",
"1dg6",
"1du3",
"1i9r",
"1iqa",
"1jh5",
"1jtz",
"1kd7",
"1kxg",
"1oqd",
"1oqe",
"1osg",
"1rj7",
"1rj8",
"1s55",
"1tnf",
"1tnr",
"1u5x",
"1u5y",
"1u5z",
"1xu1",
"1xu2",
"2az5",
"2e7a",
"2hev",
"2hew",
"2hey",
"2o0o"... | 150 | [
"PUB00000299",
"PUB00000886",
"PUB00000899",
"PUB00001264",
"PUB00002011",
"PUB00002042",
"PUB00002689",
"PUB00004130",
"PUB00006091",
"PUB00006095",
"PUB00006098",
"PUB00006101",
"PUB00015257"
] | [
"3061461",
"7916655",
"7505205",
"8076595",
"8777713",
"8095800",
"1850405",
"1377364",
"2989794",
"3349526",
"2777790",
"2268312",
"15335677"
] | [
"The history, properties, and biological effects of cachectin.",
"Lymphotoxin beta, a novel member of the TNF family that forms a heteromeric complex with lymphotoxin on the cell surface.",
"Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family.",
"Molecular ch... | [
1988,
1993,
1993,
1994,
1995,
1993,
1991,
1992,
1985,
1988,
1989,
1990,
1993
] | 13 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Metazoa",
"Viruses"
] | [
4,
14462,
3
] | 3 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
48,
1,
76,
65,
61
] | 5 | true | Domain | Tumour necrosis factor domain | Tumour necrosis factor domain | TNF_dom | 8 |
IPR006053 | 6,053 | Tumour necrosis factor | TNF | Family | 2,326 | false | false | Cytokines can be grouped into a family on the basis of sequence, functional and structural similarities [ , , ]. Tumor necrosis factor (TNF) (also known as TNF-alpha or cachectin) is a monocyte-derived cytotoxin that has been implicated in tumour regression, septic shock and cachexia [ , ]. The protein is synthesised a... | [
"GO:0005164",
"GO:0006955",
"GO:0016020"
] | [
"tumor necrosis factor receptor binding",
"immune response",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01234"
] | [
"TNECROSISFCT"
] | [
2326
] | 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-5668541",
"R-BTA-5669034",
"R-BTA-5676594",
"R-CFA-5357786",
"R-CFA-5357905",
"R-CFA-5357956",
"R-CFA-5626978",
"R-CFA-5668541",
"R-CFA-5669034",
"R-CFA-5676594",
"R-CFA-75893",
"R-HSA-140534",
"R-HSA-3371378",
"R-HSA-381340",
"R-HSA-5213460",
"R-HSA-5218900",
"R-HSA-5357786",... | [
"REACTOME:R-BTA-5668541",
"REACTOME:R-BTA-5669034",
"REACTOME:R-BTA-5676594",
"REACTOME:R-CFA-5357786",
"REACTOME:R-CFA-5357905",
"REACTOME:R-CFA-5357956",
"REACTOME:R-CFA-5626978",
"REACTOME:R-CFA-5668541",
"REACTOME:R-CFA-5669034",
"REACTOME:R-CFA-5676594",
"REACTOME:R-CFA-75893",
"REACTOME:... | 58 | [
"1a8m",
"1tnf",
"1tnr",
"2az5",
"2e7a",
"2o0o",
"2qe3",
"2re9",
"2rjk",
"2rjl",
"2tnf",
"2tun",
"2zjc",
"2zpx",
"3alq",
"3it8",
"3k51",
"3l9j",
"3mi8",
"3wd5",
"4en0",
"4g3y",
"4j6g",
"4kg8",
"4kgg",
"4kgq",
"4msv",
"4mxv",
"4mxw",
"4rsu",
"4tsv",
"4twt"... | 71 | [
"PUB00002042",
"PUB00004130",
"PUB00006091",
"PUB00006095",
"PUB00006098",
"PUB00006101",
"PUB00015257"
] | [
"8095800",
"1377364",
"2989794",
"3349526",
"2777790",
"2268312",
"15335677"
] | [
"A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.",
"Emerging cytokine family.",
"Molecular cloning of mouse tumour necrosis factor cDNA and its eukaryotic expression.",
"A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein:... | [
1993,
1992,
1985,
1988,
1989,
1990,
1993
] | 7 | [] | [
"IPR002959",
"IPR002960",
"IPR002961",
"IPR028326"
] | 0 | 4 | 0 | [
"Chordata"
] | [
2326
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
28,
19,
14
] | 4 | true | Family | Tumour necrosis factor | Tumour necrosis factor | TNF | 1 |
IPR006054 | 6,054 | DNA polymerase III epsilon subunit, exonuclease domain | DnaQ | Domain | 34,434 | false | false | All proteins in this entry for which functions are known are components of the DNA polymerase III complex (epsilon subunit). There is, however, an outgroup that includes paralogs in some gammaproteobacteria and the N-terminal region of DinG from some low GC Gram-positive bacteria. | [
"GO:0003677",
"GO:0003887",
"GO:0006260"
] | [
"DNA binding",
"DNA-directed DNA polymerase activity",
"DNA replication"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00573"
] | [
"dnaq"
] | [
34434
] | 1 | [
"EC"
] | [
"2.7.7.7"
] | [
"EC:2.7.7.7"
] | 1 | [
"1j53",
"1j54",
"2gui",
"2ido",
"2p1j",
"2xy8",
"5fku",
"5fkv",
"5fkw",
"5m1s",
"8h18",
"8h2f",
"8zef",
"9ii8",
"9qpc",
"9qrl",
"9qrn"
] | 17 | [] | [] | [] | [] | 0 | [
"IPR013520"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"unclassified sequences"
] | [
33884,
81,
21,
25,
423
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
1
] | 2 | true | Domain | DNA polymerase III epsilon subunit, exonuclease domain | DNA polymerase III epsilon subunit, exonuclease domain | DnaQ | 8 |
IPR006056 | 6,056 | RidA family | RidA | Family | 25,699 | false | false | This entry represents part of the RidA subfamily. Its members include 2-iminobutanoate/2-iminopropanoate deaminase from mammal and bacteria (RidA) and the yeast Protein HMF1 (YER057C). However, this entry does not include RutC, which is represented in . Mammal RidA, also known as UK114 antigen homolog, catalyses the hy... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00004"
] | [
""
] | [
25699
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00838",
"R-BTA-8849175",
"R-CEL-8849175",
"R-DME-8849175",
"R-HSA-8849175",
"R-MMU-8849175",
"R-RNO-8849175",
"R-SCE-8849175",
"R-SPO-8849175"
] | [
"PROSITEDOC:PDOC00838",
"REACTOME:R-BTA-8849175",
"REACTOME:R-CEL-8849175",
"REACTOME:R-DME-8849175",
"REACTOME:R-HSA-8849175",
"REACTOME:R-MMU-8849175",
"REACTOME:R-RNO-8849175",
"REACTOME:R-SCE-8849175",
"REACTOME:R-SPO-8849175"
] | 9 | [
"1j7h",
"1jd1",
"1nq3",
"1oni",
"1qah",
"1qd9",
"1qu9",
"1x25",
"1xrg",
"2b33",
"2csl",
"2cvl",
"2cw4",
"2cwj",
"2dyy",
"2uyj",
"2uyk",
"2uyn",
"2uyp",
"3k0t",
"3l7q",
"3m1x",
"3m4s",
"3mqw",
"3quw",
"3r0p",
"3vcz",
"5hp7",
"5hp8",
"5v4d",
"5y6u",
"5yu2"... | 51 | [
"PUB00006517",
"PUB00007949",
"PUB00028112",
"PUB00028113",
"PUB00028737",
"PUB00054810",
"PUB00056792",
"PUB00064878",
"PUB00074576",
"PUB00076975",
"PUB00076977",
"PUB00076979",
"PUB00076980",
"PUB00103945",
"PUB00103946"
] | [
"10557275",
"10400702",
"10595546",
"11442631",
"12112709",
"19899170",
"20400551",
"22094463",
"18296521",
"11577990",
"11003673",
"25975565",
"4632080",
"29565811",
"30930054"
] | [
"Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family.",
"Ribonuclease activity of rat liver perchloric acid-soluble protein, a potent inhibitor of protein synthesis.",
"A test case for structure-based functional assignment: the 1.2 A crystal st... | [
1999,
1999,
1999,
2001,
2002,
2010,
2010,
2012,
2008,
2001,
2000,
2015,
1973,
2018,
2019
] | 15 | [
"IPR006175"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
884,
17709,
6786,
1,
319
] | 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",... | [
3,
1,
2,
1,
2,
3,
1,
2,
2,
4,
2,
2,
2
] | 13 | true | Family | RidA family | RidA family | RidA | 7 |
IPR006058 | 6,058 | 2Fe-2S ferredoxin, iron-sulphur binding site | 2Fe2S_fd_BS | Binding_site | 126,283 | false | false | Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions [ , ]; they can be classified into several subgroups according to the nature of their iron-sulphur cluster(s). One group, originally found in chloroplast membranes, has been termed 'chloroplast-type' or 'plant-type' a... | [
"GO:0051537"
] | [
"2 iron, 2 sulfur cluster binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00197"
] | [
"2FE2S_FER_1"
] | [
126283
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00175",
"R-CEL-71403",
"R-CEL-964975",
"R-DDI-71403",
"R-DDI-74259",
"R-DDI-964975",
"R-DDI-9748787",
"R-DME-71403",
"R-DME-74259",
"R-DME-964975",
"R-DME-9748787",
"R-DRE-71403",
"R-GGA-372987",
"R-GGA-421178",
"R-HSA-611105",
"R-HSA-71403",
"R-HSA-74259",
"R-HSA-8851680",
... | [
"PROSITEDOC:PDOC00175",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-964975",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-74259",
"REACTOME:R-DDI-964975",
"REACTOME:R-DDI-9748787",
"REACTOME:R-DME-71403",
"REACTOME:R-DME-74259",
"REACTOME:R-DME-964975",
"REACTOME:R-DME-9748787",
"REACTOME:R-DRE-71403",... | 36 | [
"1a70",
"1awd",
"1czp",
"1dgj",
"1doi",
"1dox",
"1doy",
"1e0z",
"1e10",
"1e7p",
"1ewy",
"1fiq",
"1fo4",
"1frd",
"1frr",
"1fxa",
"1fxi",
"1gaq",
"1iue",
"1j7a",
"1j7b",
"1j7c",
"1jq4",
"1jro",
"1jrp",
"1kf6",
"1kfy",
"1krh",
"1l0v",
"1n5x",
"1off",
"1pfd"... | 265 | [
"PUB00000122",
"PUB00000345",
"PUB00003406",
"PUB00005157"
] | [
"1444257",
"1902376",
"2506358",
"1280857"
] | [
"The electron-transport proteins of hydroxylating bacterial dioxygenases.",
"Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120.",
"Examination of protein sequence homologies: V. New perspectives on evolution between bacterial and chlo... | [
1992,
1991,
1989,
1992
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
1761,
102604,
20524,
59,
4,
1331
] | 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",... | [
55,
5,
5,
10,
6,
16,
23,
3,
33,
27,
1,
1,
90
] | 13 | true | Binding_site | 2Fe-2S ferredoxin, iron-sulphur binding site | 2Fe-2S ferredoxin, iron-sulphur binding site | 2Fe2S_fd_BS | 4 |
IPR006059 | 6,059 | Bacterial-type extracellular solute-binding protein | SBP | Family | 263,060 | false | false | Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one or two transmembrane permease proteins, one or two nucleotide-binding proteins and a highly specific periplasmic solute-bi... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF01547",
"PF13416"
] | [
"SBP_bac_1",
"SBP_bac_8"
] | [
141662,
121409
] | 2 | [
"GP"
] | [
"GenProp1124"
] | [
"GP:GenProp1124"
] | 1 | [
"1a7l",
"1a99",
"1anf",
"1d9v",
"1d9y",
"1dmb",
"1elj",
"1eu8",
"1ez9",
"1ezo",
"1ezp",
"1fqa",
"1fqb",
"1fqc",
"1fqd",
"1hsj",
"1iud",
"1j1n",
"1jvx",
"1jvy",
"1jw4",
"1jw5",
"1kwh",
"1lax",
"1lls",
"1mdp",
"1mdq",
"1mg1",
"1mh3",
"1mh4",
"1mpb",
"1mpc"... | 1,009 | [
"PUB00003346",
"PUB00003610",
"PUB00049123",
"PUB00071925",
"PUB00071938"
] | [
"7853407",
"8336670",
"18177053",
"18310026",
"8003968"
] | [
"Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein.",
"Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria.",
"Structural similarities between thiamin-binding protein and thiaminase-I suggest a comm... | [
1995,
1993,
2008,
2008,
1994
] | 5 | [] | [
"IPR001188",
"IPR006060",
"IPR014597",
"IPR022386",
"IPR022387"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctLeG9",
"unclassified sequences"
] | [
3234,
256638,
1040,
1,
2147
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
2,
8
] | 2 | true | Family | Bacterial-type extracellular solute-binding protein | Bacterial-type extracellular solute-binding protein | SBP | 8 |
IPR006060 | 6,060 | Maltose/Cyclodextrin ABC transporter, substrate-binding protein | Maltose/Cyclodextrin-bd | Family | 6,257 | false | false | Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one or two transmembrane permease proteins, one or two nucleotide-binding proteins and a highly specific periplasmic solute-bi... | [
"GO:0015144",
"GO:0008643"
] | [
"carbohydrate transmembrane transporter activity",
"carbohydrate transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00181"
] | [
"MALTOSEBP"
] | [
6257
] | 1 | [
"GP"
] | [
"GenProp1204"
] | [
"GP:GenProp1204"
] | 1 | [
"1a7l",
"1anf",
"1dmb",
"1elj",
"1ez9",
"1ezo",
"1ezp",
"1fqa",
"1fqb",
"1fqc",
"1fqd",
"1hsj",
"1iud",
"1jvx",
"1jvy",
"1jw4",
"1jw5",
"1lax",
"1lls",
"1mdp",
"1mdq",
"1mg1",
"1mh3",
"1mh4",
"1mpb",
"1mpc",
"1mpd",
"1n3w",
"1n3x",
"1nl5",
"1nmu",
"1omp"... | 634 | [
"PUB00000375",
"PUB00003346",
"PUB00007931",
"PUB00071925",
"PUB00071938",
"PUB00085820",
"PUB00096634"
] | [
"8399200",
"7853407",
"1420181",
"18310026",
"8003968",
"11682178",
"27501980"
] | [
"Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein.",
"Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein.",
"Crystallographic evidence of a large ligand-induced hinge-twist motion between the two dom... | [
1993,
1995,
1992,
2008,
1994,
2001,
2016
] | 7 | [
"IPR006059"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
207,
6016,
9,
25
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Maltose/Cyclodextrin ABC transporter, substrate-binding protein | Maltose/Cyclodextrin ABC transporter, substrate-binding protein | Maltose/Cyclodextrin-bd | 5 |
IPR006061 | 6,061 | Solute-binding family 1, conserved site | SBP_1_CS | Conserved_site | 14,399 | false | false | Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one or two transmembrane permease proteins, one or two nucleotide-binding proteins and a highly specific periplasmic solute-bi... | [
"GO:0055085"
] | [
"transmembrane transport"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS01037"
] | [
"SBP_BACTERIAL_1"
] | [
14399
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00796"
] | [
"PROSITEDOC:PDOC00796"
] | 1 | [
"1a7l",
"1anf",
"1d9v",
"1d9y",
"1dmb",
"1elj",
"1ez9",
"1ezo",
"1ezp",
"1fqa",
"1fqb",
"1fqc",
"1fqd",
"1hsj",
"1iud",
"1jvx",
"1jvy",
"1jw4",
"1jw5",
"1lax",
"1lls",
"1mdp",
"1mdq",
"1mg1",
"1mh3",
"1mh4",
"1mpb",
"1mpc",
"1mpd",
"1mrp",
"1n3w",
"1n3x"... | 682 | [
"PUB00003346",
"PUB00003610",
"PUB00071925",
"PUB00071938"
] | [
"7853407",
"8336670",
"18310026",
"8003968"
] | [
"Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein.",
"Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria.",
"Characterization of a Pseudomonas putida ABC transporter (AatJMQP) required for acidic ... | [
1995,
1993,
2008,
1994
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
97,
14231,
25,
46
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Conserved_site | Solute-binding family 1, conserved site | Solute-binding family 1, conserved site | SBP_1_CS | 3 |
IPR006062 | 6,062 | Histidine biosynthesis protein | His_biosynth | Family | 55,436 | false | false | Histidine is formed by several complex and distinct biochemical reactions catalysed by eight enzymes. Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in one family. These enzymes are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. HisA is a phosphoribosylformi... | [
"GO:0000105"
] | [
"L-histidine biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00977"
] | [
"His_biosynth"
] | [
55436
] | 1 | [] | [] | [] | 0 | [
"1gpw",
"1h5y",
"1jvn",
"1ka9",
"1ox4",
"1ox5",
"1ox6",
"1qo2",
"1thf",
"1vh7",
"1vzw",
"2a0n",
"2agk",
"2cff",
"2lle",
"2rkx",
"2vep",
"2w6r",
"2w79",
"2wjz",
"2x30",
"2y85",
"2y88",
"2y89",
"3cwo",
"3iio",
"3iip",
"3iiv",
"3og3",
"3tdm",
"3tdn",
"3zr4"... | 102 | [] | [] | [] | [] | 0 | [] | [
"IPR004650",
"IPR004651",
"IPR044524"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1916,
46704,
5528,
8,
1280
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
10,
2,
3,
7,
2,
2,
35
] | 7 | true | Family | Histidine biosynthesis protein | Histidine biosynthesis protein | His_biosynth | 1 |
IPR006063 | 6,063 | HisA, bacterial | HisA_bact_arch | Family | 16,412 | false | false | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase ( ), also known as Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase or HisA, catalyses the fourth step in histidine biosynthesis. HisA from Lactococcus lactis was found to be inactive [ ]. The putat... | [
"GO:0003949",
"GO:0000105"
] | [
"1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity",
"L-histidine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR00007"
] | [
""
] | [
16412
] | 1 | [
"EC",
"GP"
] | [
"5.3.1.16",
"GenProp0109"
] | [
"EC:5.3.1.16",
"GP:GenProp0109"
] | 2 | [
"1qo2",
"2cff",
"4gj1",
"5a5w",
"5ab3",
"5abt",
"5ac6",
"5ac7",
"5ac8",
"5ahe",
"5ahf",
"5ahi",
"5g1t",
"5g1y",
"5g2h",
"5g2i",
"5g2w",
"5g4e",
"5g4w",
"5g5i",
"5l6u",
"5l9f"
] | 22 | [
"PUB00008010"
] | [
"7687248"
] | [
"Gene inactivation in Lactococcus lactis: histidine biosynthesis."
