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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR015835 | 15,835 | Hydroxymethyl pyrimidine (HMP)/thiamine binding protein | HMP/thiamine-bd | Family | 495 | false | false | This group represents putative hydroxymethyl pyrimidine (HMP)/thiamine binding protein YkoF. It is part of the ABC transporter complex YkoCDEF that could transport HMP and/or thiamine. YkoF binds thiamine via its HMP moiety [ ]. | [
"GO:0030975"
] | [
"thiamine binding"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF021331"
] | [
"YkoF"
] | [
495
] | 1 | [] | [] | [] | 0 | [
"1s7h",
"1s99",
"1sbr"
] | 3 | [
"PUB00027817"
] | [
"15451668"
] | [
"The structure and ligand binding properties of the B. subtilis YkoF gene product, a member of a novel family of thiamin/HMP-binding proteins."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
489,
6
] | 2 | [] | [] | 0 | true | Family | Hydroxymethyl pyrimidine (HMP)/thiamine binding protein | Hydroxymethyl pyrimidine (HMP)/thiamine binding protein | HMP/thiamine-bd | 6 |
IPR015837 | 15,837 | Uncharacterised conserved protein UCP026622, CAAX protease-type | UCP026622_CAAX_protease | Family | 1,435 | false | false | This group represents a predicted uncharacterised protein with CAAX amino terminal protease domain. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF026622"
] | [
"Proteas_026622"
] | [
1435
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Actinomycetota",
"ecological metagenomes"
] | [
1416,
19
] | 2 | [] | [] | 0 | true | Family | Uncharacterised conserved protein UCP026622, CAAX protease-type | Uncharacterised conserved protein UCP026622, CAAX protease-type | UCP026622_CAAX_protease | 4 |
IPR015838 | 15,838 | Uncharacterised conserved protein UCP027923, rubrerythrin-type | UCP027923_rubrerythrin | Family | 5 | false | false | This group represents an uncharacterised protein with rubrerythrin domain. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF027923"
] | [
"Rubrer_027923"
] | [
5
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
5
] | 1 | [] | [] | 0 | true | Family | Uncharacterised conserved protein UCP027923, rubrerythrin-type | Uncharacterised conserved protein UCP027923, rubrerythrin-type | UCP027923_rubrerythrin | 5 |
IPR015839 | 15,839 | Bifunctional chloromethane dehalogenation methyltransferase corrinoid-binding protein CmuA | CmuA | Family | 19 | false | false | The pathway of chloromethane utilization, which allows the microorganisms that possess it to grow with chloromethane as the sole carbon and energy source, is believed to be initiated by a corrinoid-dependent methyltransferase system involving methyltransferase I (CmuA) and methyltransferase II (CmuB), which transfer th... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036688"
] | [
"CmuA"
] | [
19
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016918",
"PUB00016919",
"PUB00016920"
] | [
"10200311",
"10447694",
"11358510"
] | [
"A corrinoid-dependent catabolic pathway for growth of a Methylobacterium strain with chloromethane.",
"Properties of the methylcobalamin:H4folate methyltransferase involved in chloromethane utilization by Methylobacterium sp. strain CM4.",
"Chloromethane: tetrahydrofolate methyl transfer by two proteins from M... | [
1999,
1999,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
19
] | 1 | [] | [] | 0 | true | Family | Bifunctional chloromethane dehalogenation methyltransferase corrinoid-binding protein CmuA | Bifunctional chloromethane dehalogenation methyltransferase corrinoid-binding protein CmuA | CmuA | 6 |
IPR015840 | 15,840 | DNA methyase, ParB domain-containing | DNA_MeTrfase_ParB | Family | 3,081 | false | false | This group represents an adenine methyltransferase with ParB-like nuclease domain. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036758"
] | [
"Aden_M_ParB"
] | [
3081
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"Opisthokonta",
"Viruses",
"metagenomes"
] | [
2830,
12,
5,
173,
61
] | 5 | [] | [] | 0 | true | Family | DNA methyase, ParB domain-containing | DNA methyase, ParB domain-containing | DNA_MeTrfase_ParB | 5 |
IPR015841 | 15,841 | RNA-directed RNA polymerase, tospovirus | RNA-dir_pol_tospovirus | Family | 188 | false | false | RNA-directed RNA polymerase (RdRp) ( ) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage [ , ]. It catalyses synthesis of the RNA strand complementary to a given RNA template, but the precise molecular mechanism remains unclear. The postulated RNA replication process is a tw... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036872"
] | [
"L_TospoV"
] | [
188
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009392",
"PUB00030617",
"PUB00033622",
"PUB00033623",
"PUB00033624",
"PUB00033625"
] | [
"9878607",
"9309225",
"2759231",
"8709232",
"11531403",
"10827187"
] | [
"Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure.",
"Structure of the RNA-dependent RNA polymerase of poliovirus.",
"Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relat... | [
1998,
1997,
1989,
1996,
2001,
2000
] | 6 | [] | [] | 0 | 0 | null | [
"Elliovirales"
] | [
188
] | 1 | [] | [] | 0 | true | Family | RNA-directed RNA polymerase, tospovirus | RNA-directed RNA polymerase, tospovirus | RNA-dir_pol_tospovirus | 7 |
IPR015842 | 15,842 | RNA-directed RNA polymerase, tenuivirus | RNA-dir_pol_tenuivirus | Family | 37 | false | false | RNA-directed RNA polymerase (RdRp) ( ) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage [ , ]. It catalyses synthesis of the RNA strand complementary to a given RNA template, but the precise molecular mechanism remains unclear. The postulated RNA replication process is a tw... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036873"
] | [
"L_TenuV"
] | [
37
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009392",
"PUB00030617",
"PUB00033622",
"PUB00033623",
"PUB00033624",
"PUB00033625",
"PUB00101107",
"PUB00101108"
] | [
"9878607",
"9309225",
"2759231",
"8709232",
"11531403",
"10827187",
"30439393",
"31948728"
] | [
"Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure.",
"Structure of the RNA-dependent RNA polymerase of poliovirus.",
"Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relat... | [
1998,
1997,
1989,
1996,
2001,
2000,
2019,
2020
] | 8 | [] | [] | 0 | 0 | null | [
"Tenuivirus"
] | [
37
] | 1 | [] | [] | 0 | true | Family | RNA-directed RNA polymerase, tenuivirus | RNA-directed RNA polymerase, tenuivirus | RNA-dir_pol_tenuivirus | 7 |
IPR015843 | 15,843 | RNA-directed RNA polymerase, nairovirus | RNA-dir_pol_nairovirus | Family | 200 | false | false | RNA-directed RNA polymerase (RdRp) ( ) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage [ , ]. It catalyses synthesis of the RNA strand complementary to a given RNA template, but the precise molecular mechanism remains unclear. The postulated RNA replication process is a tw... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036900"
] | [
"RdRPol_NRV"
] | [
200
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009392",
"PUB00030617",
"PUB00033622",
"PUB00033623",
"PUB00033624",
"PUB00033625"
] | [
"9878607",
"9309225",
"2759231",
"8709232",
"11531403",
"10827187"
] | [
"Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure.",
"Structure of the RNA-dependent RNA polymerase of poliovirus.",
"Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relat... | [
1998,
1997,
1989,
1996,
2001,
2000
] | 6 | [] | [] | 0 | 0 | null | [
"Orthonairovirus"
] | [
200
] | 1 | [] | [] | 0 | true | Family | RNA-directed RNA polymerase, nairovirus | RNA-directed RNA polymerase, nairovirus | RNA-dir_pol_nairovirus | 6 |
IPR015844 | 15,844 | Pantothenate kinase, acetyl-CoA regulated, two-domain type | PanK_long | Family | 1,469 | false | false | Pantothenate kinase (PanK, ) catalyses the conversion of CAATP and pantothenate to ADP and D-4'-phosphopantothenate, the key regulatory step in the biosynthesis of coenzyme A (CoA) [ ]. Members in this entry represents a two-domain form with an additional C-terminal domain of unknown function. This type of pantothenate... | [
"GO:0004594",
"GO:0015937"
] | [
"pantothenate kinase activity",
"coenzyme A biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF036939"
] | [
"PanK_long"
] | [
1469
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"3.1.3.-",
"PWY-4702",
"PWY-5491",
"PWY-6148",
"PWY-6352",
"PWY-6365",
"PWY-6366",
"PWY-6368",
"PWY-6456",
"PWY-6575",
"PWY-6627",
"PWY-6664",
"PWY-6686",
"PWY-6720",
"PWY-6724",
"PWY-6955",
"PWY-6990",
"PWY-6991",
