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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR006128 | 6,128 | Adhesion lipoprotein PsaA-like | Lipoprotein_PsaA-like | Family | 24,778 | false | false | The Streptococcus pneumoniae psaA gene encodes a protein with significant similarity to previously-reported Streptococcal proteins, SsaB (80% similarity) and FimA (92.3% similarity), from Streptococcus sanguis and Streptococcus parasanguis [ ]. These homologues are associated with bacterial adhesion [ ]. PsaA is part o... | [
"GO:0007155"
] | [
"cell adhesion"
] | [
"biological_process"
] | 1 | [
"PRINTS"
] | [
"PR00690"
] | [
"ADHESNFAMILY"
] | [
24778
] | 1 | [
"REACTOME"
] | [
"R-HSA-9638482"
] | [
"REACTOME:R-HSA-9638482"
] | 1 | [
"1k0f",
"1psz",
"1toa",
"1xvl",
"2o1e",
"2ogw",
"2osv",
"2ov1",
"2ov3",
"2prs",
"2ps0",
"2ps3",
"2ps9",
"2xh8",
"3cx3",
"3gi1",
"3hh8",
"3hjt",
"3mfq",
"3ujp",
"3zk7",
"3zk8",
"3zk9",
"3zka",
"3ztt",
"4cl2",
"4h0f",
"4irm",
"4k3v",
"4nno",
"4nnp",
"4oxq"... | 89 | [
"PUB00002025",
"PUB00002030",
"PUB00015631",
"PUB00058462"
] | [
"1671775",
"7505262",
"9379902",
"22072971"
] | [
"Nucleotide sequence of a gene coding for a saliva-binding protein (SsaB) from Streptococcus sanguis 12 and possible role of the protein in coaggregation with actinomyces.",
"Cloning and nucleotide sequence analysis of psaA, the Streptococcus pneumoniae gene encoding a 37-kilodalton protein homologous to previous... | [
1991,
1994,
1997,
2011
] | 4 | [
"IPR006127"
] | [
"IPR006129"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
181,
24306,
4,
27,
260
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Adhesion lipoprotein PsaA-like | Adhesion lipoprotein PsaA-like | Lipoprotein_PsaA-like | 4 |
IPR006129 | 6,129 | Adhesin B | AdhesinB | Family | 22,818 | false | false | The Streptococcus pneumoniae psaA gene encodes a protein with significant similarity to previously-reported Streptococcal proteins, SsaB (80% similarity) and FimA (92.3% similarity), from Streptococcus sanguis and Streptococcus parasanguis [ ]. These homologues are associated with bacterial adhesion, and PsaA may play ... | [
"GO:0007155"
] | [
"cell adhesion"
] | [
"biological_process"
] | 1 | [
"PRINTS"
] | [
"PR00691"
] | [
"ADHESINB"
] | [
22818
] | 1 | [] | [] | [] | 0 | [
"1k0f",
"1psz",
"1toa",
"1xvl",
"2o1e",
"3cx3",
"3gi1",
"3hh8",
"3hjt",
"3mfq",
"3ujp",
"3zk7",
"3zk8",
"3zk9",
"3zka",
"3ztt",
"4cl2",
"4h0f",
"4irm",
"4k3v",
"4nno",
"4nnp",
"4oxq",
"4oxr",
"4udn",
"4udo",
"4uto",
"4utp",
"5afs",
"5hdq",
"5hx7",
"5i4k"... | 79 | [
"PUB00002025",
"PUB00002030"
] | [
"1671775",
"7505262"
] | [
"Nucleotide sequence of a gene coding for a saliva-binding protein (SsaB) from Streptococcus sanguis 12 and possible role of the protein in coaggregation with actinomyces.",
"Cloning and nucleotide sequence analysis of psaA, the Streptococcus pneumoniae gene encoding a 37-kilodalton protein homologous to previous... | [
1991,
1994
] | 2 | [
"IPR006128"
] | [
"IPR022434"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
159,
22379,
4,
25,
251
] | 5 | [] | [] | 0 | true | Family | Adhesin B | Adhesin B | AdhesinB | 5 |
IPR006130 | 6,130 | Aspartate/ornithine carbamoyltransferase | Asp/Orn_carbamoylTrfase | Family | 64,849 | false | false | This family contains two related enzymes: Aspartate carbamoyltransferase ( ) (ATCase) catalyses the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novo biosynthesis of pyrimidine nucleotides [ ]. In prokaryotes ATCase consists of two subunits: a catalytic chain (gene py... | [
"GO:0016597",
"GO:0016743",
"GO:0006520"
] | [
"amino acid binding",
"carboxyl- or carbamoyltransferase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS",
"PROSITE"
] | [
"PR00100",
"PS00097"
] | [
"AOTCASE",
"CARBAMOYLTRANSFERASE"
] | [
64084,
54845
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTO... | [
"2.1.3",
"2.1.3.2",
"PWY-5686",
"PWY-7790",
"PWY-7791",
"PDOC00091",
"R-CEL-500753",
"R-DDI-500753",
"R-DME-500753",
"R-GGA-187630",
"R-HSA-1268020",
"R-HSA-500753",
"R-HSA-70635",
"R-MMU-1268020",
"R-MMU-500753",
"R-MMU-70635",
"R-RNO-1268020",
"R-RNO-70635",
"R-SCE-1268020",
... | [
"EC:2.1.3",
"EC:2.1.3.2",
"METACYC:PWY-5686",
"METACYC:PWY-7790",
"METACYC:PWY-7791",
"PROSITEDOC:PDOC00091",
"REACTOME:R-CEL-500753",
"REACTOME:R-DDI-500753",
"REACTOME:R-DME-500753",
"REACTOME:R-GGA-187630",
"REACTOME:R-HSA-1268020",
"REACTOME:R-HSA-500753",
"REACTOME:R-HSA-70635",
"REAC... | 24 | [
"1a1s",
"1acm",
"1akm",
"1at1",
"1c9y",
"1d09",
"1duv",
"1dxh",
"1ekx",
"1ep9",
"1ezz",
"1f1b",
"1fb5",
"1fvo",
"1i5o",
"1js1",
"1ml4",
"1nbe",
"1ort",
"1oth",
"1pg5",
"1pvv",
"1q95",
"1r0b",
"1r0c",
"1raa",
"1rab",
"1rac",
"1rad",
"1rae",
"1raf",
"1rag"... | 192 | [
"PUB00000710",
"PUB00000720",
"PUB00001352",
"PUB00002421",
"PUB00004604",
"PUB00004607",
"PUB00074256"
] | [
"2662961",
"8098212",
"3109911",
"3015959",
"6377306",
"6379651",
"24332717"
] | [
"Evolutionary aspects of urea cycle enzyme genes.",
"The evolutionary history of the first three enzymes in pyrimidine biosynthesis.",
"Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoylt... | [
1989,
1993,
1987,
1986,
1984,
1984,
2014
] | 7 | [] | [
"IPR002082",
"IPR002292",
"IPR017702",
"IPR043695",
"IPR043696"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1908,
52720,
8778,
7,
1436
] | 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,
5,
3,
4,
8,
9,
2,
4,
14,
2,
2,
34
] | 13 | true | Family | Aspartate/ornithine carbamoyltransferase | Aspartate/ornithine carbamoyltransferase | Asp/Orn_carbamoylTrfase | 2 |
IPR006131 | 6,131 | Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain | Asp_carbamoyltransf_Asp/Orn-bd | Domain | 64,856 | false | false | This family contains two related enzymes: Aspartate carbamoyltransferase ( ) (ATCase) catalyzes the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novo biosynthesis of pyrimidine nucleotides [ ]. In prokaryotes ATCase consists of two subunits: a catalytic chain (gene py... | [
"GO:0016597",
"GO:0016743",
"GO:0006520"
] | [
"amino acid binding",
"carboxyl- or carbamoyltransferase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF00185"
] | [
"OTCace"
] | [
64856
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.3",
"2.1.3.2",
"PWY-5686",
"PWY-7790",
"PWY-7791",
"R-CEL-500753",
"R-DDI-500753",
"R-DME-500753",
"R-GGA-187630",
"R-HSA-1268020",
"R-HSA-500753",
"R-HSA-70635",
"R-MMU-1268020",
"R-MMU-500753",
"R-MMU-70635",
"R-RNO-1268020",
"R-RNO-70635",
"R-SCE-1268020",
"R-SCE-500753",... | [
"EC:2.1.3",
"EC:2.1.3.2",
"METACYC:PWY-5686",
"METACYC:PWY-7790",
"METACYC:PWY-7791",
"REACTOME:R-CEL-500753",
"REACTOME:R-DDI-500753",
"REACTOME:R-DME-500753",
"REACTOME:R-GGA-187630",
"REACTOME:R-HSA-1268020",
"REACTOME:R-HSA-500753",
"REACTOME:R-HSA-70635",
"REACTOME:R-MMU-1268020",
"RE... | 23 | [
"1a1s",
"1acm",
"1akm",
"1at1",
"1c9y",
"1d09",
"1duv",
"1dxh",
"1ekx",
"1ep9",
"1ezz",
"1f1b",
"1fb5",
"1fvo",
"1i5o",
"1js1",
"1ml4",
"1nbe",
"1ort",
"1oth",
"1pg5",
"1pvv",
"1q95",
"1r0b",
"1r0c",
"1raa",
"1rab",
"1rac",
"1rad",
"1rae",
"1raf",
"1rag"... | 192 | [
"PUB00000710",
"PUB00000720",
"PUB00001352",
"PUB00002421",
"PUB00004604",
"PUB00004607",
"PUB00007942"
] | [
"2662961",
"8098212",
"3109911",
"3015959",
"6377306",
"6379651",
"10318893"
] | [
"Evolutionary aspects of urea cycle enzyme genes.",
"The evolutionary history of the first three enzymes in pyrimidine biosynthesis.",
"Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoylt... | [
1989,
1993,
1987,
1986,
1984,
1984,
1999
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1900,
52849,
8701,
6,
1400
] | 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,
5,
3,
4,
6,
9,
2,
4,
13,
2,
2,
51
] | 13 | true | Domain | Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain | Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain | Asp_carbamoyltransf_Asp/Orn-bd | 2 |
IPR006132 | 6,132 | Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding | Asp/Orn_carbamoyltranf_P-bd | Domain | 64,771 | false | false | This entry contains two related enzymes: Aspartate carbamoyltransferase ( ) (ATCase) catalyzes the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novo biosynthesis of pyrimidine nucleotides [ ]. In prokaryotes ATCase consists of two subunits: a catalytic chain (gene pyr... | [
"GO:0016743",
"GO:0006520"
] | [
"carboxyl- or carbamoyltransferase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF02729"
] | [
"OTCace_N"
] | [
64771
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.3",
"2.1.3.2",
"PWY-5686",
"PWY-7790",
"PWY-7791",
"R-CEL-500753",
"R-DDI-500753",
"R-DME-500753",
"R-GGA-187630",
"R-HSA-1268020",
"R-HSA-500753",
"R-HSA-70635",
"R-MMU-1268020",
"R-MMU-500753",
"R-MMU-70635",
"R-RNO-1268020",
"R-RNO-70635",
"R-SCE-1268020",
"R-SCE-500753",... | [
"EC:2.1.3",
"EC:2.1.3.2",
"METACYC:PWY-5686",
"METACYC:PWY-7790",
"METACYC:PWY-7791",
"REACTOME:R-CEL-500753",
"REACTOME:R-DDI-500753",
"REACTOME:R-DME-500753",
"REACTOME:R-GGA-187630",
"REACTOME:R-HSA-1268020",
"REACTOME:R-HSA-500753",
"REACTOME:R-HSA-70635",
"REACTOME:R-MMU-1268020",
"RE... | 23 | [
"1a1s",
"1acm",
"1akm",
"1at1",
"1c9y",
"1d09",
"1duv",
"1dxh",
"1ekx",
"1ep9",
"1ezz",
"1f1b",
"1fb5",
"1fvo",
"1i5o",
"1js1",
"1ml4",
"1nbe",
"1ort",
"1oth",
"1pg5",
"1pvv",
"1q95",
"1r0b",
"1r0c",
"1raa",
"1rab",
"1rac",
"1rad",
"1rae",
"1raf",
"1rag"... | 192 | [
"PUB00000710",
"PUB00000720",
"PUB00001352",
"PUB00002421",
"PUB00004604",
"PUB00004607",
"PUB00007942"
] | [
"2662961",
"8098212",
"3109911",
"3015959",
"6377306",
"6379651",
"10318893"
] | [
"Evolutionary aspects of urea cycle enzyme genes.",
"The evolutionary history of the first three enzymes in pyrimidine biosynthesis.",
"Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoylt... | [
1989,
1993,
1987,
1986,
1984,
1984,
1999
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1895,
52922,
8572,
6,
1376
] | 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,
5,
3,
4,
9,
8,
2,
3,
13,
2,
2,
40
] | 13 | true | Domain | Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding | Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding | Asp/Orn_carbamoyltranf_P-bd | 5 |
IPR006133 | 6,133 | DNA-directed DNA polymerase, family B, exonuclease domain | DNA-dir_DNA_pol_B_exonuc | Domain | 28,469 | false | false | DNA is the biological information that instructs cells how to exist in an ordered fashion: accurate replication is thus one of the most important events in the life cycle of a cell. This function is performed by DNA- directed DNA-polymerases ) by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03104"
] | [
"DNA_pol_B_exo1"
] | [
28469
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.7",
"R-CEL-110314",
"R-CEL-5651801",
"R-CEL-5656169",
"R-CEL-5696397",
"R-CEL-5696400",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-69091",
"R-CEL-69166",
"R-CEL-69183",
"R-DDI-110314",
"R-DDI-113501",
"R-DDI-5651801",
"R-DDI-5656169",
"R-DDI-5696397",
"R-DDI-6782135",
"R-DDI-6... | [
"EC:2.7.7.7",
"REACTOME:R-CEL-110314",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-5656169",
"REACTOME:R-CEL-5696397",
"REACTOME:R-CEL-5696400",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-69091",
"REACTOME:R-CEL-69166",
"REACTOME:R-CEL-69183",
"REACTOME:R-DDI-110314",
... | 141 | [
"1clq",
"1d5a",
"1ig9",
"1ih7",
"1noy",
"1noz",
"1q8i",
"1q9x",
"1q9y",
"1qht",
"1qqc",
"1s5j",
"1tgo",
"1waf",
"1waj",
"1wn7",
"1wns",
"2atq",
"2dtu",
"2dy4",
"2gv9",
"2jgu",
"2oyq",
"2ozm",
"2ozs",
"2p5g",
"2p5o",
"2vwj",
"2vwk",
"2xhb",
"3a2f",
"3cfo"... | 353 | [
"PUB00000436",
"PUB00010600"
] | [
"8679562",
"9757117"
] | [
"Crystal structures of an NH2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions.",
"Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon."
] | [
1996,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1220,
4323,
19595,
2926,
405
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
32,
6,
6,
7,
1,
23,
12,
4,
10,
20,
4,
4,
44
] | 13 | true | Domain | DNA-directed DNA polymerase, family B, exonuclease domain | DNA-directed DNA polymerase, family B, exonuclease domain | DNA-dir_DNA_pol_B_exonuc | 8 |
IPR006134 | 6,134 | DNA-directed DNA polymerase, family B, multifunctional domain | DNA-dir_DNA_pol_B_multi_dom | Domain | 31,604 | false | false | DNA is the biological information that instructs cells how to exist in an ordered fashion: accurate replication is thus one of the most important events in the life cycle of a cell. This function is performed by DNA- directed DNA-polymerases ) by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growi... | [
"GO:0000166",
"GO:0003677"
] | [
"nucleotide binding",
"DNA binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00136"
] | [
"DNA_pol_B"
] | [
31604
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.7",
"R-CEL-110314",
"R-CEL-5651801",
"R-CEL-5656169",
"R-CEL-5696397",
"R-CEL-5696400",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-69091",
"R-CEL-69166",
"R-CEL-69183",
"R-DDI-110314",
"R-DDI-113501",
"R-DDI-5651801",
"R-DDI-5656169",
"R-DDI-5696397",
"R-DDI-6782135",
"R-DDI-6... | [
"EC:2.7.7.7",
"REACTOME:R-CEL-110314",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-5656169",
"REACTOME:R-CEL-5696397",
"REACTOME:R-CEL-5696400",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-69091",
"REACTOME:R-CEL-69166",
"REACTOME:R-CEL-69183",
"REACTOME:R-DDI-110314",
... | 139 | [
"1clq",
"1d5a",
"1ig9",
"1ih7",
"1q8i",
"1q9x",
"1q9y",
"1qht",
"1qqc",
"1s5j",
"1tgo",
"1waf",
"1waj",
"1wn7",
"1wns",
"2atq",
"2dtu",
"2dy4",
"2gv9",
"2jgu",
"2oyq",
"2ozm",
"2ozs",
"2p5g",
"2p5o",
"2vwj",
"2vwk",
"2xhb",
"3a2f",
"3cfo",
"3cfp",
"3cfr"... | 301 | [
"PUB00000436",
"PUB00010600",
"PUB00036457",
"PUB00097416",
"PUB00097417"
] | [
"8679562",
"9757117",
"7516581",
"19718023",
"23940661"
] | [
"Crystal structures of an NH2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions.",
"Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon.",
"Crystal structure of rat DNA polymerase bet... | [
1996,
1998,
1994,
2009,
2013
] | 5 | [] | [
"IPR045846"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1716,
4875,
17539,
7012,
462
] | 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,
5,
5,
7,
1,
28,
8,
3,
6,
19,
3,
3,
29
] | 13 | true | Domain | DNA-directed DNA polymerase, family B, multifunctional domain | DNA-directed DNA polymerase, family B, multifunctional domain | DNA-dir_DNA_pol_B_multi_dom | 5 |
IPR006135 | 6,135 | Type III secretion system substrate exporter | T3SS_substrate_exporter | Family | 24,431 | false | false | Salmonella, and related proteobacteria, secrete large amounts of proteins into the culture media. The major secreted proteins are either flagellar proteins or virulence factors [ ], secreted through the flagellar or virulence export structures respectively. Both secretion systems penetrate the inner and outer membranes... | [
"GO:0009306",
"GO:0016020"
] | [
"protein secretion",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF01312",
"PR00950",
"PTHR30531"
] | [
"Bac_export_2",
"TYPE3IMSPROT",
""
] | [
24431,
18045,
24075
] | 3 | [] | [] | [] | 0 | [
"2jlh",
"2jli",
"2jlj",
"2ml9",
"2v5g",
"2vt1",
"2w0r",
"3b0z",
"3b1s",
"3bzl",
"3bzo",
"3bzp",
"3bzr",
"3bzs",
"3bzt",
"3bzv",
"3bzx",
"3bzy",
"3bzz",
"3c00",
"3c01",
"3c03",
"3t7y",
"5cul",
"6ejp",
"6s3l",
"6z0w",
"8axk",
"8z5s",
"8z5u",
"8z5x",
"8z60"... | 32 | [
"PUB00003585",
"PUB00007583",
"PUB00007898",
"PUB00020771",
"PUB00049582",
"PUB00054227",
"PUB00054229"
] | [
"9618447",
"10564516",
"10334981",
"8169210",
"8045883",
"9554854",
"16246842"
] | [
"Type III protein secretion systems in bacterial pathogens of animals and plants.",
"Flagellar proteins and type III-exported virulence factors are the predominant proteins secreted into the culture media of Salmonella typhimurium.",
"Type III secretion machines: bacterial devices for protein delivery into host... | [
1998,
1999,
1999,
1994,
1994,
1998,
2005
] | 7 | [] | [
"IPR004683",
"IPR006136",
"IPR006307"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
24108,
37,
286
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Type III secretion system substrate exporter | Type III secretion system substrate exporter | T3SS_substrate_exporter | 1 |
IPR006136 | 6,136 | Flagellar biosynthetic protein FlhB | FlhB | Family | 10,329 | false | false | FlhB and its functionally equivalent orthologues, from among a larger superfamily of proteins involved in type III protein export systems, are involved in flagellar protein export [ ]. Proteins in this entry play roles specifically related to flagellar structures [ ]. | [
"GO:0015031",
"GO:0044780",
"GO:0016020"
] | [
"protein transport",
"bacterial-type flagellum assembly",
"membrane"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00328"
] | [
"flhB"
] | [
10329
] | 1 | [
"GP"
] | [
"GenProp0879"
] | [
"GP:GenProp0879"
] | 1 | [
"6s3l",
"8z5s",
"8z5u",
"8z5x",
"8z60"
] | 5 | [
"PUB00002258",
"PUB00076719"
] | [
"8002587",
"26244937"
] | [
"Molecular characterization of the Salmonella typhimurium flhB operon and its protein products.",
"Weak Interactions between Salmonella enterica FlhB and Other Flagellar Export Apparatus Proteins Govern Type III Secretion Dynamics."