] | [
1993
] | 1 | [
"IPR023016"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
635,
15534,
22,
221
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | HisA, bacterial | HisA, bacterial | HisA_bact_arch | 7 |
IPR006064 | 6,064 | Cytokinin glycosidase | Glycosidase | Domain | 468 | false | false | This domain is found in Cytokinin-beta-glucosidases, Protein-tyrosine phosphatase rolB and related proteins. It is also found N-terminal in Tryptophan 2-monooxygenase. These enzymes correspond to Agrobacterium rolC and were characterised along with rolB. RolB and rolC were originally classified as glycoside hydrolase f... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02027"
] | [
"RolB_RolC"
] | [
468
] | 1 | [] | [] | [] | 0 | [
"3aq2",
"3aq3"
] | 2 | [
"PUB00008489"
] | [
"8596628"
] | [
"A plant oncogene as a phosphatase."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Plasmid Ti",
"Pseudomonadota"
] | [
77,
2,
389
] | 3 | [] | [] | 0 | true | Domain | Cytokinin glycosidase | Cytokinin glycosidase | Glycosidase | 2 |
IPR006065 | 6,065 | Glycoside hydrolase, family 41 | Glyco_hydro_41 | Family | 46 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0008422",
"GO:0005975"
] | [
"beta-glucosidase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00746"
] | [
"GLHYDRLASE41"
] | [
46
] | 1 | [
"CAZY",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
... | [
"GH41",
"3.2.1.-",
"PWY-1921",
"PWY-5821",
"PWY-5976",
"PWY-6527",
"PWY-6717",
"PWY-6735",
"PWY-6737",
"PWY-6749",
"PWY-6784",
"PWY-6821",
"PWY-6848",
"PWY-6855",
"PWY-6906",
"PWY-6972",
"PWY-7056",
"PWY-7057",
"PWY-7074",
"PWY-7091",
"PWY-7133",
"PWY-7134",
"PWY-7256",
... | [
"CAZY:GH41",
"EC:3.2.1.-",
"METACYC:PWY-1921",
"METACYC:PWY-5821",
"METACYC:PWY-5976",
"METACYC:PWY-6527",
"METACYC:PWY-6717",
"METACYC:PWY-6735",
"METACYC:PWY-6737",
"METACYC:PWY-6749",
"METACYC:PWY-6784",
"METACYC:PWY-6821",
"METACYC:PWY-6848",
"METACYC:PWY-6855",
"METACYC:PWY-6906",
... | 32 | [] | 0 | [
"PUB00000762",
"PUB00001210",
"PUB00004870",
"PUB00005266"
] | [
"7764693",
"1915268",
"7624375",
"8535779"
] | [
"Nucleotide sequence of the rol region of the mikimopine-type root-inducing plasmid pRi1724.",
"The plant oncogene rolC is responsible for the release of cytokinins from glucoside conjugates.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"S... | [
1994,
1991,
1995,
1995
] | 4 | [] | [] | 0 | 0 | null | [
"Pentapetalae",
"Rhizobium/Agrobacterium group"
] | [
33,
13
] | 2 | [] | [] | 0 | true | Family | Glycoside hydrolase, family 41 | Glycoside hydrolase, family 41 | Glyco_hydro_41 | 7 |
IPR006066 | 6,066 | Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site | NO2/SO3_Rdtase_FeS/sirohaem_BS | Binding_site | 35,839 | false | false | Nitrite reductases and bacterial sulphite reductases catalyse the 6-electron reduction of nitrite (sulphite) to ammonia (sulphide) [ ]. On the basis of physiological function, 2 types of nitrite reductase can be defined: the assimilatory type, which is involved in nitrate assimilation (denitrification); and the dissimi... | [
"GO:0016491",
"GO:0020037",
"GO:0051536"
] | [
"oxidoreductase activity",
"heme binding",
"iron-sulfur cluster binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PRINTS",
"PROSITE"
] | [
"PR00397",
"PS00365"
] | [
"SIROHAEM",
"NIR_SIR"
] | [
33711,
32331
] | 2 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME"
] | [
"1.8.1.2",
"PWY-6683",
"PDOC00314",
"R-MTU-936721"
] | [
"EC:1.8.1.2",
"METACYC:PWY-6683",
"PROSITEDOC:PDOC00314",
"REACTOME:R-MTU-936721"
] | 4 | [
"1aop",
"1zj8",
"1zj9",
"2akj",
"2aop",
"2gep",
"3aop",
"3b0g",
"3b0h",
"3b0j",
"3b0l",
"3b0m",
"3b0n",
"3geo",
"3vkp",
"3vkq",
"3vkr",
"3vks",
"3vkt",
"3vlx",
"3vly",
"3vlz",
"3vm0",
"3vm1",
"4aop",
"4g38",
"4g39",
"4gep",
"4htr",
"5aop",
"5gep",
"5h8v"... | 44 | [
"PUB00002132",
"PUB00002508",
"PUB00005356"
] | [
"1704886",
"2670946",
"2204158"
] | [
"Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite.",
"Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite re... | [
1991,
1989,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1043,
29575,
4947,
274
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
11,
2,
2,
11,
1,
1,
15
] | 7 | true | Binding_site | Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site | Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site | NO2/SO3_Rdtase_FeS/sirohaem_BS | 2 |
IPR006067 | 6,067 | Nitrite/sulphite reductase 4Fe-4S domain | NO2/SO3_Rdtase_4Fe4S_dom | Domain | 53,351 | false | false | Sulphite reductases (SiRs) and related nitrite reductases (NiRs) catalyse the six-electron reduction reactions of sulphite to sulphide, and nitrite to ammonia, respectively. The Escherichia coli SiR enzyme is a complex composed of two proteins, a flavoprotein alpha-component (SiR-FP) and a hemoprotein beta-component (S... | [
"GO:0016491",
"GO:0020037",
"GO:0051536"
] | [
"oxidoreductase activity",
"heme binding",
"iron-sulfur cluster binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PFAM"
] | [
"PF01077"
] | [
"NIR_SIR"
] | [
53351
] | 1 | [
"EC",
"GP",
"GP",
"METACYC",
"REACTOME"
] | [
"1.8.1.2",
"GenProp1554",
"GenProp1746",
"PWY-6683",
"R-MTU-936721"
] | [
"EC:1.8.1.2",
"GP:GenProp1554",
"GP:GenProp1746",
"METACYC:PWY-6683",
"REACTOME:R-MTU-936721"
] | 5 | [
"1aop",
"1zj8",
"1zj9",
"2akj",
"2aop",
"2gep",
"2v4j",
"2xsj",
"3aop",
"3b0g",
"3b0h",
"3b0j",
"3b0l",
"3b0m",
"3b0n",
"3geo",
"3mm5",
"3mm6",
"3mm7",
"3mm8",
"3mm9",
"3mma",
"3mmb",
"3mmc",
"3or1",
"3or2",
"3vkp",
"3vkq",
"3vkr",
"3vks",
"3vkt",
"3vlx"... | 56 | [
"PUB00014351",
"PUB00014496"
] | [
"10984484",
"7569952"
] | [
"A simplifed functional version of the Escherichia coli sulfite reductase.",
"Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions."
] | [
2000,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
1192,
45383,
3,
5210,
1563
] | 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"
] | [
11,
2,
2,
12,
1,
1,
16
] | 7 | true | Domain | Nitrite/sulphite reductase 4Fe-4S domain | Nitrite/sulphite reductase 4Fe-4S domain | NO2/SO3_Rdtase_4Fe4S_dom | 9 |
IPR006068 | 6,068 | Cation-transporting P-type ATPase, C-terminal | ATPase_P-typ_cation-transptr_C | Domain | 97,033 | false | false | This entry represents the conserved C-terminal region found in several classes of cation-transporting P-type ATPases, including those that transport H + ( ), Na + ( ), Ca 2+ ( ), Na + /K + ( ), and H + /K + ( ). In the H + /K + -and Na + /K + -exchange P-ATPases, this domain is found in the catalytic alpha chain. Trans... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00689"
] | [
"Cation_ATPase_C"
] | [
97033
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"7.2.2",
"R-BTA-418359",
"R-BTA-5578775",
"R-BTA-936837",
"R-CEL-418359",
"R-CEL-5578775",
"R-CEL-936837",
"R-CFA-418359",
"R-CFA-5578775",
"R-CFA-936837",
"R-DDI-418359",
"R-DDI-5578775",
"R-DDI-936837",
"R-DME-418359",
"R-DME-5578775",
"R-DME-936837",
"R-GGA-418359",
"R-GGA-55787... | [
"EC:7.2.2",
"REACTOME:R-BTA-418359",
"REACTOME:R-BTA-5578775",
"REACTOME:R-BTA-936837",
"REACTOME:R-CEL-418359",
"REACTOME:R-CEL-5578775",
"REACTOME:R-CEL-936837",
"REACTOME:R-CFA-418359",
"REACTOME:R-CFA-5578775",
"REACTOME:R-CFA-936837",
"REACTOME:R-DDI-418359",
"REACTOME:R-DDI-5578775",
"... | 42 | [
"1iwo",
"1kju",
"1su4",
"1t5s",
"1t5t",
"1vfp",
"1wpg",
"1xp5",
"2agv",
"2by4",
"2c88",
"2c8k",
"2c8l",
"2c9m",
"2dqs",
"2ear",
"2eat",
"2eau",
"2o9j",
"2oa0",
"2voy",
"2xzb",
"2yfy",
"2yn9",
"2zbd",
"2zbe",
"2zbf",
"2zbg",
"2zxe",
"3a3y",
"3ar2",
"3ar3"... | 245 | [
"PUB00009616",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789",
"PUB00160065",
"PUB00160066"
] | [
"9419228",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106",
"37264943",
"37838176"
] | [
"Evolution of substrate specificities in the P-type ATPase superfamily.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases... | [
1998,
2004,
2004,
2010,
2008,
1992,
1998,
2023,
2023
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
927,
32095,
63588,
9,
414
] | 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",... | [
76,
22,
104,
35,
1,
75,
71,
7,
40,
93,
5,
3,
154
] | 13 | true | Domain | Cation-transporting P-type ATPase, C-terminal | Cation-transporting P-type ATPase, C-terminal | ATPase_P-typ_cation-transptr_C | 1 |
IPR006070 | 6,070 | Threonylcarbamoyl-AMP synthase-like domain | Sua5-like_dom | Domain | 54,773 | false | false | This domain has been shown to bind preferentially to dsRNA [ ]. This domain is found in Sua5 ( ) and carbamoyltransferase HypF. The threonylcarbamoyl-AMP synthase Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA [ , ]. Sua5 has been shown to be required for translational regulation [ ] an... | [
"GO:0003725"
] | [
"double-stranded RNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"NCBIFAM"
] | [
"PF01300",
"PS51163",
"TIGR00057"
] | [
"Sua5_yciO_yrdC",
"YRDC",
""
] | [
54682,
54309,
36797
] | 3 | [
"EC",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.87",
"GenProp1060",
"GenProp1570",
"PDOC00883",
"R-BTA-6787450",
"R-HSA-6787450",
"R-MMU-6787450",
"R-RNO-6787450"
] | [
"EC:2.7.7.87",
"GP:GenProp1060",
"GP:GenProp1570",
"PROSITEDOC:PDOC00883",
"REACTOME:R-BTA-6787450",
"REACTOME:R-HSA-6787450",
"REACTOME:R-MMU-6787450",
"REACTOME:R-RNO-6787450"
] | 8 | [
"1hru",
"1jcu",
"1k7j",
"1kk9",
"2eqa",
"2mx1",
"3aje",
"3l7v",
"3tsp",
"3tsq",
"3tsu",
"3ttc",
"3ttd",
"3ttf",
"3vth",
"3vti",
"4e1b",
"4g9i",
"6f87",
"6f89",
"6f8y",
"8ide",
"9dg5",
"9dsq",
"9dsv",
"9dsw"
] | 26 | [
"PUB00011086",
"PUB00054278",
"PUB00063343",
"PUB00063344",
"PUB00163278"
] | [
"11206077",
"19287007",
"20309016",
"19884342",
"37963869"
] | [
"The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding.",
"The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA.",
"Sua5p is required for telomere recombination in Saccharomyces cerevisiae.",
"The Sua5 p... | [
2000,
2009,
2010,
2010,
2023
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Pandoravirus",
"unclassified sequences"
] | [
1358,
45369,
7016,
6,
1024
] | 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",... | [
11,
3,
16,
1,
3,
1,
2,
1,
5,
5,
1,
1,
10
] | 13 | true | Domain | Threonylcarbamoyl-AMP synthase-like domain | Threonylcarbamoyl-AMP synthase-like domain | Sua5-like_dom | 1 |
IPR006072 | 6,072 | Odorant/pheromone binding protein, Lepidoptera | Odorant/phero-bd_Lep | Family | 736 | false | false | Pheromone binding proteins (PBPs) are abundant, secreted antennal proteins present in olfactory sensilla. They lie in the lymph that surrounds the dendrites of olfactory receptor neurons [ ]. The olfactory receptors of terrestrial animals exist in an aqueous environment, yet detect odorants that are primarily hydrophob... | [
"GO:0005549"
] | [
"odorant binding"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF015604",
"PR00484"
] | [
"Odorant/phero_bd",
"PBPGOBP"
] | [
633,
731
] | 2 | [] | [] | [] | 0 | [
"1dqe",
"1gm0",
"1ls8",
"1qwv",
"1two",
"1xfr",
"2fjy",
"2jpo",
"2kph",
"2p70",
"2p71",
"2wc5",
"2wc6",
"2wch",
"2wcj",
"2wck",
"2wcl",
"2wcm",
"4inw",
"4inx",
"6um9",
"6vq5",
"7uo6",
"7vw8",
"7vw9",
"7vwa"
] | 26 | [
"PUB00002853",
"PUB00003450"
] | [
"8206941",
"2010751"
] | [
"Putative Drosophila pheromone-binding proteins expressed in a subregion of the olfactory system.",
"Odorant-binding-protein subfamilies associate with distinct classes of olfactory receptor neurons in insects."