"PWY-7018",
"PWY-7119",
"PWY-7321",
"PWY-7531",
"PWY-7771... | [
"EC:3.1.3.-",
"METACYC:PWY-4702",
"METACYC:PWY-5491",
"METACYC:PWY-6148",
"METACYC:PWY-6352",
"METACYC:PWY-6365",
"METACYC:PWY-6366",
"METACYC:PWY-6368",
"METACYC:PWY-6456",
"METACYC:PWY-6575",
"METACYC:PWY-6627",
"METACYC:PWY-6664",
"METACYC:PWY-6686",
"METACYC:PWY-6720",
"METACYC:PWY-6... | 39 | [] | 0 | [
"PUB00015016",
"PUB00015017",
"PUB00015018",
"PUB00027731"
] | [
"11238410",
"12760898",
"9890959",
"11479594"
] | [
"fumble encodes a pantothenate kinase homolog required for proper mitosis and meiosis in Drosophila melanogaster.",
"Inhibitors of pantothenate kinase: novel antibiotics for staphylococcal infections.",
"Cloning and characterization of a eukaryotic pantothenate kinase gene (panK) from Aspergillus nidulans.",
... | [
2001,
2003,
1999,
2001
] | 4 | [
"IPR004567"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
1469
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
5,
4,
1,
2,
4,
1
] | 8 | true | Family | Pantothenate kinase, acetyl-CoA regulated, two-domain type | Pantothenate kinase, acetyl-CoA regulated, two-domain type | PanK_long | 2 |
IPR015845 | 15,845 | Agropine synthesis reductase | Mas1 | Family | 23 | false | false | Several agrobacteria cause neoplastic diseases in plants, including crown gall disease (Agrobacterium tumefaciens) and hairy root disease (Agrobacterium rhizogenes). The mechanism involves transfer via infective plasmids and subsequent expression of both oncogenes and genes for the synthesis of opines, which can be spe... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF036951"
] | [
"Mas1"
] | [
23
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00027843",
"PUB00027844",
"PUB00027926",
"PUB00027978"
] | [
"11743194",
"11743193",
"12927971",
"1909028"
] | [
"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58.",
"The genome of the natural genetic engineer Agrobacterium tumefaciens C58.",
"Agrobacterium tumefaciens as an agent of disease.",
"Agrobacterium rhizogenes pRi8196 T-DNA: mapping and DNA sequence of functions invol... | [
2001,
2001,
2003,
1991
] | 4 | [
"IPR013078"
] | [] | 1 | 0 | 1 | [
"Rhizobium/Agrobacterium group"
] | [
23
] | 1 | [] | [] | 0 | true | Family | Agropine synthesis reductase | Agropine synthesis reductase | Mas1 | 7 |
IPR015847 | 15,847 | Exoribonuclease, phosphorolytic domain 2 | ExoRNase_PH_dom2 | Domain | 59,002 | false | false | This entry represents the phosphorolytic (PH) domain 2, which has a core 3-layer α/β/α structure. This domain is found in bacterial/organelle PNPases and in archaeal/eukaryotic exosomes [ ]. The PH (phosphorolytic) domain is responsible for 3'-5' exoribonuclease activity, although in some proteins this domain has lost ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03725"
] | [
"RNase_PH_C"
] | [
59002
] | 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",
"R-BTA-429958",
"R-BTA-450385",
"R-BTA-450513",
"R-BTA-450604",
"R-BTA-6791226",
"R-BTA-9930044",
"R-CEL-429958",
"R-CEL-450385",
"R-CEL-450513",
"R-CEL-6791226",
"R-CEL-9930044",
"R-DDI-429958",
"R-DDI-450385",
"R-DDI-450513",
"R-DDI-6791226",
"R-HSA-380994",
"R-HSA-42995... | [
"EC:2.7.7",
"REACTOME:R-BTA-429958",
"REACTOME:R-BTA-450385",
"REACTOME:R-BTA-450513",
"REACTOME:R-BTA-450604",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-9930044",
"REACTOME:R-CEL-429958",
"REACTOME:R-CEL-450385",
"REACTOME:R-CEL-450513",
"REACTOME:R-CEL-6791226",
"REACTOME:R-CEL-9930044",
"... | 42 | [
"1oyp",
"1oyr",
"1oys",
"1r6l",
"1r6m",
"1udn",
"1udo",
"1udq",
"1uds",
"2ba0",
"2ba1",
"2br2",
"2c37",
"2c38",
"2c39",
"2je6",
"2jea",
"2jeb",
"2nn6",
"2pnz",
"2po0",
"2po1",
"2po2",
"2wnr",
"2wp8",
"3b4t",
"3cdi",
"3cdj",
"3dd6",
"3gcm",
"3gll",
"3gme"... | 85 | [
"PUB00000954",
"PUB00035567",
"PUB00035568",
"PUB00035569",
"PUB00035570",
"PUB00035571",
"PUB00035572"
] | [
"9390555",
"17084501",
"15951817",
"17174896",
"16285927",
"16713559",
"17380186"
] | [
"The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases.",
"Genetic analysis of polynucleotide phosphorylase structure and functions.",
"The archaeal exosome core is a hexameric ring structure with three catalytic subunits.",
"Reconstitution, activities, and st... | [
1997,
2007,
2005,
2006,
2005,
2006,
2007
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Myoviridae sp. ct2798",
"unclassified sequences"
] | [
1046,
38219,
18904,
1,
832
] | 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",... | [
31,
5,
6,
8,
2,
21,
21,
1,
22,
28,
3,
3,
71
] | 13 | true | Domain | Exoribonuclease, phosphorolytic domain 2 | Exoribonuclease, phosphorolytic domain 2 | ExoRNase_PH_dom2 | 6 |
IPR015848 | 15,848 | Polyribonucleotide nucleotidyltransferase, RNA-binding domain | PNPase_PH_RNA-bd_bac/org-type | Domain | 26,649 | false | false | The PH (phosphorolytic) domain is responsible for 3'-5' exoribonuclease activity, although in some proteins this domain has lost its catalytic function. An active PH domain uses inorganic phosphate as a nucleophile, adding it across the phosphodiester bond between the end two nucleotides in order to release ribonucleos... | [
"GO:0003723",
"GO:0006396"
] | [
"RNA binding",
"RNA processing"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF03726"
] | [
"PNPase"
] | [
26649
] | 1 | [
"EC",
"REACTOME"
] | [
"2.7.7.8",
"R-HSA-9836573"
] | [
"EC:2.7.7.8",
"REACTOME:R-HSA-9836573"
] | 2 | [
"1e3h",
"1e3p",
"1whu",
"3cdi",
"3cdj",
"3gcm",
"3gll",
"3gme",
"3h1c",
"3h36",
"3u1k",
"4aid",
"4aim",
"4am3",
"4nbq",
"5xex",
"5yjj",
"5zf6",
"6d6k",
"7ld5",
"7ogk",
"7ogl",
"7ogm",
"8vah",
"8vak",
"8wwp",
"8wx0",
"8wxf",
"8zaw",
"9gms",
"9gmt",
"9ibh"... | 36 | [
"PUB00035567",
"PUB00035568",
"PUB00035569",
"PUB00035570",
"PUB00035571",
"PUB00035572"
] | [
"17084501",
"15951817",
"17174896",
"16285927",
"16713559",
"17380186"
] | [
"Genetic analysis of polynucleotide phosphorylase structure and functions.",
"The archaeal exosome core is a hexameric ring structure with three catalytic subunits.",
"Reconstitution, activities, and structure of the eukaryotic RNA exosome.",
"Structural framework for the mechanism of archaeal exosomes in RNA... | [
2007,
2005,
2006,
2005,
2006,
2007
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured marine thaumarchaeote KM3_46_G10"
] | [
23961,
2277,
410,
1
] | 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"
] | [
3,
1,
1,
4,
1,
1,
4,
2,
3,
4
] | 10 | true | Domain | Polyribonucleotide nucleotidyltransferase, RNA-binding domain | Polyribonucleotide nucleotidyltransferase, RNA-binding domain | PNPase_PH_RNA-bd_bac/org-type | 9 |
IPR015849 | 15,849 | Amyloidogenic glycoprotein, heparin-binding | Amyloid_glyco_heparin-bd | Domain | 6,758 | false | false | Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [ , , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with D... | [
"GO:0008201"
] | [
"heparin binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02177"
] | [
"APP_N"
] | [
6758
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-114608",
"R-CEL-3000178",
"R-CEL-381426",
"R-CEL-416476",
"R-CEL-8957275",
"R-CEL-9609523",
"R-DME-114608",
"R-DME-3000178",
"R-DME-381426",
"R-DME-416476",
"R-DME-8957275",
"R-DME-9609523",
"R-DME-9837999",
"R-HSA-114608",
"R-HSA-3000178",
"R-HSA-381426",
"R-HSA-416476",
"R... | [
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-3000178",
"REACTOME:R-CEL-381426",
"REACTOME:R-CEL-416476",
"REACTOME:R-CEL-8957275",
"REACTOME:R-CEL-9609523",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-3000178",
"REACTOME:R-DME-381426",
"REACTOME:R-DME-416476",
"REACTOME:R-DME-8957275",
"REACTOME:R-DM... | 67 | [
"1mwp",
"3ktm",
"4jfn",
"4pqd",
"4pwq",
"7mqy",
"7mrk",
"7mrm",
"7mrn",
"7mrs",
"8kew",
"8kf1",
"8kf3",
"8kf4",
"8kf5",
"8kf6",
"8otf"
] | 17 | [
"PUB00027475",
"PUB00029624",
"PUB00033916",
"PUB00033917",
"PUB00033918",
"PUB00099232",
"PUB00099233"
] | [
"10201399",
"12611883",
"16301322",
"16406235",
"16364896",
"28713158",
"33302541"
] | [
"Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein.",
"Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis.",
"Structural changes of region 1-16 of the Alzheimer disease amyloid beta-... | [
1999,
2003,
2006,
2006,
2005,
2017,
2020
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eumetazoa",
"marine sediment metagenome"
] | [
2,
6755,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
16,
6,
23,
22,
16
] | 6 | true | Domain | Amyloidogenic glycoprotein, heparin-binding | Amyloidogenic glycoprotein, heparin-binding | Amyloid_glyco_heparin-bd | 2 |