] | [
1994,
2015
] | 2 | [
"IPR006135"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
10220,
8,
101
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flagellar biosynthetic protein FlhB | Flagellar biosynthetic protein FlhB | FlhB | 4 |
IPR006138 | 6,138 | NADH-ubiquinone oxidoreductase, 20 Kd subunit | NADH_UQ_OxRdtase_20Kd_su | Family | 38,641 | false | false | Among the many polypeptide subunits that make up complex I, there is one with a molecular weight of 20kDa (in mammals) [ ], which is a component of the iron-sulphur (IP) fragment of the enzyme. It seems to bind a 4Fe-4S iron-sulphur cluster. The 20kDa subunit has been found to be nuclear encoded, as a precursor form wi... | [
"GO:0008137",
"GO:0048038",
"GO:0051539"
] | [
"NADH dehydrogenase (ubiquinone) activity",
"quinone binding",
"4 iron, 4 sulfur cluster binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"HAMAP",
"PROSITE",
"NCBIFAM"
] | [
"MF_01356",
"PS01150",
"TIGR01957"
] | [
"NDH1_NuoB",
"COMPLEX1_20K",
"nuoB_fam"
] | [
34898,
32412,
36827
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.1.1.-",
"GenProp0135",
"GenProp1198",
"GenProp1230",
"GenProp1254",
"GenProp1341",
"GenProp1537",
"GenProp1583",
"GenProp1608",
"GenProp1637",
"GenProp1751",
"PDOC00858",
"R-BTA-611105",
"R-BTA-6799198",
"R-CEL-6799198",
"R-DDI-6799198",
"R-HSA-611105",
"R-HSA-6799198",
"R-MMU... | [
"EC:7.1.1.-",
"GP:GenProp0135",
"GP:GenProp1198",
"GP:GenProp1230",
"GP:GenProp1254",
"GP:GenProp1341",
"GP:GenProp1537",
"GP:GenProp1583",
"GP:GenProp1608",
"GP:GenProp1637",
"GP:GenProp1751",
"PROSITEDOC:PDOC00858",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-CEL-679... | 20 | [
"2fug",
"2ybb",
"3i9v",
"3iam",
"3ias",
"3m9s",
"4hea",
"4wz7",
"5gpn",
"5gup",
"5lc5",
"5ldw",
"5ldx",
"5lnk",
"5o31",
"5xtb",
"5xtd",
"5xth",
"5xti",
"6g2j",
"6g72",
"6gcs",
"6h8k",
"6hum",
"6i0d",
"6i1p",
"6khi",
"6khj",
"6l7o",
"6l7p",
"6nbq",
"6nbx"... | 334 | [
"PUB00001635",
"PUB00005074",
"PUB00043561",
"PUB00045437"
] | [
"1577158",
"1470679",
"10940377",
"18394423"
] | [
"NADH: ubiquinone oxidoreductase from bovine heart mitochondria. A fourth nuclear encoded subunit with a homologue encoded in chloroplast genomes.",
"The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.",
"The respiratory complex I of bacteria, archaea and eukarya and its module common with mem... | [
1992,
1992,
2000,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
796,
18969,
18350,
526
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
7,
1,
1,
3,
3,
7,
1,
1,
12,
6,
14
] | 11 | true | Family | NADH-ubiquinone oxidoreductase, 20 Kd subunit | NADH-ubiquinone oxidoreductase, 20 Kd subunit | NADH_UQ_OxRdtase_20Kd_su | 7 |
IPR006139 | 6,139 | D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain | D-isomer_2_OHA_DH_cat_dom | Domain | 133,947 | false | false | A number of NAD-dependent 2-hydroxyacid dehydrogenases which seem to be specific for the D-isomer of their substrate have been shown to be functionally and structurally related. The catalytic domain contains a number of conserved charged residues which may play a role in the catalytic mechanism [ ]. The NAD-binding dom... | [
"GO:0016616",
"GO:0051287"
] | [
"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor",
"NAD binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00389"
] | [
"2-Hacid_dh"
] | [
133947
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"1.1.1",
"GenProp1267",
"GenProp1633",
"GenProp1747",
"R-BTA-4641265",
"R-BTA-9764725",
"R-CEL-3769402",
"R-CEL-4641265",
"R-CEL-9764725",
"R-DME-3769402",
"R-DME-3899300",
"R-DME-4641265",
"R-DME-9764725",
"R-HSA-3769402",
"R-HSA-389661",
"R-HSA-3899300",
"R-HSA-4641265",
"R-HSA-5... | [
"EC:1.1.1",
"GP:GenProp1267",
"GP:GenProp1633",
"GP:GenProp1747",
"REACTOME:R-BTA-4641265",
"REACTOME:R-BTA-9764725",
"REACTOME:R-CEL-3769402",
"REACTOME:R-CEL-4641265",
"REACTOME:R-CEL-9764725",
"REACTOME:R-DME-3769402",
"REACTOME:R-DME-3899300",
"REACTOME:R-DME-4641265",
"REACTOME:R-DME-97... | 33 | [
"1dxy",
"1gdh",
"1hku",
"1hl3",
"1j49",
"1j4a",
"1mx3",
"1psd",
"1qp8",
"1sc6",
"1wwk",
"1xdw",
"1yba",
"1ygy",
"2cuk",
"2d0i",
"2dbq",
"2dbr",
"2dbz",
"2dld",
"2ekl",
"2fss",
"2g76",
"2gcg",
"2go1",
"2gsd",
"2gug",
"2h1s",
"2hu2",
"2j6i",
"2nac",
"2nad"... | 182 | [
"PUB00019065"
] | [
"9126843"
] | [
"Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2611,
96702,
33146,
13,
1475
] | 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",... | [
39,
2,
60,
18,
4,
26,
15,
7,
42,
23,
4,
5,
73
] | 13 | true | Domain | D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain | D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain | D-isomer_2_OHA_DH_cat_dom | 5 |
IPR006140 | 6,140 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain | D-isomer_DH_NAD-bd | Domain | 166,655 | false | false | A number of NAD-dependent 2-hydroxyacid dehydrogenases which seem to be specific for the D-isomer of their substrate have been shown to be functionally and structurally related. All contain a glycine-rich region located in the central section of these enzymes, this region corresponds to the NAD-binding domain. This dom... | [
"GO:0051287"
] | [
"NAD binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02826"
] | [
"2-Hacid_dh_C"
] | [
166655
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"1.1.1",
"GenProp1267",
"GenProp1633",
"GenProp1747",
"PDOC00063",
"R-BTA-4641265",
"R-BTA-9764725",
"R-CEL-3769402",
"R-CEL-4641265",
"R-CEL-9764725",
"R-DME-3769402",
"R-DME-3899300",
"R-DME-4641265",
"R-DME-9764725",
"R-HSA-3769402",
"R-HSA-389661",
"R-HSA-3899300",
"R-HSA-46412... | [
"EC:1.1.1",
"GP:GenProp1267",
"GP:GenProp1633",
"GP:GenProp1747",
"PROSITEDOC:PDOC00063",
"REACTOME:R-BTA-4641265",
"REACTOME:R-BTA-9764725",
"REACTOME:R-CEL-3769402",
"REACTOME:R-CEL-4641265",
"REACTOME:R-CEL-9764725",
"REACTOME:R-DME-3769402",
"REACTOME:R-DME-3899300",
"REACTOME:R-DME-4641... | 34 | [
"1dxy",
"1gdh",
"1hku",
"1hl3",
"1j49",
"1j4a",
"1mx3",
"1psd",
"1qp8",
"1sc6",
"1wwk",
"1xdw",
"1yba",
"1ygy",
"2cuk",
"2d0i",
"2dbq",
"2dbr",
"2dbz",
"2dld",
"2ekl",
"2fss",
"2g76",
"2gcg",
"2go1",
"2gsd",
"2gug",
"2h1s",
"2hu2",
"2j6i",
"2nac",
"2nad"... | 217 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2773,
120705,
40978,
15,
2184
] | 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",... | [
48,
3,
61,
19,
5,
25,
13,
9,
52,
21,
7,
5,
114
] | 13 | true | Domain | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain | D-isomer_DH_NAD-bd | 3 |
IPR006141 | 6,141 | Intein N-terminal splicing region | Intein_N | PTM | 18,484 | false | false | Inteins, or protein introns, are parts of protein sequences that are post-translationally excised, their flanking regions (exteins) being spliced together to yield an additional protein product [ , ]. This process is believed to be self-catalysed, apparently initiating at the C-terminal splice junction, where a conserv... | [
"GO:0016539"
] | [
"intein-mediated protein splicing"
] | [
"biological_process"
] | 1 | [
"PROFILE",
"NCBIFAM"
] | [
"PS50817",
"TIGR01445"
] | [
"INTEIN_N_TER",
"intein_Nterm"
] | [
18393,
6331
] | 2 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp0010",
"PDOC00687",
"R-DDI-76061",
"R-DDI-76066",
"R-DME-209338",
"R-DME-209471",
"R-DME-5358346",
"R-DME-5362798",
"R-DME-5632681",
"R-DRE-5358346",
"R-DRE-5362798",
"R-DRE-5632681",
"R-HSA-373080",
"R-HSA-5358346",
"R-HSA-5362768",
"R-HSA-5362798",
"R-HSA-5632681",
"R-HSA... | [
"GP:GenProp0010",
"PROSITEDOC:PDOC00687",
"REACTOME:R-DDI-76061",
"REACTOME:R-DDI-76066",
"REACTOME:R-DME-209338",
"REACTOME:R-DME-209471",
"REACTOME:R-DME-5358346",
"REACTOME:R-DME-5362798",
"REACTOME:R-DME-5632681",
"REACTOME:R-DRE-5358346",
"REACTOME:R-DRE-5362798",
"REACTOME:R-DRE-5632681"... | 35 | [
"1am2",
"1at0",
"1dfa",
"1dq3",
"1gpp",
"1lws",
"1lwt",
"1mi8",
"1vde",
"1zd7",
"1zde",
"2cw7",
"2cw8",
"2imz",
"2in0",
"2in8",
"2in9",
"2jmz",
"2jnq",
"2keq",
"2l8l",
"2lcj",
"2lqm",
"2lwy",
"3ifj",
"3igd",
"3nzm",
"4e2t",
"4e2u",
"4gig",
"4kl5",
"4kl6"... | 62 | [
"PUB00004447",
"PUB00006583",
"PUB00007299",
"PUB00007300",
"PUB00007301",
"PUB00009828"
] | [
"8165123",
"7756989",
"11092822",
"9092614",
"10592269",
"12142479"
] | [
"Protein splicing elements: inteins and exteins--a definition of terms and recommended nomenclature.",
"Conserved sequence features of inteins (protein introns) and their use in identifying new inteins and related proteins.",
"Protein-splicing intein: Genetic mobility, origin, and evolution.",
"Compilation an... | [
1994,
1994,
2000,
1997,
2000,
2002
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1756,
10170,
4914,
935,
709
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
10,
20,
1,
4,
6,
8,
1
] | 8 | true | PTM | Intein N-terminal splicing region | Intein N-terminal splicing region | Intein_N | 9 |
IPR006142 | 6,142 | Intein | INTEIN | Domain | 6,968 | false | false | Inteins, or protein introns, are parts of protein sequences that are post-translationally excised, their flanking regions (exteins) being spliced together to yield an additional protein product [ , ]. This process is believed to be self-catalysed, apparently initiating at the C-terminal splice junction, where a conserv... | [
"GO:0016539"
] | [
"intein-mediated protein splicing"
] | [
"biological_process"
] | 1 | [
"PRINTS"
] | [
"PR00379"
] | [
"INTEIN"
] | [
6968
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-SCE-1222556",
"R-SCE-77387",
"R-SCE-917977",
"R-SCE-9639288"
] | [
"REACTOME:R-SCE-1222556",
"REACTOME:R-SCE-77387",
"REACTOME:R-SCE-917977",
"REACTOME:R-SCE-9639288"
] | 4 | [
"1b24",
"1dfa",
"1dq3",
"1ef0",
"1jva",
"1lws",
"1lwt",
"1um2",
"1vde",
"2cw7",
"2cw8",
"2vs7",
"2vs8",
"4d6n",
"4d6o",
"4un7",
"4un8",
"4un9",
"4una",
"4unb",
"4unc",
"4ut0",
"5a0w",
"5ak9",
"5akf",
"5akm",
"5akn",
"5o6g",
"5o6i",
"7qss",
"7qst",
"7qsu"... | 33 | [
"PUB00004447",
"PUB00006583",
"PUB00009828"
] | [
"8165123",
"7756989",
"12142479"
] | [
"Protein splicing elements: inteins and exteins--a definition of terms and recommended nomenclature.",
"Conserved sequence features of inteins (protein introns) and their use in identifying new inteins and related proteins.",
"Inteins: structure, function, and evolution."
] | [
1994,
1994,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1392,
4553,
310,
338,
375
] | 5 | [
"Arabidopsis thaliana",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
2
] | 2 | true | Domain | Intein | Intein | INTEIN | 6 |
IPR006143 | 6,143 | RND efflux pump, membrane fusion protein | RND_pump_MFP | Family | 145,258 | false | false | This entry represents a large family of polypeptides, the MFP (for membrane fusion protein) family. MFPs are a component of the RND family of transporters (RND refers to resistance, nodulation, and cell division). MFPs are proposed to span the periplasm in some way linking the inner and outer membranes [ ]. However, so... | [
"GO:0022857",
"GO:0055085",
"GO:0016020"
] | [
"transmembrane transporter activity",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01730"
] | [
"RND_mfp"
] | [
145258
] | 1 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1168",
"R-HSA-9638334",
"R-HSA-9760173",
"R-HSA-9913143"
] | [
"GP:GenProp1168",
"REACTOME:R-HSA-9638334",
"REACTOME:R-HSA-9760173",
"REACTOME:R-HSA-9913143"
] | 4 | [
"1t5e",
"1vf7",
"2f1m",
"2v4d",
"3fpp",
"3h94",
"3lnn",
"3ne5",
"3ooc",
"3opo",
"3ow7",
"3t51",
"3t53",
"3t56",
"4dk0",
"4dk1",
"4dnr",
"4dnt",
"4dop",
"4kks",
"4kkt",
"4kku",
"4l8j",
"5ng5",
"5nik",
"5nil",
"5o66",
"5v5s",
"6iok",
"6iol",
"6ta5",
"6ta6"... | 37 | [
"PUB00000138",
"PUB00001184",
"PUB00001199",
"PUB00001820",
"PUB00007661",
"PUB00032073",
"PUB00055580"
] | [
"1622271",
"2184029",
"2249654",
"1427098",
"1495479",
"15117957",
"16237030"
] | [
"Molecular analyses of the lactococcin A gene cluster from Lactococcus lactis subsp. lactis biovar diacetylactis WM4.",
"Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin.",
"Genetic analysis of an MDR-like export system: the... | [
1992,
1990,
1990,
1992,
1992,
2004,
2005
] | 7 | [] | [
"IPR005695",
"IPR022824",
"IPR022871",
"IPR058194",
"IPR058623",
"IPR058628",
"IPR061505"
] | 0 | 7 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Plasmid pMCBF1",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
143645,
160,
2,
1,
2,
1448
] | 6 | [
"Escherichia coli (strain K12)"
] | [
8
] | 1 | true | Family | RND efflux pump, membrane fusion protein | RND efflux pump, membrane fusion protein | RND_pump_MFP | 3 |
IPR006144 | 6,144 | Secretion protein HlyD, conserved site | Secretion_HlyD_CS | Conserved_site | 8,433 | false | false | Gram-negative bacteria produce a number of proteins which are secreted into the growth medium by a mechanism that does not require a cleaved N-terminal signal sequence. These proteins, while having different functions, require the help of two or more proteins for their secretion across the cell envelope. The secretion ... | [
"GO:0009306",
"GO:0016020"
] | [
"protein secretion",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00543"
] | [
"HLYD_FAMILY"
] | [
8433
] | 1 | [
"PROSITEDOC",
"REACTOME"
] | [
"PDOC00469",
"R-HSA-9760173"
] | [
"PROSITEDOC:PDOC00469",
"REACTOME:R-HSA-9760173"
] | 2 | [
"5nen",
"7sgr",
"8dck"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nitrosopumilus salarius BD31",
"Eukaryota",
"Peduovirinae sp. ctGB41",
"metagenomes"
] | [
8364,
1,
18,
1,
49
] | 5 | [] | [] | 0 | true | Conserved_site | Secretion protein HlyD, conserved site | Secretion protein HlyD, conserved site | Secretion_HlyD_CS | 9 |
IPR006145 | 6,145 | Pseudouridine synthase, RsuA/RluA-like | PsdUridine_synth_RsuA/RluA | Domain | 151,422 | false | false | Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine (Psi) in a variety of RNA molecules, and may function as RNA chaperones. Pseudouridine is the most abundant modified nucleotide found in all cellular RNAs. There are four distinct families of pseudouridine synthases that share no global sequ... | [
"GO:0003723",
"GO:0009982",
"GO:0001522",
"GO:0009451"
] | [
"RNA binding",
"pseudouridine synthase activity",
"pseudouridine synthesis",
"RNA modification"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PFAM",
"CDD"
] | [
"PF00849",
"cd02869"
] | [
"PseudoU_synth_2",
"PseudoU_synth_RluA_like"
] | [
151335,
77977
] | 2 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"5.4.99",
"R-HSA-6793080",
"R-HSA-9937008"
] | [
"EC:5.4.99",
"REACTOME:R-HSA-6793080",
"REACTOME:R-HSA-9937008"
] | 3 | [
"1ksk",
"1ksl",
"1ksv",
"1prz",
"1qyu",
"1v9f",
"1v9k",
"1vio",
"1xpi",
"2gml",
"2i82",
"2ist",
"2olw",
"2oml",
"3dh3",
"4lab",
"4lgt",
"5uba",
"5vbb",
"6yxx",
"6yxy",
"7am2",
"7aoi",
"7bl5",
"9cl9"
] | 25 | [
"PUB00018355",
"PUB00032035",
"PUB00037409",
"PUB00037953",
"PUB00045922",
"PUB00092579",
"PUB00095796"
] | [
"11953756",
"15078091",
"14659742",
"16511038",
"10529181",
"19664587",
"11720289"
] | [
"Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP.",
"Crystal structures of the catalytic domains of pseudouridine synthases RluC and RluD from Escherichia coli.",
"Crystal structure of the RluD pseudouridine synthase catalytic module, an enzyme that modifies 23S rRNA and is essenti... | [
2002,
2004,
2004,
2005,
1999,
2009,
2001
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Viruses",
"unclassified sequences"
] | [
131432,
18159,
37,
7,
1787
] | 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",... | [
45,
3,
8,
4,
8,
20,
8,
1,
20,
14,
4,
1,
64
] | 13 | true | Domain | Pseudouridine synthase, RsuA/RluA-like | Pseudouridine synthase, RsuA/RluA-like | PsdUridine_synth_RsuA/RluA | 8 |
IPR006146 | 6,146 | 5'-Nucleotidase, conserved site | 5'-Nucleotdase_CS | Conserved_site | 25,465 | false | false | 5'-nucleotidases ( ) are enzymes that catalyse the hydrolysis of phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules. 5'-nucleotidase is a ubiquitous enzyme found in a wide variety of species and which occurs in different cellular locations. All these proteins share regions ... | [
"GO:0000166",
"GO:0016788",
"GO:0046872"
] | [
"nucleotide binding",
"hydrolase activity, acting on ester bonds",
"metal ion binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00785",
"PS00786"
] | [
"5_NUCLEOTIDASE_1",
"5_NUCLEOTIDASE_2"
] | [
13187,
20151
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3",
"3.1.3.5",
"PWY-5381",
"PWY-5695",
"PWY-6596",
"PWY-6606",
"PWY-6607",
"PWY-6608",
"PWY-7185",
"PWY-7821",
"PDOC00627",
"R-HSA-196807",
"R-HSA-73621",
"R-HSA-74259",
"R-HSA-9660826",
"R-MMU-196807",
"R-MMU-73621",
"R-MMU-74259",
"R-RNO-196807",
"R-RNO-73621",
"R-RNO-... | [
"EC:3.1.3",
"EC:3.1.3.5",
"METACYC:PWY-5381",
"METACYC:PWY-5695",
"METACYC:PWY-6596",
"METACYC:PWY-6606",
"METACYC:PWY-6607",
"METACYC:PWY-6608",
"METACYC:PWY-7185",
"METACYC:PWY-7821",
"PROSITEDOC:PDOC00627",
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-73621",
"REACTOME:R-HSA-74259",
"REAC... | 21 | [
"1ho5",
"1hp1",
"1hpu",
"1oi8",
"1oid",
"1oie",
"1ush",
"2ush",
"2z1a",
"3gve",
"3ivd",
"3ive",
"3jyf",
"3qfk",
"3ztv",
"3zu0",
"4h1s",
"4h1y",
"4h2b",
"4h2f",
"4h2g",
"4h2i",
"4q7f",
"4wwl",
"5eqv",
"5h7w",
"6hxw",
"6s7f",
"6s7h",
"6tve",
"6tvg",
"6tvx"... | 69 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
60,
21833,
2,
3461,
109
] | 5 | [
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
5,
2,
5,
3,
5
] | 6 | true | Conserved_site | 5'-Nucleotidase, conserved site | 5'-Nucleotidase, conserved site | 5'-Nucleotdase_CS | 5 |
IPR006148 | 6,148 | Glucosamine/galactosamine-6-phosphate isomerase | Glc/Gal-6P_isomerase | Domain | 43,735 | false | false | This domain is characteristic of the enzymes 6-phosphogluconolactonase ( ), Glucosamine-6-phosphate isomerase ( ), and Galactosamine-6-phosphate isomerase. 6-Phosphogluconolactonase is the enzyme responsible for the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate, the second step in the pentose phosphate pa... | [
"GO:0005975"
] | [
"carbohydrate metabolic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01182"
] | [
"Glucosamine_iso"
] | [
43735
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.5.99.6",
"PWY-5514",
"PWY-6855",
"PWY-6906",
"R-BTA-70171",
"R-CEL-70171",
"R-CEL-71336",
"R-DDI-70171",
"R-DDI-71336",
"R-DME-70171",
"R-DME-71336",
"R-HSA-70171",
"R-HSA-71336",
"R-MMU-70171",
"R-MMU-71336",
"R-PFA-5628897",
"R-PFA-71336",
"R-RNO-71336",
"R-SCE-71336",
"R-... | [
"EC:3.5.99.6",
"METACYC:PWY-5514",
"METACYC:PWY-6855",
"METACYC:PWY-6906",
"REACTOME:R-BTA-70171",
"REACTOME:R-CEL-70171",
"REACTOME:R-CEL-71336",
"REACTOME:R-DDI-70171",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-70171",
"REACTOME:R-DME-71336",
"REACTOME:R-HSA-70171",
"REACTOME:R-HSA-71336",
... | 21 | [
"1cd5",
"1dea",
"1fqo",
"1frz",
"1fs5",
"1fs6",
"1fsf",
"1hor",
"1hot",
"1jt9",
"1ne7",
"1pbt",
"1vl1",
"1y89",
"2bkv",
"2bkx",
"2j0e",
"2ri0",
"2ri1",
"2wu1",
"3ch7",
"3css",
"3e15",
"3e7f",
"3eb9",
"3hn6",
"3ico",
"3lhi",
"3lwd",
"3nwp",
"3oc6",
"3tx2"... | 41 | [
"PUB00005253"
] | [
"8747459"
] | [
"Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution."