] | [
1994,
1991
] | 2 | [
"IPR006170"
] | [] | 1 | 0 | 1 | [
"Neoptera"
] | [
736
] | 1 | [] | [] | 0 | true | Family | Odorant/pheromone binding protein, Lepidoptera | Odorant/pheromone binding protein, Lepidoptera | Odorant/phero-bd_Lep | 7 |
IPR006073 | 6,073 | GTP binding domain | GTP-bd | Domain | 295,580 | false | false | Several proteins have recently been shown to contain the 5 structural motifs characteristic of GTP-binding proteins [ ]. These include murine DRG protein; GTP1 protein from Schizosaccharomyces pombe; OBG protein from Bacillus subtilis [ ]; ferrous iron transport protein B [ ] and several others. | [
"GO:0005525"
] | [
"GTP binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF01926",
"PR00326"
] | [
"MMR_HSR1",
"GTP1OBG"
] | [
277806,
181355
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9629569",
"R-BTA-9937383",
"R-CEL-114608",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-6791226",
"R-CEL-9937383",
"R-DDI-6791226",
"R-DDI-9629569",
"R-DME-114608",
"R-DME-6791226",
"R-DME-9629569",
"R-DRE-114608",
"R-DRE-5389840",... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9629569",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-5389840",
"REACTOME:R-CEL-5419276",
"REACTOME:R-CEL-6791226",
"REACTOME:R-CEL-9937383",
"REACTOME:R-DDI-6791226",
"REACTOME:... | 44 | [
"1ega",
"1jal",
"1lnz",
"1mky",
"1ni3",
"1pui",
"1puj",
"1rfl",
"1sul",
"1svi",
"1svw",
"1udx",
"1wf3",
"1wxq",
"1x18",
"1x1l",
"1xzp",
"1xzq",
"2cxx",
"2dby",
"2dwq",
"2dyk",
"2e87",
"2gj8",
"2gj9",
"2gja",
"2hjg",
"2ohf",
"2qtf",
"2qth",
"2qu8",
"2wia"... | 304 | [
"PUB00000217",
"PUB00027072",
"PUB00054426"
] | [
"1449490",
"12429099",
"20123128"
] | [
"DRG: a novel developmentally regulated GTP-binding protein.",
"Structural and biochemical analysis of the Obg GTP binding protein.",
"Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB."
] | [
1992,
2002,
2010
] | 3 | [] | [
"IPR031167"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5704,
199168,
86964,
17,
3727
] | 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",... | [
153,
17,
49,
24,
9,
71,
46,
14,
88,
76,
14,
13,
212
] | 13 | true | Domain | GTP binding domain | GTP binding domain | GTP-bd | 9 |
IPR006075 | 6,075 | Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic | Asn/Gln-tRNA_Trfase_suB/E_cat | Domain | 29,653 | false | false | Glutamyl-tRNA(Gln) amidotransferase subunit B ( ) [ ] is a microbial enzyme that furnishes a means for formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP th... | [
"GO:0016874"
] | [
"ligase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02934"
] | [
"GatB_N"
] | [
29653
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"6.3.5.-",
"PWY-5297",
"PWY-7811",
"PWY-8229"
] | [
"EC:6.3.5.-",
"METACYC:PWY-5297",
"METACYC:PWY-7811",
"METACYC:PWY-8229"
] | 4 | [
"1zq1",
"2d6f",
"2df4",
"2dqn",
"2f2a",
"2g5h",
"2g5i",
"3al0",
"3h0l",
"3h0m",
"3h0r",
"3ip4",
"3kfu",
"4n0h",
"4n0i",
"4wj3"
] | 16 | [
"PUB00007932"
] | [
"9342321"
] | [
"Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1757,
22006,
5271,
619
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
3,
1,
1,
2,
8,
3,
1,
2,
7,
1,
1,
6
] | 12 | true | Domain | Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic | Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic | Asn/Gln-tRNA_Trfase_suB/E_cat | 3 |
IPR006076 | 6,076 | FAD dependent oxidoreductase | FAD-dep_OxRdtase | Domain | 246,083 | false | false | null | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01266"
] | [
"DAO"
] | [
246083
] | 1 | [
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1414",
"GenProp1434",
"GenProp1504",
"GenProp1555",
"GenProp1563",
"GenProp1567",
"GenProp1626",
"GenProp1750",
"R-BTA-1483166",
"R-BTA-163560",
"R-BTA-389661",
"R-BTA-71064",
"R-BTA-880009",
"R-BTA-9033241",
"R-CEL-1483166",
"R-CEL-163560",
"R-CEL-389661",
"R-CEL-71064",
... | [
"GP:GenProp1414",
"GP:GenProp1434",
"GP:GenProp1504",
"GP:GenProp1555",
"GP:GenProp1563",
"GP:GenProp1567",
"GP:GenProp1626",
"GP:GenProp1750",
"REACTOME:R-BTA-1483166",
"REACTOME:R-BTA-163560",
"REACTOME:R-BTA-389661",
"REACTOME:R-BTA-71064",
"REACTOME:R-BTA-880009",
"REACTOME:R-BTA-90332... | 58 | [
"1an9",
"1c0i",
"1c0k",
"1c0l",
"1c0p",
"1dao",
"1ddo",
"1el5",
"1el7",
"1el8",
"1el9",
"1eli",
"1evi",
"1kif",
"1l9c",
"1l9d",
"1l9e",
"1ng3",
"1ng4",
"1pj5",
"1pj6",
"1pj7",
"1ryi",
"1ve9",
"1vrq",
"1x31",
"1y56",
"1zov",
"2a89",
"2cvj",
"2du8",
"2e48"... | 180 | [
"PUB00002345",
"PUB00002712"
] | [
"1673125",
"1601857"
] | [
"Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization.",
"The primary structure of the flavoprotein D-aspartate oxidase from beef kidney."
] | [
1991,
1992
] | 2 | [] | [
"IPR017610"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3024,
180779,
59331,
11,
2938
] | 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",... | [
62,
17,
22,
24,
8,
66,
30,
11,
32,
38,
2,
7,
56
] | 13 | true | Domain | FAD dependent oxidoreductase | FAD dependent oxidoreductase | FAD-dep_OxRdtase | 7 |
IPR006077 | 6,077 | Vinculin/alpha-catenin | Vinculin/catenin | Family | 13,904 | false | false | Vinculin is a eukaryotic protein that seems to be involved in the attachment of the actin-based microfilaments to the plasma membrane. Vinculin is located at the cytoplasmic side of focal contacts or adhesion plaques [ ]. In addition to actin, vinculin interacts with other structural proteins such as talin and alpha-ac... | [
"GO:0051015",
"GO:0007155"
] | [
"actin filament binding",
"cell adhesion"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01044"
] | [
"Vinculin"
] | [
13904
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-114608",
"R-CEL-445355",
"R-CEL-5218920",
"R-CEL-5674135",
"R-CEL-6798695",
"R-CEL-9764561",
"R-DME-114608",
"R-DME-418990",
"R-DME-445355",
"R-DME-5218920",
"R-DME-525793",
"R-DME-5674135",
"R-DME-6798695",
"R-DME-9764561",
"R-DME-9766229",
"R-DRE-5218920",
"R-DRE-525793",
... | [
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-445355",
"REACTOME:R-CEL-5218920",
"REACTOME:R-CEL-5674135",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-9764561",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-418990",
"REACTOME:R-DME-445355",
"REACTOME:R-DME-5218920",
"REACTOME:R-DME-525793",
"REACTOME:R-DM... | 73 | [
"1dov",
"1dow",
"1h6g",
"1l7c",
"1qkr",
"1rkc",
"1rke",
"1st6",
"1syq",
"1t01",
"1tr2",
"1u6h",
"1xwj",
"1ydi",
"1zvz",
"1zw2",
"1zw3",
"2gdc",
"2gww",
"2hsq",
"2ibf",
"3h2u",
"3h2v",
"3jbi",
"3jbk",
"3myi",
"3rf3",
"3s90",
"3tj5",
"3tj6",
"3vf0",
"3zdl"... | 72 | [
"PUB00000977",
"PUB00004758"
] | [
"2112986",
"1924379"
] | [
"Vinculin.",
"The uvomorulin-anchorage protein alpha catenin is a vinculin homologue."
] | [
1990,
1991
] | 2 | [] | [
"IPR001033",
"IPR017997"
] | 0 | 2 | 0 | [
"Eukaryota"
] | [
13904
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
16,
12,
61,
23,
28
] | 6 | true | Family | Vinculin/alpha-catenin | Vinculin/alpha-catenin | Vinculin/catenin | 6 |
IPR006079 | 6,079 | Lantibiotic, Type A, Bacillales-type | Lantibiotic_typ-A_Bacillales | Family | 267 | false | false | Lantibiotics are heavily-modified bacteriocin-like peptides from Gram-positive bacteria. They contain alpha,beta-unsaturated amino acids (dehydroalanine and dehydrobutyrine) and lanthionine or 3-methyllanthionine rings (collectively known as thioether rings). There are 2 types of lantibiotic: Type A (which include nisi... | [
"GO:0042742",
"GO:0005576"
] | [
"defense response to bacterium",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PRINTS",
"PRINTS",
"NCBIFAM"
] | [
"PF02052",
"PR00323",
"PR00324",
"TIGR03731"
] | [
"Gallidermin",
"GALLIDERMIN",
"NISIN",
"lantibio_gallid"
] | [
255,
17,
81,
233
] | 4 | [
"GP"
] | [
"GenProp0853"
] | [
"GP:GenProp0853"
] | 1 | [
"1wco",
"6m7y",
"7k1q",
"9g05"
] | 4 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
267
] | 1 | [] | [] | 0 | true | Family | Lantibiotic, Type A, Bacillales-type | Lantibiotic, Type A, Bacillales-type | Lantibiotic_typ-A_Bacillales | 7 |
IPR006080 | 6,080 | Beta/alpha-defensin, C-terminal | Beta/alpha-defensin_C | Domain | 516 | false | false | This is a cysteine-rich domain found at the C-terminal end of alpha and beta defensins mainly from mammals that lyse bacteria, fungi and enveloped viruses by forming multimeric membrane-spanning channels. Defensins are 2-6kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria,... | [
"GO:0006952",
"GO:0005576"
] | [
"defense response",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"SMART"
] | [
"SM00048"
] | [
"DEFSN"
] | [
516
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-1461957",
"R-BTA-1461973",
"R-HSA-1461957",
"R-HSA-1461973",
"R-HSA-1462054",
"R-HSA-6798695",
"R-HSA-9841251",
"R-MMU-1461973",
"R-MMU-1462054",
"R-MMU-6798695",
"R-RNO-1461973",
"R-RNO-1462054",
"R-RNO-6798695",
"R-SSC-1461957"
] | [
"REACTOME:R-BTA-1461957",
"REACTOME:R-BTA-1461973",
"REACTOME:R-HSA-1461957",
"REACTOME:R-HSA-1461973",
"REACTOME:R-HSA-1462054",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9841251",
"REACTOME:R-MMU-1461973",
"REACTOME:R-MMU-1462054",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-1461973",
"REACTOM... | 14 | [
"1bnb",
"1dfn",
"1e4q",
"1fd3",
"1fd4",
"1fqq",
"1tv0",
"1zmh",
"1zmi",
"1zmk",
"1zmm",
"1zmp",
"1zmq",
"2gw9",
"2gwp",
"2k1i",
"2kht",
"2lew",
"2ley",
"2lxo",
"2lxz",
"2mit",
"2pm1",
"2pm4",
"2pm5",
"3gny",
"3go0",
"3h6c",
"3hj2",
"3hjd",
"3i5w",
"3lo1"... | 61 | [
"PUB00001093",
"PUB00053764",
"PUB00053765"
] | [
"8528769",
"15616305",
"15620707"
] | [
"Structure, function, and membrane integration of defensins.",
"Antibacterial activity and specificity of the six human {alpha}-defensins.",
"Human neutrophil alpha-defensin 4 inhibits HIV-1 infection in vitro."
] | [
1995,
2005,
2005
] | 3 | [] | [
"IPR006081"
] | 0 | 1 | 0 | [
"Bilateria"
] | [
516
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
36,
13
] | 3 | true | Domain | Beta/alpha-defensin, C-terminal | Beta/alpha-defensin, C-terminal | Beta/alpha-defensin_C | 7 |
IPR006081 | 6,081 | Alpha-defensin, C-terminal | Alpha-defensin_C | Domain | 443 | false | false | This entry represents the C-terminal domain of a group of alpha-defensins and similar sequences mainly found in mammals. Defensins are 2-6kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses [ , ] containing three pairs of intramolecular disulph... | [
"GO:0006952",
"GO:0005576"
] | [
"defense response",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PROSITE"
] | [
"PF00323",
"PS00269"
] | [
"Defensin_1",
"DEFENSIN"
] | [
357,
409
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00242",
"R-HSA-1461973",
"R-HSA-1462054",
"R-HSA-6798695",
"R-HSA-9841251",
"R-MMU-1461973",
"R-MMU-1462054",
"R-MMU-6798695",
"R-RNO-1461973",
"R-RNO-1462054",
"R-RNO-6798695"
] | [
"PROSITEDOC:PDOC00242",
"REACTOME:R-HSA-1461973",
"REACTOME:R-HSA-1462054",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9841251",
"REACTOME:R-MMU-1461973",
"REACTOME:R-MMU-1462054",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-1461973",
"REACTOME:R-RNO-1462054",
"REACTOME:R-RNO-6798695"
] | 11 | [
"1dfn",
"1tv0",
"1zmh",
"1zmi",
"1zmk",
"1zmm",
"1zmp",
"1zmq",
"2gw9",
"2gwp",
"2k1i",
"2kht",
"2lxz",
"2mit",
"2mxq",
"2pm1",
"2pm4",
"2pm5",
"3gny",
"3go0",
"3h6c",
"3hj2",
"3hjd",
"3i5w",
"3lo1",
"3lo2",
"3lo4",
"3lo6",
"3lo9",
"3loe",
"3lvx",
"3qte"... | 50 | [
"PUB00001093",
"PUB00100838"
] | [
"8528769",
"30658057"
] | [
"Structure, function, and membrane integration of defensins.",
"Systematic mutational analysis of human neutrophil α-defensin HNP4."