IPR015853 | 15,853 | ABC transporter, ferric cation import, FbpC | ABC_transpr_FbpC | Domain | 20,181 | false | false | ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily, which uses the hydrolysis of ATP to energise diverse biological systems. ABC transporters minimally consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These can be found o... | [
"GO:0005524",
"GO:0015408",
"GO:0006826",
"GO:0016020"
] | [
"ATP binding",
"ABC-type ferric iron transporter activity",
"iron ion transport",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"CDD"
] | [
"cd03259"
] | [
"ABC_Carb_Solutes_like"
] | [
20181
] | 1 | [
"EC",
"PROSITEDOC"
] | [
"7.2.2.7",
"PDOC51237"
] | [
"EC:7.2.2.7",
"PROSITEDOC:PDOC51237"
] | 2 | [
"1oxs",
"1oxt",
"1oxu",
"1oxv",
"1oxx",
"3fvq",
"9j4r"
] | 7 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00035601",
"PUB00043654",
"PUB00060285"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"8606197",
"11421270",
"10338533"
] | [
"Crystal structure of the ATP-binding subunit of an ABC transporter.",
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"ABC transporters: physiology, structure and mechanism--an overview.",
"ABC transporters: from microorgani... | [
1998,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
1996,
2001,
1999
] | 13 | [
"IPR003439"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
432,
19414,
48,
287
] | 4 | [] | [] | 0 | true | Domain | ABC transporter, ferric cation import, FbpC | ABC transporter, ferric cation import, FbpC | ABC_transpr_FbpC | 9 |
IPR015854 | 15,854 | ABC transporter, lipoprotein release, LolD-like | ABC_transpr_LolD-like | Family | 124,982 | false | false | LolD is part of the LolCDE complex. LolCDE is an ATP-binding cassette (ABC) transporter, releasing lipoproteins from the inner membrane of Escherichia coli, thereby initiating lipoprotein sorting to the outer membrane. The LolCDE complex is composed of two copies of an ATPase subunit, LolD, and one copy each of integra... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR24220"
] | [
""
] | [
124982
] | 1 | [
"EC",
"PROSITEDOC"
] | [
"7.6.2.-",
"PDOC51237"
] | [
"EC:7.6.2.-",
"PROSITEDOC:PDOC51237"
] | 2 | [
"1f3o",
"1l2t",
"3tif",
"5lj9",
"5lja",
"6z4w",
"6z63",
"6z67",
"7arh",
"7ari",
"7arj",
"7ark",
"7arl",
"7arm",
"7mdx",
"7mdy",
"7v8i",
"7v8l",
"7v8m",
"7w78",
"7w79",
"7w7a",
"7w7b",
"7w7c",
"7w7d",
"8hd0",
"8i6o",
"8i6q",
"8i6r",
"8i6s",
"8idb",
"8idc"... | 48 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00035602",
"PUB00035603",
"PUB00043654"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"16585747",
"11844772",
"11421270"
] | [
"Crystal structure of the ATP-binding subunit of an ABC transporter.",
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"ABC transporters: physiology, structure and mechanism--an overview.",
"ABC transporters: from microorgani... | [
1998,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
2006,
2002,
2001
] | 13 | [] | [
"IPR005286"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2022,
120659,
553,
9,
1739
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | ABC transporter, lipoprotein release, LolD-like | ABC transporter, lipoprotein release, LolD-like | ABC_transpr_LolD-like | 9 |
IPR015855 | 15,855 | ABC transporter, maltose/maltodextrin import, MalK-like | ABC_transpr_MalK-like | Domain | 51,496 | false | false | This is the ATP-binding domain found at the N terminus of MalK and closely related ATP-binding subunits of ABC transporter complexes, such as UgpC, SugC, LacK [ , , ]. MalK is part of the ABC transporter complex involved in maltose/maltodextrin import. The complex is composed of two ATP-binding proteins (MalK), two tra... | [
"GO:0005524",
"GO:0140359",
"GO:0008643"
] | [
"ATP binding",
"ABC-type transporter activity",
"carbohydrate transport"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"CDD"
] | [
"cd03301"
] | [
"ABC_MalK_N"
] | [
51496
] | 1 | [
"EC",
"GP",
"GP",
"PROSITEDOC"
] | [
"7.6.2.10",
"GenProp1159",
"GenProp1204",
"PDOC51237"
] | [
"EC:7.6.2.10",
"GP:GenProp1159",
"GP:GenProp1204",
"PROSITEDOC:PDOC51237"
] | 4 | [
"1g29",
"1q12",
"1q1b",
"1q1e",
"1v43",
"1vci",
"2awn",
"2awo",
"2d62",
"2it1",
"2r6g",
"3fh6",
"3puv",
"3puw",
"3pux",
"3puy",
"3puz",
"3pv0",
"3rlf",
"4jbw",
"4khz",
"4ki0",
"4tqu",
"4tqv",
"4xig",
"4xtc",
"6yir",
"7cad",
"7cae",
"7caf",
"7cag",
"7x0q"... | 41 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00035604",
"PUB00035605",
"PUB00035606",
"PUB00043654",
"PUB00049270",
"PUB00071820",
"PUB00150993",
"PUB00150994"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"12180984",
"9765559",
"10671470",
"11421270",
"18033289",
"23013274",
"32092417",
"30089751"
] | [
"Crystal structure of the ATP-binding subunit of an ABC transporter.",
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"ABC transporters: physiology, structure and mechanism--an overview.",
"ABC transporters: from microorgani... | [
1998,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
2002,
1998,
2000,
2001,
2007,
2012,
2020,
2018
] | 18 | [
"IPR003439"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1785,
49361,
41,
309
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | ABC transporter, maltose/maltodextrin import, MalK-like | ABC transporter, maltose/maltodextrin import, MalK-like | ABC_transpr_MalK-like | 6 |
IPR015856 | 15,856 | ABC transporter, CbiO/EcfA subunit | ABC_transpr_CbiO/EcfA_su | Domain | 49,009 | false | false | This entry represents a domain found in the energy-coupling factor transporter ATP-binding proteins CbiO (from the CbiMNOQ complex, involved in cobalt import) and EcfA (from the common ECF ABC-transporter complex) [ ]. | [
"GO:0005524",
"GO:0055085",
"GO:0016020"
] | [
"ATP binding",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"CDD"
] | [
"cd03225"
] | [
"ABC_cobalt_CbiO_domain1"
] | [
49009
] | 1 | [
"PROSITEDOC"
] | [
"PDOC51237"
] | [
"PROSITEDOC:PDOC51237"
] | 1 | [
"2ihy",
"2yz2",
"3gfo",
"4hlu",
"4huq",
"4hzu",
"4mki",
"4rfs",
"4zir",
"5d3m",
"5jsz",
"5x3x",
"5x40",
"5x41",
"6fnp",
"6zg3",
"7nnt",
"7nnu",
"8bmp",
"8bmq",
"8bmr",
"8bms",
"9kym"
] | 23 | [
"PUB00087412"
] | [
"28322252"
] | [
"Structure and mechanism of a group-I cobalt energy coupling factor transporter."
] | [
2017
] | 1 | [
"IPR003439"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
1990,
45139,
1278,
3,
599
] | 5 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
5,
13
] | 3 | true | Domain | ABC transporter, CbiO/EcfA subunit | ABC transporter, CbiO/EcfA subunit | ABC_transpr_CbiO/EcfA_su | 7 |
IPR015860 | 15,860 | ABC transporter, teichoic acids export TagH-like | ABC_transpr_TagH-like | Domain | 21,807 | false | false | This entry contains the ATP-binding subunit, TagH, of the ABC transporter complex involved in the export of teichoic acids. The Bacillus subtilis complex is composed of two ATP-binding proteins (TagH) and two transmembrane proteins (TagG) [ ]. Protein containing this domain also include KpsT, which is involved with the... | [
"GO:0005524",
"GO:0140359",
"GO:0016020"
] | [
"ATP binding",
"ABC-type transporter activity",
"membrane"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"CDD"
] | [
"cd03220"
] | [
"ABC_KpsT_Wzt"
] | [
21807
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"7.5.2.4",
"PWY-7815",
"PWY-7816",
"PWY-7819",
"PDOC51237"
] | [
"EC:7.5.2.4",
"METACYC:PWY-7815",
"METACYC:PWY-7816",
"METACYC:PWY-7819",
"PROSITEDOC:PDOC51237"
] | 5 | [
"6amx",
"6an5",
"6jbh",
"6m96",
"6oih",
"7dd0",
"7k2t",
"8dku",
"8dl0",
"8dn8",
"8dnc",
"8dne",
"8dou",
"8tsh",
"8tsi",
"8tsl",
"8tsw",
"8tt3",
"8tun",
"9cfl",
"9cfp",
"9mhd",
"9mhu",
"9mhz"
] | 24 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00035610",
"PUB00043654",
"PUB00097513"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"7565096",
"11421270",
"8051103"
] | [
"Crystal structure of the ATP-binding subunit of an ABC transporter.",
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"ABC transporters: physiology, structure and mechanism--an overview.",
"ABC transporters: from microorgani... | [
1998,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
1995,
2001,
1994
] | 13 | [
"IPR003439"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
152,
21277,
20,
358
] | 4 | [] | [] | 0 | true | Domain | ABC transporter, teichoic acids export TagH-like | ABC transporter, teichoic acids export TagH-like | ABC_transpr_TagH-like | 5 |