] | [
1995
] | 1 | [] | [
"IPR005900"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Marseillevirus LCMAC201",
"unclassified sequences"
] | [
7,
30238,
13044,
1,
445
] | 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",... | [
18,
2,
6,
4,
3,
15,
20,
2,
7,
16,
4,
1,
16
] | 13 | true | Domain | Glucosamine/galactosamine-6-phosphate isomerase | Glucosamine/galactosamine-6-phosphate isomerase | Glc/Gal-6P_isomerase | 4 |
IPR006150 | 6,150 | Cysteine-rich repeat | Cys_repeat_1 | Repeat | 7,050 | false | false | This repeat, originally named as Worm-specific repeat type 1, is found in several Caenorhabditis elegans proteins, as well as some other eukaryotes. The region contains several conserved cysteines that probably form disulphide bridges and is often found associated with kunitz domains that may function as serine peptida... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00289"
] | [
"WR1"
] | [
7050
] | 1 | [
"REACTOME"
] | [
"R-CEL-114608"
] | [
"REACTOME:R-CEL-114608"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
26,
7024
] | 2 | [
"Caenorhabditis elegans",
"Drosophila melanogaster"
] | [
76,
16
] | 2 | true | Repeat | Cysteine-rich repeat | Cysteine-rich repeat | Cys_repeat_1 | 5 |
IPR006151 | 6,151 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | Shikm_DH/Glu-tRNA_Rdtase | Domain | 42,896 | false | false | This entry represents a domain found in shikimate and quinate dehydrogenases, as well as glutamyl-tRNA reductases. Shikimate 5-dehydrogenase ( ) catalyses the conversion of shikimate to 5-dehydroshikimate [ , ]. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01488"
] | [
"Shikimate_DH"
] | [
42896
] | 1 | [] | [] | [] | 0 | [
"1gpj",
"1nvt",
"1nyt",
"1p74",
"1p77",
"1wxd",
"2cy0",
"2d5c",
"2egg",
"2ev9",
"2gpt",
"2hk7",
"2hk8",
"2hk9",
"2o7q",
"2o7s",
"3don",
"3doo",
"3fbt",
"3o8q",
"3oj0",
"3pgj",
"3pwz",
"3sef",
"3u62",
"4n7r",
"4omu",
"5che",
"5yjl",
"6bmb",
"6bmq",
"7cok"... | 37 | [
"PUB00014334",
"PUB00028042",
"PUB00028043",
"PUB00035783"
] | [
"15012217",
"12906831",
"12837789",
"16228559"
] | [
"THE SHIKIMATE PATHWAY.",
"Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution.",
"The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode.",
"Structure and function of glutamyl-tRNA reductase, the first enzyme of tetrapy... | [
1999,
2003,
2003,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1575,
34729,
5943,
649
] | 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)",
"Zea mays"
] | [
18,
2,
3,
11,
1,
32
] | 6 | true | Domain | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | Shikm_DH/Glu-tRNA_Rdtase | 9 |
IPR006153 | 6,153 | Cation/H+ exchanger, transmembrane domain | Cation/H_exchanger_TM | Domain | 156,832 | false | false | This entry represents the transmembrane region of a number of cation/proton exchangers, including Na+/H+ exchangers, K+/H+ exchangers and Na+(K+,Li+,Rb+)/H+ exchangers. Sodium proton exchangers (NHEs) constitute a large family of integral membrane protein transporters that are responsible for the counter-transport of p... | [
"GO:0015297",
"GO:0006812",
"GO:0055085",
"GO:1902600",
"GO:0016020"
] | [
"antiporter activity",
"monoatomic cation transport",
"transmembrane transport",
"proton transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PFAM"
] | [
"PF00999"
] | [
"Na_H_Exchanger"
] | [
156832
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-2160916",
"R-BTA-425986",
"R-CEL-2160916",
"R-CEL-425986",
"R-DDI-425986",
"R-HSA-2160916",
"R-HSA-2672351",
"R-HSA-425986",
"R-HSA-5619052",
"R-HSA-5619092",
"R-MMU-2160916",
"R-MMU-2672351",
"R-MMU-425986",
"R-RNO-2160916",
"R-RNO-425986",
"R-SCE-425986",
"R-SPO-425986",
"... | [
"REACTOME:R-BTA-2160916",
"REACTOME:R-BTA-425986",
"REACTOME:R-CEL-2160916",
"REACTOME:R-CEL-425986",
"REACTOME:R-DDI-425986",
"REACTOME:R-HSA-2160916",
"REACTOME:R-HSA-2672351",
"REACTOME:R-HSA-425986",
"REACTOME:R-HSA-5619052",
"REACTOME:R-HSA-5619092",
"REACTOME:R-MMU-2160916",
"REACTOME:R-... | 18 | [
"2mdf",
"4bwz",
"4cz8",
"4cz9",
"4cza",
"4czb",
"4d0a",
"5bz2",
"5bz3",
"6z3y",
"6z3z",
"7b4l",
"7b4m",
"7dsv",
"7dsw",
"7dsx",
"7p1i",
"7p1j",
"7p1k",
"7x2u",
"7y3e",
"8bxg",
"8by2",
"8hya",
"8iwo",
"8j2m",
"8jd9",
"8jda",
"8otq",
"8otw",
"8otx",
"8pcz"... | 63 | [
"PUB00001715",
"PUB00002996",
"PUB00003039",
"PUB00044828",
"PUB00044829",
"PUB00044830",
"PUB00044831",
"PUB00044832",
"PUB00044833",
"PUB00044834"
] | [
"9537504",
"9278382",
"9507001",
"12027219",
"12502567",
"16734752",
"17071327",
"16513813",
"11187762",
"17218973"
] | [
"Comparative molecular analysis of Na+/H+ exchangers: a unified model for Na+/H+ antiport?",
"Na+/H+ exchangers of mammalian cells.",
"Identification of a mitochondrial Na+/H+ exchanger.",
"The Na+/H+ exchanger gene family.",
"Multiple modes of regulation of Na+/H+ exchangers.",
"Na+/H+ exchangers and the... | [
1998,
1997,
1998,
2002,
2002,
2006,
2006,
2006,
2000,
2006
] | 10 | [] | [
"IPR004771"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
2972,
93964,
3,
58943,
950
] | 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",... | [
195,
18,
33,
34,
5,
53,
35,
5,
92,
51,
3,
4,
284
] | 13 | true | Domain | Cation/H+ exchanger, transmembrane domain | Cation/H+ exchanger, transmembrane domain | Cation/H_exchanger_TM | 6 |
IPR006155 | 6,155 | Josephin domain | Josephin | Domain | 7,988 | false | false | The Josephin domain is an eukaryotic protein module of about 180 residues, which occurs in stand-alone form in Josephin-like proteins, and as an amino- terminal domain associated with two or three copies of the ubiquitin- interacting motif (UIM) in ataxin 3-like proteins. Josephin domain-containing proteins function as... | [
"GO:0004843",
"GO:0016579"
] | [
"cysteine-type deubiquitinase activity",
"protein deubiquitination"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF02099",
"PS50957",
"SM01246"
] | [
"Josephin",
"JOSEPHIN",
"Josephin"
] | [
7797,
7731,
7502
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.19.12",
"PDOC50957",
"R-CEL-5689877",
"R-CEL-9615017",
"R-DME-5689877",
"R-GGA-5689877",
"R-HSA-5689877",
"R-HSA-9615017",
"R-MMU-5689877",
"R-MMU-9615017",
"R-RNO-5689877",
"R-RNO-9615017"
] | [
"EC:3.4.19.12",
"PROSITEDOC:PDOC50957",
"REACTOME:R-CEL-5689877",
"REACTOME:R-CEL-9615017",
"REACTOME:R-DME-5689877",
"REACTOME:R-GGA-5689877",
"REACTOME:R-HSA-5689877",
"REACTOME:R-HSA-9615017",
"REACTOME:R-MMU-5689877",
"REACTOME:R-MMU-9615017",
"REACTOME:R-RNO-5689877",
"REACTOME:R-RNO-9615... | 12 | [
"1yzb",
"2aga",
"2dos",
"2jri",
"3o65",
"6pgv"
] | 6 | [
"PUB00018425",
"PUB00018426",
"PUB00018427",
"PUB00081482",
"PUB00081486"
] | [
"12486728",
"12944423",
"14559776",
"17696782",
"19382171"
] | [
"Structural modeling of ataxin-3 reveals distant homology to adaptins.",
"Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics.",
"The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity.",
"Josephin domain-containing pro... | [
2003,
2003,
2003,
2007,
2009
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
39,
7935,
3,
11
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
9,
2,
8,
2,
210,
14,
6,
14,
14
] | 9 | true | Domain | Josephin domain | Josephin domain | Josephin | 6 |
IPR006156 | 6,156 | Dihydroneopterin aldolase | Dihydroneopterin_aldolase | Family | 23,953 | false | false | Dihydroneopterin aldolase catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate. The enzyme form a homo-octamers. Aldolase can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldih... | [
"GO:0004150",
"GO:0006760"
] | [
"dihydroneopterin aldolase activity",
"folic acid-containing compound metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR42844",
"TIGR00525"
] | [
"",
"folB"
] | [
22098,
18648
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.2.25",
"GenProp0038",
"PWY-6147",
"PWY-6148",
"PWY-6797",
"PWY-7539"
] | [
"EC:4.1.2.25",
"GP:GenProp0038",
"METACYC:PWY-6147",
"METACYC:PWY-6148",
"METACYC:PWY-6797",
"METACYC:PWY-7539"
] | 6 | [
"1b9l",
"1dhn",
"1nbu",
"1rri",
"1rrw",
"1rry",
"1rs2",
"1rs4",
"1rsd",
"1rsi",
"1sql",
"1u68",
"1z9w",
"2cg8",
"2dhn",
"2nm2",
"2nm3",
"2o90",
"3o1k",
"3r2e",
"3v9o",
"4aey",
"5f3m",
"5far",
"6ojo",
"7su4",
"7su6",
"7su7",
"7su8",
"8su7",
"8sv5",
"9b2e"... | 32 | [
"PUB00007944"
] | [
"9651328"
] | [
"Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
13,
21705,
1808,
5,
422
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
15,
2,
7,
6
] | 4 | true | Family | Dihydroneopterin aldolase | Dihydroneopterin aldolase | Dihydroneopterin_aldolase | 4 |
IPR006157 | 6,157 | Dihydroneopterin aldolase/epimerase domain | FolB_dom | Domain | 27,056 | false | false | Dihydroneopterin aldolase (DHNA or folB) catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate [ ]. Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids, as well as formyl-tRNA. Mammalian c... | [
"GO:0004150",
"GO:0006760"
] | [
"dihydroneopterin aldolase activity",
"folic acid-containing compound metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART",
"NCBIFAM",
"CDD"
] | [
"PF02152",
"SM00905",
"TIGR00526",
"cd00534"
] | [
"FolB",
"FolB",
"folB_dom",
"DHNA_DHNTPE"
] | [
27017,
26906,
24170,
15788
] | 4 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.2.25",
"PWY-6147",
"PWY-6148",
"PWY-6797",
"PWY-7539"
] | [
"EC:4.1.2.25",
"METACYC:PWY-6147",
"METACYC:PWY-6148",
"METACYC:PWY-6797",
"METACYC:PWY-7539"
] | 5 | [
"1b9l",
"1dhn",
"1nbu",
"1rri",
"1rrw",
"1rry",
"1rs2",
"1rs4",
"1rsd",
"1rsi",
"1sql",
"1u68",
"1z9w",
"2cg8",
"2dhn",
"2nm2",
"2nm3",
"2o90",
"3o1k",
"3r2e",
"3v9o",
"4aey",
"5f3m",
"5far",
"6ojo",
"7su4",
"7su6",
"7su7",
"7su8",
"8evk",
"8su7",
"8sv5"... | 33 | [
"PUB00007944",
"PUB00010575",
"PUB00081680",
"PUB00081681",
"PUB00081682",
"PUB00081683"
] | [
"9651328",
"9709001",
"9182560",
"9006053",
"12039964",
"10737935"
] | [
"Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase.",
"Single amino acid substitutions disrupt tetramer formation in the dihydroneopterin aldolase enzyme of Pneumocystis carinii.",
"Purification, cloning... | [
1998,
1998,
1997,
1997,
2002,
2000
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
20,
23691,
2868,
11,
466
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
15,
2,
1,
8,
1,
1,
8
] | 7 | true | Domain | Dihydroneopterin aldolase/epimerase domain | Dihydroneopterin aldolase/epimerase domain | FolB_dom | 6 |
IPR006158 | 6,158 | Cobalamin (vitamin B12)-binding domain | Cobalamin-bd | Domain | 76,345 | false | false | The cobalamin (vitamin B12) binding domain can bind two different forms of the cobalamin cofactor, with cobalt bonded either to a methyl group (methylcobalamin) or to 5'-deoxyadenosine (adenosylcobalamin). Cobalamin-binding domains are mainly found in two families of enzymes present in animals and prokaryotes, which pe... | [
"GO:0031419",
"GO:0046872"
] | [
"cobalamin binding",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF02310",
"PS51332"
] | [
"B12-binding",
"B12_BINDING"
] | [
71507,
74449
] | 2 | [
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1439",
"GenProp1629",
"GenProp1723",
"R-CEL-156581",
"R-CEL-1614635",
"R-CEL-71032",
"R-CEL-9013407",
"R-CEL-9759218",
"R-DDI-156581",
"R-DDI-1614635",
"R-DDI-9013407",
"R-DDI-9759218",
"R-HSA-156581",
"R-HSA-1614635",
"R-HSA-3359467",
"R-HSA-3359469",
"R-HSA-3359475",
"R-H... | [
"GP:GenProp1439",
"GP:GenProp1629",
"GP:GenProp1723",
"REACTOME:R-CEL-156581",
"REACTOME:R-CEL-1614635",
"REACTOME:R-CEL-71032",
"REACTOME:R-CEL-9013407",
"REACTOME:R-CEL-9759218",
"REACTOME:R-DDI-156581",
"REACTOME:R-DDI-1614635",
"REACTOME:R-DDI-9013407",
"REACTOME:R-DDI-9759218",
"REACTOM... | 30 | [
"1b1a",
"1be1",
"1bmt",
"1cb7",
"1ccw",
"1e1c",
"1fmf",
"1i9c",
"1id8",
"1k7y",
"1k98",
"1req",
"1xrs",
"1y80",
"2i2x",
"2req",
"2xij",
"2xiq",
"2yxb",
"3bic",
"3bul",
"3ezx",
"3iv9",
"3iva",
"3kow",
"3kox",
"3koy",
"3koz",
"3kp0",
"3kp1",
"3req",
"3whp"... | 91 | [
"PUB00005279",
"PUB00008237",
"PUB00014004",
"PUB00014831",
"PUB00016228",
"PUB00043708",
"PUB00043709"
] | [
"8805541",
"7992050",
"11731805",
"9242908",
"10467146",
"16042603",
"14527323"
] | [
"How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution.",
"How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase.",
"Domain alternation switches B(12)-dependent methionine synthase to the activation conformati... | [
1996,
1994,
2002,
1997,
1999,
2005,
2003
] | 7 | [] | [
"IPR006159"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
2656,
66913,
4,
4199,
2573
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
2,
22,
4,
7
] | 6 | true | Domain | Cobalamin (vitamin B12)-binding domain | Cobalamin (vitamin B12)-binding domain | Cobalamin-bd | 8 |
IPR006159 | 6,159 | Methylmalonyl-CoA mutase, C-terminal | Acid_CoA_mut_C | Domain | 19,710 | false | false | This entry represents the C-terminal domain of eukaryotic and prokaryotic MUT enzymes. This domain covers the whole length of the protein in some members such as Glutamate mutase sigma subunit (GlmS), Fused isobutyryl-CoA mutase (IcmF, [ , ]) and Pivalyl-CoA mutase small subunit [ ]. It seems to have evolutionary relat... | [
"GO:0016853"
] | [
"isomerase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00640"
] | [
"acid_CoA_mut_C"
] | [
19710
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.4.99",
"GenProp1439",
"GenProp1629",
"GenProp1723",
"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",
"GP:GenProp1439",
"GP:GenProp1629",
"GP:GenProp1723",
"REACTOME:R-CEL-71032",
"REACTOME:R-CEL-9759218",
"REACTOME:R-HSA-3359475",
"REACTOME:R-HSA-3359478",
"REACTOME:R-HSA-71032",
"REACTOME:R-HSA-9759218",
"REACTOME:R-MMU-71032",
"REACTOME:R-MMU-9759218"
] | 12 | [
"1e1c",
"1req",
"2req",
"2xij",
"2xiq",
"2yxb",
"3bic",
"3req",
"4r3u",
"4req",
"4xc6",
"4xc7",
"4xc8",
"5cjt",
"5cju",
"5cjv",
"5cjw",
"5req",
"6oxc",
"6oxd",
"6req",
"7req",
"8dpb",
"8dyj",
"8dyl",
"8gju",
"8ssl",
"8sta"
] | 28 | [
"PUB00014831",
"PUB00023208",
"PUB00079971",
"PUB00079972",
"PUB00150973",
"PUB00150974",
"PUB00150975",
"PUB00151026"
] | [
"9242908",
"9772164",
"22167181",
"26134562",
"25125334",
"27167370",
"28101778",
"28130442"
] | [
"Structure-based perspectives on B12-dependent enzymes.",
"Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase.",
"Novel coenzyme B12-dependent interconversion of isovaleryl-CoA and pivalyl-CoA.",
"Engineered and Native Coenzyme B12-dependent Isovaleryl-CoA/Pi... | [
1997,
1998,
2012,
2015,
2014,
2016,
2017,
2017
] | 8 | [
"IPR006158"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
596,
16753,
1860,
501
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
1,
14,
3,
3
] | 6 | true | Domain | Methylmalonyl-CoA mutase, C-terminal | Methylmalonyl-CoA mutase, C-terminal | Acid_CoA_mut_C | 7 |
IPR006160 | 6,160 | Short chain fatty acid transporter AtoE | SCFA_transpt_AtoE | Family | 5,431 | false | false | Members of this family may be short chain fatty acid transporters although there has been no experimental characterisation of this function. | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF02667",
"PTHR41983"
] | [
"SCFA_trans",
""
] | [
5427,
5408
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [
"IPR006161"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Chaetothyriales",
"metagenomes"
] | [
209,
5177,
2,
43
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Short chain fatty acid transporter AtoE | Short chain fatty acid transporter AtoE | SCFA_transpt_AtoE | 3 |
IPR006161 | 6,161 | Conserved hypothetical protein CHP00336 | CHP00366 | Family | 545 | false | false | This is a family of conserved hypothetical proteins of no clearly defined function, although they may act as short chain fatty acid transporters. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00366"
] | [
""
] | [
545
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR006160"
] | [] | 1 | 0 | 1 | [
"Archaeoglobus fulgidus",
"Bacteria"
] | [
3,
542
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Conserved hypothetical protein CHP00336 | Conserved hypothetical protein CHP00336 | CHP00366 | 5 |
IPR006162 | 6,162 | Phosphopantetheine attachment site | Ppantetheine_attach_site | PTM | 143,157 | false | false | Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups [ ]. The amino-terminal region of the ACP proteins is well defined and consists of fo... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00012"
] | [
"PHOSPHOPANTETHEINE"
] | [
143157
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00012",
"R-DDI-77289",
"R-DDI-9857492",
"R-HSA-163765",
"R-HSA-196757",
"R-HSA-199220",
"R-HSA-2426168",
"R-HSA-611105",
"R-HSA-6799198",
"R-HSA-75105",
"R-HSA-77289",
"R-HSA-9029558",
"R-HSA-9857492",
"R-HSA-9937383",
"R-MMU-196757",
"R-MMU-199220",
"R-MMU-611105",
"R-MMU-679... | [
"PROSITEDOC:PDOC00012",
"REACTOME:R-DDI-77289",
"REACTOME:R-DDI-9857492",
"REACTOME:R-HSA-163765",
"REACTOME:R-HSA-196757",
"REACTOME:R-HSA-199220",
"REACTOME:R-HSA-2426168",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-6799198",
"REACTOME:R-HSA-75105",
"REACTOME:R-HSA-77289",
"REACTOME:R-HSA-9029... | 28 | [
"1acp",
"1af8",
"1dny",
"1fh1",
"1hy8",
"1l0h",
"1l0i",
"1nq4",
"1t8k",
"1vku",
"1x3o",
"2af8",
"2ava",
"2dnw",
"2ehs",
"2eht",
"2fac",
"2fad",
"2fae",
"2fhs",
"2fq0",
"2fq2",
"2fva",
"2fve",
"2fvf",
"2gdw",
"2gdx",
"2gdy",
"2jgp",
"2ju1",
"2ju2",
"2k0x"... | 565 | [
"PUB00002372",
"PUB00007945"
] | [
"5321311",
"11825906"
] | [
"Studies on the mechanism of fatty acid synthesis. XIV. The prosthetic group of acyl carrier protein and the mode of its attachment to the protein.",
"The solution structure of acyl carrier protein from Mycobacterium tuberculosis."
] | [
1965,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
17,
105733,
36869,
6,
532
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae ... | [
38,
7,
7,
2,
8,
13,
9,
28,
11,
2,
3,
65
] | 12 | true | PTM | Phosphopantetheine attachment site | Phosphopantetheine attachment site | Ppantetheine_attach_site | 2 |
IPR006164 | 6,164 | Ku70/Ku80, DNA-binding domain | DNA_bd_Ku70/Ku80 | Domain | 22,472 | false | false | The Ku heterodimer (composed of Ku70 and Ku80) contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining pathway. This is the central DNA-binding β-barrel domain. This domain is found in both the Ku70 and Ku80 proteins that form a DNA b... | [
"GO:0003677",
"GO:0006303"
] | [
"DNA binding",
"double-strand break repair via nonhomologous end joining"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF02735",
"SM00559"
] | [
"Ku",
"Ku78"
] | [
22457,
21622
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-5693571",
"R-DDI-6798695",
"R-DME-6798695",
"R-GGA-353423",
"R-HSA-164843",
"R-HSA-1834949",
"R-HSA-3270619",
"R-HSA-5693571",
"R-HSA-6798695",
"R-MMU-5693571",
"R-MMU-6798695",
"R-SCE-6798695",
"R-SPO-6798695"
] | [
"REACTOME:R-DDI-5693571",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DME-6798695",
"REACTOME:R-GGA-353423",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-1834949",
"REACTOME:R-HSA-3270619",
"REACTOME:R-HSA-5693571",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-5693571",
"REACTOME:R-MMU-6798695",
"REACTOME:... | 13 | [
"1jeq",
"1jey",
"5y3r",
"5y58",
"6erf",
"6erg",
"6erh",
"6zha",
"6zhe",
"7axz",
"7k0y",
"7k1j",
"7k1k",
"7k1n",
"7lsy",
"7lt3",
"7nfc",
"7nfe",
"7sgl",
"7su3",
"7sud",
"7z6o",
"7z87",
"7z88",
"7zt6",
"7zvt",
"7zwa",
"7zyg",
"8ag4",
"8ag5",
"8asc",
"8bh3"... | 51 | [
"PUB00007947"
] | [
"11493912"
] | [
"Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair."
] | [
2001
] | 1 | [] | [
"IPR047087"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
29,
12660,
9706,
19,
58
] | 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... | [
10,
3,
8,
37,
9,
4,
2,
4,
11,
2,
2,
21
] | 12 | true | Domain | Ku70/Ku80, DNA-binding domain | Ku70/Ku80, DNA-binding domain | DNA_bd_Ku70/Ku80 | 9 |
IPR006166 | 6,166 | ERCC4 domain | ERCC4_domain | Domain | 15,876 | false | false | This entry represents a structural domain found in several DNA repair nucleases, such as Rad1, XPF and crossover junction endonucleases EME1 and Mus81 [ , ]. The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essentia... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF02732",
"SM00891"
] | [
"ERCC4",
"ERCC4"
] | [
14846,
14443
] | 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-DDI-5696395",
"R-DDI-6782135",
"R-DME-5696395",
"R-DME-5696400",
"R-DME-6782135",
"R-DRE-5693568",
"R-HSA-5685938",
"R-HSA-5693568",
"R-HSA-5696395",
"R-HSA-5696400",
"R-HSA-6782135",
"R-HSA-6783310",
"R-HSA-9833482",
"R-MMU-5685938",
"R-MMU-5693568",
"R-MMU-5696395",
"R-MMU-56964... | [
"REACTOME:R-DDI-5696395",
"REACTOME:R-DDI-6782135",
"REACTOME:R-DME-5696395",
"REACTOME:R-DME-5696400",
"REACTOME:R-DME-6782135",
"REACTOME:R-DRE-5693568",
"REACTOME:R-HSA-5685938",
"REACTOME:R-HSA-5693568",
"REACTOME:R-HSA-5696395",
"REACTOME:R-HSA-5696400",
"REACTOME:R-HSA-6782135",
"REACTOM... | 29 | [
"1j22",
"1j23",
"1j24",
"1j25",
"2bgw",
"2bhn",
"2ziu",
"2ziv",
"2ziw",
"2zix",
"4bxo",
"4m6w",
"4p0p",
"4p0q",
"4p0r",
"4p0s",
"6sxa",
"6sxb",
"7f6l",
"9f98",
"9f99",
"9f9a",
"9f9k",
"9f9l",
"9f9m",
"9hjo"
] | 26 | [
"PUB00026231",
"PUB00044977"
] | [
"12679022",
"14527419"
] | [
"X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease: similarity between its endonuclease domain and restriction enzymes.",
"The endogenous Mus81-Eme1 complex resolves Holliday junctions by a nick and counternick mechanism."
] | [
2003,
2003
] | 2 | [] | [
"IPR047416",
"IPR047418",
"IPR047520",
"IPR047521",
"IPR047522",
"IPR047523",
"IPR047524"
] | 0 | 7 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1009,
915,
13470,
99,
383
] | 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... | [
26,
3,
30,
5,
27,
12,
3,
4,
24,
3,
3,
33
] | 12 | true | Domain | ERCC4 domain | ERCC4 domain | ERCC4_domain | 8 |
IPR006167 | 6,167 | DNA repair protein XPF | XPF | Family | 2,258 | false | false | This entry includes XPF from animals and its fungal orthologues Rad1 from budding yeasts and Rad16 from fission yeasts. Human XPF is a catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. It is involved in homologous recombination that assists in re... | [
"GO:0003697",
"GO:0004520",
"GO:0006281"
] | [
"single-stranded DNA binding",
"DNA endonuclease activity",
"DNA repair"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00596"
] | [
"rad1"
] | [
2258
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-5696395",
"R-DME-5696400",
"R-DME-6782135",
"R-HSA-5685938",
"R-HSA-5696395",
"R-HSA-5696400",
"R-HSA-6782135",
"R-HSA-6783310",
"R-MMU-5685938",
"R-MMU-5696395",
"R-MMU-5696400",
"R-MMU-6782135",
"R-MMU-6783310",
"R-SCE-6782135",
"R-SPO-5696395",
"R-SPO-5696400",
"R-SPO-67821... | [
"REACTOME:R-DME-5696395",
"REACTOME:R-DME-5696400",
"REACTOME:R-DME-6782135",
"REACTOME:R-HSA-5685938",
"REACTOME:R-HSA-5696395",
"REACTOME:R-HSA-5696400",
"REACTOME:R-HSA-6782135",
"REACTOME:R-HSA-6783310",
"REACTOME:R-MMU-5685938",
"REACTOME:R-MMU-5696395",
"REACTOME:R-MMU-5696400",
"REACTOM... | 17 | [
"6sxa",
"6sxb"
] | 2 | [
"PUB00075885",
"PUB00079368",
"PUB00103448",
"PUB00103449",
"PUB00103450",
"PUB00103451"
] | [
"19596235",
"8479526",
"17183314",
"23623389",
"8797827",
"23623386"
] | [
"Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair.",
"Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a single-stranded-DNA endonuclease.",
"A new progeroid syndrome reveals that genotoxic stress suppresses the somatotroph axis.",
"Malfunction ... | [
2009,
1993,
2006,
2013,
1996,
2013
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2258
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
3,
2,
4,
1,
1,
3,
1,
1
] | 8 | true | Family | DNA repair protein XPF | DNA repair protein XPF | XPF | 5 |
IPR006169 | 6,169 | GTP1/OBG domain | GTP1_OBG_dom | Domain | 33,713 | false | false | The N-terminal domain of GTPase Obg has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded β-sandwich. These regions form six left-handed collagen-like helices packed and H-bonded together. Several proteins have recently been shown to contain the 5 structural motifs characteris... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF01018",
"PS51883"
] | [
"GTP1_OBG",
"OBG"
] | [
33357,
33653
] | 2 | [
"EC"
] | [
"3.6.5.-"
] | [
"EC:3.6.5.-"
] | 1 | [
"1lnz",
"1udx",
"4csu",
"5m04",
"7bl2",
"7bl3",
"7bl4",
"7bl5",
"7bl6",
"7o9k",
"7odt",
"7of5",
"7of7",
"7oi6",
"8pk0",
"9e9c",
"9hcf"
] | 17 | [
"PUB00000217",
"PUB00001824",
"PUB00002073"
] | [
"1449490",
"8462872",
"2537815"
] | [
"DRG: a novel developmentally regulated GTP-binding protein.",
"Sequence of the Schizosaccharomyces pombe gtp1 gene and identification of a novel family of putative GTP-binding proteins.",
"The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein."
] | [
1992,
1993,
1989
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Marine Group I thaumarchaeote",
"unclassified sequences"
] | [
25042,
8120,
1,
550
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
7,
2,
3,
4,
1,
11,
9,
1,
15,
8,
1,
1,
21
] | 13 | true | Domain | GTP1/OBG domain | GTP1/OBG domain | GTP1_OBG_dom | 6 |
IPR006170 | 6,170 | Pheromone/general odorant binding protein | PBP/GOBP | Family | 13,854 | false | false | The olfactory receptors of terrestrial animals exist in an aqueous environment, yet detect odorants that are primarily hydrophobic. The aqueous solubility of hydrophobic odorants is thought to be greatly enhanced via odorant binding proteins which exist in the extracellular fluid surrounding the odorant receptors [ ]. ... | [
"GO:0005549"
] | [
"odorant binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF01395",
"SM00708"
] | [
"PBP_GOBP",
"PhBP"
] | [
13830,
8942
] | 2 | [] | [] | [] | 0 | [
"1c3y",
"1c3z",
"1dqe",
"1gm0",
"1ls8",
"1oof",
"1oog",
"1ooh",
"1ooi",
"1org",
"1ow4",
"1p28",
"1qwv",
"1t14",
"1tuj",
"1two",
"1xfr",
"2erb",
"2fjy",
"2gte",
"2h8v",
"2jpo",
"2kph",
"2l2c",
"2p70",
"2p71",
"2pql",
"2qdi",
"2qeb",
"2qeh",
"2qeo",
"2qev"... | 133 | [
"PUB00003450",
"PUB00153413",
"PUB00155430"
] | [
"2010751",
"35568118",
"30926880"
] | [
"Odorant-binding-protein subfamilies associate with distinct classes of olfactory receptor neurons in insects.",
"Functional aspects of evolution in a cluster of salivary protein genes from mosquitoes.",
"Functional and structural similarities of D7 proteins in the independently-evolved salivary secretions of s... | [
1991,
2022,
2019
] | 3 | [] | [
"IPR006072",
"IPR022354"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota"
] | [
7,
13847
] | 2 | [
"Drosophila melanogaster"
] | [
218
] | 1 | true | Family | Pheromone/general odorant binding protein | Pheromone/general odorant binding protein | PBP/GOBP | 3 |
IPR006171 | 6,171 | TOPRIM domain | TOPRIM_dom | Domain | 198,925 | false | false | The Toprim (topoisomerase-primase) domain is a structurally conserved domain of ~100 amino acids that is found in bacterial DnaG-type primases, small primase-like proteins from bacteria and archaea, type IA and type II topoisomerases, bacterial and archaeal nucleases of the OLD family and bacterial DNA repair proteins ... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01751",
"PF13362",
"PF13662",
"PS50880",
"SM00493"
] | [
"Toprim",
"Toprim_3",
"Toprim_4",
"TOPRIM",
"TOPRIM"
] | [
128918,
9109,
35345,
184232,
118429
] | 5 | [
"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-4615885",
"R-CEL-5693607",
"R-DDI-4615885",
"R-DME-4615885",
"R-HSA-1362277",
"R-HSA-4615885",
"R-HSA-5685938",
"R-HSA-5685942",
"R-HSA-5693554",
"R-HSA-5693568",
"R-HSA-5693579",
"R-HSA-5693607",
"R-HSA-5693616",
"R-HSA-6804756",
"R-HSA-69473",
"R-HSA-912446",
"R-HSA-9638771"... | [
"REACTOME:R-CEL-4615885",
"REACTOME:R-CEL-5693607",
"REACTOME:R-DDI-4615885",
"REACTOME:R-DME-4615885",
"REACTOME:R-HSA-1362277",
"REACTOME:R-HSA-4615885",
"REACTOME:R-HSA-5685938",
"REACTOME:R-HSA-5685942",
"REACTOME:R-HSA-5693554",
"REACTOME:R-HSA-5693568",
"REACTOME:R-HSA-5693579",
"REACTOM... | 37 | [
"1bgw",
"1bjt",
"1cy0",
"1cy1",
"1cy2",
"1cy4",
"1cy6",
"1cy7",
"1cy8",
"1d6m",
"1dd9",
"1dde",
"1ecl",
"1eqn",
"1gku",
"1gl9",
"1i7d",
"1mw8",
"1mw9",
"1nui",
"1q57",
"1t6t",
"1vdd",
"2au3",
"2fcj",
"2gai",
"2gaj",
"2i5r",
"2o19",
"2o54",
"2o59",
"2o5c"... | 239 | [
"PUB00004485",
"PUB00059904",
"PUB00068727"
] | [
"9722641",
"19596812",
"16077031"
] | [
"Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins.",
"Crystal structure of DNA gyrase B' domain sheds lights on the mechanism for T-segment navigation.",
"The 5S rRNA maturase, ribonuclease M5, is a Toprim domain family member."