] | [
1995,
2019
] | 2 | [
"IPR006080"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
10,
433
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
30,
17
] | 3 | true | Domain | Alpha-defensin, C-terminal | Alpha-defensin, C-terminal | Alpha-defensin_C | 5 |
IPR006082 | 6,082 | Phosphoribulokinase | PRK | Family | 6,273 | false | false | Phosphoribulokinase (PRK) catalyses the ATP-dependent phosphorylation of ribulose-5-phosphate to ribulose-1,5-phosphate, a key step in the pentose phosphate pathway where carbon dioxide is assimilated by autotrophic organisms [ ]. In general, plant enzymes are light-activated by the thioredoxin/ferredoxin system, while... | [
"GO:0005524",
"GO:0008974",
"GO:0005975"
] | [
"ATP binding",
"phosphoribulokinase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS",
"PROSITE"
] | [
"PR00478",
"PS00567"
] | [
"PHRIBLKINASE",
"PHOSPHORIBULOKINASE"
] | [
6194,
5032
] | 2 | [
"EC",
"METACYC",
"PROSITEDOC"
] | [
"2.7.1.19",
"PWY-5723",
"PDOC00490"
] | [
"EC:2.7.1.19",
"METACYC:PWY-5723",
"PROSITEDOC:PDOC00490"
] | 3 | [
"1a7j",
"5b3f",
"6gve",
"6h7g",
"6h7h",
"6hzk",
"6hzl",
"6kev",
"6kew",
"6kex",
"6kez"
] | 11 | [
"PUB00000332",
"PUB00002460"
] | [
"2175647",
"2826432"
] | [
"The form II fructose 1,6-bisphosphatase and phosphoribulokinase genes form part of a large operon in Rhodobacter sphaeroides: primary structure and insertional mutagenesis analysis.",
"Characterization of the regulatory thioredoxin site of phosphoribulokinase."
] | [
1990,
1988
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
61,
4698,
1421,
2,
91
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
2,
1,
6,
11
] | 4 | true | Family | Phosphoribulokinase | Phosphoribulokinase | PRK | 4 |
IPR006083 | 6,083 | Phosphoribulokinase/uridine kinase | PRK/URK | Domain | 51,598 | false | false | Phosphoribulokinase (PRK) catalyses the ATP-dependent phosphorylation of ribulose-5-phosphate to ribulose-1,5-phosphate, a key step in the pentose phosphate pathway where carbon dioxide is assimilated by autotrophic organisms [ ]. In general, plant enzymes are light-activated by the thioredoxin/ferredoxin system, while... | [
"GO:0005524",
"GO:0016301"
] | [
"ATP binding",
"kinase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00485"
] | [
"PRK"
] | [
51598
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1",
"GenProp1747",
"R-CEL-73614",
"R-DDI-196807",
"R-DDI-73614",
"R-DME-73614",
"R-DRE-73614",
"R-HSA-73614",
"R-MMU-73614",
"R-RNO-73614",
"R-SCE-73614",
"R-SPO-73614",
"R-XTR-73614"
] | [
"EC:2.7.1",
"GP:GenProp1747",
"REACTOME:R-CEL-73614",
"REACTOME:R-DDI-196807",
"REACTOME:R-DDI-73614",
"REACTOME:R-DME-73614",
"REACTOME:R-DRE-73614",
"REACTOME:R-HSA-73614",
"REACTOME:R-MMU-73614",
"REACTOME:R-RNO-73614",
"REACTOME:R-SCE-73614",
"REACTOME:R-SPO-73614",
"REACTOME:R-XTR-73614... | 13 | [
"1a7j",
"1esm",
"1esn",
"1rz3",
"1sq5",
"1udw",
"1uei",
"1uej",
"1ufq",
"1uj2",
"1xrj",
"2ges",
"2get",
"2geu",
"2gev",
"2jeo",
"2uvq",
"2zs7",
"2zs8",
"2zs9",
"2zsa",
"2zsb",
"2zsd",
"2zse",
"2zsf",
"3aez",
"3af0",
"3af1",
"3af2",
"3af3",
"3af4",
"3asy"... | 71 | [
"PUB00000332"
] | [
"2175647"
] | [
"The form II fructose 1,6-bisphosphatase and phosphoribulokinase genes form part of a large operon in Rhodobacter sphaeroides: primary structure and insertional mutagenesis analysis."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
282,
30758,
20055,
34,
469
] | 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",... | [
55,
5,
16,
6,
3,
10,
14,
2,
28,
16,
3,
3,
76
] | 13 | true | Domain | Phosphoribulokinase/uridine kinase | Phosphoribulokinase/uridine kinase | PRK/URK | 5 |
IPR006085 | 6,085 | XPG, N-terminal | XPG_DNA_repair_N | Domain | 22,935 | false | false | Xeroderma pigmentosum (XP) [ ] is a human autosomal recessive disease, characterised by a high incidence of sunlight-induced skin cancer. People's skin cells with this condition are hypersensitive to ultraviolet light, due to defects in the incision step of DNA excision repair. There are a minimum of seven genetic comp... | [
"GO:0004518"
] | [
"nuclease activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF00752",
"SM00485"
] | [
"XPG_N",
"XPGN"
] | [
22625,
20576
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00658",
"R-BTA-110362",
"R-BTA-174437",
"R-BTA-5651801",
"R-BTA-5685939",
"R-BTA-69166",
"R-CEL-5651801",
"R-CEL-5685939",
"R-CEL-69166",
"R-DDI-110362",
"R-DDI-5358565",
"R-DDI-5651801",
"R-DDI-69166",
"R-DME-5358565",
"R-DME-5651801",
"R-DME-5685939",
"R-DME-5693607",
"R-DME... | [
"PROSITEDOC:PDOC00658",
"REACTOME:R-BTA-110362",
"REACTOME:R-BTA-174437",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5685939",
"REACTOME:R-BTA-69166",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-5685939",
"REACTOME:R-CEL-69166",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-5358565",
"REACTOME:R-DDI-5... | 82 | [
"1a76",
"1a77",
"1b43",
"1mc8",
"1rxv",
"1rxw",
"1ul1",
"2izo",
"3ory",
"3q8k",
"3q8l",
"3q8m",
"3qe9",
"3qea",
"3qeb",
"4q0r",
"4q0w",
"4q0z",
"4q10",
"4wa8",
"5cnq",
"5co8",
"5fv7",
"5k97",
"5kse",
"5t9j",
"5um9",
"5uzv",
"5v04",
"5v05",
"5v06",
"5v07"... | 72 | [
"PUB00002851",
"PUB00004160",
"PUB00004189",
"PUB00004415",
"PUB00005433",
"PUB00097845"
] | [
"8206890",
"8247134",
"8090225",
"8464724",
"8160271",
"32821917"
] | [
"Isolation of active recombinant XPG protein, a human DNA repair endonuclease.",
"Yeast excision repair gene RAD2 encodes a single-stranded DNA endonuclease.",
"XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair.",
"Evolutionary conservation of excision repair in Schizosaccharomyce... | [
1994,
1993,
1994,
1993,
1994,
2020
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
969,
3,
21570,
184,
209
] | 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... | [
41,
4,
15,
8,
24,
22,
5,
12,
12,
6,
5,
42
] | 12 | true | Domain | XPG, N-terminal | XPG, N-terminal | XPG_DNA_repair_N | 1 |
IPR006086 | 6,086 | XPG-I domain | XPG-I_dom | Domain | 24,161 | false | false | This entry represents a domain found on Xeroderma Pigmentosum Complementation Group G (XPG) protein [ ]. XPG is a DNA endonuclease involved in DNA excision repair [ ]. The internal XPG (XPG-I) domain contains many cysteine and glutamate amino acid residues that are frequently found in various enzyme active sites of DNA... | [
"GO:0004518"
] | [
"nuclease activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF00867",
"SM00484"
] | [
"XPG_I",
"XPGI"
] | [
23961,
22868
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00658",
"R-BTA-110362",
"R-BTA-174437",
"R-BTA-5651801",
"R-BTA-5685939",
"R-BTA-69166",
"R-CEL-5651801",
"R-CEL-5685939",
"R-CEL-69166",
"R-DDI-110362",
"R-DDI-5358565",
"R-DDI-5651801",
"R-DDI-69166",
"R-DME-5358565",
"R-DME-5651801",
"R-DME-5685939",
"R-DME-5693607",
"R-DME... | [
"PROSITEDOC:PDOC00658",
"REACTOME:R-BTA-110362",
"REACTOME:R-BTA-174437",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5685939",
"REACTOME:R-BTA-69166",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-5685939",
"REACTOME:R-CEL-69166",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-5358565",
"REACTOME:R-DDI-5... | 82 | [
"1a76",
"1a77",
"1b43",
"1mc8",
"1rxv",
"1rxw",
"1ul1",
"2izo",
"3ory",
"3q8k",
"3q8l",
"3q8m",
"3qe9",
"3qea",
"3qeb",
"4q0r",
"4q0w",
"4q0z",
"4q10",
"4wa8",
"5cnq",
"5co8",
"5fv7",
"5k97",
"5kse",
"5t9j",
"5um9",
"5uzv",
"5v04",
"5v05",
"5v06",
"5v07"... | 72 | [
"PUB00002851",
"PUB00062818",
"PUB00075589"
] | [
"8206890",
"14726017",
"8078765"
] | [
"Isolation of active recombinant XPG protein, a human DNA repair endonuclease.",
"The XPG story.",
"Human xeroderma pigmentosum group G gene encodes a DNA endonuclease."
] | [
1994,
2003,
1994
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
972,
4,
22445,
515,
225
] | 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... | [
42,
4,
15,
9,
16,
21,
5,
12,
9,
6,
4,
50
] | 12 | true | Domain | XPG-I domain | XPG-I domain | XPG-I_dom | 4 |
IPR006089 | 6,089 | Acyl-CoA dehydrogenase, conserved site | Acyl-CoA_DH_CS | Conserved_site | 142,921 | false | false | Mammalian Co-A dehydrogenases ( ) are enzymes that catalyse the first step in each cycle of beta-oxidation in mitochondion. Acyl-CoA dehydrogenases [ , , ] catalyze the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. Re... | [
"GO:0003995"
] | [
"acyl-CoA dehydrogenase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00072",
"PS00073"
] | [
"ACYL_COA_DH_1",
"ACYL_COA_DH_2"
] | [
92921,
116999
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.3.8",
"PDOC00070",
"R-BTA-70895",
"R-BTA-71064",
"R-BTA-77288",
"R-BTA-77305",
"R-BTA-77346",
"R-BTA-77348",
"R-BTA-9837999",
"R-CEL-71064",
"R-DDI-70895",
"R-DDI-71064",
"R-DDI-9837999",
"R-DME-77288",
"R-DME-77346",
"R-DME-77348",
"R-HSA-1989781",
"R-HSA-381038",
"R-HSA-6799... | [
"EC:1.3.8",
"PROSITEDOC:PDOC00070",
"REACTOME:R-BTA-70895",
"REACTOME:R-BTA-71064",
"REACTOME:R-BTA-77288",
"REACTOME:R-BTA-77305",
"REACTOME:R-BTA-77346",
"REACTOME:R-BTA-77348",
"REACTOME:R-BTA-9837999",
"REACTOME:R-CEL-71064",
"REACTOME:R-DDI-70895",
"REACTOME:R-DDI-71064",
"REACTOME:R-DD... | 59 | [
"1buc",
"1egc",
"1egd",
"1ege",
"1ivh",
"1jqi",
"1rx0",
"1siq",
"1sir",
"1t9g",
"1udy",
"1ukw",
"1ws9",
"2a1t",
"2cx9",
"2d29",
"2dvl",
"2eba",
"2ix5",
"2ix6",
"2jif",
"2pg0",
"2r0m",
"2r0n",
"2uxw",
"2vig",
"2z1q",
"3b96",
"3d6b",
"3djl",
"3eom",
"3eon"... | 90 | [
"PUB00001328",
"PUB00002511",
"PUB00002861",
"PUB00007933"
] | [
"3326738",
"2777793",
"8034667",
"8356049"
] | [
"Molecular basis of isovaleric acidemia and medium-chain acyl-CoA dehydrogenase deficiency.",
"Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of t... | [
1987,
1989,
1994,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured marine phage"
] | [
2431,
110888,
28010,
1591,
1
] | 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",... | [
11,
17,
16,
10,
3,
100,
26,
3,
12,
44,
28
] | 11 | true | Conserved_site | Acyl-CoA dehydrogenase, conserved site | Acyl-CoA dehydrogenase, conserved site | Acyl-CoA_DH_CS | 9 |
IPR006091 | 6,091 | Acyl-CoA dehydrogenase/oxidase, middle domain | AcylCoA_DH/ox_M | Domain | 284,928 | false | false | This entry represents the middle domain in medium chain acyl-CoA dehydrogenases, as well as in the related peroxisomal acyl-CoA oxidase-II enzymes. Acyl-CoA oxidase (ACO; ) catalyses the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids [ ]. Acyl-CoA dehydrogenases ( ) are a family of fla... | [
"GO:0016627"
] | [
"oxidoreductase activity, acting on the CH-CH group of donors"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02770"
] | [
"Acyl-CoA_dh_M"
] | [
284928
] | 1 | [
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1308",
"GenProp1510",
"GenProp1533",
"GenProp1544",
"GenProp1562",
"GenProp1572",
"GenProp1673",
"GenProp1717",
"R-BTA-2046106",
"R-BTA-390247",
"R-BTA-70895",
"R-BTA-71064",
"R-BTA-77288",
"R-BTA-77305",
"R-BTA-77346",
"R-BTA-77348",
"R-BTA-9033241",
"R-BTA-9837999",
"R-... | [
"GP:GenProp1308",
"GP:GenProp1510",
"GP:GenProp1533",
"GP:GenProp1544",
"GP:GenProp1562",