IPR015864 | 15,864 | FAD synthetase | FAD_synthase | Domain | 26,720 | false | false | Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase ( ), which converts it into FMN, and FAD synthetase ( ), which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out b... | [
"GO:0003919",
"GO:0009231"
] | [
"FMN adenylyltransferase activity",
"riboflavin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"CDD"
] | [
"PF06574",
"cd02064"
] | [
"FAD_syn",
"FAD_synthetase_N"
] | [
26714,
25448
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.1.26",
"2.7.7.2",
"PWY-5523",
"PWY-6167",
"PWY-6168",
"PWY-7863"
] | [
"EC:2.7.1.26",
"EC:2.7.7.2",
"METACYC:PWY-5523",
"METACYC:PWY-6167",
"METACYC:PWY-6168",
"METACYC:PWY-7863"
] | 6 | [
"1mrz",
"1s4m",
"1t6x",
"1t6y",
"1t6z",
"2i1l",
"2x0k",
"3op1",
"3zug",
"4uze",
"4uzf",
"5fnz",
"5fo0",
"5fo1"
] | 14 | [
"PUB00010127",
"PUB00030175",
"PUB00035657"
] | [
"12517446",
"14580199",
"17049878"
] | [
"A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer.",
"Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism.",
"Over-expression in Escherichia coli, purification and characterization of isoform 2 ... | [
2003,
2003,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermococcus litoralis",
"unclassified sequences"
] | [
25411,
730,
1,
578
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
15,
1,
2,
3
] | 4 | true | Domain | FAD synthetase | FAD synthetase | FAD_synthase | 5 |
IPR015865 | 15,865 | Riboflavin kinase domain, bacterial/eukaryotic | Riboflavin_kinase_bac/euk | Domain | 31,347 | false | false | This entry represents the riboflavin kinase domains from bacteria and eukaryotes. Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase ( ), which converts it into FMN, and FAD synthetase ( ), which adenylates FMN to FAD. Eukaryotes usually have two separate enzym... | [
"GO:0008531",
"GO:0009398"
] | [
"riboflavin kinase activity",
"FMN biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF01687",
"SM00904"
] | [
"Flavokinase",
"Flavokinase"
] | [
31333,
30889
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.26",
"GenProp1764",
"PWY-5523",
"PWY-6168",
"PWY-7863",
"R-DME-196843",
"R-HSA-196843",
"R-MMU-196843",
"R-SCE-196843",
"R-SPO-196843"
] | [
"EC:2.7.1.26",
"GP:GenProp1764",
"METACYC:PWY-5523",
"METACYC:PWY-6168",
"METACYC:PWY-7863",
"REACTOME:R-DME-196843",
"REACTOME:R-HSA-196843",
"REACTOME:R-MMU-196843",
"REACTOME:R-SCE-196843",
"REACTOME:R-SPO-196843"
] | 10 | [
"1mrz",
"1n05",
"1n06",
"1n07",
"1n08",
"1nb0",
"1nb9",
"1p4m",
"1q9s",
"1s4m",
"1t6x",
"1t6y",
"1t6z",
"2i1l",
"2x0k",
"3bnw",
"3op1",
"3zug",
"4uze",
"4uzf",
"5a88",
"5a89",
"5a8a",
"5fnz",
"5fo0",
"5fo1"
] | 26 | [
"PUB00010127",
"PUB00030175",
"PUB00035657"
] | [
"12517446",
"14580199",
"17049878"
] | [
"A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer.",
"Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism.",
"Over-expression in Escherichia coli, purification and characterization of isoform 2 ... | [
2003,
2003,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
25166,
5593,
5,
583
] | 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",... | [
4,
1,
1,
2,
1,
3,
1,
2,
5,
4,
1,
1,
16
] | 13 | true | Domain | Riboflavin kinase domain, bacterial/eukaryotic | Riboflavin kinase domain, bacterial/eukaryotic | Riboflavin_kinase_bac/euk | 6 |
IPR015866 | 15,866 | Serine-tRNA synthetase, type1, N-terminal | Ser-tRNA-synth_1_N | Domain | 34,993 | false | false | This entry represents the N-terminal domain of Serine-tRNA synthetase, which consists of two helices in a long α-hairpin and corresponds to the tRNA binding domain. Serine-tRNA synthetase ( ) exists as monomer and belongs to class IIa aminoacyl-tRNA synthetase [ ]. Aminoacyl-tRNA synthetases (also known as aminoacyl-tR... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02403"
] | [
"Seryl_tRNA_N"
] | [
34993
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME"
] | [
"6.1.1.11",
"PWY-6281",
"R-HSA-2408557",
"R-HSA-379716"
] | [
"EC:6.1.1.11",
"METACYC:PWY-6281",
"REACTOME:R-HSA-2408557",
"REACTOME:R-HSA-379716"
] | 4 | [
"1ser",
"1ses",
"1set",
"1sry",
"2dq0",
"2dq3",
"2zr2",
"2zr3",
"3lsq",
"3lss",
"3qne",
"3qo5",
"3qo7",
"3qo8",
"3vbb",
"4l87",
"4rqe",
"4rqf",
"6blj",
"6gir",
"6h9x",
"6hdz",
"6he1",
"6he3",
"6hhy",
"6hhz",
"6hi0",
"6ote",
"6r1m",
"6r1n",
"6r1o",
"6rlt"... | 45 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006326",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"7540217",
"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,
1995,
2000,
1990,
1999,
2000,
2002
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
794,
26459,
7176,
17,
547
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
13,
1,
1,
2,
1,
5,
8,
2,
11,
4,
1,
2,
35
] | 13 | true | Domain | Serine-tRNA synthetase, type1, N-terminal | Serine-tRNA synthetase, type1, N-terminal | Ser-tRNA-synth_1_N | 5 |
IPR015867 | 15,867 | Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal | N-reg_PII/ATP_PRibTrfase_C | Homologous_superfamily | 101,003 | false | false | This entry represents a structural domain found in the nitrogen regulatory protein PII, in ATP phosphribosyltransferases (C-terminal domain), and in some bacterial hypothetical proteins. This domain consists of a ferredoxin-like α/β sandwich, which forms trimeric structures with orthogonally packed β-sheets around a th... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.70.120"
] | [
""
] | [
101003
] | 1 | [] | [] | [] | 0 | [
"1gnk",
"1h3d",
"1hwu",
"1j2v",
"1kr4",
"1naq",
"1nh7",
"1nh8",
"1nza",
"1o51",
"1o5j",
"1osc",
"1p1l",
"1pil",
"1q1k",
"1qy7",
"1ufl",
"1uku",
"1ul3",
"1umj",
"1v3r",
"1v3s",
"1v6h",
"1v9o",
"1vfj",
"1vhf",
"1xk8",
"2cz4",
"2dcl",
"2e66",
"2eg1",
"2eg2"... | 176 | [
"PUB00003738",
"PUB00022501",
"PUB00035665"
] | [
"1702507",
"14741209",
"16860774"
] | [
"Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense.",
"The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition.",
"Characterization of pII family (Gl... | [
1990,
2004,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2972,
88343,
7902,
19,
1767
] | 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,
1,
6,
2,
4,
4,
5,
2,
9,
10,
1,
1,
11
] | 13 | true | Homologous_superfamily | Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal | Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal | N-reg_PII/ATP_PRibTrfase_C | 5 |
IPR015868 | 15,868 | Glutaminase | Glutaminase | Family | 19,310 | false | false | Glutaminases ( ) deaminate glutamine to glutamate. In Bacillus subtilis, glutaminase is encoded by glnA, which is part of an operon, glnA-glnT (formerly ybgJ-ybgH), where glnT encodes a glutamine transporter. The glnA-glnT operon is regulated by the 2-component system GlnK-GlnL in response to glutamine [ ]. This entry ... | [
"GO:0004359",
"GO:0006541"
] | [
"glutaminase activity",
"glutamine metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00313",
"PF04960",
"PTHR12544",
"TIGR03814"
] | [
"Glutaminase",
"Glutaminase",
"",
"Gln_ase"
] | [
16626,
19052,
19223,
16665
] | 4 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.5.1.2",
"PWY-5921",
"R-CEL-210500",
"R-CEL-5628897",
"R-CEL-8964539",
"R-HSA-210500",
"R-HSA-5628897",
"R-HSA-8964539",
"R-MMU-210500",
"R-MMU-5628897",
"R-MMU-8964539",
"R-RNO-210500",
"R-RNO-5628897",
"R-RNO-8964539"
] | [
"EC:3.5.1.2",
"METACYC:PWY-5921",
"REACTOME:R-CEL-210500",
"REACTOME:R-CEL-5628897",
"REACTOME:R-CEL-8964539",
"REACTOME:R-HSA-210500",
"REACTOME:R-HSA-5628897",
"REACTOME:R-HSA-8964539",
"REACTOME:R-MMU-210500",
"REACTOME:R-MMU-5628897",
"REACTOME:R-MMU-8964539",
"REACTOME:R-RNO-210500",
"R... | 14 | [
"1mki",
"1u60",
"2osu",
"2pby",
"3agd",
"3age",
"3agf",
"3brm",
"3czd",
"3if5",
"3ih8",
"3ih9",
"3iha",
"3ihb",
"3ss3",
"3ss4",
"3ss5",
"3unw",
"3uo9",
"3voy",
"3voz",
"3vp0",
"3vp1",
"3vp2",
"3vp3",
"3vp4",
"4bqm",
"4jkt",
"4o7d",
"5d3o",
"5fi2",
"5fi6"... | 73 | [
"PUB00033342"
] | [
"15995196"
] | [
"Enhancement of glutamine utilization in Bacillus subtilis through the GlnK-GlnL two-component regulatory system."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"Megaviridae environmental sample",
"metagenomes"
] | [
12750,
1,
6492,
2,
65
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
23,
12,
2,
23,
11,
20
] | 7 | true | Family | Glutaminase | Glutaminase | Glutaminase | 9 |
IPR015869 | 15,869 | Transcription antitermination protein, NusG, bacteria, conserved site | Transcrpt_antiterm_NusG_bac_CS | Conserved_site | 17,274 | false | false | Bacterial transcription antitermination protein, NusG, is a component of the transcription complex and interacts with the termination factor Rho and RNA polymerase [ , ]. NusG is a bacterial transcriptional elongation factor involved in transcription termination and anti-termination [ ]. | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01014"