] | [
1998,
2009,
2005
] | 3 | [] | [
"IPR034137",
"IPR034141",
"IPR034142",
"IPR034144",
"IPR034149",
"IPR034151",
"IPR034157",
"IPR034160"
] | 0 | 8 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
3172,
171347,
19100,
1881,
22,
3403
] | 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",... | [
42,
5,
8,
4,
7,
16,
20,
3,
16,
10,
2,
2,
107
] | 13 | true | Domain | TOPRIM domain | TOPRIM domain | TOPRIM_dom | 4 |
IPR006172 | 6,172 | DNA-directed DNA polymerase, family B | DNA-dir_DNA_pol_B | Family | 33,145 | false | false | DNA is the biological information that instructs cells how to exist in an ordered fashion: accurate replication is thus one of the most important events in the life cycle of a cell. This function is performed by DNA- directed DNA-polymerases ( ) by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the gro... | [
"GO:0000166",
"GO:0003676",
"GO:0003887"
] | [
"nucleotide binding",
"nucleic acid binding",
"DNA-directed DNA polymerase activity"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PRINTS",
"SMART"
] | [
"PR00106",
"SM00486"
] | [
"DNAPOLB",
"POLBc"
] | [
26419,
29801
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.7",
"PDOC00107",
"R-CEL-110314",
"R-CEL-5651801",
"R-CEL-5656169",
"R-CEL-5696397",
"R-CEL-5696400",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-69091",
"R-CEL-69166",
"R-CEL-69183",
"R-DDI-110314",
"R-DDI-113501",
"R-DDI-5651801",
"R-DDI-5656169",
"R-DDI-5696397",
"R-DDI-67821... | [
"EC:2.7.7.7",
"PROSITEDOC:PDOC00107",
"REACTOME:R-CEL-110314",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-5656169",
"REACTOME:R-CEL-5696397",
"REACTOME:R-CEL-5696400",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-69091",
"REACTOME:R-CEL-69166",
"REACTOME:R-CEL-69183",
"... | 142 | [
"1clq",
"1d5a",
"1ig9",
"1ih7",
"1q8i",
"1q9x",
"1q9y",
"1qht",
"1qqc",
"1s5j",
"1tgo",
"1waf",
"1waj",
"1wn7",
"1wns",
"1xhx",
"1xhz",
"1xi1",
"2atq",
"2dtu",
"2dy4",
"2ex3",
"2gv9",
"2jgu",
"2oyq",
"2ozm",
"2ozs",
"2p5g",
"2p5o",
"2py5",
"2pyj",
"2pyl"... | 357 | [
"PUB00000436",
"PUB00004353",
"PUB00010600"
] | [
"8679562",
"2461550",
"9757117"
] | [
"Crystal structures of an NH2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions.",
"A sequence motif in many polymerases.",
"Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon."
] | [
1996,
1988,
1998
] | 3 | [] | [
"IPR014382",
"IPR014416",
"IPR015833",
"IPR029703",
"IPR034749"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1590,
4788,
20809,
5512,
446
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
32,
7,
7,
7,
1,
26,
12,
4,
10,
20,
4,
4,
42
] | 13 | true | Family | DNA-directed DNA polymerase, family B | DNA-directed DNA polymerase, family B | DNA-dir_DNA_pol_B | 2 |
IPR006173 | 6,173 | Staphylococcal/Streptococcal toxin, OB-fold | Staph_tox_OB | Domain | 646 | false | false | Streptococcus pyogenes (group A streptococcus) cause a wide range of human infections, in a range from acute illness in an initial exposure such as pharyngitis or impetigo to serious and life-threatening infections in humans like toxic shock syndrome (TSS) with or without necrotizing fasciitis and myositis. This pathog... | [
"GO:0090729"
] | [
"toxin activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01123"
] | [
"Stap_Strp_toxin"
] | [
646
] | 1 | [] | [] | [] | 0 | [
"1an8",
"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",
"1jck"... | 97 | [
"PUB00094494",
"PUB00094495"
] | [
"23824366",
"26433203"
] | [
"Staphylococcal and streptococcal superantigen exotoxins.",
"Streptococcal toxins: role in pathogenesis and disease."
] | [
2013,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Plasmid pIB485"
] | [
638,
7,
1
] | 3 | [] | [] | 0 | true | Domain | Staphylococcal/Streptococcal toxin, OB-fold | Staphylococcal/Streptococcal toxin, OB-fold | Staph_tox_OB | 2 |
IPR006175 | 6,175 | YjgF/YER057c/UK114 family | YjgF/YER057c/UK114 | Family | 95,266 | false | false | The YjgF/YER057c/UK114 family (also known as the Rid family) of proteins is conserved in all domains of life [ ]. A phylogenetic analysis applied by Lambrecht et al. has divided the Rid family into a widely distributed archetypal RidA (YjgF) subfamily and seven other subfamilies (Rid1 to Rid7) that are largely confined... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF01042",
"PTHR11803"
] | [
"Ribonuc_L-PSP",
""
] | [
95129,
60802
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8849175",
"R-CEL-8849175",
"R-DME-8849175",
"R-HSA-8849175",
"R-MMU-8849175",
"R-RNO-8849175",
"R-SCE-5358493",
"R-SCE-8849175",
"R-SPO-5358493",
"R-SPO-8849175"
] | [
"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-5358493",
"REACTOME:R-SCE-8849175",
"REACTOME:R-SPO-5358493",
"REACTOME:R-SPO-8849175"
] | 10 | [
"1j7h",
"1jd1",
"1nq3",
"1oni",
"1pf5",
"1qah",
"1qd9",
"1qu9",
"1x25",
"1xrg",
"2b33",
"2csl",
"2cvl",
"2cw4",
"2cwj",
"2dyy",
"2ig8",
"2uyj",
"2uyk",
"2uyn",
"2uyp",
"3gtz",
"3i3f",
"3i7t",
"3k0t",
"3k12",
"3kjj",
"3kjk",
"3l7q",
"3lme",
"3lyb",
"3m1x"... | 76 | [
"PUB00006517",
"PUB00007949",
"PUB00028112",
"PUB00028113",
"PUB00028737",
"PUB00054810",
"PUB00056792",
"PUB00064878",
"PUB00074576",
"PUB00076977",
"PUB00076979",
"PUB00076980",
"PUB00103945",
"PUB00103946"
] | [
"10557275",
"10400702",
"10595546",
"11442631",
"12112709",
"19899170",
"20400551",
"22094463",
"18296521",
"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,
2000,
2015,
1973,
2018,
2019
] | 14 | [] | [
"IPR006056",
"IPR019898",
"IPR035709",
"IPR038743"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1272,
75809,
17049,
26,
1110
] | 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,
7,
2,
5,
3,
1,
3,
6,
4,
3,
3,
18
] | 13 | true | Family | YjgF/YER057c/UK114 family | YjgF/YER057c/UK114 family | YjgF/YER057c/UK114 | 6 |
IPR006177 | 6,177 | Staphylococcal/streptococcal toxin, bacterial | Toxin_bac | Family | 428 | false | false | Staphylococcal enterotoxins and streptococcal pyrogenic exotoxins belong to a family of related toxins [ , ] that share the ability to bind to the major histocompatibility complex proteins of their hosts. A more distant relative of the family is the Staphylococcus aureus toxic shock syndrome toxin, which shares only a ... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00279"
] | [
"BACTRLTOXIN"
] | [
428
] | 1 | [] | [] | [] | 0 | [
"1an8",
"1b1z",
"1bxt",
"1ck1",
"1cqv",
"1d5m",
"1d5x",
"1d5z",
"1d6e",
"1dyq",
"1enf",
"1esf",
"1et6",
"1eu3",
"1ewc",
"1f77",
"1fnu",
"1fnv",
"1fnw",
"1goz",
"1ha5",
"1hqr",
"1hxy",
"1i4g",
"1i4h",
"1i4p",
"1i4q",
"1i4r",
"1i4x",
"1jck",
"1jwm",
"1jws"... | 88 | [
"PUB00000115",
"PUB00005127"
] | [
"2679358",
"2185544"
] | [
"Genetic analysis of extracellular toxins of Staphylococcus aureus.",
"The staphylococcal enterotoxins and their relatives."
] | [
1989,
1990
] | 2 | [
"IPR013307"
] | [] | 1 | 0 | 1 | [
"Bacilli",
"Caudoviricetes"
] | [
421,
7
] | 2 | [] | [] | 0 | true | Family | Staphylococcal/streptococcal toxin, bacterial | Staphylococcal/streptococcal toxin, bacterial | Toxin_bac | 4 |
IPR006178 | 6,178 | Major allergen I polypeptide chain 1 | CH1-like | Family | 318 | false | false | This entry includes major allergen I polypeptide chain 1 (Fel d 1 chain 1) from cat and related proteins, such as SCGB1B from mice. 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. ... | [] | [] | [] | 0 | [
"PRINTS",
"PANTHER"
] | [
"PR00827",
"PTHR21226"
] | [
"FELALLERGEN",
""
] | [
312,
317
] | 2 | [] | [] | [] | 0 | [
"1puo",
"1zkr",
"2ejn",
"5vyf"
] | 4 | [
"PUB00035399",
"PUB00042589",
"PUB00069601"
] | [
"12851385",
"17543334",
"22155607"
] | [
"The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family.",
"Structural characterization of the tetrameric form of the major cat allergen Fel d 1.",
"Update of the human secretoglobin (SCGB) gene superfamily and an example of 'evolutionary bloom' of androgen-binding protein... | [
2003,
2007,
2011
] | 3 | [
"IPR016126"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
318
] | 1 | [
"Mus musculus",
"Rattus norvegicus"
] | [
23,
6
] | 2 | true | Family | Major allergen I polypeptide chain 1 | Major allergen I polypeptide chain 1 | CH1-like | 6 |
IPR006179 | 6,179 | 5'-Nucleotidase/apyrase | 5_nucleotidase/apyrase | Family | 52,534 | false | false | 5'-nucleotidases [ ] are enzymes that catalyze the hydrolysis of phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules. 5'-nucleotidase is a ubiquitous enzyme found in a wide variety of species and which occurs in different cellular locations. The extracellular 5'-nucleotidase... | [
"GO:0016787",
"GO:0009166"
] | [
"hydrolase activity",
"nucleotide catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS",
"PANTHER"
] | [
"PR01607",
"PTHR11575"
] | [
"APYRASEFAMLY",
""
] | [
46378,
51711
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3",
"R-HSA-196807",
"R-HSA-73621",
"R-HSA-74259",
"R-HSA-9660826",
"R-MMU-196807",
"R-MMU-73621",
"R-MMU-74259",
"R-RNO-196807",
"R-RNO-73621",
"R-RNO-74259"
] | [
"EC:3.1.3",
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-73621",
"REACTOME:R-HSA-74259",
"REACTOME:R-HSA-9660826",
"REACTOME:R-MMU-196807",
"REACTOME:R-MMU-73621",
"REACTOME:R-MMU-74259",
"REACTOME:R-RNO-196807",
"REACTOME:R-RNO-73621",
"REACTOME:R-RNO-74259"
] | 11 | [
"1ho5",
"1hp1",
"1hpu",
"1oi8",
"1oid",
"1oie",
"1ush",
"2ush",
"2wdc",
"2wdd",
"2wde",
"2wdf",
"2z1a",
"3c9f",
"3gve",
"3ivd",
"3ive",
"3jyf",
"3qfk",
"3ztv",
"3zu0",
"4h1s",
"4h1y",
"4h2b",
"4h2f",
"4h2g",
"4h2i",
"4q7f",
"4uwq",
"4wwl",
"5eqv",
"5h7w"... | 75 | [
"PUB00000512",
"PUB00004869",
"PUB00008988",
"PUB00008989"
] | [
"1637327",
"7846038",
"9015312",
"2550543"
] | [
"5'-Nucleotidase: molecular structure and functional aspects.",
"The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5'-nucleotidase family.",
"Differential regulation and function of CD73, a glycosyl-phosphatidylinositol-linked 70-kD adhesion molecule, on lymphocytes and endoth... | [
1992,
1995,
1997,
1989
] | 4 | [] | [
"IPR006294",
"IPR006420",
"IPR011240",
"IPR014485",
"IPR014579",
"IPR030998"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
570,
40402,
11118,
23,
421
] | 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",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe... | [
2,
20,
2,
8,
5,
3,
6,
1,
3
] | 9 | true | Family | 5'-Nucleotidase/apyrase | 5'-Nucleotidase/apyrase | 5_nucleotidase/apyrase | 3 |
IPR006180 | 6,180 | 3-hydroxyacyl-CoA dehydrogenase, conserved site | 3-OHacyl-CoA_DH_CS | Conserved_site | 31,381 | false | false | 3-hydroxyacyl-CoA dehydrogenase ( ) (HCDH) [ ] is an enzyme involved in fatty acid metabolism, it catalyzes 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 | [
"PROSITE"
] | [
"PS00067"
] | [
"3HCDH"
] | [
31381
] | 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... | 90 | [
"1f0y",
"1f12",
"1f14",
"1f17",
"1il0",
"1lsj",
"1lso",
"1m76",
"1wdk",
"1wdl",
"1wdm",
"1zcj",
"2d3t",
"2hdh",
"2wtb",
"2x58",
"3ado",
"3adp",
"3f3s",
"3had",
"3hdh",
"3mog",
"3rqs",
"3zw8",
"3zw9",
"3zwa",
"3zwb",
"3zwc",
"4j0e",
"4j0f",
"4kue",
"4kug"... | 56 | [
"PUB00001734",
"PUB00002465",
"PUB00004380",
"PUB00004646"
] | [
"8001771",
"3170592",
"2204034",
"3479790"
] | [
"Genes encoding homologues of three consecutive enzymes in the butyrate/butanol-producing pathway of Clostridium acetobutylicum are clustered on the Clostridium difficile chromosome.",
"Lambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases.",
"Nucleotide sequence of... | [
1994,
1988,
1990,
1987
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
359,
20653,
10154,
215
] | 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",... | [
11,
5,
6,
3,
3,
22,
6,
1,
15,
18,
23
] | 11 | true | Conserved_site | 3-hydroxyacyl-CoA dehydrogenase, conserved site | 3-hydroxyacyl-CoA dehydrogenase, conserved site | 3-OHacyl-CoA_DH_CS | 5 |
IPR006181 | 6,181 | D-amino acid oxidase, conserved site | D-amino_acid_oxidase_CS | Conserved_site | 7,580 | false | false | D-amino acid oxidase ( ) (DAMOX or DAO) is an FAD flavoenzyme that catalyzes the oxidation of neutral and basic D-amino acids into their corresponding keto acids. DAOs have been characterised and sequenced in fungi and vertebrates where they are known to be located in the peroxisomes. D-aspartate oxidase ( ) (DASOX) [ ... | [
"GO:0003884"
] | [
"D-amino-acid oxidase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00677"
] | [
"DAO"
] | [
7580
] | 1 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.4.3.3",
"PWY-5283",
"PDOC00573",
"R-BTA-389661",
"R-BTA-9033241",
"R-CEL-389661",
"R-CEL-9033241",
"R-DDI-389661",
"R-DDI-9033241",
"R-HSA-389661",
"R-HSA-9033241",
"R-MMU-389661",
"R-MMU-9033241",
"R-RNO-389661",
"R-RNO-9033241",
"R-SSC-389661",
"R-SSC-9033241"
] | [
"EC:1.4.3.3",
"METACYC:PWY-5283",
"PROSITEDOC:PDOC00573",
"REACTOME:R-BTA-389661",
"REACTOME:R-BTA-9033241",
"REACTOME:R-CEL-389661",
"REACTOME:R-CEL-9033241",
"REACTOME:R-DDI-389661",
"REACTOME:R-DDI-9033241",
"REACTOME:R-HSA-389661",
"REACTOME:R-HSA-9033241",
"REACTOME:R-MMU-389661",
"REAC... | 17 | [
"1an9",
"1c0i",
"1c0k",
"1c0l",
"1c0p",
"1dao",
"1ddo",
"1evi",
"1kif",
"1ve9",
"2du8",
"2e48",
"2e49",
"2e4a",
"2e82",
"3cuk",
"3g3e",
"3w4i",
"3w4j",
"3w4k",
"3wgt",
"3znn",
"3zno",
"3znp",
"3znq",
"4qfc",
"4qfd",
"4yjd",
"4yjf",
"4yjg",
"4yjh",
"5wwv"... | 41 | [
"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 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"marine metagenome"
] | [
1414,
6146,
16,
4
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus"
] | [
4,
7,
5,
6,
2,
2,
2
] | 7 | true | Conserved_site | D-amino acid oxidase, conserved site | D-amino acid oxidase, conserved site | D-amino_acid_oxidase_CS | 6 |
IPR006182 | 6,182 | Flagellar M-ring, N-terminal | FliF_N_dom | Domain | 17,656 | false | false | This domain is found at the N terminus of the flagellar M-ring protein FliF. It can also be found in YscJ lipoprotein, where it covers most of the sequence. FliF is the major protein of the M-ring in bacterial flagellar basal body [ ]. The basal body consists of four rings (L,P,S and M) surrounding the flagellar rod, w... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01514"
] | [
"YscJ_FliF"
] | [
17656
] | 1 | [] | [] | [] | 0 | [
"1yj7",
"2y9j",
"3j6d",
"4oyc",
"5tcp",
"5tcr",
"6duz",
"6pem",
"6q14",
"6q15",
"6q16",
"6rwx",
"6scn",
"6sd1",
"6sd2",
"6sd3",
"6sd4",
"6sd5",
"6tre",
"6uot",
"6uov",
"7ah9",
"7ahi",
"7bk0",
"7cg7",
"7cgo",
"7cik",
"7d84",
"7e81",
"7nvg",
"8axk",
"8axn"... | 73 | [
"PUB00002086",
"PUB00003254",
"PUB00007583",
"PUB00007701",
"PUB00007898"
] | [
"2544561",
"2129540",
"10564516",
"8733226",
"10334981"
] | [
"L-, P-, and M-ring proteins of the flagellar basal body of Salmonella typhimurium: gene sequences and deduced protein sequences.",
"FlgB, FlgC, FlgF and FlgG. A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium.",
"Flagellar proteins and type III-exported virulence f... | [
1989,
1990,
1999,
1996,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
17472,
25,
159
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Flagellar M-ring, N-terminal | Flagellar M-ring, N-terminal | FliF_N_dom | 2 |
IPR006183 | 6,183 | 6-phosphogluconate dehydrogenase | Pgluconate_DH | Family | 34,669 | false | false | This entry represents prokaryotic and eukaryotic 6PGD and a truncated prokaryotic 6PGD that lacks of a central region of about 140 residues, such as yqeC from Bacillus subtilis [ ]. Bacillus subtilis contains three classes of 6-phosphogluconate dehydrogenases (6PGD), including Gnd (YqjI), GntZ and YqeC. All of them are... | [
"GO:0004616"
] | [
"phosphogluconate dehydrogenase (decarboxylating) activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS",
"PANTHER"
] | [
"PR00076",
"PTHR11811"
] | [
"6PGDHDRGNASE",
""
] | [
32613,
34533
] | 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",
"2jkv",
"2p4q",
"2pgd",
"2w8z",
"2w90",
"2zya",
"2zyd",
"2zyg",
"3fwn",
"4e21",
"4gwg",
"4gwk",
"5uq9",
"6fqx",
"6fqy",
"6fqz",
"6vpb",
"6xeq",
"7cb0",
"7cb2",
"7cb5",
"7cb6",
"8c79"... | 36 | [
"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 | [] | [
"IPR004849",
"IPR006113"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
370,
24886,
9025,
61,
327
] | 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,
9,
4,
2,
6,
5,
2,
1,
23
] | 13 | true | Family | 6-phosphogluconate dehydrogenase | 6-phosphogluconate dehydrogenase | Pgluconate_DH | 4 |
IPR006184 | 6,184 | 6-phosphogluconate-binding site | 6PGdom_BS | Binding_site | 20,961 | 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 | [
"PROSITE"
] | [
"PS00461"
] | [
"6PGD"
] | [
20961
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1.44",
"PDOC00390",
"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",
"PROSITEDOC:PDOC00390",
"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"
] | 11 | [
"1pgj",
"1pgn",
"1pgo",
"1pgp",
"1pgq",
"2iyo",
"2iyp",
"2iz0",
"2iz1",
"2jkv",
"2p4q",
"2pgd",
"2w8z",
"2w90",
"2zya",
"2zyd",
"2zyg",
"3fwn",
"4gwg",
"4gwk",
"5uq9",
"7cb0",
"7cb2",
"7cb5",
"7cb6",
"8c79",
"8i4n",
"8i4q"
] | 28 | [
"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 | [
"Bacteria",
"Eukaryota",
"Nitrososphaerota incertae sedis",
"metagenomes"
] | [
15603,
5267,
8,
83
] | 4 | [
"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)",
... | [
1,
1,
4,
1,
6,
4,
1,
4,
2,
1
] | 10 | true | Binding_site | 6-phosphogluconate-binding site | 6-phosphogluconate-binding site | 6PGdom_BS | 2 |
IPR006186 | 6,186 | Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase | Ser/Thr-sp_prot-phosphatase | Domain | 78,208 | false | false | Protein phosphorylation plays a central role in the regulation of cell functions [ ], causing the activation or inhibition of many enzymes involved in various biochemical pathways [ ]. Kinases and phosphatases are the enzymes responsible for this, and may themselves be subject to control through the action of hormones ... | [
"GO:0016787"
] | [
"hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS",
"PROSITE",
"SMART"
] | [
"PR00114",
"PS00125",
"SM00156"
] | [
"STPHPHTASE",
"SER_THR_PHOSPHATASE",
"PP2Ac"
] | [
74617,
64691,
69019
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.3.16",
"PDOC00115",
"R-BTA-113501",
"R-BTA-1295596",
"R-BTA-141444",
"R-BTA-180024",
"R-BTA-195253",
"R-BTA-196299",
"R-BTA-198753",
"R-BTA-2025928",
"R-BTA-202670",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-2565942",
"R-BTA-2871809",
"R-BTA-2995383",
"R-BTA-389356",
"R-BTA-389... | [
"EC:3.1.3.16",
"PROSITEDOC:PDOC00115",
"REACTOME:R-BTA-113501",
"REACTOME:R-BTA-1295596",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-180024",
"REACTOME:R-BTA-195253",
"REACTOME:R-BTA-196299",
"REACTOME:R-BTA-198753",
"REACTOME:R-BTA-2025928",
"REACTOME:R-BTA-202670",
"REACTOME:R-BTA-2467813",
... | 317 | [
"1aui",
"1fjm",
"1g5b",
"1it6",
"1jk7",
"1m63",
"1mf8",
"1s70",
"1s95",
"1tco",
"1u32",
"1wao",
"2bcd",
"2bdx",
"2iae",
"2ie3",
"2ie4",
"2jog",
"2npp",
"2nyl",
"2nym",
"2o8a",
"2o8g",
"2p6b",
"2zbm",
"3c5w",
"3dw8",
"3e7a",
"3e7b",
"3egg",
"3egh",
"3fga"... | 178 | [
"PUB00000291",
"PUB00005960"
] | [
"2827745",
"2176161"
] | [
"Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A.",
"Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A."