"GP:GenProp1572",
"GP:GenProp1673",
"GP:GenProp1717",
"REACTOME:R-BTA-2046106",
"REACTOME:R-BTA-390247",
"REACTOME:R-BTA-70895",
"REACTOME:R-BTA-71064",
"REACTOME:R-BTA-77288",
"REACTOME:R-BTA-77305",... | 91 | [
"1buc",
"1egc",
"1egd",
"1ege",
"1is2",
"1ivh",
"1jqi",
"1r2j",
"1rx0",
"1siq",
"1sir",
"1t9g",
"1udy",
"1ukw",
"1w07",
"1ws9",
"2a1t",
"2cx9",
"2d29",
"2ddh",
"2dvl",
"2eba",
"2fon",
"2ix5",
"2ix6",
"2jif",
"2pg0",
"2r0m",
"2r0n",
"2uxw",
"2vig",
"2wbi"... | 162 | [
"PUB00013228",
"PUB00013229",
"PUB00026133"
] | [
"11812788",
"9214289",
"11872165"
] | [
"Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.",
"Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.",
"Three-dimensional structure of the flavoenzyme acyl-... | [
2002,
1997,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
3680,
226719,
50941,
2,
6,
3580
] | 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",... | [
34,
19,
26,
20,
4,
100,
38,
7,
23,
68,
1,
79
] | 12 | true | Domain | Acyl-CoA dehydrogenase/oxidase, middle domain | Acyl-CoA dehydrogenase/oxidase, middle domain | AcylCoA_DH/ox_M | 9 |
IPR006093 | 6,093 | Oxygen oxidoreductase covalent FAD-binding site | Oxy_OxRdtase_FAD_BS | Binding_site | 19,525 | false | false | This entry represents the conserved region around the histidine that binds the FAD group, which is conserved in these enzymes. Some oxygen-dependent oxidoreductases are flavoproteins that contain a covalently bound FAD group which is attached to a histidine via an 8-alpha- (N3-histidyl)-riboflavin linkage. These protei... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00862"
] | [
"OX2_COVAL_FAD"
] | [
19525
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00674"
] | [
"PROSITEDOC:PDOC00674"
] | 1 | [
"1w1o",
"1w1q",
"1w1r",
"1w1s",
"1zr6",
"2axr",
"2bvf",
"2bvg",
"2bvh",
"2qkn",
"2qpm",
"2y08",
"2y3r",
"2y3s",
"2y4g",
"3bw7",
"3c0p",
"3d2d",
"3d2h",
"3d2j",
"3dq0",
"3fw8",
"3fw9",
"3fwa",
"3gsy",
"3hsu",
"3kjm",
"3pop",
"3pqb",
"3s1c",
"3s1d",
"3s1e"... | 69 | [
"PUB00001355",
"PUB00002249",
"PUB00002469",
"PUB00004761",
"PUB00010580"
] | [
"3622516",
"7517396",
"3338984",
"1946465",
"10094636"
] | [
"6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase.",
"Cloning and analysis of a locus (mcr) involved in mitomycin C resistance in Streptomyces lavendulae.",
"Isolation and sequence analysis of a complementary DNA encodin... | [
1987,
1994,
1988,
1991,
1998
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
238,
10640,
8609,
38
] | 4 | [
"Arabidopsis thaliana",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
40,
2,
2,
20,
3,
1,
36
] | 7 | true | Binding_site | Oxygen oxidoreductase covalent FAD-binding site | Oxygen oxidoreductase covalent FAD-binding site | Oxy_OxRdtase_FAD_BS | 6 |
IPR006095 | 6,095 | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase | Glu/Leu/Phe/Val/Trp_DH | Family | 45,046 | false | false | Glutamate, leucine, phenylalanine, valine and tryptophan dehydrogenases are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction. Glutamate dehydrogenases ( ... | [
"GO:0016491",
"GO:0006520"
] | [
"oxidoreductase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00082"
] | [
"GLFDHDRGNASE"
] | [
45046
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.4.1",
"PDOC00071",
"R-DDI-2151201",
"R-DDI-8964539",
"R-DDI-9837999",
"R-DME-2151201",
"R-DME-8964539",
"R-DME-9837999",
"R-HSA-2151201",
"R-HSA-8964539",
"R-HSA-9837999",
"R-MMU-2151201",
"R-MMU-8964539",
"R-MMU-9837999",
"R-RNO-2151201",
"R-RNO-8964539",
"R-RNO-9837999",
"R-SS... | [
"EC:1.4.1",
"PROSITEDOC:PDOC00071",
"REACTOME:R-DDI-2151201",
"REACTOME:R-DDI-8964539",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-2151201",
"REACTOME:R-DME-8964539",
"REACTOME:R-DME-9837999",
"REACTOME:R-HSA-2151201",
"REACTOME:R-HSA-8964539",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-2151201"... | 20 | [
"1aup",
"1b26",
"1b3b",
"1bgv",
"1bvu",
"1bw9",
"1bxg",
"1c1d",
"1c1x",
"1euz",
"1gtm",
"1hrd",
"1hwy",
"1k89",
"1l1f",
"1leh",
"1nqt",
"1nr1",
"1nr7",
"1v9l",
"2bma",
"2tmg",
"2yfh",
"2yfq",
"3aoe",
"3aog",
"3etd",
"3ete",
"3etg",
"3jcz",
"3jd0",
"3jd1"... | 142 | [
"PUB00000302",
"PUB00001430",
"PUB00002221",
"PUB00002347",
"PUB00002418",
"PUB00003424",
"PUB00004656",
"PUB00101895",
"PUB00101896"
] | [
"3069133",
"1358610",
"8320231",
"1880121",
"2989290",
"8315654",
"3368458",
"27815281",
"24835098"
] | [
"Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases.",
"Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases.",
"Sequence, transcriptional, and function... | [
1988,
1992,
1993,
1991,
1985,
1993,
1988,
2017,
2014
] | 9 | [] | [
"IPR014362",
"IPR016211"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1493,
33302,
9686,
6,
559
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
20,
1,
2,
5,
1,
14,
2,
1,
7,
3,
2,
1,
25
] | 13 | true | Family | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase | Glu/Leu/Phe/Val/Trp_DH | 7 |
IPR006096 | 6,096 | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal | Glu/Leu/Phe/Val/Trp_DH_C | Domain | 51,350 | false | false | Glutamate, leucine, phenylalanine, valine and tryptophan dehydrogenases are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction. Glutamate dehydrogenases ( ... | [
"GO:0016491",
"GO:0006520"
] | [
"oxidoreductase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF00208",
"SM00839"
] | [
"ELFV_dehydrog",
"ELFV_dehydrog"
] | [
51281,
48989
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.4.1",
"GenProp1288",
"GenProp1472",
"GenProp1554",
"R-DDI-2151201",
"R-DDI-8964539",
"R-DDI-9837999",
"R-DME-2151201",
"R-DME-8964539",
"R-DME-9837999",
"R-HSA-2151201",
"R-HSA-8964539",
"R-HSA-9837999",
"R-MMU-2151201",
"R-MMU-8964539",
"R-MMU-9837999",
"R-RNO-2151201",
"R-RNO-... | [
"EC:1.4.1",
"GP:GenProp1288",
"GP:GenProp1472",
"GP:GenProp1554",
"REACTOME:R-DDI-2151201",
"REACTOME:R-DDI-8964539",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-2151201",
"REACTOME:R-DME-8964539",
"REACTOME:R-DME-9837999",
"REACTOME:R-HSA-2151201",
"REACTOME:R-HSA-8964539",
"REACTOME:R-HSA-98... | 22 | [
"1aup",
"1b26",
"1b3b",
"1bgv",
"1bvu",
"1bw9",
"1bxg",
"1c1d",
"1c1x",
"1euz",
"1gtm",
"1hrd",
"1hwy",
"1k89",
"1l1f",
"1leh",
"1nqt",
"1nr1",
"1nr7",
"1v9l",
"2bma",
"2tmg",
"2yfh",
"2yfq",
"3aoe",
"3aog",
"3etd",
"3ete",
"3etg",
"3jcz",
"3jd0",
"3jd1"... | 149 | [
"PUB00000302",
"PUB00001430",
"PUB00002221",
"PUB00002347",
"PUB00002418",
"PUB00003424",
"PUB00004656",
"PUB00101895",
"PUB00101896"
] | [
"3069133",
"1358610",
"8320231",
"1880121",
"2989290",
"8315654",
"3368458",
"27815281",
"24835098"
] | [
"Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases.",
"Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases.",
"Sequence, transcriptional, and function... | [
1988,
1992,
1993,
1991,
1985,
1993,
1988,
2017,
2014
] | 9 | [] | [
"IPR033922"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1841,
35739,
13053,
14,
703
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
21,
1,
2,
5,
1,
14,
3,
2,
6,
3,
3,
2,
26
] | 13 | true | Domain | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal | Glu/Leu/Phe/Val/Trp_DH_C | 3 |
IPR006097 | 6,097 | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain | Glu/Leu/Phe/Val/Trp_DH_dimer | Domain | 48,520 | false | false | Glutamate, leucine, phenylalanine, valine and tryptophan dehydrogenases are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction. Glutamate dehydrogenases ( ... | [
"GO:0016491",
"GO:0006520"
] | [
"oxidoreductase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF02812"
] | [
"ELFV_dehydrog_N"
] | [
48520
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.4.1",
"GenProp1288",
"GenProp1472",
"GenProp1554",
"R-DDI-2151201",
"R-DDI-8964539",
"R-DDI-9837999",
"R-DME-2151201",
"R-DME-8964539",
"R-DME-9837999",
"R-HSA-2151201",
"R-HSA-8964539",
"R-HSA-9837999",
"R-MMU-2151201",
"R-MMU-8964539",
"R-MMU-9837999",
"R-RNO-2151201",
"R-RNO-... | [
"EC:1.4.1",
"GP:GenProp1288",
"GP:GenProp1472",
"GP:GenProp1554",
"REACTOME:R-DDI-2151201",
"REACTOME:R-DDI-8964539",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-2151201",
"REACTOME:R-DME-8964539",
"REACTOME:R-DME-9837999",
"REACTOME:R-HSA-2151201",
"REACTOME:R-HSA-8964539",
"REACTOME:R-HSA-98... | 22 | [
"1aup",
"1b26",
"1b3b",
"1bgv",
"1bvu",
"1bw9",
"1bxg",
"1c1d",
"1c1x",
"1euz",
"1gtm",
"1hrd",
"1hwy",
"1k89",
"1l1f",
"1leh",
"1nqt",
"1nr1",
"1nr7",
"1v9l",
"2bma",
"2tmg",
"2yfh",
"2yfq",
"3aoe",
"3aog",
"3etd",
"3ete",
"3etg",
"3jcz",
"3jd0",
"3jd1"... | 144 | [
"PUB00000302",
"PUB00001430",
"PUB00002221",
"PUB00002347",
"PUB00002418",
"PUB00003424",
"PUB00004656",
"PUB00101895",
"PUB00101896"
] | [
"3069133",
"1358610",
"8320231",
"1880121",
"2989290",
"8315654",
"3368458",
"27815281",
"24835098"
] | [
"Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases.",
"Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases.",
"Sequence, transcriptional, and function... | [
1988,
1992,
1993,
1991,
1985,
1993,
1988,
2017,
2014
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1521,
35018,
11377,
6,
598
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
21,
1,
2,
4,
1,
18,
1,
1,
8,
4,
2,
1,
30
] | 13 | true | Domain | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain | Glu/Leu/Phe/Val/Trp_DH_dimer | 4 |
IPR006098 | 6,098 | Methylmalonyl-CoA mutase, alpha chain, catalytic | MMCoA_mutase_a_cat | Domain | 22,368 | false | false | Methylmalonyl-CoA mutase ( ) (MCM) [ ] is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyses the isomerization between methylmalonyl-CoA and succinyl-CoA. MCM is involved in various catabolic or biosynthetic pathways; for example in human it is involved in the degradation of several amino acids, odd-cha... | [
"GO:0004494",
"GO:0031419"
] | [
"methylmalonyl-CoA mutase activity",
"cobalamin binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR00641"
] | [
"acid_CoA_mut_N"
] | [
22368
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.4.99.2",
"GenProp1439",
"GenProp1629",
"GenProp1723",
"PWY-5743",
"PWY-5789",
"PWY-6728",
"PWY-7384",
"PWY-7854",
"PWY-8086",
"R-CEL-71032",
"R-CEL-9759218",
"R-HSA-3359475",
"R-HSA-3359478",
"R-HSA-71032",
"R-HSA-9759218",
"R-MMU-71032",
"R-MMU-9759218"
] | [
"EC:5.4.99.2",
"GP:GenProp1439",
"GP:GenProp1629",
"GP:GenProp1723",
"METACYC:PWY-5743",
"METACYC:PWY-5789",
"METACYC:PWY-6728",
"METACYC:PWY-7384",
"METACYC:PWY-7854",
"METACYC:PWY-8086",
"REACTOME:R-CEL-71032",
"REACTOME:R-CEL-9759218",
"REACTOME:R-HSA-3359475",
"REACTOME:R-HSA-3359478",... | 18 | [
"1e1c",
"1req",
"2req",
"2xij",
"2xiq",
"3bic",
"3req",
"4r3u",
"4req",
"4xc6",
"4xc7",
"4xc8",
"5cjt",
"5cju",
"5cjv",
"5cjw",
"5req",
"6oxc",
"6oxd",
"6req",
"7req",
"8dyj",
"8dyl",
"8gju",
"8ssl",
"8sta"
] | 26 | [
"PUB00000715",
"PUB00002563"
] | [
"1975493",
"2197274"
] | [
"Perspectives on methylmalonic acidemia resulting from molecular cloning of methylmalonyl CoA mutase.",
"Cloning, sequencing, and expression of the genes encoding the adenosylcobalamin-dependent ethanolamine ammonia-lyase of Salmonella typhimurium."