] | [
"NUSG"
] | [
17274
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00775"
] | [
"PROSITEDOC:PDOC00775"
] | 1 | [
"1m1g",
"1m1h",
"1npp",
"1npr",
"1nz9",
"2jvv",
"2kvq",
"2lq8",
"2mi6",
"2xhc",
"5ms0",
"5tbz",
"6c6u",
"6duq",
"6gov",
"6tqn",
"6tqo",
"6vu3",
"6vyq",
"6vyr",
"6vys",
"6vyt",
"6vyu",
"6vyw",
"6vyx",
"6vyy",
"6vyz",
"6vz2",
"6vz5",
"6x6t",
"6x7f",
"6x7k"... | 97 | [
"PUB00001884",
"PUB00001911",
"PUB00002759"
] | [
"7505669",
"8422985",
"1532577"
] | [
"NusG alters rho-dependent termination of transcription in vitro independent of kinetic coupling.",
"Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription.",
"NusG, a new Escherichia coli elongation factor involved in transcriptional antitermin... | [
1993,
1993,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured marine phage"
] | [
3,
16894,
50,
326,
1
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Conserved_site | Transcription antitermination protein, NusG, bacteria, conserved site | Transcription antitermination protein, NusG, bacteria, conserved site | Transcrpt_antiterm_NusG_bac_CS | 7 |
IPR015870 | 15,870 | UDP-3-O-acyl N-acetylglucosamine deacetylase, N-terminal | UDP-acyl_N-AcGlcN_deAcase_N | Homologous_superfamily | 14,493 | false | false | This entry represents the N-terminal domain which is required for deacetylase activity. UDP-3-O-N-acetylglucosamine deacetylases are zinc-dependent metalloamidases that catalyse the second and committed step in the biosynthesis of lipid A. Lipid A anchors lipopolysaccharide (the major constituent of the outer membrane)... | [
"GO:0103117",
"GO:0009245"
] | [
"UDP-3-O-acyl-N-acetylglucosamine deacetylase activity",
"lipid A biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.230.20"
] | [
""
] | [
14493
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.5.1.108",
"PWY-8073",
"PWY-8245",
"PWY-8283"
] | [
"EC:3.5.1.108",
"METACYC:PWY-8073",
"METACYC:PWY-8245",
"METACYC:PWY-8283"
] | 4 | [
"1p42",
"1xxe",
"1yh8",
"1yhc",
"2go3",
"2go4",
"2ier",
"2ies",
"2j65",
"2jt2",
"2o3z",
"2ves",
"3nzk",
"3p3c",
"3p3e",
"3p3g",
"3p76",
"3ps1",
"3ps2",
"3ps3",
"3u1y",
"3uhm",
"4fw3",
"4fw4",
"4fw5",
"4fw6",
"4fw7",
"4is9",
"4isa",
"4j3d",
"4lcf",
"4lcg"... | 95 | [
"PUB00029703",
"PUB00032543",
"PUB00035690"
] | [
"12819349",
"15667205",
"17296300"
] | [
"Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis.",
"Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design.",
"Amphipathic benzoic acid derivatives: synthesis and binding i... | [
2003,
2005,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"unclassified sequences"
] | [
13341,
1,
855,
296
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
9,
1,
6,
6
] | 4 | true | Homologous_superfamily | UDP-3-O-acyl N-acetylglucosamine deacetylase, N-terminal | UDP-3-O-acyl N-acetylglucosamine deacetylase, N-terminal | UDP-acyl_N-AcGlcN_deAcase_N | 8 |
IPR015871 | 15,871 | Transcription initiation factor IIA, gamma subunit, C-terminal | TFIIA_gsu_C | Domain | 4,564 | false | false | Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-in... | [
"GO:0006367",
"GO:0005672"
] | [
"transcription initiation at RNA polymerase II promoter",
"transcription factor TFIIA complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"CDD"
] | [
"PF02751",
"cd10014"
] | [
"TFIIA_gamma_C",
"TFIIA_gamma_C"
] | [
4551,
4520
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-674695",
"R-CEL-6807505",
"R-CEL-73776",
"R-CEL-73779",
"R-CEL-75953",
"R-CEL-76042",
"R-DDI-674695",
"R-DDI-6807505",
"R-DDI-73776",
"R-DDI-73779",
"R-DDI-75953",
"R-DDI-76042",
"R-DDI-9018519",
"R-DME-674695",
"R-DME-6807505",
"R-DME-73776",
"R-DME-73779",
"R-DME-75953",
... | [
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6807505",
"REACTOME:R-CEL-73776",
"REACTOME:R-CEL-73779",
"REACTOME:R-CEL-75953",
"REACTOME:R-CEL-76042",
"REACTOME:R-DDI-674695",
"REACTOME:R-DDI-6807505",
"REACTOME:R-DDI-73776",
"REACTOME:R-DDI-73779",
"REACTOME:R-DDI-75953",
"REACTOME:R-DDI-76042",
... | 58 | [
"1nh2",
"1nvp",
"1rm1",
"1ytf",
"5fmf",
"5fur",
"5fyw",
"5fz5",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5iya",
"5iyb",
"5iyc",
"5iyd",
"5m4s",
"5oqj",
"5oqm",
"5sva",
"6gyk",
"6gyl",
"6gym",
"6mzm",
"6o9l",
"7edx",
"7eg7",
"7eg8",
"7eg9",
"7ega",
"7egb",
"7egc"... | 85 | [
"PUB00013248",
"PUB00013320"
] | [
"12818428",
"8610010"
] | [
"TFIIA abrogates the effects of inhibition by HMGB1 but not E1A during the early stages of assembly of the transcriptional preinitiation complex.",
"Crystal structure of a yeast TFIIA/TBP/DNA complex."
] | [
2003,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4564
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
3,
2,
1,
4,
4,
5,
1,
5,
6,
1,
1,
14
] | 12 | true | Domain | Transcription initiation factor IIA, gamma subunit, C-terminal | Transcription initiation factor IIA, gamma subunit, C-terminal | TFIIA_gsu_C | 4 |
IPR015872 | 15,872 | Transcription initiation factor IIA, gamma subunit, N-terminal | TFIIA_gsu_N | Domain | 4,629 | false | false | Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-in... | [
"GO:0006367",
"GO:0005672"
] | [
"transcription initiation at RNA polymerase II promoter",
"transcription factor TFIIA complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"CDD"
] | [
"PF02268",
"cd10145"
] | [
"TFIIA_gamma_N",
"TFIIA_gamma_N"
] | [
4616,
4121
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-674695",
"R-CEL-6807505",
"R-CEL-73776",
"R-CEL-73779",
"R-CEL-75953",
"R-CEL-76042",
"R-DDI-674695",
"R-DDI-6807505",
"R-DDI-73776",
"R-DDI-73779",
"R-DDI-75953",
"R-DDI-76042",
"R-DDI-9018519",
"R-DME-674695",
"R-DME-6807505",
"R-DME-73776",
"R-DME-73779",
"R-DME-75953",
... | [
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6807505",
"REACTOME:R-CEL-73776",
"REACTOME:R-CEL-73779",
"REACTOME:R-CEL-75953",
"REACTOME:R-CEL-76042",
"REACTOME:R-DDI-674695",
"REACTOME:R-DDI-6807505",
"REACTOME:R-DDI-73776",
"REACTOME:R-DDI-73779",
"REACTOME:R-DDI-75953",
"REACTOME:R-DDI-76042",
... | 58 | [
"1nh2",
"1nvp",
"1rm1",
"1ytf",
"5fmf",
"5fur",
"5fyw",
"5fz5",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5iya",
"5iyb",
"5iyc",
"5iyd",
"5m4s",
"5oqj",
"5oqm",
"5sva",
"6gyk",
"6gyl",
"6gym",
"6mzm",
"6o9l",
"7edx",
"7eg7",
"7eg8",
"7eg9",
"7ega",
"7egb",
"7egc"... | 85 | [
"PUB00013248",
"PUB00013320"
] | [
"12818428",
"8610010"
] | [
"TFIIA abrogates the effects of inhibition by HMGB1 but not E1A during the early stages of assembly of the transcriptional preinitiation complex.",
"Crystal structure of a yeast TFIIA/TBP/DNA complex."
] | [
2003,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4629
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
2,
1,
4,
5,
9,
1,
4,
9,
1,
1,
7
] | 12 | true | Domain | Transcription initiation factor IIA, gamma subunit, N-terminal | Transcription initiation factor IIA, gamma subunit, N-terminal | TFIIA_gsu_N | 5 |
IPR015875 | 15,875 | IMP dehydrogenase / GMP reductase, conserved site | IMP_DH/GMP_Rdtase_CS | Conserved_site | 38,852 | false | false | null | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00487"
] | [
"IMP_DH_GMP_RED"
] | [
38852
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.7.1.7",
"PDOC00391",
"R-BTA-6798695",
"R-BTA-73817",
"R-BTA-9748787",
"R-CEL-6798695",
"R-CEL-73817",
"R-CEL-74217",
"R-CEL-9748787",
"R-DDI-6798695",
"R-DDI-73817",
"R-DDI-9748787",
"R-DME-6798695",
"R-DME-73817",
"R-DME-9748787",
"R-DRE-6798695",
"R-DRE-73817",
"R-DRE-9748787"... | [
"EC:1.7.1.7",
"PROSITEDOC:PDOC00391",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-73817",
"REACTOME:R-BTA-9748787",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-73817",
"REACTOME:R-CEL-74217",
"REACTOME:R-CEL-9748787",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-73817",
"REACTOME:R-DDI-9748787",
"R... | 38 | [
"1ak5",
"1b3o",
"1eep",
"1jcn",
"1jr1",
"1lrt",
"1me7",
"1me8",
"1me9",
"1meh",
"1mei",
"1mew",
"1nf7",
"1nfb",
"1pvn",
"1vrd",
"1ypf",
"1zfj",
"2a1y",
"2a7r",
"2ble",
"2bwg",
"2bzn",
"2c6q",
"2cu0",
"3ffs",
"3khj",
"3tsb",
"3tsd",
"3usb",
"3zfh",
"4af0"... | 185 | [
"PUB00000471",
"PUB00002466",
"PUB00002609"
] | [
"2904262",
"2902093",
"1969416"
] | [
"Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12.",
"Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs.",
"Two distinct cDNAs for human IMP dehydrogenase."