] | [
1987,
1990
] | 2 | [
"IPR004843"
] | [
"IPR041751",
"IPR041753",
"IPR041754",
"IPR041758"
] | 1 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
269,
6991,
70696,
176,
76
] | 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",... | [
105,
53,
59,
43,
2,
87,
41,
9,
43,
77,
12,
10,
223
] | 13 | true | Domain | Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase | Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase | Ser/Thr-sp_prot-phosphatase | 9 |
IPR006187 | 6,187 | Claudin | Claudin | Family | 23,944 | false | false | Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [ , , ]. They can also form heteropolymers with each other within and between tight junction strands [ ]. Most ... | [
"GO:0005198",
"GO:0005923"
] | [
"structural molecule activity",
"bicellular tight junction"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PANTHER"
] | [
"PTHR12002"
] | [
""
] | [
23944
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC01045",
"R-HSA-420029",
"R-HSA-8935964",
"R-HSA-9925563"
] | [
"PROSITEDOC:PDOC01045",
"REACTOME:R-HSA-420029",
"REACTOME:R-HSA-8935964",
"REACTOME:R-HSA-9925563"
] | 4 | [
"3x29",
"4p79",
"5b2g",
"6ake",
"6akf",
"6akg",
"6ov2",
"6ov3",
"7kp4",
"7tdm",
"7tdn",
"8u4v",
"8u5b",
"9bei",
"9cmh",
"9cmi"
] | 16 | [
"PUB00070979",
"PUB00070980",
"PUB00070981",
"PUB00070982"
] | [
"24665401",
"20188437",
"21372174",
"10562289"
] | [
"Claudin interactions in and out of the tight junction.",
"The protoplasmic or exoplasmic face association of tight junction particles cannot predict paracellular permeability or heterotypic claudin compatibility.",
"Role of claudin species-specific dynamics in reconstitution and remodeling of the zonula occlud... | [
2013,
2010,
2011,
1999
] | 4 | [
"IPR004031"
] | [
"IPR003548",
"IPR003549",
"IPR003550",
"IPR003551",
"IPR003552",
"IPR003553",
"IPR003554",
"IPR003555",
"IPR003925",
"IPR003927",
"IPR003928",
"IPR005411",
"IPR008094"
] | 1 | 13 | 0 | [
"Bilateria"
] | [
23944
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
74,
53,
63,
72
] | 4 | true | Family | Claudin | Claudin | Claudin | 9 |
IPR006189 | 6,189 | CHASE domain | CHASE_dom | Domain | 14,791 | false | false | The CHASE domain is an extracellular domain of 200-230 amino acids, which is found in transmembrane receptors from bacteria, lower eukaryotes and plants. It has been named CHASE (Cyclases/Histidine Kinases Associated Sensory Extracellular) because of its presence in diverse receptor-like proteins with histidine kinase ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF03924",
"PS50839",
"SM01079"
] | [
"CHASE",
"CHASE",
"CHASE"
] | [
13325,
14219,
13514
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME"
] | [
"2.7.13.3",
"PDOC50839",
"R-DDI-2514859"
] | [
"EC:2.7.13.3",
"PROSITEDOC:PDOC50839",
"REACTOME:R-DDI-2514859"
] | 3 | [
"3pvj",
"3t4j",
"3t4k",
"3t4l",
"3t4o",
"3t4q",
"3t4s",
"3t4t",
"3v15",
"3v17",
"6k62"
] | 11 | [
"PUB00007950",
"PUB00018314"
] | [
"11590001",
"11590000"
] | [
"CHASE: an extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants.",
"The CHASE domain: a predicted ligand-binding module in plant cytokinin receptors and other eukaryotic and bacterial receptors."
] | [
2001,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
62,
11221,
3394,
7,
107
] | 5 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
14,
11,
50
] | 3 | true | Domain | CHASE domain | CHASE domain | CHASE_dom | 5 |
IPR006194 | 6,194 | Glycine-tRNA synthetase, heterodimeric | Gly-tRNA-synth_heterodimer | Family | 31,458 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [
"GO:0000166",
"GO:0004820",
"GO:0005524",
"GO:0006426",
"GO:0005737"
] | [
"nucleotide binding",
"glycine-tRNA ligase activity",
"ATP binding",
"glycyl-tRNA aminoacylation",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"PROFILE",
"PANTHER"
] | [
"PS50861",
"PTHR30075"
] | [
"AA_TRNA_LIGASE_II_GLYAB",
""
] | [
31045,
30893
] | 2 | [
"EC",
"PROSITEDOC"
] | [
"6.1.1.14",
"PDOC00363"
] | [
"EC:6.1.1.14",
"PROSITEDOC:PDOC00363"
] | 2 | [
"1j5w",
"3rf1",
"3rgl",
"3ufg",
"5f5w",
"7eiv",
"7lu4",
"7qcf",
"7xjy",
"7xjz",
"7xk0",
"7xk1",
"7xof",
"7yse",
"8h1c",
"8ie2"
] | 16 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00060645",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"8839980",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
1996,
2000,
2002
] | 10 | [] | [
"IPR002310",
"IPR015944"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
16,
29585,
1312,
3,
542
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
2,
3,
11
] | 4 | true | Family | Glycine-tRNA synthetase, heterodimeric | Glycine-tRNA synthetase, heterodimeric | Gly-tRNA-synth_heterodimer | 6 |
IPR006195 | 6,195 | Aminoacyl-tRNA synthetase, class II | aa-tRNA-synth_II | Domain | 324,514 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50862"
] | [
"AA_TRNA_LIGASE_II"
] | [
324514
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1",
"PDOC00363",
"R-CEL-9856649",
"R-DDI-9856649",
"R-DME-9856649",
"R-HSA-2408522",
"R-HSA-2408557",
"R-HSA-379716",
"R-HSA-379726",
"R-HSA-6782315",
"R-HSA-9856649",
"R-MMU-9856649",
"R-RNO-9856649",
"R-SCE-9856649",
"R-SPO-9856649"
] | [
"EC:6.1.1",
"PROSITEDOC:PDOC00363",
"REACTOME:R-CEL-9856649",
"REACTOME:R-DDI-9856649",
"REACTOME:R-DME-9856649",
"REACTOME:R-HSA-2408522",
"REACTOME:R-HSA-2408557",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-9856649",
... | 15 | [
"11as",
"12as",
"1adj",
"1ady",
"1asy",
"1asz",
"1ati",
"1b70",
"1b76",
"1b7y",
"1b8a",
"1bbu",
"1bbw",
"1c0a",
"1e1o",
"1e1t",
"1e22",
"1e24",
"1efw",
"1eiy",
"1eov",
"1eqr",
"1evk",
"1evl",
"1fyf",
"1g51",
"1ggm",
"1h4q",
"1h4s",
"1h4t",
"1h4v",
"1hc7"... | 550 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [] | [
"IPR002314",
"IPR004364",
"IPR041715"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
7407,
229011,
82889,
156,
5051
] | 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",... | [
105,
21,
32,
28,
11,
82,
57,
18,
69,
85,
17,
16,
185
] | 13 | true | Domain | Aminoacyl-tRNA synthetase, class II | Aminoacyl-tRNA synthetase, class II | aa-tRNA-synth_II | 5 |
IPR006196 | 6,196 | RNA-binding domain, S1, IF1 type | RNA-binding_domain_S1_IF1 | Domain | 45,093 | false | false | The S1 domain of around 70 amino acids, originally identified in ribosomal protein S1, is found in a large number of RNA-associated proteins. It has been shown that S1 proteins bind RNA through their S1 domains with some degree of sequence specificity. This type of S1 domain is found in translation initiation factor 1.... | [
"GO:0003723",
"GO:0003743",
"GO:0006413"
] | [
"RNA binding",
"translation initiation factor activity",
"translational initiation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PROFILE"
] | [
"PF01176",
"PS50832"
] | [
"eIF-1a",
"S1_IF1_TYPE"
] | [
44642,
43910
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50126",
"R-DDI-156827",
"R-DDI-72689",
"R-DDI-72695",
"R-DDI-72702",
"R-HSA-156827",
"R-HSA-72649",
"R-HSA-72689",
"R-HSA-72695",
"R-HSA-72702",
"R-HSA-72706",
"R-MMU-156827",
"R-MMU-72649",
"R-MMU-72689",
"R-MMU-72695",
"R-MMU-72702",
"R-MMU-72706",
"R-RNO-156827",
"R-RNO-7... | [
"PROSITEDOC:PDOC50126",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-72689",
"REACTOME:R-DDI-72695",
"REACTOME:R-DDI-72702",
"REACTOME:R-HSA-156827",
"REACTOME:R-HSA-72649",
"REACTOME:R-HSA-72689",
"REACTOME:R-HSA-72695",
"REACTOME:R-HSA-72702",
"REACTOME:R-HSA-72706",
"REACTOME:R-MMU-156827",
"... | 33 | [
"1ah9",
"1d7q",
"1hr0",
"1jt8",
"1zo1",
"2dgy",
"2n3s",
"2n78",
"2n8n",
"2nch",
"2oqk",
"3i4o",
"3j80",
"3j81",
"3jam",
"3jap",
"3wbk",
"3zjy",
"4bts",
"4kzy",
"4kzz",
"4mno",
"4ql5",
"4uer",
"5jb3",
"5jbh",
"5lmn",
"5lmo",
"5lmp",
"5lmq",
"5lmr",
"5lms"... | 100 | [
"PUB00000944"
] | [
"9008164"
] | [
"The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1408,
24665,
18330,
38,
652
] | 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,
3,
4,
1,
10,
21,
2,
12,
11,
1,
2,
14
] | 13 | true | Domain | RNA-binding domain, S1, IF1 type | RNA-binding domain, S1, IF1 type | RNA-binding_domain_S1_IF1 | 8 |
IPR006197 | 6,197 | Peptidase S24, LexA-like | Peptidase_S24_LexA | Family | 27,973 | false | false | This signature defines serine peptidases belong to MEROPS peptidase family S24 (LexA family, clan SF). They include: LexA, the repressor of genes in the cellular SOS response to DNA damage MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage RumA a pla... | [
"GO:0003677",
"GO:0006355"
] | [
"DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00726"
] | [
"LEXASERPTASE"
] | [
27973
] | 1 | [
"EC"
] | [
"3.4.21.88"
] | [
"EC:3.4.21.88"
] | 1 | [
"1ay9",
"1i4v",
"1jhc",
"1jhe",
"1jhf",
"1jhh",
"1umu",
"3jso",
"3jsp",
"3k2z",
"3k3r",
"6a2q",
"6a2r",
"6a2s",
"6a2t",
"7b5g",
"7ocj",
"7zra",
"8b0v",
"8gms",
"8gmt",
"8s7g",
"8trg"
] | 23 | [
"PUB00011456",
"PUB00011870",
"PUB00011871",
"PUB00011872",
"PUB00011873",
"PUB00011874",
"PUB00011875"
] | [
"12423347",
"10692372",
"11483531",
"9925794",
"11016960",
"11114935",
"8709953"
] | [
"The RuvABC resolvasome.",
"Analysis of Escherichia coli RecA interactions with LexA, lambda CI, and UmuD by site-directed mutagenesis of recA.",
"Converting a DNA damage checkpoint effector (UmuD2C) into a lesion bypass polymerase (UmuD'2C).",
"Intermolecular cleavage by UmuD-like enzymes: identification of ... | [
2002,
2000,
2001,
1999,
2000,
2001,
1996
] | 7 | [] | [
"IPR006200"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
27424,
40,
23,
6,
480
] | 5 | [
"Escherichia coli (strain K12)",
"Rattus norvegicus"
] | [
2,
1
] | 2 | true | Family | Peptidase S24, LexA-like | Peptidase S24, LexA-like | Peptidase_S24_LexA | 8 |
IPR006200 | 6,200 | Transcription regulator LexA | LexA | Family | 21,100 | false | false | LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity ( ) of LexA, where the active site Ser is part of LexA. The autolyt... | [
"GO:0004252",
"GO:0009432",
"GO:0045892"
] | [
"serine-type endopeptidase activity",
"SOS response",
"negative regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00015",
"TIGR00498"
] | [
"LexA",
"lexA"
] | [
19595,
21087
] | 2 | [
"EC",
"GP"
] | [
"3.4.21.88",
"GenProp0215"
] | [
"EC:3.4.21.88",
"GP:GenProp0215"
] | 2 | [
"1jhc",
"1jhe",
"1jhf",
"1jhh",
"1lea",
"1leb",
"3jso",
"3jsp",
"3k2z",
"3k3r",
"6a2q",
"6a2r",
"6a2s",
"6a2t",
"7b5g",
"7ocj",
"7zra",
"8b0v",
"8gms",
"8s7g",
"8trg"
] | 21 | [
"PUB00017442",
"PUB00017443"
] | [
"8798618",
"9555905"
] | [
"Interaction of Escherichia coli RecA protein with LexA repressor. II. Inhibition of DNA strand exchange by the uncleavable LexA S119A repressor argues that recombination and SOS induction are competitive processes.",
"The Bacillus subtilis DinR binding site: redefinition of the consensus sequence."
] | [
1996,
1998
] | 2 | [
"IPR006197"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences",
"uncultured marine thaumarchaeote KM3_68_B04"
] | [
20677,
23,
3,
396,
1
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Transcription regulator LexA | Transcription regulator LexA | LexA | 7 |
IPR006201 | 6,201 | Neurotransmitter-gated ion-channel | Neur_channel | Family | 93,934 | false | false | The receptors are composed of varying numbers and types of subunit. Each subunit contains a large extracellular N-terminal ligand-binding region; 3 hydrophobic transmembrane domains; a large intracellular region; and a fourth hydrophobic domain. The GABA, acetylcholine, serotonin 5HT3 and glycine receptors share a degr... | [
"GO:0004888",
"GO:0005216",
"GO:0034220",
"GO:0016020"
] | [
"transmembrane signaling receptor activity",
"monoatomic ion channel activity",
"monoatomic ion transmembrane transport",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"PR00252",
"PTHR18945",
"TIGR00860"
] | [
"NRIONCHANNEL",
"",
"LIC"
] | [
75295,
93408,
53609
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00209",
"R-BTA-112314",
"R-BTA-629587",
"R-BTA-629594",
"R-BTA-629597",
"R-BTA-977443",
"R-CEL-112314",
"R-CEL-629587",
"R-CEL-629594",
"R-CEL-629597",
"R-CEL-6798695",
"R-CEL-977443",
"R-DME-112314",
"R-DME-629587",
"R-DME-629594",
"R-DME-629597",
"R-DME-6798695",
"R-DME-9774... | [
"PROSITEDOC:PDOC00209",
"REACTOME:R-BTA-112314",
"REACTOME:R-BTA-629587",
"REACTOME:R-BTA-629594",
"REACTOME:R-BTA-629597",
"REACTOME:R-BTA-977443",
"REACTOME:R-CEL-112314",
"REACTOME:R-CEL-629587",
"REACTOME:R-CEL-629594",
"REACTOME:R-CEL-629597",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-977... | 45 | [
"1i9b",
"1oed",
"1uv6",
"1uw6",
"1ux2",
"1vry",
"1yi5",
"2bg9",
"2bj0",
"2br7",
"2br8",
"2byn",
"2byp",
"2byq",
"2byr",
"2bys",
"2c9t",
"2ksr",
"2lly",
"2lm2",
"2m6b",
"2m6i",
"2maw",
"2pgz",
"2ph9",
"2qc1",
"2uz6",
"2vl0",
"2w8f",
"2w8g",
"2wn9",
"2wnc"... | 785 | [
"PUB00002675",
"PUB00003455",
"PUB00010340",
"PUB00044612",
"PUB00044613",
"PUB00044614",
"PUB00044615",
"PUB00087336"
] | [
"1721053",
"1846404",
"10026168",
"18446614",
"15383648",
"18760291",
"15165736",
"1356407"
] | [
"Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor.",
"Generation of two forms of the gamma-aminobutyric acidA receptor gamma 2-subunit in mice by alternative splicing.",
"Structural features of the ligand-binding domain of the serotonin 5HT3 receptor.",
"Assembly and... | [
1991,
1991,
1999,
2008,
2004,
2008,
2004,
1992
] | 8 | [] | [
"IPR002394",
"IPR006028",
"IPR008060",
"IPR008132"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
23,
399,
93493,
4,
15
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
176,
229,
106,
192,
132,
183
] | 6 | true | Family | Neurotransmitter-gated ion-channel | Neurotransmitter-gated ion-channel | Neur_channel | 8 |
IPR006202 | 6,202 | Neurotransmitter-gated ion-channel ligand-binding domain | Neur_chan_lig-bd | Domain | 91,433 | false | false | This entry presents the extracellular ligand binding domain of these ion channels. This domain forms a pentameric arrangement in the known structure. Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmi... | [
"GO:0005230",
"GO:0006811",
"GO:0016020"
] | [
"extracellular ligand-gated monoatomic ion channel activity",
"monoatomic ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF02931"
] | [
"Neur_chan_LBD"
] | [
91433
] | 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-112314",
"R-BTA-629587",
"R-BTA-629594",
"R-BTA-629597",
"R-BTA-977443",
"R-CEL-112314",
"R-CEL-629587",
"R-CEL-629594",
"R-CEL-629597",
"R-CEL-6798695",
"R-CEL-977443",
"R-DME-112314",
"R-DME-629587",
"R-DME-629594",
"R-DME-629597",
"R-DME-6798695",
"R-DME-977443",
"R-DRE-1... | [
"REACTOME:R-BTA-112314",
"REACTOME:R-BTA-629587",
"REACTOME:R-BTA-629594",
"REACTOME:R-BTA-629597",
"REACTOME:R-BTA-977443",
"REACTOME:R-CEL-112314",
"REACTOME:R-CEL-629587",
"REACTOME:R-CEL-629594",
"REACTOME:R-CEL-629597",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-977443",
"REACTOME:R-DME-11... | 44 | [
"1i9b",
"1uv6",
"1uw6",
"1ux2",
"1yi5",
"2bg9",
"2bj0",
"2br7",
"2br8",
"2byn",
"2byp",
"2byq",
"2byr",
"2bys",
"2c9t",
"2pgz",
"2ph9",
"2qc1",
"2uz6",
"2vl0",
"2w8f",
"2w8g",
"2wn9",
"2wnc",
"2wnj",
"2wnl",
"2wzy",
"2x00",
"2xnt",
"2xnu",
"2xnv",
"2xq3"... | 775 | [
"PUB00002675",
"PUB00003455",
"PUB00010340",
"PUB00044612",
"PUB00044613",
"PUB00044614",
"PUB00044615"
] | [
"1721053",
"1846404",
"10026168",
"18446614",
"15383648",
"18760291",
"15165736"
] | [
"Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor.",
"Generation of two forms of the gamma-aminobutyric acidA receptor gamma 2-subunit in mice by alternative splicing.",
"Structural features of the ligand-binding domain of the serotonin 5HT3 receptor.",
"Assembly and... | [
1991,
1991,
1999,
2008,
2004,
2008,
2004
] | 7 | [] | [
"IPR047023",
"IPR047031",
"IPR047079"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Imitervirales",
"Methanomicrobiaceae",
"unclassified sequences"
] | [
297,
91114,
3,
8,
11
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
175,
215,
112,
206,
132,
182
] | 6 | true | Domain | Neurotransmitter-gated ion-channel ligand-binding domain | Neurotransmitter-gated ion-channel ligand-binding domain | Neur_chan_lig-bd | 3 |
IPR006203 | 6,203 | GHMP kinase, ATP-binding, conserved site | GHMP_knse_ATP-bd_CS | Conserved_site | 39,978 | false | false | The galacto- ( ), homoserine ( ), mevalonate ( ) and phosphomevalonate ( ) kinases contain, in their N-terminal section, a conserved Gly/Ser-rich region which is probably involved in the binding of ATP [ , ]. This group of kinases has been called 'GHMP' (from the first letter of their substrates). This site is also fou... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00627"
] | [
"GHMP_KINASES_ATP"
] | [
39978
] | 1 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1",
"2.7.1.39",
"PWY-702",
"PDOC00545",
"R-BTA-191273",
"R-BTA-70370",
"R-CFA-70370",
"R-DDI-191273",
"R-HSA-191273",
"R-HSA-2426168",
"R-HSA-5609976",
"R-HSA-70370",
"R-MMU-191273",
"R-MMU-70370",
"R-RNO-191273",
"R-SCE-191273",
"R-SPO-191273"
] | [
"EC:2.7.1",
"EC:2.7.1.39",
"METACYC:PWY-702",
"PROSITEDOC:PDOC00545",
"REACTOME:R-BTA-191273",
"REACTOME:R-BTA-70370",
"REACTOME:R-CFA-70370",
"REACTOME:R-DDI-191273",
"REACTOME:R-HSA-191273",
"REACTOME:R-HSA-2426168",
"REACTOME:R-HSA-5609976",
"REACTOME:R-HSA-70370",
"REACTOME:R-MMU-191273"... | 17 | [
"1fwk",
"1fwl",
"1h72",
"1h73",
"1h74",
"1kkh",
"1kvk",
"1pie",
"1s4e",
"1vis",
"1wuu",
"2a2c",
"2a2d",
"2aj4",
"2cz9",
"2dei",
"2dej",
"2gs8",
"2r3v",
"2r42",
"2x7i",
"3hul",
"4hac",
"4p52",
"4rpf",
"5was",
"5wat",
"6cyz",
"6gr2",
"6mde",
"6mdf",
"6q3w"... | 53 | [
"PUB00003676",
"PUB00006508",
"PUB00041428"
] | [
"1846667",
"10562426",
"17583736"
] | [
"Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase.",
"Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene.",
"Crystal structures of Trypanosom... | [
1991,
1999,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctmP19",
"metagenomes"
] | [
1144,
26140,
12244,
1,
449
] | 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",... | [
12,
1,
3,
1,
2,
20,
15,
3,
9,
20,
4,
3,
30
] | 13 | true | Conserved_site | GHMP kinase, ATP-binding, conserved site | GHMP kinase, ATP-binding, conserved site | GHMP_knse_ATP-bd_CS | 2 |
IPR006204 | 6,204 | GHMP kinase N-terminal domain | GHMP_kinase_N_dom | Domain | 91,669 | false | false | The galacto- ( ), homoserine ( ), mevalonate ( ) and phosphomevalonate ( ) kinases contain, in their N-terminal section, a conserved domain with a Gly/Ser-rich region which is involved in the binding of ATP [ , , ]. This group of kinases has been called 'GHMP' (from the first letter of their substrates). | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00288"
] | [
"GHMP_kinases_N"
] | [
91669
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1",
"GenProp1312",
"GenProp1330",
"GenProp1347",
"R-BTA-191273",
"R-BTA-70370",
"R-CFA-70370",
"R-DDI-191273",
"R-HSA-191273",
"R-HSA-2426168",
"R-HSA-5609976",
"R-HSA-6787639",
"R-HSA-70370",
"R-MMU-191273",
"R-MMU-6787639",
"R-MMU-70370",
"R-RNO-191273",
"R-SCE-191273",
"R... | [
"EC:2.7.1",
"GP:GenProp1312",
"GP:GenProp1330",
"GP:GenProp1347",
"REACTOME:R-BTA-191273",
"REACTOME:R-BTA-70370",
"REACTOME:R-CFA-70370",
"REACTOME:R-DDI-191273",
"REACTOME:R-HSA-191273",
"REACTOME:R-HSA-2426168",
"REACTOME:R-HSA-5609976",
"REACTOME:R-HSA-6787639",
"REACTOME:R-HSA-70370",
... | 19 | [
"1fwk",
"1fwl",
"1h72",
"1h73",
"1h74",
"1k47",
"1kkh",
"1kvk",
"1oj4",
"1pie",
"1s4e",
"1uek",
"1vis",
"1wuu",
"2a2c",
"2a2d",
"2aj4",
"2cz9",
"2dei",
"2dej",
"2hfs",
"2hfu",
"2oi2",
"2r3v",
"2r42",
"2v2q",
"2v2v",
"2v2z",
"2v34",
"2v8p",
"2vf3",
"2ww4"... | 96 | [
"PUB00003676",
"PUB00006508",
"PUB00015644",
"PUB00041428"
] | [
"1846667",
"10562426",
"11188689",
"17583736"
] | [
"Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase.",
"Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene.",
"Structure and mechanism of homos... | [
1991,
1999,
2000,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
4135,
64229,
8,
21863,
1434
] | 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",... | [
51,
2,
6,
2,
3,
26,
17,
4,
27,
26,
5,
3,
89
] | 13 | true | Domain | GHMP kinase N-terminal domain | GHMP kinase N-terminal domain | GHMP_kinase_N_dom | 8 |
IPR006205 | 6,205 | Mevalonate kinase | Mev_gal_kin | Family | 9,852 | false | false | Mevalonate kinase is well-characterised among eukaryotes, where it plays a role in the synthesis of isopentanyl pyrophosphate, a common intermediate for a number of pathways including cholesterol biosynthesis. It is also involved in mevalonate catabolism [ , , , ]. Close homologues are found in archaea. Related bacteri... | [
"GO:0004496",
"GO:0005524",
"GO:0008299",
"GO:0005737"
] | [
"mevalonate kinase activity",
"ATP binding",
"isoprenoid biosynthetic process",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR43290",
"TIGR00549"
] | [
"",
"mevalon_kin"
] | [
9398,
7771
] | 2 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.36",
"GenProp0047",
"GenProp1432",
"PWY-6174",
"PWY-7391",
"PWY-8125",
"PWY-922",
"R-BTA-191273",
"R-DDI-191273",
"R-HSA-191273",
"R-HSA-2426168",
"R-MMU-191273",
"R-RNO-191273",
"R-SCE-191273",
"R-SPO-191273"
] | [
"EC:2.7.1.36",
"GP:GenProp0047",
"GP:GenProp1432",
"METACYC:PWY-6174",
"METACYC:PWY-7391",
"METACYC:PWY-8125",
"METACYC:PWY-922",
"REACTOME:R-BTA-191273",
"REACTOME:R-DDI-191273",
"REACTOME:R-HSA-191273",
"REACTOME:R-HSA-2426168",
"REACTOME:R-MMU-191273",
"REACTOME:R-RNO-191273",
"REACTOME... | 15 | [
"1kkh",
"1kvk",
"1vis",
"2hfs",
"2hfu",
"2oi2",
"2r3v",
"2r42",
"2x7i",
"4hac",
"6mde",
"6mdf",
"8teb",
"8tfo"
] | 14 | [
"PUB00049240",
"PUB00100288",
"PUB00100292",
"PUB00100293"
] | [
"18302342",
"9325256",
"11278915",
"9392419"
] | [
"Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism.",
"Identification of catalytic residues in human mevalonate kinase.",
"Investigation of invariant serine/threonine residues in mevalonate kinase. Tests of the functional significance of a proposed substrate... | [
2008,
1997,
2001,
1997
] | 4 | [
"IPR006206"
] | [
"IPR022937"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
908,
3620,
5243,
81
] | 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,
18,
1,
1,
13,
6,
1,
4,
7,
1,
1,
23
] | 12 | true | Family | Mevalonate kinase | Mevalonate kinase | Mev_gal_kin | 1 |
IPR006206 | 6,206 | Mevalonate/galactokinase | Mevalonate/galactokinase | Family | 21,342 | false | false | Mevalonate kinase ( ) and galactokinases ( ) belong to this family. Mevalonate kinase may be a regulatory site in the cholesterol biosynthetic pathway. It is also involved in mevalonate catabolism. Galactokinase takes part in the first reaction of galactose metabolism by converting galactose to galactose-1-phosphate. | [
"GO:0005524",
"GO:0016301",
"GO:0016773",
"GO:0005737"
] | [
"ATP binding",
"kinase activity",
"phosphotransferase activity, alcohol group as acceptor",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"cellular_component"
] | 4 | [
"PIRSF"
] | [
"PIRSF000530"
] | [
"Galactokinase"
] | [
21342
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.6",
"PWY-3821",
"PWY-6317",
"PWY-6527",
"R-BTA-70370",
"R-CFA-70370",
"R-HSA-5609976",
"R-HSA-70370",
"R-MMU-70370"
] | [
"EC:2.7.1.6",
"METACYC:PWY-3821",
"METACYC:PWY-6317",
"METACYC:PWY-6527",
"REACTOME:R-BTA-70370",
"REACTOME:R-CFA-70370",
"REACTOME:R-HSA-5609976",
"REACTOME:R-HSA-70370",
"REACTOME:R-MMU-70370"
] | 9 | [
"1kkh",
"1pie",
"1s4e",
"1vis",
"1wuu",
"2a2c",
"2a2d",
"2aj4",
"2cz9",
"2dei",
"2dej",
"3v2u",
"3v5r",
"6gr2",
"6q3w",
"6q3x",
"6q8z",
"6q90",
"6q91",
"6qje",
"6tep",
"6teq",
"6ter",
"6zfh",
"6zgv",
"6zgw",
"6zgx",
"6zgy",
"6zgz",
"6zh0",
"7ozx",
"7rcl"... | 35 | [] | [] | [] | [] | 0 | [] | [
"IPR000705",
"IPR006205"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctmP19",
"unclassified sequences"
] | [
184,
14351,
6607,
1,
199
] | 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,
2,
1,
1,
7,
9,
1,
4,
12,
2,
1,
13
] | 13 | true | Family | Mevalonate/galactokinase | Mevalonate/galactokinase | Mevalonate/galactokinase | 7 |
IPR006207 | 6,207 | Cystine knot, C-terminal | Cys_knot_C | Domain | 26,266 | false | false | Four recent crystal structures of growth factors--nerve growth factor, transforming growth factor-beta, platelet-derived growth factor, and human chorionic gonadotropin--from four separate superfamilies revealed that these proteins are structurally related and share a common overall topology [ ]. These proteins have ve... | [] | [] | [] | 0 | [
"PROSITE",
"PROFILE",
"SMART"
] | [
"PS01185",
"PS01225",
"SM00041"
] | [
"CTCK_1",
"CTCK_2",
"CT"
] | [
15246,
22854,
23337
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00912",
"R-CEL-376176",
"R-CEL-9010553",
"R-CFA-114608",
"R-CFA-216083",
"R-CFA-354192",
"R-CFA-354194",
"R-CFA-372708",
"R-CFA-430116",
"R-CFA-5674135",
"R-CFA-75892",
"R-DME-376176",
"R-DME-428890",
"R-DME-9010553",
"R-GGA-201451",
"R-GGA-381426",
"R-GGA-8957275",
"R-HSA-114... | [
"PROSITEDOC:PDOC00912",
"REACTOME:R-CEL-376176",
"REACTOME:R-CEL-9010553",
"REACTOME:R-CFA-114608",
"REACTOME:R-CFA-216083",
"REACTOME:R-CFA-354192",
"REACTOME:R-CFA-354194",
"REACTOME:R-CFA-372708",
"REACTOME:R-CFA-430116",
"REACTOME:R-CFA-5674135",
"REACTOME:R-CFA-75892",
"REACTOME:R-DME-376... | 98 | [
"2k8p",
"4jph",
"4my2",
"4nt5",
"4x1j",
"4yu8",
"5aej",
"5bpu",
"5bq8",
"5bqb",
"5bqc",
"5bqe",
"5cl1",
"5hk5",
"6l6r",
"7qcu",
"8b7h",
"8enb",
"8end",
"8enf",
"8wvx",
"8wvy",
"9khh",
"9uok"
] | 24 | [
"PUB00000091",
"PUB00000890",
"PUB00001089"
] | [
"7663117",
"8490958",
"7583638"
] | [
"The cystine-knot growth-factor superfamily.",
"A structural superfamily of growth factors containing a cystine knot motif.",
"Cystine knots."