] | [
1990,
1990
] | 2 | [
"IPR006099"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
894,
19059,
1899,
516
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
1,
13,
2,
3
] | 6 | true | Domain | Methylmalonyl-CoA mutase, alpha chain, catalytic | Methylmalonyl-CoA mutase, alpha chain, catalytic | MMCoA_mutase_a_cat | 6 |
IPR006101 | 6,101 | Glycoside hydrolase, family 2 | Glyco_hydro_2 | Family | 35,319 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00132"
] | [
"GLHYDRLASE2"
] | [
35319
] | 1 | [
"CAZY",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH2",
"3.2.1.23",
"PWY-6807",
"PDOC00531",
"R-HSA-2024101",
"R-HSA-2160916",
"R-HSA-2206292",
"R-HSA-6798695",
"R-HSA-9953080",
"R-MMU-2024101",
"R-MMU-2160916",
"R-MMU-6798695",
"R-RNO-2024101",
"R-RNO-2160916",
"R-RNO-6798695",
"R-SSC-2024101",
"R-SSC-2160916",
"R-SSC-6798695"
] | [
"CAZY:GH2",
"EC:3.2.1.23",
"METACYC:PWY-6807",
"PROSITEDOC:PDOC00531",
"REACTOME:R-HSA-2024101",
"REACTOME:R-HSA-2160916",
"REACTOME:R-HSA-2206292",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9953080",
"REACTOME:R-MMU-2024101",
"REACTOME:R-MMU-2160916",
"REACTOME:R-MMU-6798695",
"REACTOME:R-R... | 18 | [
"1bhg",
"1dp0",
"1f4a",
"1f4h",
"1hn1",
"1jyn",
"1jyv",
"1jyw",
"1jyx",
"1jz2",
"1jz3",
"1jz4",
"1jz5",
"1jz6",
"1jz7",
"1jz8",
"1px3",
"1px4",
"1yq2",
"3bga",
"3cmg",
"3czj",
"3dec",
"3dym",
"3dyo",
"3dyp",
"3e1f",
"3fn9",
"3gm8",
"3hn3",
"3i3b",
"3i3d"... | 213 | [
"PUB00002709",
"PUB00004870",
"PUB00005266"
] | [
"1350782",
"7624375",
"8535779"
] | [
"Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1992,
1995,
1995
] | 3 | [] | [
"IPR023933",
"IPR048229",
"IPR048230"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Heunggongvirae",
"unclassified sequences"
] | [
171,
29129,
5732,
4,
283
] | 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",... | [
10,
1,
1,
8,
4,
3,
2,
2,
3,
5,
14
] | 11 | true | Family | Glycoside hydrolase, family 2 | Glycoside hydrolase, family 2 | Glyco_hydro_2 | 3 |
IPR006102 | 6,102 | Glycoside hydrolase family 2, immunoglobulin-like beta-sandwich | Ig-like_GH2 | Domain | 57,109 | false | false | This entry describes the immunoglobulin-like β-sandwich domain [ ]. Glycoside hydrolase family 2 comprises enzymes with several known activities: beta-galactosidase ( ); beta-mannosidase ( ); beta-glucuronidase ( ). These enzymes contain a conserved glutamic acid residue which has been shown [ ], in Escherichia coli la... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00703"
] | [
"Glyco_hydro_2"
] | [
57109
] | 1 | [
"CAZY",
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH2",
"3.2.1",
"3.2.1.23",
"PWY-6807",
"R-CEL-6798695",
"R-CEL-8853383",
"R-HSA-2024101",
"R-HSA-2160916",
"R-HSA-2206292",
"R-HSA-6798695",
"R-HSA-9953080",
"R-MMU-2024101",
"R-MMU-2160916",
"R-MMU-6798695",
"R-RNO-2024101",
"R-RNO-2160916",
"R-RNO-6798695",
"R-SSC-2024101",
"R... | [
"CAZY:GH2",
"EC:3.2.1",
"EC:3.2.1.23",
"METACYC:PWY-6807",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-8853383",
"REACTOME:R-HSA-2024101",
"REACTOME:R-HSA-2160916",
"REACTOME:R-HSA-2206292",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9953080",
"REACTOME:R-MMU-2024101",
"REACTOME:R-MMU-2160916",... | 20 | [
"1bhg",
"1dp0",
"1f4a",
"1f4h",
"1hn1",
"1jyn",
"1jyv",
"1jyw",
"1jyx",
"1jz2",
"1jz3",
"1jz4",
"1jz5",
"1jz6",
"1jz7",
"1jz8",
"1px3",
"1px4",
"2je8",
"2vjx",
"2vl4",
"2vmf",
"2vo5",
"2vot",
"2vqt",
"2vqu",
"2vr4",
"2vzo",
"2vzs",
"2vzt",
"2vzu",
"2vzv"... | 239 | [
"PUB00002709",
"PUB00004183",
"PUB00004870",
"PUB00005266"
] | [
"1350782",
"8008071",
"7624375",
"8535779"
] | [
"Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli.",
"Three-dimensional structure of beta-galactosidase from E. coli.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures a... | [
1992,
1994,
1995,
1995
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
339,
44914,
11383,
4,
469
] | 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",... | [
14,
2,
2,
8,
4,
3,
2,
6,
6,
4,
22
] | 11 | true | Domain | Glycoside hydrolase family 2, immunoglobulin-like beta-sandwich | Glycoside hydrolase family 2, immunoglobulin-like beta-sandwich | Ig-like_GH2 | 8 |
IPR006103 | 6,103 | Glycoside hydrolase family 2, catalytic domain | Glyco_hydro_2_cat | Domain | 53,749 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF02836"
] | [
"Glyco_hydro_2_C"
] | [
53749
] | 1 | [
"CAZY",
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH2",
"3.2.1",
"3.2.1.23",
"PWY-6807",
"R-HSA-2024101",
"R-HSA-2160916",
"R-HSA-2206292",
"R-HSA-6798695",
"R-HSA-8853383",
"R-HSA-9953080",
"R-MMU-2024101",
"R-MMU-2160916",
"R-MMU-6798695",
"R-MMU-8853383",
"R-RNO-2024101",
"R-RNO-2160916",
"R-RNO-6798695",
"R-RNO-8853383",
"R... | [
"CAZY:GH2",
"EC:3.2.1",
"EC:3.2.1.23",
"METACYC:PWY-6807",
"REACTOME:R-HSA-2024101",
"REACTOME:R-HSA-2160916",
"REACTOME:R-HSA-2206292",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8853383",
"REACTOME:R-HSA-9953080",
"REACTOME:R-MMU-2024101",
"REACTOME:R-MMU-2160916",
"REACTOME:R-MMU-6798695",... | 21 | [
"1bhg",
"1dp0",
"1f4a",
"1f4h",
"1hn1",
"1jyn",
"1jyv",
"1jyw",
"1jyx",
"1jz2",
"1jz3",
"1jz4",
"1jz5",
"1jz6",
"1jz7",
"1jz8",
"1px3",
"1px4",
"1yq2",
"3bga",
"3cmg",
"3czj",
"3dec",
"3dym",
"3dyo",
"3dyp",
"3e1f",
"3fn9",
"3gm8",
"3hn3",
"3i3b",
"3i3d"... | 233 | [
"PUB00002709",
"PUB00004183",
"PUB00004870",
"PUB00005266"
] | [
"1350782",
"8008071",
"7624375",
"8535779"
] | [
"Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli.",
"Three-dimensional structure of beta-galactosidase from E. coli.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures a... | [
1992,
1994,
1995,
1995
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
232,
43088,
9915,
5,
509
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
15,
1,
2,
8,
4,
14,
4,
3,
3,
8,
15
] | 11 | true | Domain | Glycoside hydrolase family 2, catalytic domain | Glycoside hydrolase family 2, catalytic domain | Glyco_hydro_2_cat | 3 |
IPR006104 | 6,104 | Glycosyl hydrolases family 2, sugar binding domain | Glyco_hydro_2_N | Domain | 42,888 | false | false | Proteins containing this domain include beta-galactosidases, beta-mannosidases and beta-glucuronidases. The domain has a jelly-roll fold [ ]. | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF02837"
] | [
"Glyco_hydro_2_N"
] | [
42888
] | 1 | [
"CAZY",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH2",
"3.2.1.23",
"PWY-6807",
"R-HSA-2024101",
"R-HSA-2160916",
"R-HSA-2206292",
"R-HSA-6798695",
"R-HSA-9953080",
"R-MMU-2024101",
"R-MMU-2160916",
"R-MMU-6798695",
"R-RNO-2024101",
"R-RNO-2160916",
"R-RNO-6798695",
"R-SSC-2024101",
"R-SSC-2160916",
"R-SSC-6798695"
] | [
"CAZY:GH2",
"EC:3.2.1.23",
"METACYC:PWY-6807",
"REACTOME:R-HSA-2024101",
"REACTOME:R-HSA-2160916",
"REACTOME:R-HSA-2206292",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9953080",
"REACTOME:R-MMU-2024101",
"REACTOME:R-MMU-2160916",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-2024101",
"REACTOME:R... | 17 | [
"1bhg",
"1dp0",
"1f4a",
"1f4h",
"1hn1",
"1jyn",
"1jyv",
"1jyw",
"1jyx",
"1jz2",
"1jz3",
"1jz4",
"1jz5",
"1jz6",
"1jz7",
"1jz8",
"1px3",
"1px4",
"1yq2",
"3bga",
"3cmg",
"3czj",
"3dec",
"3dym",
"3dyo",
"3dyp",
"3e1f",
"3fn9",
"3gm8",
"3hn3",
"3i3b",
"3i3d"... | 217 | [
"PUB00004183"
] | [
"8008071"
] | [
"Three-dimensional structure of beta-galactosidase from E. coli."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
205,
35677,
6657,
6,
343
] | 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",... | [
10,
1,
1,
8,
4,
4,
5,
3,
3,
4,
13
] | 11 | true | Domain | Glycosyl hydrolases family 2, sugar binding domain | Glycosyl hydrolases family 2, sugar binding domain | Glyco_hydro_2_N | 7 |
IPR006105 | 6,105 | Cereal seed allergen/trypsin and alpha-amylase inhibitor, conserved site | Allergen/tryp_amyl_inhib_CS | Conserved_site | 841 | false | false | The seeds of cereals contain numerous serine protease and alpha-amylase inhibitors. These inhibitors can be grouped into families based on structural similarities. This domain identifies sequences belonging to the cereal (monocotyledon) trypsin/alpha-amylase inhibitor family [ ]. It includes those annotated solely as s... | [
"GO:0004867"
] | [
"serine-type endopeptidase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00426"
] | [
"CEREAL_TRYP_AMYL_INH"
] | [
841
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00350"
] | [
"PROSITEDOC:PDOC00350"
] | 1 | [
"1b1u",
"1bea",
"1bfa",
"1bip",
"1hss",
"1tmq",
"4cvw"
] | 7 | [
"PUB00000423",
"PUB00004537",
"PUB00004563",
"PUB00014133",
"PUB00014156"
] | [
"7599120",
"2102817",
"7678765",
"14705960",
"11137459"
] | [
"Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy.",
"Cloning and characterization of a cDNA encoding the wheat (Triticum durum Desf.) CM16 protein.",
"Gene structure and expression of rice seed allergenic proteins belonging... | [
1995,
1990,
1993,
2004,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
841
] | 1 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
14,
6
] | 2 | true | Conserved_site | Cereal seed allergen/trypsin and alpha-amylase inhibitor, conserved site | Cereal seed allergen/trypsin and alpha-amylase inhibitor, conserved site | Allergen/tryp_amyl_inhib_CS | 4 |
IPR006106 | 6,106 | Cereal seed allergen/grain softness/trypsin and alpha-amylase inhibitor | Allergen/soft/tryp_amyl_inhib | Family | 1,220 | false | false | The seeds of cereals contain numerous serine protease and alpha-amylase inhibitors. These inhibitors can be grouped into families based on structural similarities and many are described as seed allergens. This family of cereal (monocotyledon) allergens, trypsin/alpha-amylase inhibitors [ ] belong to MEROPS inhibitor fa... | [
"GO:0004867"
] | [
"serine-type endopeptidase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF001657",
"PR00808"
] | [
"Allergen/amylase_inhib",
"AMLASEINHBTR"
] | [
593,
1220
] | 2 | [] | [] | [] | 0 | [
"1b1u",
"1bea",
"1bfa",
"1bip",
"1hss",
"1tmq",
"4cvw",
"9qlu"
] | 8 | [
"PUB00000423",
"PUB00004537",
"PUB00014133",
"PUB00014156"
] | [
"7599120",
"2102817",
"14705960",
"11137459"
] | [
"Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy.",
"Cloning and characterization of a cDNA encoding the wheat (Triticum durum Desf.) CM16 protein.",
"Evolutionary families of peptidase inhibitors.",
"Purification, bioche... | [
1995,
1990,
2004,
2000
] | 4 | [] | [
"IPR002411"
] | 0 | 1 | 0 | [
"Poaceae",
"Pseudomonadota"
] | [
1218,
2
] | 2 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
20,
7
] | 2 | true | Family | Cereal seed allergen/grain softness/trypsin and alpha-amylase inhibitor | Cereal seed allergen/grain softness/trypsin and alpha-amylase inhibitor | Allergen/soft/tryp_amyl_inhib | 9 |
IPR006108 | 6,108 | 3-hydroxyacyl-CoA dehydrogenase, C-terminal | 3HC_DH_C | Domain | 84,998 | false | false | 3-hydroxyacyl-CoA dehydrogenase ( ) (HCDH) [ ] is an enzyme involved in fatty acid metabolism, it catalyses the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. Most eukaryotic cells have 2 fatty-acid beta-oxidation systems, one located in mitochondria and the other in peroxisomes. In peroxisomes 3-hydroxyacyl-CoA dehy... | [
"GO:0016491",
"GO:0016616",
"GO:0006631"
] | [
"oxidoreductase activity",
"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor",
"fatty acid metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF00725"
] | [
"3HCDH"
] | [
84998
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
... | [
"1.1.1",
"1.1.1.35",
"4.2.1.17",
"5.1.2.3",
"PWY-1361",
"PWY-5136",
"PWY-5138",
"PWY-5177",
"PWY-5789",
"PWY-6435",
"PWY-6443",
"PWY-6446",
"PWY-6458",
"PWY-6583",
"PWY-6863",
"PWY-6883",
"PWY-6944",
"PWY-6945",
"PWY-6946",
"PWY-7007",
"PWY-7094",
"PWY-7216",
"PWY-7401",
... | [
"EC:1.1.1",
"EC:1.1.1.35",
"EC:4.2.1.17",
"EC:5.1.2.3",
"METACYC:PWY-1361",
"METACYC:PWY-5136",
"METACYC:PWY-5138",
"METACYC:PWY-5177",
"METACYC:PWY-5789",
"METACYC:PWY-6435",
"METACYC:PWY-6443",
"METACYC:PWY-6446",
"METACYC:PWY-6458",
"METACYC:PWY-6583",
"METACYC:PWY-6863",
"METACYC:P... | 89 | [
"1f0y",
"1f12",
"1f14",
"1f17",
"1il0",
"1lsj",
"1lso",
"1m75",
"1m76",
"1wdk",
"1wdl",
"1wdm",
"1zcj",
"1zej",
"2d3t",
"2hdh",
"2wtb",
"2x58",
"3ado",
"3adp",
"3ctv",
"3f3s",
"3had",
"3hdh",
"3k6j",
"3mog",
"3rqs",
"3zw8",
"3zw9",
"3zwa",
"3zwb",
"3zwc"... | 105 | [
"PUB00004380",
"PUB00004646"
] | [
"2204034",
"3479790"
] | [
"Nucleotide sequence of the fadA and fadB genes from Escherichia coli.",
"Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution."
] | [
1990,
1987
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1744,
66169,
16070,
1015
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
12,
11,
6,
5,
3,
21,
6,
4,
16,
18,
34
] | 11 | true | Domain | 3-hydroxyacyl-CoA dehydrogenase, C-terminal | 3-hydroxyacyl-CoA dehydrogenase, C-terminal | 3HC_DH_C | 9 |
IPR006109 | 6,109 | Glycerol-3-phosphate dehydrogenase, NAD-dependent, C-terminal | G3P_DH_NAD-dep_C | Domain | 37,149 | false | false | NAD-dependent glycerol-3-phosphate dehydrogenase ( ) (GPD) catalyzes the reversible reduction of dihydroxyacetone phosphate to glycerol-3-phosphate. It is a cytoplasmic protein, active as a homodimer [ ], each monomer containing an N-terminal NAD binding site [ ]. In insects, it acts in conjunction with a mitochondrial... | [
"GO:0005975",
"GO:0006072"
] | [
"carbohydrate metabolic process",
"glycerol-3-phosphate metabolic process"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF07479"
] | [
"NAD_Gly3P_dh_C"
] | [
37149
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1.94",
"PWY-5667",
"PWY-5981",
"PWY-7902",
"R-CEL-1483166",
"R-DME-1483166",
"R-DRE-1483166",
"R-HSA-1483166",
"R-MMU-1483166",
"R-RNO-1483166",
"R-SCE-1483166",
"R-SPO-1483166",
"R-XTR-1483166"
] | [
"EC:1.1.1.94",
"METACYC:PWY-5667",
"METACYC:PWY-5981",
"METACYC:PWY-7902",
"REACTOME:R-CEL-1483166",
"REACTOME:R-DME-1483166",
"REACTOME:R-DRE-1483166",
"REACTOME:R-HSA-1483166",
"REACTOME:R-MMU-1483166",
"REACTOME:R-RNO-1483166",
"REACTOME:R-SCE-1483166",
"REACTOME:R-SPO-1483166",
"REACTOME... | 13 | [
"1evy",
"1evz",
"1jdj",
"1m66",
"1m67",
"1n1e",
"1n1g",
"1txg",
"1wpq",
"1x0v",
"1x0x",
"1yj8",
"1z82",
"2pla",
"3k96",
"4fgw",
"6e8y",
"6e8z",
"6e90",
"6iuy",
"6pyp"
] | 21 | [
"PUB00001336",
"PUB00004686"
] | [
"6773774",
"2500660"
] | [
"Prediction of secondary structural elements in glycerol-3-phosphate dehydrogenase by comparison with other dehydrogenases.",
"Structural characterization of the alpha-glycerol-3-phosphate dehydrogenase-encoding gene of Drosophila melanogaster."