] | [
1988,
1988,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
627,
27789,
9919,
12,
505
] | 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,
4,
17,
3,
2,
29,
13,
1,
6,
20,
4,
1,
8
] | 13 | true | Conserved_site | IMP dehydrogenase / GMP reductase, conserved site | IMP dehydrogenase / GMP reductase, conserved site | IMP_DH/GMP_Rdtase_CS | 6 |
IPR015877 | 15,877 | MAT1, centre | MAT1_centre | Domain | 4,476 | false | false | This entry represents the central region of MAT1. MAT1 (menage a trois 1) is a RING finger protein with a characteristic C3HC4 motif in its N-terminal domain that plays a crucial role in stabilizing the cyclin H-CDK7 complex, forming the functional CDK-activating kinase (CAK) enzymatic complex responsible for activatin... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06391"
] | [
"MAT1"
] | [
4476
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-HSA-112382",
"R-HSA-113418",
"R-HSA-167152",
"R-HSA-167158",
"R-HSA-167160",
"R-HSA-167161",
"R-HSA-167162",
"R-HSA-167172",
"R-HSA-167200",
"R-HSA-167246",
"R-HSA-427413",
"R-HSA-5696395",
"R-HSA-674695",
"R-HSA-6781823",
"R-HSA-6781827",
"R-HSA-6782135",
"R-HSA-6782210",
"R-HS... | [
"REACTOME:R-HSA-112382",
"REACTOME:R-HSA-113418",
"REACTOME:R-HSA-167152",
"REACTOME:R-HSA-167158",
"REACTOME:R-HSA-167160",
"REACTOME:R-HSA-167161",
"REACTOME:R-HSA-167162",
"REACTOME:R-HSA-167172",
"REACTOME:R-HSA-167200",
"REACTOME:R-HSA-167246",
"REACTOME:R-HSA-427413",
"REACTOME:R-HSA-569... | 85 | [
"5oqj",
"5oqm",
"6gym",
"6nmi",
"6o9l",
"6o9m",
"6tun",
"6xbz",
"7b5o",
"7b5q",
"7egb",
"7egc",
"7ena",
"7enc",
"7kue",
"7lbm",
"7ml0",
"7ml1",
"7ml2",
"7ml3",
"7ml4",
"7nvr",
"7nvw",
"7nvx",
"7nvy",
"7nvz",
"7nw0",
"7o4i",
"7o4j",
"7o4k",
"7o4l",
"7o72"... | 58 | [
"PUB00007681",
"PUB00007682"
] | [
"11007478",
"11447116"
] | [
"Molecular structure of human TFIIH.",
"T-loop phosphorylation stabilizes the CDK7-cyclin H-MAT1 complex in vivo and regulates its CTD kinase activity."
] | [
2000,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4476
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
11,
1,
2,
2,
4,
4,
1,
4,
6,
1,
1,
6
] | 12 | true | Domain | MAT1, centre | MAT1, centre | MAT1_centre | 7 |
IPR015878 | 15,878 | S-adenosyl-L-homocysteine hydrolase, NAD binding domain | Ado_hCys_hydrolase_NAD-bd | Domain | 33,241 | false | false | S-adenosyl-L-homocysteine hydrolase ( ) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. AdoHcyase is an ubiquitous enzyme which binds and requires NAD + as a cofactor. AdoHcyase is a highly conserved protein [... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00670",
"SM00997"
] | [
"AdoHcyase_NAD",
"AdoHcyase_NAD"
] | [
30883,
33015
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"3.13.2.1",
"PWY-5041",
"R-BTA-156581",
"R-BTA-1614635",
"R-BTA-425381",
"R-CEL-156581",
"R-CEL-1614635",
"R-DDI-156581",
"R-DDI-1614635",
"R-DME-156581",
"R-DME-1614635",
"R-DME-425381",
"R-DME-5578775",
"R-HSA-112043",
"R-HSA-1489509",
"R-HSA-156581",
"R-HSA-1614635",
"R-HSA-2029... | [
"EC:3.13.2.1",
"METACYC:PWY-5041",
"REACTOME:R-BTA-156581",
"REACTOME:R-BTA-1614635",
"REACTOME:R-BTA-425381",
"REACTOME:R-CEL-156581",
"REACTOME:R-CEL-1614635",
"REACTOME:R-DDI-156581",
"REACTOME:R-DDI-1614635",
"REACTOME:R-DME-156581",
"REACTOME:R-DME-1614635",
"REACTOME:R-DME-425381",
"RE... | 39 | [
"1a7a",
"1b3r",
"1d4f",
"1k0u",
"1ky4",
"1ky5",
"1li4",
"1v8b",
"1xwf",
"2h5l",
"2ziz",
"2zj0",
"2zj1",
"3ce6",
"3d64",
"3dhy",
"3g1u",
"3glq",
"3gvp",
"3h9u",
"3mtg",
"3n58",
"3nj4",
"3ond",
"3one",
"3onf",
"3x2e",
"3x2f",
"4lvc",
"4pfj",
"4pgf",
"4yvf"... | 133 | [
"PUB00004791"
] | [
"1631127"
] | [
"Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Pandoravirus",
"unclassified sequences"
] | [
994,
18396,
13241,
7,
603
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
20,
1,
9,
6,
13,
14,
1,
14,
20,
1,
1,
23
] | 12 | true | Domain | S-adenosyl-L-homocysteine hydrolase, NAD binding domain | S-adenosyl-L-homocysteine hydrolase, NAD binding domain | Ado_hCys_hydrolase_NAD-bd | 8 |
IPR015879 | 15,879 | Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain | Ring_hydroxy_dOase_asu_C_dom | Domain | 29,764 | false | false | This entry represents the conserved C-terminal domain found in the alpha subunit of aromatic-ring-hydroxylating dioxygenases. It is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands. Aromatic ring hydroxylating dioxygen... | [
"GO:0005506",
"GO:0051537"
] | [
"iron ion binding",
"2 iron, 2 sulfur cluster binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00848"
] | [
"Ring_hydroxyl_A"
] | [
29764
] | 1 | [
"EC"
] | [
"1.14.12"
] | [
"EC:1.14.12"
] | 1 | [
"1eg9",
"1ndo",
"1o7g",
"1o7h",
"1o7m",
"1o7n",
"1o7p",
"1o7w",
"1uli",
"1ulj",
"1uuv",
"1uuw",
"1wql",
"2b1x",
"2b24",
"2bmo",
"2bmq",
"2bmr",
"2ckf",
"2gbw",
"2gbx",
"2hmj",
"2hmk",
"2hml",
"2hmm",
"2hmn",
"2hmo",
"2xr8",
"2xrx",
"2xsh",
"2xso",
"2yfi"... | 73 | [
"PUB00002151"
] | [
"1885518"
] | [
"Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases."