] | [
1995,
1993,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Kangiella spongicola"
] | [
26265,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
86,
15,
64,
66,
77
] | 6 | true | Domain | Cystine knot, C-terminal | Cystine knot, C-terminal | Cys_knot_C | 5 |
IPR006208 | 6,208 | Glycoprotein hormone subunit beta | Glyco_hormone_CN | Domain | 12,211 | false | false | This domain is found at the C-terminal of glycoprotein hormones and various extracellular proteins. It is believed to be involved in disulphide-linked dimerisation [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00007"
] | [
"Cys_knot"
] | [
12211
] | 1 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp0292",
"R-BTA-193048",
"R-BTA-193993",
"R-BTA-209822",
"R-BTA-209968",
"R-BTA-375281",
"R-BTA-418555",
"R-BTA-8866910",
"R-BTA-975578",
"R-GGA-209822",
"R-GGA-209968",
"R-GGA-375281",
"R-GGA-381426",
"R-GGA-418555",
"R-GGA-8957275",
"R-HSA-193048",
"R-HSA-193993",
"R-HSA-20... | [
"GP:GenProp0292",
"REACTOME:R-BTA-193048",
"REACTOME:R-BTA-193993",
"REACTOME:R-BTA-209822",
"REACTOME:R-BTA-209968",
"REACTOME:R-BTA-375281",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-8866910",
"REACTOME:R-BTA-975578",
"REACTOME:R-GGA-209822",
"REACTOME:R-GGA-209968",
"REACTOME:R-GGA-375281",
... | 53 | [
"1fl7",
"1hcn",
"1hrp",
"1qfw",
"1xwd",
"4ay9",
"4mqw",
"4my2",
"5bpu",
"5bq8",
"5bqb",
"5bqc",
"5bqe",
"5cl1",
"6p57",
"7fig",
"7fih",
"7fii",
"7qcu",
"7t9i",
"7utz",
"7xw5",
"8enb",
"8end",
"8enf",
"8i2g",
"8wvx",
"8wvy",
"9khh",
"9uok"
] | 30 | [
"PUB00001661"
] | [
"7687569"
] | [
"The modular architecture of a new family of growth regulators related to connective tissue growth factor."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Kangiella spongicola"
] | [
12210,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
29,
5,
49,
29,
38
] | 6 | true | Domain | Glycoprotein hormone subunit beta | Glycoprotein hormone subunit beta | Glyco_hormone_CN | 7 |
IPR006211 | 6,211 | Furin-like cysteine-rich domain | Furin-like_Cys-rich_dom | Domain | 14,367 | false | false | The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation [ , , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00757"
] | [
"Furin-like"
] | [
14367
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.1",
"R-CEL-1227986",
"R-CEL-1250196",
"R-CEL-1251985",
"R-CEL-1253288",
"R-CEL-1257604",
"R-CEL-177929",
"R-CEL-179812",
"R-CEL-180292",
"R-CEL-180336",
"R-CEL-182971",
"R-CEL-1963642",
"R-CEL-2179392",
"R-CEL-416572",
"R-CEL-445144",
"R-CEL-5673001",
"R-CEL-6785631",
"R-CE... | [
"EC:2.7.10.1",
"REACTOME:R-CEL-1227986",
"REACTOME:R-CEL-1250196",
"REACTOME:R-CEL-1251985",
"REACTOME:R-CEL-1253288",
"REACTOME:R-CEL-1257604",
"REACTOME:R-CEL-177929",
"REACTOME:R-CEL-179812",
"REACTOME:R-CEL-180292",
"REACTOME:R-CEL-180336",
"REACTOME:R-CEL-182971",
"REACTOME:R-CEL-1963642"... | 191 | [
"1igr",
"1ivo",
"1m6b",
"1mox",
"1n8y",
"1n8z",
"1nql",
"1s78",
"1yy9",
"2a91",
"2ahx",
"2hr7",
"3b2v",
"3be1",
"3i2t",
"3ltf",
"3ltg",
"3mzw",
"3n85",
"3njp",
"3p11",
"3qwq",
"3u2p",
"3u7u",
"3u9u",
"3w11",
"3w12",
"3w13",
"3wlw",
"3wsq",
"4kro",
"4krp"... | 189 | [
"PUB00006268",
"PUB00093566",
"PUB00095139"
] | [
"1936959",
"23756652",
"25480784"
] | [
"Interallelic complementation among DER/flb alleles: implications for the mechanism of signal transduction by receptor-tyrosine kinases.",
"Structural basis for R-spondin recognition by LGR4/5/6 receptors.",
"Crystal structure of LGR4-Rspo1 complex: insights into the divergent mechanisms of ligand recognition b... | [
1991,
2013,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Candidatus Dojkabacteria bacterium",
"Opisthokonta"
] | [
1,
14366
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
50,
157,
33,
19,
53
] | 6 | true | Domain | Furin-like cysteine-rich domain | Furin-like cysteine-rich domain | Furin-like_Cys-rich_dom | 8 |
IPR006212 | 6,212 | Furin-like repeat | Furin_repeat | Repeat | 39,451 | false | false | The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation [ , , ]. | [] | [] | [] | 0 | [
"SMART",
"CDD"
] | [
"SM00261",
"cd00064"
] | [
"FU",
"FU"
] | [
36448,
33276
] | 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-4641263",
"R-CEL-1227986",
"R-CEL-1250196",
"R-CEL-1251985",
"R-CEL-1253288",
"R-CEL-1257604",
"R-CEL-177929",
"R-CEL-179812",
"R-CEL-180292",
"R-CEL-180336",
"R-CEL-182971",
"R-CEL-1963642",
"R-CEL-2179392",
"R-CEL-416572",
"R-CEL-445144",
"R-CEL-5673001",
"R-CEL-6785631",
... | [
"REACTOME:R-BTA-4641263",
"REACTOME:R-CEL-1227986",
"REACTOME:R-CEL-1250196",
"REACTOME:R-CEL-1251985",
"REACTOME:R-CEL-1253288",
"REACTOME:R-CEL-1257604",
"REACTOME:R-CEL-177929",
"REACTOME:R-CEL-179812",
"REACTOME:R-CEL-180292",
"REACTOME:R-CEL-180336",
"REACTOME:R-CEL-182971",
"REACTOME:R-C... | 237 | [
"1igr",
"1ivo",
"1m6b",
"1mox",
"1n8y",
"1n8z",
"1nql",
"1s78",
"1yy9",
"2a91",
"2ahx",
"2hr7",
"3b2u",
"3b2v",
"3be1",
"3c09",
"3i2t",
"3ltf",
"3ltg",
"3mzw",
"3n85",
"3njp",
"3p0y",
"3p11",
"3qwq",
"3u2p",
"3u7u",
"3u9u",
"3w11",
"3w12",
"3w13",
"3wlw"... | 233 | [
"PUB00006268",
"PUB00093566",
"PUB00095139"
] | [
"1936959",
"23756652",
"25480784"
] | [
"Interallelic complementation among DER/flb alleles: implications for the mechanism of signal transduction by receptor-tyrosine kinases.",
"Structural basis for R-spondin recognition by LGR4/5/6 receptors.",
"Crystal structure of LGR4-Rspo1 complex: insights into the divergent mechanisms of ligand recognition b... | [
1991,
2013,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
3,
19,
39417,
5,
7
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
96,
256,
89,
49,
90
] | 6 | true | Repeat | Furin-like repeat | Furin-like repeat | Furin_repeat | 9 |
IPR006213 | 6,213 | Bax inhibitor 1, conserved site | Bax_inhbtr1_CS | Conserved_site | 3,058 | false | false | Bax inhibitor-1 (BI-1) (gene TEGT) [ ] is a suppressor of apoptosis that interacts with BCL2 and BCL-X. These are proteins of about 25kDa which seem to contain seven transmembrane domains. Homologues are found in plants and bacteria. This entry corresponds to a conserved region that starts with the beginning of the thi... | [
"GO:0043066",
"GO:0016020"
] | [
"negative regulation of apoptotic process",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS01243"
] | [
"BI1"
] | [
3058
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00957"
] | [
"PROSITEDOC:PDOC00957"
] | 1 | [] | 0 | [
"PUB00001966"
] | [
"8530040"
] | [
"Identification of a novel conserved human gene, TEGT."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes",
"uncultured Caudovirales phage"
] | [
2202,
838,
17,
1
] | 4 | [
"Arabidopsis thaliana",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus"
] | [
17,
2,
1,
6,
4,
2,
7
] | 7 | true | Conserved_site | Bax inhibitor 1, conserved site | Bax inhibitor 1, conserved site | Bax_inhbtr1_CS | 2 |
IPR006214 | 6,214 | Bax inhibitor 1-related | Bax_inhibitor_1-related | Family | 37,808 | false | false | This entry represents BI-1 and related sequences, including lifeguard proteins, which resemble BI-1 and also act as apoptotic regulators [ ]. This entry also includes bacterial and viral proteins, related to human BAX inhibitor 1, such as Transmembrane protein HWLF3 from human cytomegalovirus, a glycoprotein that contr... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF01027",
"PTHR23291"
] | [
"Bax1-I",
""
] | [
37112,
34664
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6798695",
"R-HSA-9609690",
"R-MMU-6798695"
] | [
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9609690",
"REACTOME:R-MMU-6798695"
] | 3 | [
"4pgr",
"4pgs",
"4pgu",
"4pgv",
"4pgw",
"4tkq",
"6nq7",
"6nq8",
"6nq9"
] | 9 | [
"PUB00001966",
"PUB00053809",
"PUB00053810",
"PUB00095242",
"PUB00098575",
"PUB00098576",
"PUB00162443"
] | [
"8530040",
"19704470",
"19742129",
"24904158",
"23888068",
"22128171",
"24787765"
] | [
"Identification of a novel conserved human gene, TEGT.",
"Arabidopsis Bax inhibitor-1: A rheostat for ER stress-induced programmed cell death.",
"Bax inhibitor-1, a conserved cell death suppressor, is a key molecular switch downstream from a variety of biotic and abiotic stress signals in plants.",
"Structura... | [
1995,
2008,
2009,
2014,
2013,
2012,
2014
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
16,
16774,
20495,
294,
229
] | 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",... | [
36,
7,
39,
16,
2,
47,
20,
2,
21,
34,
1,
1,
50
] | 13 | true | Family | Bax inhibitor 1-related | Bax inhibitor 1-related | Bax_inhibitor_1-related | 1 |
IPR006215 | 6,215 | Glycoside hydrolase, melibiase | Glyco_hydro_melibiase | Family | 683 | 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:0004557",
"GO:0005975"
] | [
"alpha-galactosidase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00748"
] | [
"MELIBIASE"
] | [
683
] | 1 | [
"CAZY",
"EC",
"METACYC",
"REACTOME"
] | [
"GH27",
"3.2.1.22",
"PWY-6527",
"R-SPO-6798695"
] | [
"CAZY:GH27",
"EC:3.2.1.22",
"METACYC:PWY-6527",
"REACTOME:R-SPO-6798695"
] | 4 | [
"3a5v",
"3lrk",
"3lrl",
"3lrm"
] | 4 | [
"PUB00002595",
"PUB00004870",
"PUB00005266",
"PUB00005652"
] | [
"2174888",
"7624375",
"8535779",
"7725791"
] | [
"Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Homology with human alpha-galactosidase A suggests evolution from a common ancestral gene.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydr... | [
1990,
1995,
1995,
1994
] | 4 | [
"IPR002241"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Pseudonocardia endophytica"
] | [
682,
1
] | 2 | [
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1
] | 1 | true | Family | Glycoside hydrolase, melibiase | Glycoside hydrolase, melibiase | Glyco_hydro_melibiase | 9 |
IPR006216 | 6,216 | Photosystem II cytochrome b559, conserved site | PSII_cyt_b559_CS | Conserved_site | 28,111 | false | false | Oxygenic photosynthesis uses two multi-subunit photosystems (I and II) located in the cell membranes of cyanobacteria and in the thylakoid membranes of chloroplasts in plants and algae. Photosystem II (PSII) has a P680 reaction centre containing chlorophyll 'a' that uses light energy to carry out the oxidation (splitti... | [
"GO:0020037",
"GO:0009767",
"GO:0015979",
"GO:0019684",
"GO:0009523",
"GO:0009539",
"GO:0016020"
] | [
"heme binding",
"photosynthetic electron transport chain",
"photosynthesis",
"photosynthesis, light reaction",
"photosystem II",
"photosystem II reaction center",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component",
"cellular_component",
"cellular_component"
] | 7 | [
"PROSITE"
] | [
"PS00537"
] | [
"CYTOCHROME_B559"
] | [
28111
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00464"
] | [
"PROSITEDOC:PDOC00464"
] | 1 | [
"1izl",
"1s5l",
"1w5c",
"2axt",
"3a0b",
"3a0h",
"3jcu",
"3kzi",
"3wu2",
"4fby",
"4il6",
"4ixq",
"4ixr",
"4pbu",
"4pj0",
"4rvy",
"4tnh",
"4tni",
"4tnj",
"4tnk",
"4ub6",
"4ub8",
"4v62",
"4v82",
"4yuu",
"5b5e",
"5b66",
"5e79",
"5e7c",
"5gth",
"5gti",
"5h2f"... | 168 | [
"PUB00015357",
"PUB00015358",
"PUB00015359",
"PUB00015364",
"PUB00097583",
"PUB00152828"
] | [
"12518057",
"15100025",
"14871485",
"12560096",
"30076221",
"33846594"
] | [
"Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution.",
"The evolutionary development of the protein complement of photosystem 2.",
"The low molecular mass subunits of the photosynthetic supracomplex, photosystem II.",
"Mossbauer studies of the non-heme ir... | [
2003,
2004,
2004,
2003,
2018,
2021
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
676,
27435
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
8,
10,
4
] | 3 | true | Conserved_site | Photosystem II cytochrome b559, conserved site | Photosystem II cytochrome b559, conserved site | PSII_cyt_b559_CS | 5 |
IPR006217 | 6,217 | Photosystem II cytochrome b559, alpha subunit | PSII_cyt_b559_asu | Family | 14,665 | false | false | Oxygenic photosynthesis uses two multi-subunit photosystems (I and II) located in the cell membranes of cyanobacteria and in the thylakoid membranes of chloroplasts in plants and algae. Photosystem II (PSII) has a P680 reaction centre containing chlorophyll 'a' that uses light energy to carry out the oxidation (splitti... | [
"GO:0020037",
"GO:0009767",
"GO:0015979",
"GO:0019684",
"GO:0009523"
] | [
"heme binding",
"photosynthetic electron transport chain",
"photosynthesis",
"photosynthesis, light reaction",
"photosystem II"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"HAMAP",
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"MF_00642",
"PIRSF000036",
"PTHR33391",
"TIGR01332"
] | [
"PSII_PsbE",
"PsbE",
"",
"cyt_b559_alpha"
] | [
13823,
14178,
14665,
14396
] | 4 | [
"GP"
] | [
"GenProp0661"
] | [
"GP:GenProp0661"
] | 1 | [
"1izl",
"1s5l",
"1w5c",
"2axt",
"3a0b",
"3a0h",
"3jcu",
"3kzi",
"3wu2",
"4fby",
"4il6",
"4ixq",
"4ixr",
"4pbu",
"4pj0",
"4rvy",
"4tnh",
"4tni",
"4tnj",
"4tnk",
"4ub6",
"4ub8",
"4v62",
"4v82",
"4yuu",
"5b5e",
"5b66",
"5e79",
"5e7c",
"5gth",
"5gti",
"5h2f"... | 168 | [
"PUB00015357",
"PUB00015358",
"PUB00015359",
"PUB00015364",
"PUB00097583",
"PUB00152828"
] | [
"12518057",
"15100025",
"14871485",
"12560096",
"30076221",
"33846594"
] | [
"Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution.",
"The evolutionary development of the protein complement of photosystem 2.",
"The low molecular mass subunits of the photosynthetic supracomplex, photosystem II.",
"Mossbauer studies of the non-heme ir... | [
2003,
2004,
2004,
2003,
2018,
2021
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine metagenome"
] | [
376,
14288,
1
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
5,
4,
2
] | 3 | true | Family | Photosystem II cytochrome b559, alpha subunit | Photosystem II cytochrome b559, alpha subunit | PSII_cyt_b559_asu | 9 |
IPR006218 | 6,218 | DAHP synthetase I/KDSA | DAHP1/KDSA | Domain | 48,960 | false | false | null | [
"GO:0009058"
] | [
"biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00793"
] | [
"DAHP_synth_1"
] | [
48960
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"2.5.1.55",
"PWY-1269",
"PWY-7674"
] | [
"EC:2.5.1.55",
"METACYC:PWY-1269",
"METACYC:PWY-7674"
] | 3 | [
"1d9e",
"1fwn",
"1fws",
"1fwt",
"1fww",
"1fx6",
"1fxp",
"1fxq",
"1fy6",
"1g7u",
"1g7v",
"1gg0",
"1gg1",
"1hfb",
"1jcx",
"1jcy",
"1kfl",
"1lrn",
"1lro",
"1lrq",
"1n8f",
"1o60",
"1oab",
"1of6",
"1of8",
"1ofa",
"1ofb",
"1ofo",
"1ofp",
"1ofq",
"1ofr",
"1og0"... | 142 | [
"PUB00006352",
"PUB00006452"
] | [
"8760910",
"10425687"
] | [
"Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa.",
"Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli."