] | [
1980,
1989
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"unclassified sequences"
] | [
64,
25848,
10664,
1,
572
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
15,
5,
6,
15,
1,
7,
5,
1,
8,
10,
2,
2,
18
] | 13 | true | Domain | Glycerol-3-phosphate dehydrogenase, NAD-dependent, C-terminal | Glycerol-3-phosphate dehydrogenase, NAD-dependent, C-terminal | G3P_DH_NAD-dep_C | 1 |
IPR006110 | 6,110 | RNA polymerase, subunit omega/Rpo6/RPB6 | Pol_omega/Rpo6/RPB6 | Family | 27,674 | false | false | In eukaryotes, there are three different forms of DNA-dependent RNA polymerases ( ) transcribing different sets of genes. Each class of RNA polymerase is an assemblage of ten to twelve different polypeptides. In archaebacteria, there is generally a single form of RNA polymerase which also consists of an oligomeric asse... | [
"GO:0003677",
"GO:0003899",
"GO:0006351"
] | [
"DNA binding",
"DNA-directed RNA polymerase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF01192",
"SM01409"
] | [
"RNA_pol_Rpb6",
"RNA_pol_Rpb6"
] | [
27607,
25613
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.6",
"R-CEL-112382",
"R-CEL-113418",
"R-CEL-5250924",
"R-CEL-5578749",
"R-CEL-674695",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-6796648",
"R-CEL-6803529",
"R-CEL-6807505",
"R-CEL-72086",
"R-CEL-72163",
"R-CEL-72165",
"R-CEL-72203",
"R-CEL-73762",
"R-CEL-73772... | [
"EC:2.7.7.6",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-113418",
"REACTOME:R-CEL-5250924",
"REACTOME:R-CEL-5578749",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6781823",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-6803529",
"REACTOME:R-CEL-6807505... | 217 | [
"1hqm",
"1i3q",
"1i50",
"1i6h",
"1i6v",
"1iw7",
"1k83",
"1l9u",
"1l9z",
"1nik",
"1nt9",
"1pqv",
"1qkl",
"1r5u",
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"1r9t",
"1sfo",
"1smy",
"1twa",
"1twc",
"1twf",
"1twg",
"1twh",
"1wcm",
"1y1v",
"1y1w",
"1y1y",
"1y77",
"1ynj",
"1ynn",
"1zyr",
"2a68"... | 1,167 | [
"PUB00007936"
] | [
"11158566"
] | [
"Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly."
] | [
2001
] | 1 | [] | [
"IPR003716",
"IPR006111"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
870,
21289,
4808,
67,
640
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
6,
1,
1,
2,
1,
8,
4,
1,
6,
2,
1,
1,
7
] | 13 | true | Family | RNA polymerase, subunit omega/Rpo6/RPB6 | RNA polymerase, subunit omega/Rpo6/RPB6 | Pol_omega/Rpo6/RPB6 | 7 |
IPR006111 | 6,111 | Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit | Rpo6/Rpb6 | Family | 6,178 | 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:0003677",
"GO:0003899",
"GO:0006351"
] | [
"DNA binding",
"DNA-directed RNA polymerase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PIRSF"
] | [
"MF_00192",
"PIRSF000778"
] | [
"RNApol_arch_Rpo6",
"RpoK/RPB6"
] | [
3034,
5947
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.6",
"PDOC00855",
"R-CEL-112382",
"R-CEL-113418",
"R-CEL-5250924",
"R-CEL-5578749",
"R-CEL-674695",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-6796648",
"R-CEL-6803529",
"R-CEL-6807505",
"R-CEL-72086",
"R-CEL-72163",
"R-CEL-72165",
"R-CEL-72203",
"R-CEL-73762",... | [
"EC:2.7.7.6",
"PROSITEDOC:PDOC00855",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-113418",
"REACTOME:R-CEL-5250924",
"REACTOME:R-CEL-5578749",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6781823",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-6803529",... | 217 | [
"1i3q",
"1i50",
"1i6h",
"1k83",
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"1nt9",
"1pqv",
"1qkl",
"1r5u",
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"1twf",
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"1y1v",
"1y1w",
"1y1y",
"1y77",
"2b63",
"2b8k",
"2e2h",
"2e2i",
"2e2j",
"2ja5",
"2ja6",
"2ja7",
"2ja8",
"2nvq"... | 549 | [
"PUB00000061",
"PUB00002250",
"PUB00004425",
"PUB00033173",
"PUB00059148"
] | [
"3052291",
"8045907",
"8332503",
"10499798",
"19419240"
] | [
"Structure and function of bacterial sigma factors.",
"Halobacterial S9 operon contains two genes encoding proteins homologous to subunits shared by eukaryotic RNA polymerases I, II, and III.",
"An African swine fever virus gene with a similarity to eukaryotic RNA polymerase subunit 6.",
"Crystal structure of... | [
1988,
1994,
1993,
1999,
2009
] | 5 | [
"IPR006110"
] | [
"IPR028363"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria candidate phyla",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
859,
2,
5207,
25,
85
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
6,
1,
1,
2,
6,
5,
1,
5,
2,
1,
1,
7
] | 12 | true | Family | Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit | Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit | Rpo6/Rpb6 | 8 |
IPR006113 | 6,113 | 6-phosphogluconate dehydrogenase, decarboxylating | 6PGDH_Gnd/GntZ | Family | 20,498 | false | false | 6-Phosphogluconate dehydrogenase ( ) (6PGD) is a key enzyme that produces NADPH by converting 6-phospho D-gluconolactone to D-ribulose 5-phosphate in the pentose phosphate pathways (PPP) [ , ]. NADPH provides the major reducing power required for lipid production and protecting the cell against oxidative stress. 6PGD h... | [
"GO:0004616",
"GO:0006098"
] | [
"phosphogluconate dehydrogenase (decarboxylating) activity",
"pentose-phosphate shunt"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF000109",
"TIGR00873"
] | [
"6PGD",
"gnd"
] | [
19386,
19643
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1.44",
"GenProp0120",
"GenProp1438",
"GenProp1520",
"R-CEL-71336",
"R-DDI-71336",
"R-DME-71336",
"R-HSA-71336",
"R-HSA-9818028",
"R-MMU-71336",
"R-RNO-71336",
"R-SCE-71336",
"R-SPO-71336"
] | [
"EC:1.1.1.44",
"GP:GenProp0120",
"GP:GenProp1438",
"GP:GenProp1520",
"REACTOME:R-CEL-71336",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-71336",
"REACTOME:R-HSA-71336",
"REACTOME:R-HSA-9818028",
"REACTOME:R-MMU-71336",
"REACTOME:R-RNO-71336",
"REACTOME:R-SCE-71336",
"REACTOME:R-SPO-71336"
] | 13 | [
"1pgj",
"1pgn",
"1pgo",
"1pgp",
"1pgq",
"2iyo",
"2iyp",
"2iz0",
"2iz1",
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"6fqz",
"7cb0",
"7cb2",
"7cb5",
"7cb6",
"8c79",
"8i4n",
"8i4q"
] | 31 | [
"PUB00001132",
"PUB00002112",
"PUB00003806",
"PUB00043231",
"PUB00073768",
"PUB00073769"
] | [
"6641716",
"2113917",
"1659648",
"17570834",
"24726622",
"15231785"
] | [
"The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution.",
"Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase.",
"Analysis of the gluconate (gnt) operon of Bacillus subtilis.",
"... | [
1983,
1990,
1991,
2007,
2014,
2004
] | 6 | [
"IPR006183"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Nitrososphaerota incertae sedis",
"metagenomes"
] | [
14412,
6013,
7,
66
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
9,
1,
1,
3,
1,
4,
4,
2,
5,
4,
2,
1,
13
] | 13 | true | Family | 6-phosphogluconate dehydrogenase, decarboxylating | 6-phosphogluconate dehydrogenase, decarboxylating | 6PGDH_Gnd/GntZ | 8 |
IPR006114 | 6,114 | 6-phosphogluconate dehydrogenase, C-terminal | 6PGDH_C | Domain | 34,169 | false | false | 6-Phosphogluconate dehydrogenase ( ) (6PGD) is an oxidative carboxylase that catalyses the decarboxylating reduction of 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP. This reaction is a component of the hexose mono-phosphate shunt and pentose phosphate pathways (PPP) [ , ]. Prokaryotic and eukary... | [
"GO:0004616",
"GO:0006098"
] | [
"phosphogluconate dehydrogenase (decarboxylating) activity",
"pentose-phosphate shunt"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF00393",
"SM01350"
] | [
"6PGD",
"6PGD"
] | [
34155,
33712
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1.44",
"R-CEL-71336",
"R-DDI-71336",
"R-DME-71336",
"R-HSA-71336",
"R-HSA-9818028",
"R-MMU-71336",
"R-RNO-71336",
"R-SCE-71336",
"R-SPO-71336"
] | [
"EC:1.1.1.44",
"REACTOME:R-CEL-71336",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-71336",
"REACTOME:R-HSA-71336",
"REACTOME:R-HSA-9818028",
"REACTOME:R-MMU-71336",
"REACTOME:R-RNO-71336",
"REACTOME:R-SCE-71336",
"REACTOME:R-SPO-71336"
] | 10 | [
"1pgj",
"1pgn",
"1pgo",
"1pgp",
"1pgq",
"2iyo",
"2iyp",
"2iz0",
"2iz1",
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"6fqz",
"6vpb",
"6xeq",
"7cb0",
"7cb2",
"7cb5",
"7cb6",
"8c79"... | 36 | [
"PUB00001132",
"PUB00002112",
"PUB00003806"
] | [
"6641716",
"2113917",
"1659648"
] | [
"The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution.",
"Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase.",
"Analysis of the gluconate (gnt) operon of Bacillus subtilis."
] | [
1983,
1990,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
367,
24663,
8801,
48,
290
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
9,
1,
1,
4,
1,
8,
4,
2,
6,
4,
2,
1,
19
] | 13 | true | Domain | 6-phosphogluconate dehydrogenase, C-terminal | 6-phosphogluconate dehydrogenase, C-terminal | 6PGDH_C | 5 |
IPR006115 | 6,115 | 6-phosphogluconate dehydrogenase, NADP-binding | 6PGDH_NADP-bd | Domain | 110,120 | false | false | 6-Phosphogluconate dehydrogenase ( ) (6PGD) is an oxidative carboxylase that catalyses the decarboxylating reduction of 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP. This reaction is a component of the hexose mono-phosphate shunt and pentose phosphate pathways (PPP) [ , ]. Prokaryotic and eukary... | [
"GO:0050661"
] | [
"NADP binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF03446"
] | [
"NAD_binding_2"
] | [
110120
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"R-BTA-70895",
"R-CEL-70895",
"R-CEL-71336",
"R-DDI-70895",
"R-DDI-71336",
"R-DME-70895",
"R-DME-71336",
"R-HSA-70895",
"R-HSA-71336",
"R-HSA-9818028",
"R-MMU-70895",
"R-MMU-71336",
"R-RNO-70895",
"R-RNO-71336",
"R-SCE-71336",
"R-SPO-71336"
] | [
"EC:1.1.1",
"REACTOME:R-BTA-70895",
"REACTOME:R-CEL-70895",
"REACTOME:R-CEL-71336",
"REACTOME:R-DDI-70895",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-70895",
"REACTOME:R-DME-71336",
"REACTOME:R-HSA-70895",
"REACTOME:R-HSA-71336",
"REACTOME:R-HSA-9818028",
"REACTOME:R-MMU-70895",
"REACTOME:R-MM... | 17 | [
"1pgj",
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"1pgp",
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"3cky",
"3doj",
"3fwn",
"3g0o",
"3l6d",
"3obb",
"3pdu",
"3pef"... | 161 | [
"PUB00001132",
"PUB00002112",
"PUB00003806",
"PUB00094296"
] | [
"6641716",
"2113917",
"1659648",
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"The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution.",
"Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase.",
"Analysis of the gluconate (gnt) operon of Bacillus subtilis.",
"... | [
1983,
1990,
1991,
2006
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
828,
83131,
25083,
64,
1014
] | 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",... | [
46,
2,
15,
8,
5,
13,
8,
7,
22,
14,
3,
2,
79
] | 13 | true | Domain | 6-phosphogluconate dehydrogenase, NADP-binding | 6-phosphogluconate dehydrogenase, NADP-binding | 6PGDH_NADP-bd | 1 |
IPR006116 | 6,116 | 2-5OAS/ClassI-CCAase, nucleotidyltransferase domain | NT_2-5OAS_ClassI-CCAase | Domain | 6,756 | false | false | Proteins containing this domain include human OAS1, -2, -3, and OASL. CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This class I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CC... | [
"GO:0016779"
] | [
"nucleotidyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"CDD"
] | [
"cd05400"
] | [
"NT_2-5OAS_ClassI-CCAase"
] | [
6756
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7",
"PDOC00653",
"R-HSA-877300",
"R-HSA-8983711",
"R-HSA-909733",
"R-HSA-9833110",
"R-MMU-8983711",
"R-RNO-8983711"
] | [
"EC:2.7.7",
"PROSITEDOC:PDOC00653",
"REACTOME:R-HSA-877300",
"REACTOME:R-HSA-8983711",
"REACTOME:R-HSA-909733",
"REACTOME:R-HSA-9833110",
"REACTOME:R-MMU-8983711",
"REACTOME:R-RNO-8983711"
] | 8 | [
"1px5",
"1r89",
"1r8a",
"1r8b",
"1r8c",
"1sz1",
"1tfw",
"1tfy",
"1uet",
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"1uev",
"2dr5",
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"2zh3",
"2zh4",
"2zh5",
"2zh6",
"2zh7",
"2zh8",
"2zh9",
"2zha",
"2zhb",
"3ouy",
"3ov7",
"3ova"... | 89 | [
"PUB00010740",
"PUB00013566",
"PUB00015732",
"PUB00094140"
] | [
"8809016",
"10075991",
"14636575",
"17408844"
] | [
"CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: characterization of the CCA-adding enzyme from the archaeal hyperthermophile Sulfolobus shibatae.",
"DNA polymerase beta-like nucleotidyltransferase superfamily: identification of three new families, classi... | [
1996,
1999,
2003,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
988,
3589,
2110,
2,
67
] | 5 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
51,
21,
29
] | 3 | true | Domain | 2-5OAS/ClassI-CCAase, nucleotidyltransferase domain | 2-5OAS/ClassI-CCAase, nucleotidyltransferase domain | NT_2-5OAS_ClassI-CCAase | 4 |
IPR006117 | 6,117 | 2-5-oligoadenylate synthetase, C-terminal conserved site | 2-5OAS_C_CS | Conserved_site | 1,736 | false | false | In vertebrates, 2-5OASs (2'-5'-oligoadenylate synthetases) are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00833"
] | [
"25A_SYNTH_2"
] | [
1736
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.84",
"PDOC00653",
"R-HSA-877300",
"R-HSA-8983711",
"R-HSA-909733",
"R-HSA-9833110",
"R-MMU-8983711",
"R-RNO-8983711"
] | [
"EC:2.7.7.84",
"PROSITEDOC:PDOC00653",
"REACTOME:R-HSA-877300",
"REACTOME:R-HSA-8983711",
"REACTOME:R-HSA-909733",
"REACTOME:R-HSA-9833110",
"REACTOME:R-MMU-8983711",
"REACTOME:R-RNO-8983711"