] | [
1991
] | 1 | [] | [
"IPR043264",
"IPR043266"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"plasmids",
"unclassified sequences"
] | [
192,
25260,
3729,
3,
580
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
2,
3,
6
] | 4 | true | Domain | Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain | Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain | Ring_hydroxy_dOase_asu_C_dom | 4 |
IPR015881 | 15,881 | Aromatic-ring-hydroxylating dioxygenase ARHD, Rieske 2Fe-2S-binding site | ARHD_Rieske_2Fe_2S | Binding_site | 13,982 | false | false | This entry represents the Rieske type 2Fe-2S binding site found at the N-terminal in the alpha-subunit of ARHD proteins and related non-heme iron oxygenases. The Rieske-type [2Fe-2S] cluster is coordinated to its protein by two cysteine residues and two histidine residues [ , ]. Aromatic-ring-hydroxylating dioxygenases... | [
"GO:0005506",
"GO:0051537"
] | [
"iron ion binding",
"2 iron, 2 sulfur cluster binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00570"
] | [
"RING_HYDROXYL_ALPHA"
] | [
13982
] | 1 | [
"EC",
"PROSITEDOC"
] | [
"1.14.12",
"PDOC00493"
] | [
"EC:1.14.12",
"PROSITEDOC:PDOC00493"
] | 2 | [
"1eg9",
"1ndo",
"1o7g",
"1o7h",
"1o7m",
"1o7n",
"1o7p",
"1o7w",
"1uli",
"1ulj",
"1uuv",
"1uuw",
"1wql",
"2b1x",
"2b24",
"2bmo",
"2bmq",
"2bmr",
"2ckf",
"2gbw",
"2gbx",
"2hmj",
"2hmk",
"2hml",
"2hmm",
"2hmn",
"2hmo",
"2xr8",
"2xrx",
"2xsh",
"2xso",
"2yfi"... | 85 | [
"PUB00002151",
"PUB00005305",
"PUB00043836",
"PUB00043837"
] | [
"1885518",
"9634695",
"16168954",
"16271700"
] | [
"Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases.",
"Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase.",
"Rieske business: structure-function of Rieske non-heme ... | [
1991,
1998,
2005,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"plasmids",
"unclassified sequences"
] | [
68,
12146,
1549,
2,
217
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
2,
2,
16
] | 4 | true | Binding_site | Aromatic-ring-hydroxylating dioxygenase ARHD, Rieske 2Fe-2S-binding site | Aromatic-ring-hydroxylating dioxygenase ARHD, Rieske 2Fe-2S-binding site | ARHD_Rieske_2Fe_2S | 6 |
IPR015882 | 15,882 | Beta-hexosaminidase, bacterial type, N-terminal | HEX_bac_N | Domain | 23,869 | false | false | This entry represents the N-terminal domain of the beta-hexosaminidases mostly from bacteria, some yeasts and invertebrates. This domain has a zincin-like fold and can be found in chitobiases, hyaluronoglucosaminidases, N,N'-diacetylchitobiases and O-GlcNAcase NagJ. They belong to either the glycosyl hydrolase 84 or th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02838"
] | [
"Glyco_hydro_20b"
] | [
23869
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.2.1.52",
"PWY-6902",
"PWY-7822",
"PWY-7883"
] | [
"EC:3.2.1.52",
"METACYC:PWY-6902",
"METACYC:PWY-7822",
"METACYC:PWY-7883"
] | 4 | [
"1c7s",
"1c7t",
"1hp4",
"1hp5",
"1jak",
"1m01",
"1m03",
"1m04",
"1qba",
"1qbb",
"2cbi",
"2cbj",
"2chn",
"2cho",
"2j47",
"2j4g",
"2j62",
"2jiw",
"2v5c",
"2v5d",
"2vur",
"2vvn",
"2vvs",
"2w4x",
"2w66",
"2w67",
"2wb5",
"2wca",
"2wzh",
"2wzi",
"2x0h",
"2x0y"... | 116 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
20,
21983,
1659,
1,
206
] | 5 | [] | [] | 0 | true | Domain | Beta-hexosaminidase, bacterial type, N-terminal | Beta-hexosaminidase, bacterial type, N-terminal | HEX_bac_N | 7 |
IPR015883 | 15,883 | Beta-hexosaminidase, catalytic domain | GH20_cat | Domain | 38,727 | false | false | This entry represents the glycoside hydrolase family 20 catalytic domain. This domain has a TIM barrel fold. Glycoside hydrolase family 20 ( ) comprises enzymes with several known activities; beta-hexosaminidase ( ); lacto-N-biosidase ( ); beta-1,6-N-acetylglucosaminidase); and beta-6-SO3-N-acetylglucosaminidase. Carbo... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00728"
] | [
"Glyco_hydro_20"
] | [
38727
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME... | [
"3.2.1",
"3.2.1.52",
"PWY-6902",
"PWY-7822",
"PWY-7883",
"R-BTA-2022857",
"R-BTA-2024101",
"R-BTA-2160916",
"R-BTA-9840310",
"R-CEL-2022857",
"R-CEL-2024101",
"R-CEL-2160916",
"R-CEL-6798695",
"R-CEL-9840310",
"R-DDI-2022857",
"R-DDI-2024101",
"R-DDI-2160916",
"R-DDI-6798695",
"R... | [
"EC:3.2.1",
"EC:3.2.1.52",
"METACYC:PWY-6902",
"METACYC:PWY-7822",
"METACYC:PWY-7883",
"REACTOME:R-BTA-2022857",
"REACTOME:R-BTA-2024101",
"REACTOME:R-BTA-2160916",
"REACTOME:R-BTA-9840310",
"REACTOME:R-CEL-2022857",
"REACTOME:R-CEL-2024101",
"REACTOME:R-CEL-2160916",
"REACTOME:R-CEL-6798695... | 41 | [
"1c7s",
"1c7t",
"1hp4",
"1hp5",
"1jak",
"1m01",
"1m03",
"1m04",
"1nou",
"1now",
"1np0",
"1o7a",
"1qba",
"1qbb",
"1yht",
"2gjx",
"2gk1",
"2yl5",
"2yl6",
"2yl8",
"2yl9",
"2yla",
"2yll",
"3gh4",
"3gh5",
"3gh7",
"3lmy",
"3nsm",
"3nsn",
"3ozo",
"3ozp",
"3rcn"... | 113 | [
"PUB00097352"
] | [
"26024355"
] | [
"Structural-Functional Analysis Reveals a Specific Domain Organization in Family GH20 Hexosaminidases."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
36,
22000,
16392,
5,
294
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
12,
7,
8,
11,
29,
15,
2,
17,
17,
26
] | 10 | true | Domain | Beta-hexosaminidase, catalytic domain | Beta-hexosaminidase, catalytic domain | GH20_cat | 2 |
IPR015884 | 15,884 | Malic enzyme, conserved site | Malic_enzyme_CS | Conserved_site | 33,479 | false | false | Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate, a reaction important in a number of metabolic pathways - e.g. carbon dioxide released from the reaction may be used in sugar production during the Calvin cycle of photosynthesis [ ]. There are 3 forms of the enzyme... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00331"
] | [
"MALIC_ENZYMES"
] | [
33479
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"1.1.1.38",
"PWY-3641",
"PWY-7115",
"PWY-7118",
"PWY-7384",
"PWY-7686",
"PDOC00294",
"R-HSA-1989781",
"R-HSA-70268",
"R-HSA-9818025",
"R-HSA-9837999",
"R-HSA-9861718",
"R-MMU-70268",
"R-MMU-9837999",
"R-MMU-9861718",
"R-RNO-70268",
"R-RNO-9861718"
] | [
"EC:1.1.1",
"EC:1.1.1.38",
"METACYC:PWY-3641",
"METACYC:PWY-7115",
"METACYC:PWY-7118",
"METACYC:PWY-7384",
"METACYC:PWY-7686",
"PROSITEDOC:PDOC00294",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-70268",
"REACTOME:R-HSA-9818025",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9861718",
"REACTOME:R... | 18 | [
"1do8",
"1efk",
"1efl",
"1gq2",
"1gz3",
"1gz4",
"1llq",
"1o0s",
"1pj2",
"1pj3",
"1pj4",
"1pjl",
"1qr6",
"1ww8",
"2a9f",
"2aw5",
"2dvm",
"3wja",
"5cee",
"5ou5",
"6ags",
"6c7n",
"6urf",
"6w29",
"6w2n",
"6w49",
"6w53",
"6w56",
"6w57",
"6w59",
"7bsj",
"7bsk"... | 48 | [
"PUB00000616",
"PUB00002681",
"PUB00002876",
"PUB00004541"
] | [
"1911848",
"1993674",
"8300616",
"2103472"
] | [
"Duck liver malic enzyme: sequence of a tryptic peptide containing the cysteine residue labeled by the substrate analog bromopyruvate.",
"Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli.",
"Cloning and analysis of the C4 photosynthetic NAD-d... | [
1991,
1991,
1994,
1990
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctYaH2",
"metagenomes"
] | [
91,
20318,
12881,
1,
188
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
25,
1,
6,
21,
2,
13,
6,
1,
27,
13,
1,
1,
70
] | 13 | true | Conserved_site | Malic enzyme, conserved site | Malic enzyme, conserved site | Malic_enzyme_CS | 7 |
IPR015886 | 15,886 | Formamidopyrimidine-DNA glycosylase, H2TH DNA-binding | H2TH_FPG | Domain | 42,347 | false | false | This entry represents a helix-2-turn-helix DNA-binding domain found in DNA glycosylase/AP lyase enzymes, which are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Formamidopyrimidine-DNA glycosylases (Fpg, MutM) are trifunctional DNA base excision repair enzymes that remove a wide r... | [
"GO:0003684",
"GO:0003906",
"GO:0008270",
"GO:0016799",
"GO:0006284"
] | [
"damaged DNA binding",
"DNA-(apurinic or apyrimidinic site) endonuclease activity",
"zinc ion binding",
"hydrolase activity, hydrolyzing N-glycosyl compounds",
"base-excision repair"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 5 | [
"PFAM",
"SMART"
] | [
"PF06831",
"SM01232"
] | [
"H2TH",
"H2TH"
] | [
40930,
42227
] | 2 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.2.2.23",
"4.2.99.18",
"R-BTA-110329",
"R-BTA-5649702",
"R-HSA-110328",
"R-HSA-110329",
"R-HSA-110330",
"R-HSA-110331",
"R-HSA-5649702",
"R-HSA-9616334",
"R-HSA-9629232",
"R-HSA-9636003",
"R-MMU-110328",
"R-MMU-110329",
"R-MMU-110330",
"R-MMU-110331",
"R-MMU-5649702"