] | [
1996,
1999
] | 2 | [] | [
"IPR006268"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
158,
42984,
4981,
60,
777
] | 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"
] | [
9,
4,
2,
3,
2,
2,
5
] | 7 | true | Domain | DAHP synthetase I/KDSA | DAHP synthetase I/KDSA | DAHP1/KDSA | 4 |
IPR006219 | 6,219 | DAHP synthase, class 1 | DAHP_synth_1 | Family | 22,277 | false | false | Members of this group catalyze the first enzymatic reaction of the shikimate pathway. The common (shikimate) pathway links metabolism of carbohydrates to biosynthesis of aromatic amino acids phenylalanine, tyrosine, tryptophan, and derivatives in microorganisms and in plants. In a sequence of seven enzymatic reactions,... | [
"GO:0003849",
"GO:0009073"
] | [
"3-deoxy-7-phosphoheptulonate synthase activity",
"aromatic amino acid family biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"PIRSF001361",
"PTHR21225",
"TIGR00034"
] | [
"DAHP_synthase",
"",
"aroFGH"
] | [
20624,
22262,
21797
] | 3 | [
"EC",
"GP",
"GP",
"METACYC"
] | [
"2.5.1.54",
"GenProp0001",
"GenProp1731",
"PWY-6164"
] | [
"EC:2.5.1.54",
"GP:GenProp0001",
"GP:GenProp1731",
"METACYC:PWY-6164"
] | 4 | [
"1gg1",
"1hfb",
"1kfl",
"1n8f",
"1oab",
"1of6",
"1of8",
"1ofa",
"1ofb",
"1ofo",
"1ofp",
"1ofq",
"1ofr",
"1og0",
"1qr7",
"3tqk",
"4hsn",
"4hso",
"4ixx",
"4uc5",
"4ucg",
"4uma",
"4umb",
"4umc",
"5cks",
"5cz0",
"5czs",
"5czt",
"5d02",
"5d03",
"5d04",
"5d05"... | 52 | [
"PUB00006352",
"PUB00006452",
"PUB00014334",
"PUB00015966",
"PUB00016050",
"PUB00016117",
"PUB00016158",
"PUB00016190",
"PUB00016205",
"PUB00016207",
"PUB00089814"
] | [
"8760910",
"10425687",
"15012217",
"12743122",
"10926516",
"12126632",
"12667068",
"12540830",
"11244581",
"1682314",
"17990954"
] | [
"Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa.",
"Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli.",
"THE SHIKIMATE... | [
1996,
1999,
1999,
2003,
2000,
2002,
2003,
2003,
2001,
1991,
2007
] | 11 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Micrarchaeum acidiphilum ARMAN-2",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
17920,
1,
4134,
53,
169
] | 5 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
3,
2,
2,
2
] | 4 | true | Family | DAHP synthase, class 1 | DAHP synthase, class 1 | DAHP_synth_1 | 7 |
IPR006221 | 6,221 | Anthranilate synthase/para-aminobenzoate synthase like domain | TrpG/PapA_dom | Domain | 39,529 | false | false | This entry represents the anthranilate synthase/para-aminobenzoate synthase domain, which share sequence similarity to the glutamine amidotransferase domain . Anthranilate synthase play a role in the tryptophan-biosynthetic pathway, while the para-aminobenzoate synthase is involved in the folate biosynthetic pathway. I... | [] | [] | [] | 0 | [
"NCBIFAM",
"CDD"
] | [
"TIGR00566",
"cd01743"
] | [
"trpG_papA",
"GATase1_Anthranilate_Synthase"
] | [
34031,
39529
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC"
] | [
"4.1.3.27",
"GenProp0037",
"PWY-5958",
"PWY-6661"
] | [
"EC:4.1.3.27",
"GP:GenProp0037",
"METACYC:PWY-5958",
"METACYC:PWY-6661"
] | 4 | [
"1i1q",
"1i7q",
"1i7s",
"1qdl",
"3r74",
"3r75",
"3r76",
"6qur",
"8hx6",
"8hx7",
"8hx8",
"8hx9",
"8rp0",
"8rp1",
"8rp2",
"8rp6",
"8rp7"
] | 17 | [
"PUB00003199",
"PUB00096162",
"PUB00096163",
"PUB00096164",
"PUB00096165",
"PUB00096166"
] | [
"6283099",
"4590474",
"8346682",
"3057324",
"50316",
"14745019"
] | [
"Nucleotide sequence of the trpD gene, encoding anthranilate synthetase component II of Escherichia coli.",
"Localization of two functions of the phosphoribosyl anthranilate transferase of Escherichia coli to distinct regions of the polypeptide chain.",
"Para-aminobenzoate synthase gene of Saccharomyces cerevis... | [
1982,
1974,
1993,
1988,
1975,
2004
] | 6 | [
"IPR017926"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1121,
31926,
5919,
8,
555
] | 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"
] | [
16,
2,
3,
5,
2,
2,
30
] | 7 | true | Domain | Anthranilate synthase/para-aminobenzoate synthase like domain | Anthranilate synthase/para-aminobenzoate synthase like domain | TrpG/PapA_dom | 7 |
IPR006222 | 6,222 | GCVT, N-terminal domain | GCVT_N | Domain | 60,090 | false | false | This entry represents the N-terminal in glycine cleavage T-proteins, which are part of the glycine cleavage multienzyme complex (GCVT) found in bacteria and the mitochondria of eukaryotes. This domain is also found in YgfZ proteins. This domain represents a possible folate-binding domain. Trimethylamine-oxide aldolase ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01571"
] | [
"GCV_T"
] | [
60090
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.2.10",
"GenProp1414",
"R-BTA-6783984",
"R-CFA-6783984",
"R-DDI-6783984",
"R-HSA-204174",
"R-HSA-6783984",
"R-HSA-6798163",
"R-MMU-204174",
"R-MMU-6783984",
"R-MMU-6798163",
"R-RNO-6798163",
"R-SCE-6783984",
"R-SPO-6783984"
] | [
"EC:2.1.2.10",
"GP:GenProp1414",
"REACTOME:R-BTA-6783984",
"REACTOME:R-CFA-6783984",
"REACTOME:R-DDI-6783984",
"REACTOME:R-HSA-204174",
"REACTOME:R-HSA-6783984",
"REACTOME:R-HSA-6798163",
"REACTOME:R-MMU-204174",
"REACTOME:R-MMU-6783984",
"REACTOME:R-MMU-6798163",
"REACTOME:R-RNO-6798163",
"... | 14 | [
"1pj5",
"1pj6",
"1pj7",
"1v5v",
"1vlo",
"1vrq",
"1woo",
"1wop",
"1wor",
"1wos",
"1wsr",
"1wsv",
"1x31",
"1yx2",
"2gag",
"2gah",
"3a8i",
"3a8j",
"3a8k",
"3ad7",
"3ad8",
"3ad9",
"3ada",
"3gir",
"3gsi",
"3tfh",
"3tfi",
"3tfj",
"3ttg",
"4p9s",
"4paa",
"4pab"... | 40 | [
"PUB00001870",
"PUB00022265",
"PUB00038140",
"PUB00043084",
"PUB00069711",
"PUB00093079",
"PUB00160522"
] | [
"9047339",
"15489424",
"16051266",
"16359333",
"20375021",
"24550299",
"20489182"
] | [
"Cloning, and molecular characterization of the GCV1 gene encoding the glycine cleavage T-protein from Saccharomyces cerevisiae.",
"Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolism.",
"Crystal structure of human T-protein of glycine... | [
1997,
2004,
2005,
2006,
2010,
2014,
2010
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1270,
44834,
12563,
1423
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
7,
7,
9,
9,
1,
38,
10,
1,
5,
20,
1,
1,
4
] | 13 | true | Domain | GCVT, N-terminal domain | GCVT, N-terminal domain | GCVT_N | 2 |
IPR006224 | 6,224 | Pseudouridine synthase, RluA-like, conserved site | PsdUridine_synth_RluA-like_CS | Conserved_site | 75,603 | false | false | Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine (Psi) in a variety of RNA molecules, and may function as RNA chaperones. Pseudouridine is the most abundant modified nucleotide found in all cellular RNAs. There are four distinct families of pseudouridine synthases that share no global sequ... | [
"GO:0003723",
"GO:0009982",
"GO:0001522",
"GO:0009451"
] | [
"RNA binding",
"pseudouridine synthase activity",
"pseudouridine synthesis",
"RNA modification"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PROSITE"
] | [
"PS01129"
] | [
"PSI_RLU"
] | [
75603
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME"
] | [
"5.4.99",
"PDOC00869",
"R-HSA-6793080",
"R-HSA-9937008"
] | [
"EC:5.4.99",
"PROSITEDOC:PDOC00869",
"REACTOME:R-HSA-6793080",
"REACTOME:R-HSA-9937008"
] | 4 | [
"1prz",
"1qyu",
"1v9f",
"1v9k",
"1xpi",
"2i82",
"2ist",
"5uba",
"7bl5"
] | 9 | [
"PUB00003020",
"PUB00032035",
"PUB00037409",
"PUB00041633",
"PUB00045922",
"PUB00092579",
"PUB00095796"
] | [
"9660827",
"15078091",
"14659742",
"17188032",
"10529181",
"19664587",
"11720289"
] | [
"The rluC gene of Escherichia coli codes for a pseudouridine synthase that is solely responsible for synthesis of pseudouridine at positions 955, 2504, and 2580 in 23 S ribosomal RNA.",
"Crystal structures of the catalytic domains of pseudouridine synthases RluC and RluD from Escherichia coli.",
"Crystal struct... | [
1998,
2004,
2004,
2006,
1999,
2009,
2001
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
66105,
8609,
29,
5,
855
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
29,
3,
1,
4,
4,
4,
2,
1,
8,
4,
4,
1,
42
] | 13 | true | Conserved_site | Pseudouridine synthase, RluA-like, conserved site | Pseudouridine synthase, RluA-like, conserved site | PsdUridine_synth_RluA-like_CS | 2 |
IPR006225 | 6,225 | Pseudouridine synthase, RluC/RluD | PsdUridine_synth_RluC/D | Family | 51,087 | false | false | This entry represents the RluC/RluD subfamily of pseudouridine synthases. RluC and RluD are homologous enzymes which each convert three specific uridine bases in Escherichia coli ribosomal 23S RNA to pseudouridine: bases uracil-955, U-2504, and U-2580 in the case of RluC and uracil-1911, U-1915, and U-1917 in the case ... | [
"GO:0003723",
"GO:0009982",
"GO:0001522",
"GO:0009451"
] | [
"RNA binding",
"pseudouridine synthase activity",
"pseudouridine synthesis",
"RNA modification"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"NCBIFAM"
] | [
"TIGR00005"
] | [
"rluA_subfam"
] | [
51087
] | 1 | [
"EC"
] | [
"5.4.99"
] | [
"EC:5.4.99"
] | 1 | [
"1prz",
"1qyu",
"1v9f",
"1v9k",
"1xpi",
"2i82",
"2ist",
"7bl5"
] | 8 | [
"PUB00032035",
"PUB00037409",
"PUB00045922",
"PUB00092579"
] | [
"15078091",
"14659742",
"10529181",
"19664587"
] | [
"Crystal structures of the catalytic domains of pseudouridine synthases RluC and RluD from Escherichia coli.",
"Crystal structure of the RluD pseudouridine synthase catalytic module, an enzyme that modifies 23S rRNA and is essential for normal cell growth of Escherichia coli.",
"Role of cysteine residues in pse... | [
2004,
2004,
1999,
2009
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
46594,
3813,
24,
3,
653
] | 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,
1,
4,
3,
3,
1,
1,
2,
2,
2,
1,
3
] | 13 | true | Family | Pseudouridine synthase, RluC/RluD | Pseudouridine synthase, RluC/RluD | PsdUridine_synth_RluC/D | 9 |
IPR006228 | 6,228 | Polycystin cation channel | Polycystin_cat | Domain | 1,006 | false | false | This represents the N-terminal region of polycystin, a member of the Polycystin Cation Channel (PCC) family. Polycystin is a huge protein of 4303aa. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lect... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00864"
] | [
"PCC"
] | [
1006
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-5620916",
"R-MMU-5620916"
] | [
"REACTOME:R-HSA-5620916",
"REACTOME:R-MMU-5620916"
] | 2 | [] | 0 | [
"PUB00001323",
"PUB00020131"
] | [
"9889186",
"10517637"
] | [
"The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease.",
"Polycystin-L is a calcium-regulated cation channel permeable to calcium ions."
] | [
1999,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1006
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
3,
1,
4
] | 4 | true | Domain | Polycystin cation channel | Polycystin cation channel | Polycystin_cat | 1 |
IPR006230 | 6,230 | Protein MutL | MutL | Family | 2,107 | false | false | This small family includes GlmL/MutL from Clostridium tetanomorphum and Clostridium cochlearium. GlmL is located between the genes for the two subunits, epsilon (GlmE) and sigma (GlmS), of the coenzyme-B12-dependent glutamate mutase (methylaspartate mutase), the first enzyme in a pathway of glutamate fermentation. Memb... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF",
"NCBIFAM"
] | [
"PF13941",
"PIRSF004729",
"TIGR01319"
] | [
"MutL",
"MutL",
"glmL_fam"
] | [
2107,
1282,
1502
] | 3 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009576"
] | [
"7880251"
] | [
"Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Thermoproteati",
"metagenomes"
] | [
2003,
4,
100
] | 3 | [] | [] | 0 | true | Family | Protein MutL | Protein MutL | MutL | 3 |
IPR006231 | 6,231 | Malate:quinone-oxidoreductase | MQO | Family | 10,595 | false | false | The membrane-associated enzyme, malate:quinone-oxidoreductase, is an alternative to the better-known NAD-dependent malate dehydrogenase as part of the TCA cycle. The reduction of a quinone rather than NAD+ makes the reaction essentially irreversible in the direction of malate oxidation to oxaloacetate. Both forms of ma... | [
"GO:0008924",
"GO:0006099"
] | [
"L-malate dehydrogenase (quinone) activity",
"tricarboxylic acid cycle"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"NCBIFAM"
] | [
"MF_00212",
"PF06039",
"TIGR01320"
] | [
"MQO",
"Mqo",
"mal_quin_oxido"
] | [
9617,
10595,
9337
] | 3 | [
"EC",
"GP",
"METACYC",
"METACYC"
] | [
"1.1.5.4",
"GenProp0033",
"PWY-5913",
"PWY-7254"
] | [
"EC:1.1.5.4",
"GP:GenProp0033",
"METACYC:PWY-5913",
"METACYC:PWY-7254"
] | 4 | [
"9dm1"
] | 1 | [
"PUB00009577"
] | [
"11092847"
] | [
"Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
15,
10310,
188,
82
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Malate:quinone-oxidoreductase | Malate:quinone-oxidoreductase | MQO | 4 |
IPR006232 | 6,232 | Sucrose-6-phosphate hydrolase | Suc6P_hydrolase | Family | 6,278 | 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:0004564",
"GO:0005975",
"GO:0005737"
] | [
"beta-fructofuranosidase activity",
"carbohydrate metabolic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01322"
] | [
"scrB_fam"
] | [
6278
] | 1 | [
"CAZY",
"EC",
"METACYC"
] | [
"GH32",
"3.2.1.26",
"PWY-8314"
] | [
"CAZY:GH32",
"EC:3.2.1.26",
"METACYC:PWY-8314"
] | 3 | [
"6nu7",
"6nu8",
"7bwb",
"7bwc",
"7vco",
"7vcp"
] | 6 | [
"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 | [
"IPR001362"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
6025,
251,
2
] | 3 | [] | [] | 0 | true | Family | Sucrose-6-phosphate hydrolase | Sucrose-6-phosphate hydrolase | Suc6P_hydrolase | 5 |
IPR006233 | 6,233 | Cystathionine beta-lyase, bacterial | Cys_b_lyase_bac | Family | 8,188 | false | false | Cystathionine beta-lyase (alternate name: beta-cystathionase) is one of several pyridoxal-dependent enzymes of cysteine, methionine, and homocysteine metabolism. This enzyme is involved in the biosynthesis of Met from Cys [ ]. | [
"GO:0047804",
"GO:0006520"
] | [
"cysteine-S-conjugate beta-lyase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR43500",
"TIGR01324"
] | [
"",
"cysta_beta_ly_B"
] | [
8188,
6865
] | 2 | [
"CAZY",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"GH32",
"4.4.1.13",
"PWY-1187",
"PWY-2821",
"PWY-601",
"PWY-6842",
"PWY-6936",
"PWY-7901",
"PWY-801",
"PWY-8302"
] | [
"CAZY:GH32",
"EC:4.4.1.13",
"METACYC:PWY-1187",
"METACYC:PWY-2821",
"METACYC:PWY-601",
"METACYC:PWY-6842",
"METACYC:PWY-6936",
"METACYC:PWY-7901",
"METACYC:PWY-801",
"METACYC:PWY-8302"
] | 10 | [
"1cl1",
"1cl2",
"2fq6",
"2gqn",
"4itg",
"4itx",
"8duy",
"8sa7",
"8sa8",
"8sa9",
"8saa",
"8sab",
"8sac",
"8sad",
"8sae",
"8u98",
"8u99"
] | 17 | [
"PUB00003370"
] | [
"8831789"
] | [
"Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A."
] | [
1996
] | 1 | [
"IPR000277"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
7995,
116,
77
] | 3 | [
"Escherichia coli (strain K12)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
1
] | 2 | true | Family | Cystathionine beta-lyase, bacterial | Cystathionine beta-lyase, bacterial | Cys_b_lyase_bac | 9 |
IPR006234 | 6,234 | O-succinylhomoserine sulfhydrylase | O-succ-hSer_sulfhydrylase | Family | 8,107 | false | false | These sequences represent O-succinylhomoserine sulfhydrylase, one of several related pyridoxal phosphate-dependent enzymes of cysteine and methionine metabolism. This enzyme is part of an alternative pathway of homocysteine biosynthesis, a step in methionine biosynthesis. | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_02056",
"TIGR01325"
] | [
"MetZ",
"O_suc_HS_sulf"
] | [
8068,
6300
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.5.1.-",
"PWY-4502",
"PWY-4681",
"PWY-5802",
"PWY-5815",
"PWY-5816",
"PWY-5817",
"PWY-5893",
"PWY-5979",
"PWY-6262",
"PWY-6403",
"PWY-6659",
"PWY-6681",
"PWY-6936",
"PWY-7372",
"PWY-7405",
"PWY-7407",
"PWY-7493",
"PWY-7520",
"PWY-7529",
"PWY-7532",
"PWY-7540",
"PWY-7543... | [
"EC:2.5.1.-",
"METACYC:PWY-4502",
"METACYC:PWY-4681",
"METACYC:PWY-5802",
"METACYC:PWY-5815",
"METACYC:PWY-5816",
"METACYC:PWY-5817",
"METACYC:PWY-5893",
"METACYC:PWY-5979",
"METACYC:PWY-6262",
"METACYC:PWY-6403",
"METACYC:PWY-6659",
"METACYC:PWY-6681",
"METACYC:PWY-6936",
"METACYC:PWY-7... | 43 | [
"3ndn",
"9iqh"
] | 2 | [] | [] | [] | [] | 0 | [
"IPR000277"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
7957,
6,
144
] | 3 | [] | [] | 0 | true | Family | O-succinylhomoserine sulfhydrylase | O-succinylhomoserine sulfhydrylase | O-succ-hSer_sulfhydrylase | 9 |
IPR006236 | 6,236 | D-3-phosphoglycerate dehydrogenase | PGDH | Family | 13,679 | false | false | Phosphoglycerate dehydrogenases (PGDH) have at least two different structural domains: the nucleotide binding and the substrate binding. There are three types of PGDH: type 3 enzymes are composed only of these two domains, type2 enzymes contain an extra C-terminal regulatory domain (ACT domain), type 1 enzymes contain ... | [
"GO:0004617",
"GO:0006564"
] | [
"phosphoglycerate dehydrogenase activity",
"L-serine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01327"
] | [
"PGDH"
] | [
13679
] | 1 | [
"EC",
"EC",
"GP",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1.399",
"1.1.1.95",
"GenProp1640",
"PWY-8010",
"PWY-8190",
"R-HSA-977347",
"R-MMU-977347",
"R-RNO-977347",
"R-SSC-977347"
] | [
"EC:1.1.1.399",
"EC:1.1.1.95",
"GP:GenProp1640",
"METACYC:PWY-8010",
"METACYC:PWY-8190",
"REACTOME:R-HSA-977347",
"REACTOME:R-MMU-977347",
"REACTOME:R-RNO-977347",
"REACTOME:R-SSC-977347"
] | 9 | [
"1ygy",
"3dc2",
"3ddn"
] | 3 | [
"PUB00032650",
"PUB00069764",
"PUB00069765"
] | [
"15668249",
"22023909",
"19924905"
] | [
"Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits.",
"Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases.",
"Transient kinetic analysis of the interaction of L-serine with Escherichia coli D... | [
2005,
2012,
2009
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
9670,
3154,
583,
272
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
8,
1,
4,
1,
10,
3,
13
] | 7 | true | Family | D-3-phosphoglycerate dehydrogenase | D-3-phosphoglycerate dehydrogenase | PGDH | 3 |
IPR006237 | 6,237 | L-methionine gamma-lyase | L-Met_gamma_lys | Family | 2,009 | false | false | This family of sequences is a methionine gamma-lyase subset of a family of PLP-dependent trans-sulphuration enzymes. The member from the parasite Trichomonas vaginalis is described as catalyzing alpha gamma- and alpha-beta eliminations and gamma-replacement reactions on methionine, cysteine, and some derivatives [ ]. T... | [
"GO:0018826"
] | [
"methionine gamma-lyase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR01328"
] | [
"met_gam_lyase"
] | [
2009
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.4.1.11",
"4.4.1.2",
"PWY-6931",
"PWY-6933",
"PWY-7793"
] | [
"EC:4.4.1.11",
"EC:4.4.1.2",
"METACYC:PWY-6931",
"METACYC:PWY-6933",
"METACYC:PWY-7793"
] | 5 | [
"1e5e",
"1e5f",
"1gc0",
"1gc2",
"1pg8",
"1ukj",
"1y4i",
"2o7c",
"2rfv",
"3jw9",
"3jwa",
"3jwb",
"3mkj",
"3vk2",
"3vk3",
"3vk4",
"4hf8",
"4mkj",
"4mkk",
"4oma",
"4p7y",
"5d5s",
"5dx5",
"5e4z",
"5k30",
"5m3z",
"5x2v",
"5x2w",
"5x2x",
"5x2y",
"5x2z",
"5x30"... | 39 | [
"PUB00017592",
"PUB00017667"
] | [
"9190812",
"1953661"
] | [
"Molecular characterization of the mde operon involved in L-methionine catabolism of Pseudomonas putida.",
"Purification and characterization of methionine gamma-lyase from Trichomonas vaginalis."
] | [
1997,
1991
] | 2 | [
"IPR000277"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
1993,
11,
5
] | 3 | [] | [] | 0 | true | Family | L-methionine gamma-lyase | L-methionine gamma-lyase | L-Met_gamma_lys | 8 |
IPR006238 | 6,238 | Cystathionine beta-lyase, eukaryotic | Cys_b_lyase_euk | Family | 2,381 | false | false | This group of sequences represent cystathionine beta-lyase (alternate name: beta-cystathionase), which catalyses the penultimate step in the de novo biosynthesis of methionine, as it converts cystathionine into homocysteine [ , , , ]. In plants, its role in methionine metabolism may affect plant development in differen... | [
"GO:0047804",
"GO:0006790"
] | [
"cysteine-S-conjugate beta-lyase activity",
"sulfur compound metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01329"
] | [
"cysta_beta_ly_E"
] | [
2381
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.4.1.13",
"GenProp1654",
"PWY-1187",
"PWY-2821",
"PWY-601",
"PWY-6842",
"PWY-6936",
"PWY-7901",
"PWY-801",
"PWY-8302"
] | [
"EC:4.4.1.13",
"GP:GenProp1654",
"METACYC:PWY-1187",
"METACYC:PWY-2821",
"METACYC:PWY-601",
"METACYC:PWY-6842",
"METACYC:PWY-6936",
"METACYC:PWY-7901",
"METACYC:PWY-801",
"METACYC:PWY-8302"
] | 10 | [
"1ibj"
] | 1 | [
"PUB00028668",
"PUB00101702",
"PUB00162476",
"PUB00162477",
"PUB00162478"
] | [
"11402193",
"16936141",
"31002461",
"35472754",
"8541513"
] | [
"The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity.",
"A peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolism.",
"Cystathionine beta-lyase is crucial for embryo patterning and the maintena... | [
2001,
2006,
2019,
2022,
1995
] | 5 | [
"IPR000277"
] | [] | 1 | 0 | 1 | [
"Acidobacteriota",
"Eukaryota"
] | [
4,
2377
] | 2 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
10,
1,
5,
1,
1,
2
] | 6 | true | Family | Cystathionine beta-lyase, eukaryotic | Cystathionine beta-lyase, eukaryotic | Cys_b_lyase_euk | 1 |
IPR006239 | 6,239 | 3(2),5 -bisphosphate nucleotidase | DPNP | Family | 3,891 | false | false | Sulphate is incorporated into 3-phosphoadenylylsulphate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulphate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. In plants these sequences represent a form of the enzyme, 3'(2'),5'-bisphosphate nucleotidase, which removes... | [
"GO:0008441",
"GO:0006790"
] | [
"3'(2'),5'-bisphosphate nucleotidase activity",
"sulfur compound metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01330"
] | [
"bisphos_HAL2"
] | [
3891
] | 1 | [
"EC"
] | [
"3.1.3.7"
] | [
"EC:3.1.3.7"
] | 1 | [
"1k9y",
"1k9z",
"1ka0",
"1ka1",
"1qgx",
"4hxv",
"4o7i",
"8f9y"
] | 8 | [
"PUB00009431",
"PUB00153367"
] | [
"10205895",
"7809627"
] | [
"The Arabidopsis HAL2-like gene family includes a novel sodium-sensitive phosphatase.",
"A salt-sensitive 3'(2'),5'-bisphosphate nucleotidase involved in sulfate activation."
] | [
1999,
1995
] | 2 | [
"IPR000760"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"hydrothermal vent metagenome"
] | [
195,
3694,
2
] | 3 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
16,
1,
9,
1,
1,
14
] | 6 | true | Family | 3(2),5 -bisphosphate nucleotidase | 3(2),5 -bisphosphate nucleotidase | DPNP | 9 |
IPR006241 | 6,241 | Photosystem II cytochrome b559, beta subunit | PSII_cyt_b559_bsu | Family | 13,918 | false | false | Oxygenic photosynthesis uses two multi-subunit photosystems (I and II) located in the cell membranes of cyanobacteria and in the thylakoid membranes of chloroplasts in plants and algae. Photosystem II (PSII) has a P680 reaction centre containing chlorophyll 'a' that uses light energy to carry out the oxidation (splitti... | [
"GO:0020037",
"GO:0009767",
"GO:0015979",
"GO:0019684",
"GO:0009523",
"GO:0009539",
"GO:0016020"
] | [
"heme binding",
"photosynthetic electron transport chain",
"photosynthesis",
"photosynthesis, light reaction",
"photosystem II",
"photosystem II reaction center",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component",
"cellular_component",
"cellular_component"
] | 7 | [
"HAMAP",
"PIRSF",
"NCBIFAM"
] | [
"MF_00643",
"PIRSF000037",
"TIGR01333"
] | [
"PSII_PsbF",
"PsbF",
"cyt_b559_beta"
] | [
13802,
13802,
13915
] | 3 | [
"GP"
] | [
"GenProp0661"
] | [
"GP:GenProp0661"
] | 1 | [
"1izl",
"1s5l",
"1w5c",
"2axt",
"3a0b",
"3a0h",
"3jcu",
"3kzi",
"3wu2",
"4fby",
"4il6",
"4ixq",
"4ixr",
"4pbu",
"4pj0",
"4rvy",
"4tnh",
"4tni",
"4tnj",
"4tnk",
"4ub6",
"4ub8",
"4v62",
"4v82",
"4yuu",
"5b5e",
"5b66",
"5e79",
"5e7c",
"5gth",
"5gti",
"5h2f"... | 168 | [
"PUB00015357",
"PUB00015358",
"PUB00015359",
"PUB00015364",
"PUB00097583",
"PUB00152828"
] | [
"12518057",
"15100025",
"14871485",
"12560096",
"30076221",
"33846594"
] | [
"Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution.",
"The evolutionary development of the protein complement of photosystem 2.",
"The low molecular mass subunits of the photosynthetic supracomplex, photosystem II.",
"Mossbauer studies of the non-heme ir... | [
2003,
2004,
2004,
2003,
2018,
2021
] | 6 | [] | [
"IPR061310"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota"
] | [
356,
13562
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
6,
2
] | 3 | true | Family | Photosystem II cytochrome b559, beta subunit | Photosystem II cytochrome b559, beta subunit | PSII_cyt_b559_bsu | 2 |
IPR006242 | 6,242 | Putative pyrophosphorylase ModD | ModD | Family | 1,057 | false | false | ModD is found with molybdenum transport genes modABC in Rhodobacter capsulatus. However, disruption of modD causes only a 4-fold (rather than 500-fold for modA, modB, modC) change in the external molybdenum concentration required to suppress an alternative nitrogenase [ ]. ModD proteins are highly similar to nicotinate... | [
"GO:0016763"
] | [
"pentosyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR01334"
] | [
"modD"
] | [
1057
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.4.2.-",
"PWY-5381",
"PWY-5800",
"PWY-6148",
"PWY-6720",
"PWY-7018",
"PWY-7025",
"PWY-7450",
"PWY-7817",
"PWY-7981"
] | [
"EC:2.4.2.-",
"METACYC:PWY-5381",
"METACYC:PWY-5800",
"METACYC:PWY-6148",
"METACYC:PWY-6720",
"METACYC:PWY-7018",
"METACYC:PWY-7025",
"METACYC:PWY-7450",
"METACYC:PWY-7817",
"METACYC:PWY-7981"
] | 10 | [] | 0 | [
"PUB00009574"
] | [
"8491722"
] | [
"Characterization of Rhodobacter capsulatus genes encoding a molybdenum transport system and putative molybdenum-pterin-binding proteins."