] | 8 | [
"1px5",
"4ig8",
"4rwn",
"4rwo",
"4rwp",
"4rwq",
"4s3n",
"4xq7",
"9h1z"
] | 9 | [
"PUB00094140"
] | [
"17408844"
] | [
"The human 2'-5'oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2'-5' instead of 3'-5' phosphodiester bond formation."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1736
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
41,
23,
31
] | 3 | true | Conserved_site | 2-5-oligoadenylate synthetase, C-terminal conserved site | 2-5-oligoadenylate synthetase, C-terminal conserved site | 2-5OAS_C_CS | 7 |
IPR006118 | 6,118 | Recombinase, conserved site | Recombinase_CS | Conserved_site | 38,025 | false | false | Site-specific recombination plays an important role in DNA rearrangement in prokaryotic organisms. Two types of site-specific recombination are known to occur: Recombination between inverted repeats resulting in the reversal of a DNA segment. Recombination between repeat sequences on two DNA molecules resulting in thei... | [
"GO:0000150",
"GO:0006310"
] | [
"DNA strand exchange activity",
"DNA recombination"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00397",
"PS00398"
] | [
"RECOMBINASES_1",
"RECOMBINASES_2"
] | [
31891,
20544
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00334"
] | [
"PROSITEDOC:PDOC00334"
] | 1 | [
"1gdr",
"1gdt",
"1ght",
"1hx7",
"1zr2",
"1zr4",
"2gm4",
"2gm5",
"2r0q",
"2rsl",
"3ilx",
"3lhf",
"3pkz",
"3uj3",
"4m6f",
"5c31",
"5c32",
"5c34",
"5c35",
"5cy1",
"5cy2",
"6dgc"
] | 22 | [
"PUB00001148",
"PUB00002098",
"PUB00003732",
"PUB00003786"
] | [
"3011407",
"2105293",
"2550763",
"2896291"
] | [
"The integrase family of site-specific recombinases: regional similarities and global diversity.",
"The cisA cistron of Bacillus subtilis sporulation gene spoIVC encodes a protein homologous to a site-specific recombinase.",
"The uvp1 gene of plasmid pR cooperates with mucAB genes in the DNA repair process.",
... | [
1986,
1990,
1989,
1987
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"other sequences",
"unclassified sequences"
] | [
531,
36567,
228,
243,
24,
432
] | 6 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Conserved_site | Recombinase, conserved site | Recombinase, conserved site | Recombinase_CS | 3 |
IPR006119 | 6,119 | Resolvase, N-terminal catalytic domain | Resolv_N | Domain | 82,466 | false | false | Site-specific recombination plays an important role in DNA rearrangement in prokaryotic organisms. Two types of site-specific recombination are known to occur: Recombination between inverted repeats resulting in the reversal of a DNA segment. Recombination between repeat sequences on two DNA molecules resulting in thei... | [
"GO:0000150",
"GO:0003677",
"GO:0006310"
] | [
"DNA strand exchange activity",
"DNA binding",
"DNA recombination"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00239",
"PS51736",
"SM00857"
] | [
"Resolvase",
"RECOMBINASES_3",
"Resolvase"
] | [
80845,
72667,
75328
] | 3 | [] | [] | [] | 0 | [
"1gdr",
"1gdt",
"1ght",
"1hx7",
"1zr2",
"1zr4",
"2gm4",
"2gm5",
"2mhc",
"2r0q",
"2rsl",
"3bvp",
"3g13",
"3guv",
"3ilx",
"3lhf",
"3lhk",
"3pkz",
"3uj3",
"4bqq",
"4m6f",
"5c31",
"5c32",
"5c34",
"5c35",
"5cy1",
"5cy2",
"6dgb",
"6dgc"
] | 29 | [
"PUB00001148",
"PUB00003786",
"PUB00019725"
] | [
"3011407",
"2896291",
"7628011"
] | [
"The integrase family of site-specific recombinases: regional similarities and global diversity.",
"Molecular characterization of the resolvase gene, res, carried by a multicopy plasmid from Clostridium perfringens: common evolutionary origin for prokaryotic site-specific recombinases.",
"Crystal structure of t... | [
1986,
1987,
1995
] | 3 | [] | [
"IPR041718"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"other sequences",
"unclassified sequences"
] | [
887,
79069,
400,
890,
25,
1195
] | 6 | [
"Escherichia coli (strain K12)",
"Mus musculus"
] | [
6,
1
] | 2 | true | Domain | Resolvase, N-terminal catalytic domain | Resolvase, N-terminal catalytic domain | Resolv_N | 2 |
IPR006120 | 6,120 | Resolvase, HTH domain | Resolvase_HTH_dom | Domain | 20,885 | false | false | Site-specific recombination plays an important role in DNA rearrangement in prokaryotic organisms. Two types of site-specific recombination are known to occur: Recombination between inverted repeats resulting in the reversal of a DNA segment. Recombination between repeat sequences on two DNA molecules resulting in thei... | [
"GO:0000150",
"GO:0003677",
"GO:0006310"
] | [
"DNA strand exchange activity",
"DNA binding",
"DNA recombination"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF02796"
] | [
"HTH_7"
] | [
20885
] | 1 | [] | [] | [] | 0 | [
"1gdt",
"1hcr",
"1ijw",
"1jj6",
"1jj8",
"1jko",
"1jkp",
"1jkq",
"1jkr",
"1res",
"1ret",
"1zr2",
"1zr4",
"2gm4",
"2r0q",
"3uj3",
"4m6f",
"5cy1",
"5cy2",
"8b4h"
] | 20 | [
"PUB00001148",
"PUB00003786"
] | [
"3011407",
"2896291"
] | [
"The integrase family of site-specific recombinases: regional similarities and global diversity.",
"Molecular characterization of the resolvase gene, res, carried by a multicopy plasmid from Clostridium perfringens: common evolutionary origin for prokaryotic site-specific recombinases."
] | [
1986,
1987
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
162,
20216,
223,
104,
17,
163
] | 6 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Domain | Resolvase, HTH domain | Resolvase, HTH domain | Resolvase_HTH_dom | 3 |
IPR006121 | 6,121 | Heavy metal-associated domain, HMA | HMA_dom | Domain | 145,937 | false | false | Proteins that transport heavy metals in micro-organisms and mammals share similarities in their sequences and structures. These proteins provide an important focus for research, some being involved in bacterial resistance to toxic metals, such as lead and cadmium, while others are involved in inherited human syndromes,... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"CDD"
] | [
"PF00403",
"PS50846",
"cd00371"
] | [
"HMA",
"HMA_2",
"HMA"
] | [
132578,
139206,
132565
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00804",
"R-CFA-6803544",
"R-DDI-3299685",
"R-HSA-3299685",
"R-HSA-6803544",
"R-HSA-936837",
"R-MMU-3299685",
"R-MMU-6803544",
"R-MMU-936837",
"R-RNO-3299685",
"R-RNO-6803544",
"R-RNO-936837",
"R-SCE-3299685",
"R-SCE-936837",
"R-SPO-936837"
] | [
"PROSITEDOC:PDOC00804",
"REACTOME:R-CFA-6803544",
"REACTOME:R-DDI-3299685",
"REACTOME:R-HSA-3299685",
"REACTOME:R-HSA-6803544",
"REACTOME:R-HSA-936837",
"REACTOME:R-MMU-3299685",
"REACTOME:R-MMU-6803544",
"REACTOME:R-MMU-936837",
"REACTOME:R-RNO-3299685",
"REACTOME:R-RNO-6803544",
"REACTOME:R-... | 15 | [
"1afi",
"1afj",
"1aw0",
"1cc7",
"1cc8",
"1cpz",
"1fd8",
"1fe0",
"1fe4",
"1fee",
"1fes",
"1fvq",
"1fvs",
"1jk9",
"1jww",
"1k0v",
"1kqk",
"1kvi",
"1kvj",
"1mwy",
"1mwz",
"1opz",
"1oq3",
"1oq6",
"1osd",
"1p6t",
"1p8g",
"1q8l",
"1qup",
"1s6o",
"1s6u",
"1sb6"... | 156 | [
"PUB00005528",
"PUB00007951"
] | [
"8091505",
"9437429"
] | [
"Wilson disease and Menkes disease: new handles on heavy-metal transport.",
"Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase."
] | [
1994,
1998
] | 2 | [] | [
"IPR006122"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
3251,
86206,
55189,
3,
5,
1283
] | 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",... | [
319,
4,
11,
12,
2,
46,
15,
5,
224,
27,
4,
2,
381
] | 13 | true | Domain | Heavy metal-associated domain, HMA | Heavy metal-associated domain, HMA | HMA_dom | 3 |
IPR006122 | 6,122 | Heavy metal-associated domain, copper ion-binding | HMA_Cu_ion-bd | Domain | 22,773 | false | false | Proteins that transport heavy metals in micro-organisms and eukaryotes share similarities in their sequences and structures. These proteins provide an important focus for research, some being involved in bacterial resistance to toxic metals, such as lead and cadmium, while others are involved in inherited human syndrom... | [
"GO:0005507"
] | [
"copper ion binding"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00003"
] | [
""
] | [
22773
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.2.2",
"R-HSA-3299685",
"R-HSA-6803544",
"R-HSA-936837",
"R-MMU-6803544",
"R-MMU-936837",
"R-RNO-6803544",
"R-RNO-936837",
"R-SCE-936837"
] | [
"EC:7.2.2",
"REACTOME:R-HSA-3299685",
"REACTOME:R-HSA-6803544",
"REACTOME:R-HSA-936837",
"REACTOME:R-MMU-6803544",
"REACTOME:R-MMU-936837",
"REACTOME:R-RNO-6803544",
"REACTOME:R-RNO-936837",
"REACTOME:R-SCE-936837"
] | 9 | [
"1cpz",
"1k0v",
"1kvi",
"1kvj",
"1p6t",
"1p8g",
"1yg0",
"2ew9",
"2k1r",
"2l3m",
"2qif",
"2rml",
"2rop",
"3cjk",
"3i9z",
"3j09",
"5t7l",
"6ff2",
"7si3",
"7si6",
"7si7",
"7xuk",
"7xum",
"7xun",
"7xuo",
"8ioy",
"8q73",
"8q74",
"8q76"
] | 29 | [
"PUB00005528"
] | [
"8091505"
] | [
"Wilson disease and Menkes disease: new handles on heavy-metal transport."
] | [
1994
] | 1 | [
"IPR006121"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
860,
11817,
9985,
111
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
16,
3,
8,
10,
32,
8,
1,
6,
14,
1,
20
] | 11 | true | Domain | Heavy metal-associated domain, copper ion-binding | Heavy metal-associated domain, copper ion-binding | HMA_Cu_ion-bd | 6 |
IPR006124 | 6,124 | Metalloenzyme | Metalloenzyme | Domain | 35,339 | false | false | This domain unites alkaline phosphatase, N-acetylgalactosamine-4-sulphatase, and cerebroside sulphatase, enzymes with known three-dimensional structures, with phosphopentomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglycerol transferase, phosphonate monoesterase, streptomycin-6-phosphate ... | [
"GO:0003824",
"GO:0046872"
] | [
"catalytic activity",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF01676"
] | [
"Metalloenzyme"
] | [
35339
] | 1 | [
"EC"
] | [
"5.4.2"
] | [
"EC:5.4.2"
] | 1 | [
"1ejj",
"1eqj",
"1o98",
"1o99",
"2ify",
"2zkt",
"3idd",
"3igy",
"3igz",
"3kd8",
"3m7v",
"3m8w",
"3m8y",
"3m8z",
"3nvl",
"3ot9",
"3twz",
"3tx0",
"3un2",
"3un3",
"3un5",
"3uny",
"3uo0",
"4lr7",
"4lr8",
"4lr9",
"4lra",
"4lrb",
"4lrc",
"4lrd",
"4lre",
"4lrf"... | 45 | [
"PUB00005056"
] | [
"10082381"
] | [
"A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Hyperionvirus sp.",
"unclassified sequences"
] | [
1260,
28915,
4522,
1,
641
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
16,
1,
3,
1,
10,
31
] | 6 | true | Domain | Metalloenzyme | Metalloenzyme | Metalloenzyme | 2 |
IPR006126 | 6,126 | Staphylococcal enterotoxin/Streptococcal pyrogenic exotoxin, conserved site | Staph/Strept_toxin_CS | Conserved_site | 1,065 | false | false | Staphylococcal enterotoxins and streptococcal pyrogenic exotoxins constitute a family of biologically and structurally related toxins produced by Staphylococcus aureus and Streptococcus pyogenes [ , ]. These toxins share the ability to bind to the major histocompatibility complex proteins of their hosts. A more distant... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00277",
"PS00278"
] | [
"STAPH_STREP_TOXIN_1",
"STAPH_STREP_TOXIN_2"
] | [
377,
975
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00250"
] | [
"PROSITEDOC:PDOC00250"
] | 1 | [
"1an8",
"1aw7",
"1b1z",
"1bxt",
"1ck1",
"1cqv",
"1d5m",
"1d5x",
"1d5z",
"1d6e",
"1dyq",
"1enf",
"1esf",
"1et6",
"1et9",
"1eu3",
"1eu4",
"1ewc",
"1f77",
"1fnu",
"1fnv",
"1fnw",
"1goz",
"1ha5",
"1hqr",
"1hxy",
"1i4g",
"1i4h",
"1i4p",
"1i4q",
"1i4r",
"1i4x"... | 139 | [
"PUB00000115",
"PUB00005127"
] | [
"2679358",
"2185544"
] | [
"Genetic analysis of extracellular toxins of Staphylococcus aureus.",
"The staphylococcal enterotoxins and their relatives."
] | [
1989,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Plasmid pIB485",
"ecological metagenomes"
] | [
1042,
7,
13,
1,
2
] | 5 | [] | [] | 0 | true | Conserved_site | Staphylococcal enterotoxin/Streptococcal pyrogenic exotoxin, conserved site | Staphylococcal enterotoxin/Streptococcal pyrogenic exotoxin, conserved site | Staph/Strept_toxin_CS | 2 |
IPR006127 | 6,127 | Periplasmic solute binding protein, ZnuA-like | ZnuA-like | Family | 39,032 | false | false | Members of this family constitute the solute-binding protein component of cluster-9 ABC transporters. This family includes periplasmic solute binding protein TroA from Treponema pallidum, which binds Zn2+ and Mn2+ [ ]. In Streptococcus suis, TroA is required for manganese acquisition [ ]. Related proteins are found in ... | [
"GO:0046872",
"GO:0030001"
] | [
"metal ion binding",
"metal ion transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01297"
] | [
"ZnuA"
] | [
39032
] | 1 | [
"REACTOME"
] | [
"R-HSA-9638482"
] | [
"REACTOME:R-HSA-9638482"
] | 1 | [
"1k0f",
"1pq4",
"1psz",
"1toa",
"1xvl",
"2o1e",
"2ogw",
"2osv",
"2ov1",
"2ov3",
"2prs",
"2ps0",
"2ps3",
"2ps9",
"2xh8",
"2xqv",
"2xy4",
"3cx3",
"3gi1",
"3hh8",
"3hjt",
"3mfq",
"3ujp",
"3zk7",
"3zk8",
"3zk9",
"3zka",
"3ztt",
"4bbp",
"4cl2",
"4h0f",
"4irm"... | 94 | [
"PUB00070762",
"PUB00070763",
"PUB00070764",
"PUB00075691",
"PUB00078715"
] | [
"21784944",
"24128931",
"16194238",
"21338480",
"17581125"
] | [
"TroA of Streptococcus suis is required for manganese acquisition and full virulence.",
"The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc.",
"The solute-binding component of a putative Mn(II) ... | [
2011,
2014,
2005,
2011,
2007
] | 5 | [] | [
"IPR006128",
"IPR035520",
"IPR047701"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
906,
37569,
49,
6,
502
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Periplasmic solute binding protein, ZnuA-like | Periplasmic solute binding protein, ZnuA-like | ZnuA-like | 4 |
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