] | [
1993
] | 1 | [
"IPR027277"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"metagenomes"
] | [
34,
1014,
9
] | 3 | [] | [] | 0 | true | Family | Putative pyrophosphorylase ModD | Putative pyrophosphorylase ModD | ModD | 2 |
IPR006243 | 6,243 | Photosystem I PsaA | PSI_PsaA | Family | 16,407 | false | false | Photosystem I is a membrane complex found in the chloroplasts of plants and cyanobacteria. It uses light energy to transfer electrons from plastocyanin to ferredoxin [ ]. The core proteins of photosystem I are PsaA and PsaB, homologous integral membrane proteins that form a heterodimer that binds the electron-donating ... | [
"GO:0046872",
"GO:0015979",
"GO:0016020"
] | [
"metal ion binding",
"photosynthesis",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00458",
"TIGR01335"
] | [
"PSI_PsaA",
"psaA"
] | [
14221,
16405
] | 2 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC"
] | [
"1.97.1.12",
"GenProp0660",
"GenProp1353",
"PWY-101",
"PWY-8270"
] | [
"EC:1.97.1.12",
"GP:GenProp0660",
"GP:GenProp1353",
"METACYC:PWY-101",
"METACYC:PWY-8270"
] | 5 | [
"1jb0",
"2o01",
"2wsc",
"2wse",
"2wsf",
"3lw5",
"3pcq",
"4fe1",
"4kt0",
"4l6v",
"4rku",
"4xk8",
"4y28",
"5l8r",
"5oy0",
"5zf0",
"5zgb",
"5zgh",
"5zji",
"6fos",
"6hqb",
"6igz",
"6ijj",
"6ijo",
"6jeo",
"6jo5",
"6jo6",
"6k33",
"6k61",
"6kif",
"6kig",
"6kmw"... | 143 | [
"PUB00000583"
] | [
"3333014"
] | [
"Structure, function and organization of the Photosystem I reaction center complex."
] | [
1987
] | 1 | [
"IPR001280"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
407,
15996,
4
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
6,
4
] | 3 | true | Family | Photosystem I PsaA | Photosystem I PsaA | PSI_PsaA | 3 |
IPR006244 | 6,244 | Photosystem I PsaB | PSI_PsaB | Family | 15,759 | false | false | Photosystem I is a membrane complex found in the chloroplasts of plants and cyanobacteria. It uses light energy to transfer electrons from plastocyanin to ferredoxin [ ]. The core proteins of photosystem I are PsaA and PsaB, homologous integral membrane proteins that form a heterodimer that binds the electron-donating ... | [
"GO:0015979",
"GO:0009522",
"GO:0009579",
"GO:0016020"
] | [
"photosynthesis",
"photosystem I",
"thylakoid",
"membrane"
] | [
"biological_process",
"cellular_component",
"cellular_component",
"cellular_component"
] | 4 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00482",
"TIGR01336"
] | [
"PSI_PsaB",
"psaB"
] | [
14174,
15757
] | 2 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC"
] | [
"1.97.1.12",
"GenProp0660",
"GenProp1353",
"PWY-101",
"PWY-8270"
] | [
"EC:1.97.1.12",
"GP:GenProp0660",
"GP:GenProp1353",
"METACYC:PWY-101",
"METACYC:PWY-8270"
] | 5 | [
"1jb0",
"2o01",
"2wsc",
"2wse",
"2wsf",
"3lw5",
"3pcq",
"4fe1",
"4kt0",
"4l6v",
"4rku",
"4xk8",
"4y28",
"5l8r",
"5oy0",
"5zf0",
"5zgb",
"5zgh",
"5zji",
"6fos",
"6hqb",
"6igz",
"6ijj",
"6ijo",
"6jeo",
"6jo5",
"6jo6",
"6k33",
"6k61",
"6kif",
"6kig",
"6kmw"... | 143 | [
"PUB00000583"
] | [
"3333014"
] | [
"Structure, function and organization of the Photosystem I reaction center complex."
] | [
1987
] | 1 | [
"IPR001280"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
454,
15301,
4
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
5,
6,
3
] | 3 | true | Family | Photosystem I PsaB | Photosystem I PsaB | PSI_PsaB | 4 |
IPR006245 | 6,245 | Allophycocyanin, beta subunit | Allophycocyanin_b | Family | 1,176 | false | false | This family of sequences represents the allophycocyanin beta subunit. The alpha and beta subunits of allophycocyanin form heterodimers, six of which associate into larger aggregates as part of the phycobilisome, a light-harvesting complex of phycobiliproteins and linker proteins [ ]. Other homologous phyobiliproteins i... | [
"GO:0015979",
"GO:0030089"
] | [
"photosynthesis",
"phycobilisome"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"NCBIFAM",
"CDD"
] | [
"TIGR01337",
"cd12126"
] | [
"apcB",
"APC_beta"
] | [
1151,
1043
] | 2 | [] | [] | [] | 0 | [
"1all",
"1b33",
"1kn1",
"2v8a",
"2vjt",
"3dbj",
"3jbb",
"4f0u",
"4po5",
"4rmp",
"5tjf",
"5y6p",
"6kgx",
"6yx7",
"6yx8",
"7ext",
"7eyd",
"7ezx",
"7sc7",
"7sc9",
"7scb",
"7scc",
"7vea",
"7y4l",
"7y5e",
"7y7a",
"8imi",
"8imj",
"8imk",
"8or7",
"8to2",
"8tpj"... | 37 | [
"PUB00013183"
] | [
"10358042"
] | [
"Crystal structure of allophycocyanin from red algae Porphyra yezoensis at 2.2-A resolution."
] | [
1999
] | 1 | [
"IPR012128"
] | [] | 1 | 0 | 1 | [
"Cyanobacteriota",
"Eukaryota"
] | [
721,
455
] | 2 | [] | [] | 0 | true | Family | Allophycocyanin, beta subunit | Allophycocyanin, beta subunit | Allophycocyanin_b | 9 |
IPR006246 | 6,246 | Phycocyanin, alpha subunit | Phycocyanin_a | Family | 763 | false | false | This family represent the phycocyanin alpha subunit. Homologous phyobiliproteins of the phycobilisome include phycocyanin alpha chain and the allophycocyanin and phycoerythrin alpha and beta chains. Not included are the closely related phycoerythrocyanin alpha subunit sequences. Phycocyanin is the major phycobiliprotei... | [
"GO:0015979",
"GO:0030089"
] | [
"photosynthesis",
"phycobilisome"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01338"
] | [
"phycocy_alpha"
] | [
763
] | 1 | [] | [] | [] | 0 | [
"1cpc",
"1f99",
"1gh0",
"1ha7",
"1i7y",
"1jbo",
"1ktp",
"1on7",
"1phn",
"2bv8",
"2uul",
"2uum",
"2uun",
"3brp",
"3kvs",
"3l0f",
"3o18",
"3o2c",
"4f0t",
"4gxe",
"4gy3",
"4h0m",
"4l1e",
"4n6s",
"4q70",
"4yjj",
"4z8k",
"4ziz",
"5mjm",
"5mjp",
"5mjq",
"5o7m"... | 69 | [
"PUB00024819"
] | [
"11463658"
] | [
"Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobilisome."
] | [
2001
] | 1 | [
"IPR012128"
] | [] | 1 | 0 | 1 | [
"Cyanobacteriota",
"Eukaryota"
] | [
526,
237
] | 2 | [] | [] | 0 | true | Family | Phycocyanin, alpha subunit | Phycocyanin, alpha subunit | Phycocyanin_a | 1 |
IPR006247 | 6,247 | Phycocyanin, beta subunit | Phycocyanin_b | Family | 751 | false | false | These sequences describe the phycocyanin beta subunit. Other, homologous phycobiliproteins of the phycobilisome include phycocyanin beta chain and the allophycocyanin and phycoerythrin alpha and beta chains. Not included are the closely related phycoerythrocyanin beta subunit sequences. | [
"GO:0015979",
"GO:0030089"
] | [
"photosynthesis",
"phycobilisome"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01339"
] | [
"phycocy_beta"
] | [
751
] | 1 | [] | [] | [] | 0 | [
"1cpc",
"1f99",
"1gh0",
"1ha7",
"1i7y",
"1jbo",
"1ktp",
"1on7",
"1phn",
"2bv8",
"2uul",
"2uum",
"2uun",
"3brp",
"3kvs",
"3l0f",
"3o18",
"3o2c",
"4f0t",
"4gxe",
"4gy3",
"4h0m",
"4l1e",
"4n6s",
"4q70",
"4yjj",
"4z8k",
"4ziz",
"5mjm",
"5mjp",
"5mjq",
"5o7m"... | 69 | [] | [] | [] | [] | 0 | [
"IPR012128"
] | [] | 1 | 0 | 1 | [
"Cyanobacteriota",
"Eukaryota"
] | [
517,
234
] | 2 | [] | [] | 0 | true | Family | Phycocyanin, beta subunit | Phycocyanin, beta subunit | Phycocyanin_b | 8 |
IPR006248 | 6,248 | Aconitase, mitochondrial-like | Aconitase_mito-like | Family | 8,988 | false | false | This entry represents mitochondrial aconitase (mAcn), as well as close homologues such as certain bacterial aconitase A (AcnA) enzymes. It also includes Aco2, a fusion protein of aconitase and mitochondrial ribosomal protein bL21 that plays essential role in mitochondrial translation in fission yeast [ ]. Aconitase (ac... | [
"GO:0003994",
"GO:0051539",
"GO:0006099"
] | [
"aconitate hydratase activity",
"4 iron, 4 sulfur cluster binding",
"tricarboxylic acid cycle"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01340"
] | [
"aconitase_mito"
] | [
8988
] | 1 | [
"EC",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"4.2.1.3",
"GenProp0033",
"GenProp1693",
"R-BTA-71403",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-71403",
"R-CEL-9837999",
"R-CEL-9854311",
"R-DDI-71403",
"R-DDI-9837999",
"R-DDI-9854311",
"R-HSA-1268020",
"R-HSA-71403",
"R-HSA-9837999",
"R-HSA-9854311",
"R-MMU-71403",
"R-MMU-983799... | [
"EC:4.2.1.3",
"GP:GenProp0033",
"GP:GenProp1693",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-9837999",
"REACTOME:R-CEL-9854311",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DDI-9854311",
"REACTOME:R-HS... | 28 | [
"1aco",
"1ami",
"1amj",
"1b0j",
"1b0k",
"1b0m",
"1c96",
"1c97",
"1fgh",
"1nis",
"1nit",
"5acn",
"6acn",
"7acn",
"8acn"
] | 15 | [
"PUB00005471",
"PUB00036012",
"PUB00036013",
"PUB00036014",
"PUB00036015",
"PUB00036016",
"PUB00036017",
"PUB00036018",
"PUB00036019",
"PUB00036021",
"PUB00086540"
] | [
"9020582",
"16850017",
"10087914",
"15877277",
"17513696",
"15882410",
"15009904",
"17185597",
"16407072",
"15604397",
"25724335"
] | [
"The aconitase family: three structural variations on a common theme.",
"The role of iron regulatory proteins in mammalian iron homeostasis and disease.",
"Moonlighting proteins.",
"Single-gene disorders: what role could moonlighting enzymes play?",
"Evolution of the iron-responsive element.",
"Switching ... | [
1997,
2006,
1999,
2005,
2007,
2005,
2004,
2006,
2006,
2004,
2015
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
85,
2535,
6289,
79
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
1,
1,
2,
14,
1,
2,
4,
2,
2
] | 9 | true | Family | Aconitase, mitochondrial-like | Aconitase, mitochondrial-like | Aconitase_mito-like | 1 |
IPR006249 | 6,249 | Aconitase/Iron-responsive element-binding protein 2 | Aconitase/IRP2 | Family | 29,949 | false | false | This entry represents Aconitate hydratase A [ ] found predominantly in bacteria. Iron-responsive element-binding protein 2 [ ] and Cytoplasmic aconitate hydratase [ ] from animals; and Aconitate hydratase [ ] from plants also belong to this family. It also includes Phosphinomethylmalate isomerase (Pmi) involved in the ... | [] | [] | [] | 0 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR11670",
"TIGR01341"
] | [
"",
"aconitase_1"
] | [
29946,
20986
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.2.1.3",
"GenProp0033",
"GenProp1265",
"GenProp1687",
"R-CEL-389542",
"R-CEL-917937",
"R-DDI-389542",
"R-DDI-917937",
"R-HSA-389542",
"R-HSA-917937",
"R-MMU-389542",
"R-MMU-917937",
"R-RNO-389542",
"R-RNO-917937",
"R-SSC-917937",
"R-XTR-917937"
] | [
"EC:4.2.1.3",
"GP:GenProp0033",
"GP:GenProp1265",
"GP:GenProp1687",
"REACTOME:R-CEL-389542",
"REACTOME:R-CEL-917937",
"REACTOME:R-DDI-389542",
"REACTOME:R-DDI-917937",
"REACTOME:R-HSA-389542",
"REACTOME:R-HSA-917937",
"REACTOME:R-MMU-389542",
"REACTOME:R-MMU-917937",
"REACTOME:R-RNO-389542",... | 16 | [
"2b3x",
"2b3y",
"3sn2",
"3snp",
"6vcd"
] | 5 | [
"PUB00005471",
"PUB00036012",
"PUB00036013",
"PUB00036014",
"PUB00036015",
"PUB00036016",
"PUB00036017",
"PUB00036018",
"PUB00036019",
"PUB00036021",
"PUB00070783",
"PUB00070785",
"PUB00090961",
"PUB00100294",
"PUB00153759"
] | [
"9020582",
"16850017",
"10087914",
"15877277",
"17513696",
"15882410",
"15009904",
"17185597",
"16407072",
"15604397",
"8041788",
"7983023",
"28956599",
"25061985",
"11472937"
] | [
"The aconitase family: three structural variations on a common theme.",
"The role of iron regulatory proteins in mammalian iron homeostasis and disease.",
"Moonlighting proteins.",
"Single-gene disorders: what role could moonlighting enzymes play?",
"Evolution of the iron-responsive element.",
"Switching ... | [
1997,
2006,
1999,
2005,
2007,
2005,
2004,
2006,
2006,
2004,
1994,
1994,
2017,
2014,
2001
] | 15 | [] | [
"IPR012708"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
377,
22212,
6869,
491
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
17,
1,
4,
9,
1,
8,
6,
11,
11,
92
] | 10 | true | Family | Aconitase/Iron-responsive element-binding protein 2 | Aconitase/Iron-responsive element-binding protein 2 | Aconitase/IRP2 | 7 |
IPR006250 | 6,250 | Aconitase, putative | Aconitase_put | Family | 2,564 | false | false | Aconitase (aconitate hydratase; ) is an iron-sulphur protein that contains a [4Fe-4S]-cluster and catalyses the interconversion of isocitrate and citrate via a cis-aconitate intermediate. Aconitase functions in both the TCA and glyoxylate cycles, however unlike the majority of iron-sulphur proteins that function as ele... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01342"
] | [
"acon_putative"
] | [
2564
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005471",
"PUB00036012",
"PUB00036013",
"PUB00036014",
"PUB00036015",
"PUB00036016",
"PUB00036017",
"PUB00036018",
"PUB00036019",
"PUB00036021"
] | [
"9020582",
"16850017",
"10087914",
"15877277",
"17513696",
"15882410",
"15009904",
"17185597",
"16407072",
"15604397"
] | [
"The aconitase family: three structural variations on a common theme.",
"The role of iron regulatory proteins in mammalian iron homeostasis and disease.",
"Moonlighting proteins.",
"Single-gene disorders: what role could moonlighting enzymes play?",
"Evolution of the iron-responsive element.",
"Switching ... | [
1997,
2006,
1999,
2005,
2007,
2005,
2004,
2006,
2006,
2004
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Kipferlia bialata",
"metagenomes"
] | [
373,
2169,
1,
21
] | 4 | [] | [] | 0 | true | Family | Aconitase, putative | Aconitase, putative | Aconitase_put | 3 |
IPR006251 | 6,251 | Homoaconitase/3-isopropylmalate dehydratase, large subunit | Homoacnase/IPMdehydase_lsu | Family | 5,587 | false | false | This entry represents the large subunit of 3-isopropylmalate dehydratase (LeuC), as well as homoaconitase, certain aconitases and uncharacterised proteins. Homoaconitase, aconitase and 3-isopropylmalate dehydratase have similar overall structures and domain organisation [ ]. All are dehydratases that bind a [4Fe-4S]-cl... | [
"GO:0016836",
"GO:0051539",
"GO:0008652"
] | [
"hydro-lyase activity",
"4 iron, 4 sulfur cluster binding",
"amino acid biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01343"
] | [
"hacA_fam"
] | [
5587
] | 1 | [
"EC",
"GP"
] | [
"4.2.1.33",
"GenProp0193"
] | [
"EC:4.2.1.33",
"GP:GenProp0193"
] | 2 | [
"4kp1",
"4kp2",
"4nqy"
] | 3 | [
"PUB00005471",
"PUB00016210",
"PUB00032014",
"PUB00033924",
"PUB00036023",
"PUB00082326"
] | [
"9020582",
"9813279",
"15522288",
"1400210",
"16524361",
"20663849"
] | [
"The aconitase family: three structural variations on a common theme.",
"The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus.",
"Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specifici... | [
1997,
1998,
2004,
1992,
2006,
2010
] | 6 | [] | [
"IPR011826"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
825,
3978,
670,
114
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
2,
12
] | 3 | true | Family | Homoaconitase/3-isopropylmalate dehydratase, large subunit | Homoaconitase/3-isopropylmalate dehydratase, large subunit | Homoacnase/IPMdehydase_lsu | 4 |
IPR006252 | 6,252 | Malate synthase A | Malate_synthA | Family | 13,843 | false | false | This entry represents glyoxysomal malate synthases and one of two bacterial forms, designated malate synthase A. Malate synthase and isocitrate lyase are the two characteristic enzymes of the glyoxylate cycle. The glyoxylate cycle allows certain organisms, like plants and fungi, to derive their carbon requirements from... | [] | [] | [] | 0 | [
"PIRSF",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"PIRSF001363",
"PTHR42902",
"TIGR01344",
"cd00727"
] | [
"Malate_synth",
"",
"malate_syn_A",
"malate_synt_A"
] | [
11377,
13808,
11179,
11192
] | 4 | [
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.3.9",
"GenProp0023",
"GenProp1265",
"GenProp1722",
"PWY-7118",
"PWY-7294",
"PWY-7295",
"PWY-7854"
] | [
"EC:2.3.3.9",
"GP:GenProp0023",
"GP:GenProp1265",
"GP:GenProp1722",
"METACYC:PWY-7118",
"METACYC:PWY-7294",
"METACYC:PWY-7295",
"METACYC:PWY-7854"
] | 8 | [
"3cux",
"3cuz",
"3cv1",
"3cv2"
] | 4 | [
"PUB00080574",
"PUB00080575",
"PUB00163367"
] | [
"11252898",
"9891796",
"37043529"
] | [
"Krebs and his trinity of cycles.",
"Regulation of acetate metabolism by protein phosphorylation in enteric bacteria.",
"Identification of hidden associations among eukaryotic genes through statistical analysis of coevolutionary transitions."
] | [
2000,
1998,
2023
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermoproteati",
"metagenomes"
] | [
9009,
4697,
53,
84
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"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)",
"Zea mays"
] | [
6,
1,
1,
1,
1,
2,
2,
5
] | 8 | true | Family | Malate synthase A | Malate synthase A | Malate_synthA | 6 |
IPR006253 | 6,253 | Malate synthase G | Malate_synthG | Family | 8,421 | false | false | Malate synthase G (MSG, 723 residues) is an enzyme of the glyoxylate pathway, that catalyses the Claisen condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA [ , ]. This biochemical bypass is used by microorganisms (bacteria, yeast, and fungi) for biosynthesis u... | [
"GO:0004474",
"GO:0006097"
] | [
"malate synthase activity",
"glyoxylate cycle"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00641",
"PTHR42739",
"TIGR01345",
"cd00728"
] | [
"Malate_synth_G",
"",
"malate_syn_G",
"malate_synt_G"
] | [
7456,
8421,
7184,
3317
] | 4 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.3.9",
"GenProp0023",
"GenProp1556",
"PWY-7118",
"PWY-7294",
"PWY-7295",
"PWY-7854"
] | [
"EC:2.3.3.9",
"GP:GenProp0023",
"GP:GenProp1556",
"METACYC:PWY-7118",
"METACYC:PWY-7294",
"METACYC:PWY-7295",
"METACYC:PWY-7854"
] | 7 | [
"1d8c",
"1n8i",
"1n8w",
"1p7t",
"1y8b",
"2gq3",
"2jqx",
"3s9i",
"3s9z",
"3sad",
"3saz",
"3sb0",
"4ex4",
"5c7v",
"5c9r",
"5c9u",
"5c9w",
"5c9x",
"5cah",
"5cak",
"5cbb",
"5cbi",
"5cbj",
"5cc3",
"5cc5",
"5cc6",
"5cc7",
"5ccz",
"5cew",
"5cjm",
"5cjn",
"5drc"... | 60 | [
"PUB00014321",
"PUB00029759",
"PUB00033596",
"PUB00033597",
"PUB00033598",
"PUB00033599",
"PUB00048047",
"PUB00051135"
] | [
"10715138",
"12930982",
"13430766",
"10963578",
"10963599",
"11452311",
"18008171",
"18714089"
] | [
"Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications.",
"Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution.",
"Synthesis of cell constituents from ... | [
2000,
2003,
1957,
2000,
2000,
2001,
2008,
2008
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Marine Group I thaumarchaeote",
"unclassified sequences"
] | [
8122,
196,
1,
102
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Malate synthase G | Malate synthase G | Malate_synthG | 6 |
IPR006254 | 6,254 | Isocitrate lyase | Isocitrate_lyase | Family | 17,273 | false | false | Isocitrate lyase ( ) [ , ] is an enzyme that catalyzes the conversion of isocitrate to succinate and glyoxylate. This is the first step in the glyoxylate bypass, an alternative to the tricarboxylic acid cycle (also known as the TCA cycle) in bacteria, fungi and plants. A cysteine, a histidine and a glutamate or asparta... | [
"GO:0004451",
"GO:0019752"
] | [
"isocitrate lyase activity",
"carboxylic acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"PF00463",
"PIRSF001362",
"PTHR21631",
"TIGR01346"
] | [
"ICL",
"Isocit_lyase",
"",
"isocit_lyase"
] | [
17209,
15819,
17124,
13489
] | 4 | [
"EC",
"GP",
"GP"
] | [
"4.1.3.1",
"GenProp0023",
"GenProp1265"
] | [
"EC:4.1.3.1",
"GP:GenProp0023",
"GP:GenProp1265"
] | 3 | [
"1dqu",
"1f61",
"1f8i",
"1f8m",
"1igw",
"3e5b",
"3eol",
"3i4e",
"3lg3",
"3oq8",
"3p0x",
"5dql",
"5e9f",
"5e9g",
"5e9h",
"6c4a",
"6c4c",
"6edw",
"6edz",
"6ee1",
"6g1o",
"6lrp",
"6lrt",
"6vb9",
"6wsi",
"6xpp",
"7cmx",
"7cmy",
"7cp1",
"7ebc",
"7ebe",
"7ebf"... | 35 | [
"PUB00002339",
"PUB00005064",
"PUB00100290",
"PUB00100291"
] | [
"2361956",
"2696959",
"11092862",
"11422389"
] | [
"Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida tropicalis: gene analysis and characterization.",
"High sequence conservation between isocitrate lyase from Escherichia coli and Ricinus communis.",
"The Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-methylisocitrate lyase i... | [
1990,
1989,
2000,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
62,
12085,
4989,
135,
2
] | 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",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / AT... | [
4,
1,
1,
2,
4,
2,
1,
8
] | 8 | true | Family | Isocitrate lyase | Isocitrate lyase | Isocitrate_lyase | 2 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.