] | [
"EC:3.2.2.23",
"EC:4.2.99.18",
"REACTOME:R-BTA-110329",
"REACTOME:R-BTA-5649702",
"REACTOME:R-HSA-110328",
"REACTOME:R-HSA-110329",
"REACTOME:R-HSA-110330",
"REACTOME:R-HSA-110331",
"REACTOME:R-HSA-5649702",
"REACTOME:R-HSA-9616334",
"REACTOME:R-HSA-9629232",
"REACTOME:R-HSA-9636003",
"REACT... | 17 | [
"1ee8",
"1k3w",
"1k3x",
"1k82",
"1kfv",
"1l1t",
"1l1z",
"1l2b",
"1l2c",
"1l2d",
"1nnj",
"1pji",
"1pjj",
"1pm5",
"1q39",
"1q3b",
"1q3c",
"1r2y",
"1r2z",
"1tdh",
"1tdz",
"1xc8",
"2ea0",
"2f5n",
"2f5o",
"2f5p",
"2f5q",
"2f5s",
"2opf",
"2oq4",
"2xzf",
"2xzu"... | 122 | [
"PUB00002832",
"PUB00003593",
"PUB00012853",
"PUB00014010",
"PUB00018046",
"PUB00018047",
"PUB00031419"
] | [
"8473347",
"7704272",
"11912217",
"10921868",
"15588838",
"12055620",
"15232006"
] | [
"Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role.",
"Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein.",
"Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA.",
"Cryst... | [
1993,
1995,
2002,
2000,
2004,
2002,
2004
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
63,
36835,
4754,
74,
621
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
8,
3,
2,
3,
7,
1,
7,
9,
8
] | 9 | true | Domain | Formamidopyrimidine-DNA glycosylase, H2TH DNA-binding | Formamidopyrimidine-DNA glycosylase, H2TH DNA-binding | H2TH_FPG | 1 |
IPR015887 | 15,887 | DNA glycosylase/AP lyase, zinc finger domain, DNA-binding site | DNA_glyclase_Znf_dom_DNA_BS | Binding_site | 22,300 | false | false | This entry represents the DNA-binding site found in the C-terminal zinc finger domain of DNA glycosylase/AP lyase enzymes. These enzymes are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. These enzymes are primarily from bacteria, and have both DNA glycosylase activity ( ) and AP l... | [
"GO:0003677",
"GO:0003906",
"GO:0008270",
"GO:0016799",
"GO:0006281"
] | [
"DNA binding",
"DNA-(apurinic or apyrimidinic site) endonuclease activity",
"zinc ion binding",
"hydrolase activity, hydrolyzing N-glycosyl compounds",
"DNA repair"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 5 | [
"PROSITE"
] | [
"PS01242"
] | [
"ZF_FPG_1"
] | [
22300
] | 1 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.2.2.23",
"4.2.99.18",
"PDOC00956",
"R-HSA-110328",
"R-HSA-110329",
"R-HSA-110330",
"R-HSA-110331",
"R-HSA-9629232",
"R-HSA-9636003",
"R-MMU-110330",
"R-MMU-110331"
] | [
"EC:3.2.2.23",
"EC:4.2.99.18",
"PROSITEDOC:PDOC00956",
"REACTOME:R-HSA-110328",
"REACTOME:R-HSA-110329",
"REACTOME:R-HSA-110330",
"REACTOME:R-HSA-110331",
"REACTOME:R-HSA-9629232",
"REACTOME:R-HSA-9636003",
"REACTOME:R-MMU-110330",
"REACTOME:R-MMU-110331"
] | 11 | [
"1ee8",
"1k3w",
"1k3x",
"1k82",
"1kfv",
"1l1t",
"1l1z",
"1l2b",
"1l2c",
"1l2d",
"1nnj",
"1pji",
"1pjj",
"1pm5",
"1q39",
"1q3c",
"1r2y",
"1r2z",
"1tdz",
"1xc8",
"2ea0",
"2f5n",
"2f5o",
"2f5p",
"2f5q",
"2f5s",
"2oq4",
"2xzf",
"2xzu",
"3c58",
"3go8",
"3gp1"... | 81 | [
"PUB00002832",
"PUB00003593",
"PUB00014010",
"PUB00014077",
"PUB00031419",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"8473347",
"7704272",
"10921868",
"12665246",
"15232006",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role.",
"Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein.",
"Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an ext... | [
1993,
1995,
2000,
2002,
2004,
2007,
2005,
2005,
1999,
2001
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
15,
21205,
2,
771,
307
] | 5 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
1,
1,
1
] | 5 | true | Binding_site | DNA glycosylase/AP lyase, zinc finger domain, DNA-binding site | DNA glycosylase/AP lyase, zinc finger domain, DNA-binding site | DNA_glyclase_Znf_dom_DNA_BS | 8 |
IPR015888 | 15,888 | L-fucose isomerase, C-terminal | Fuc_isomerase_C | Domain | 5,174 | false | false | L-fucose isomerase ( ) converts the aldose L-fucose into the corresponding ketose L-fuculose during the first step in fucose metabolism using Mn2+ as a cofactor. The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity with other ketol isomerases. The... | [
"GO:0008736",
"GO:0006004",
"GO:0005737"
] | [
"L-fucose isomerase activity",
"fucose metabolic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF02952"
] | [
"Fucose_iso_C"
] | [
5174
] | 1 | [
"EC"
] | [
"5.3.1.25"
] | [
"EC:5.3.1.25"
] | 1 | [
"1fui",
"3a9r",
"3a9s",
"3a9t",
"4c20",
"4c21",
"4c22",
"6k1f",
"6k1g"
] | 9 | [
"PUB00007428"
] | [
"9367760"
] | [
"Structure and mechanism of L-fucose isomerase from Escherichia coli."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
55,
4965,
19,
135
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | L-fucose isomerase, C-terminal | L-fucose isomerase, C-terminal | Fuc_isomerase_C | 8 |
IPR015889 | 15,889 | Intradiol ring-cleavage dioxygenase, core | Intradiol_dOase_core | Homologous_superfamily | 35,762 | false | false | Dioxygenases catalyse the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms. Cleavage of aromatic rings is one of the most important functions of dioxygenases, which play key roles in the degradation of aromatic compounds. The substrates of ring-cleavage dioxygenases... | [
"GO:0005506",
"GO:0016702"
] | [
"iron ion binding",
"oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.60.130.10",
"SSF49482"
] | [
"",
""
] | [
35466,
35671
] | 2 | [
"EC"
] | [
"1.13.11"
] | [
"EC:1.13.11"
] | 1 | [
"1dlm",
"1dlq",
"1dlt",
"1dmh",
"1eo2",
"1eo9",
"1eoa",
"1eob",
"1eoc",
"1s9a",
"1tmx",
"1ykk",
"1ykl",
"1ykm",
"1ykn",
"1yko",
"1ykp",
"2azq",
"2boy",
"2bum",
"2buq",
"2bur",
"2but",
"2buu",
"2buv",
"2buw",
"2bux",
"2buy",
"2buz",
"2bv0",
"2pcd",
"2xsr"... | 94 | [
"PUB00015256",
"PUB00015258"
] | [
"10730195",
"15060064"
] | [
"Catechol dioxygenases.",
"Crystal structure of 4-chlorocatechol 1,2-dioxygenase from the chlorophenol-utilizing gram-positive Rhodococcus opacus 1CP."
] | [
1999,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid pEMT3",
"Pulverervirus PFR1",
"unclassified sequences"
] | [
23,
26268,
9354,
1,
2,
114
] | 6 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
4
] | 1 | true | Homologous_superfamily | Intradiol ring-cleavage dioxygenase, core | Intradiol ring-cleavage dioxygenase, core | Intradiol_dOase_core | 4 |
IPR015890 | 15,890 | Chorismate-utilising enzyme, C-terminal | Chorismate_C | Domain | 72,872 | false | false | This entry represents the catalytic regions of the chorismate binding enzymes anthranilate synthase, isochorismate synthase, aminodeoxychorismate synthase and para-aminobenzoate synthase [ ]. Anthranilate synthase catalyses the reaction: chorismate + l-glutamine = anthranilate + pyruvate + l-glutamate. The enzyme is a ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00425"
] | [
"Chorismate_bind"
] | [
72872
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"4.1.3.27",
"PWY-5958",
"PWY-6661"
] | [
"EC:4.1.3.27",
"METACYC:PWY-5958",
"METACYC:PWY-6661"
] | 3 | [
"1i1q",
"1i7q",
"1i7s",
"1k0e",
"1k0g",
"1qdl",
"2eua",
"2fn0",
"2fn1",
"2g5f",
"2i6y",
"3bzm",
"3bzn",
"3gse",
"3h9m",
"3hwo",
"3log",
"3os6",
"3r74",
"3r75",
"3r76",
"3rv6",
"3rv7",
"3rv8",
"3rv9",
"3st6",
"3veh",
"4grh",
"5cwa",
"5jxz",
"5jy4",
"5jy8"... | 54 | [
"PUB00008575"
] | [
"11371633"
] | [
"The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Pandoravirus",
"unclassified sequences"
] | [
1490,
62114,
7975,
7,
1286
] | 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"
] | [
32,
4,
3,
16,
2,
2,
31
] | 7 | true | Domain | Chorismate-utilising enzyme, C-terminal | Chorismate-utilising enzyme, C-terminal | Chorismate_C | 8 |
IPR015892 | 15,892 | Carbonic anhydrase, prokaryotic-like, conserved site | Carbonic_anhydrase_CS | Conserved_site | 27,964 | false | false | Carbonic anhydrases ( ) (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of ce... | [
"GO:0004089",
"GO:0008270",
"GO:0015976"
] | [
"carbonate dehydratase activity",
"zinc ion binding",
"carbon utilization"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00704",
"PS00705"
] | [
"PROK_CO2_ANHYDRASE_1",
"PROK_CO2_ANHYDRASE_2"
] | [
22175,
20851
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"4.2.1.1",
"PWY-241",
"PWY-5743",
"PWY-5744",
"PWY-5789",
"PWY-6142",
"PWY-7115",
"PWY-7117",
"PDOC00586"
] | [
"EC:4.2.1.1",
"METACYC:PWY-241",
"METACYC:PWY-5743",
"METACYC:PWY-5744",
"METACYC:PWY-5789",
"METACYC:PWY-6142",
"METACYC:PWY-7115",
"METACYC:PWY-7117",
"PROSITEDOC:PDOC00586"
] | 9 | [
"1ddz",
"1ekj",
"1i6o",
"1i6p",
"1t75",
"1ym3",
"2a5v",
"2a8c",
"2a8d",
"2esf",
"3e1v",
"3e1w",
"3e24",
"3e28",
"3e2a",
"3e2w",
"3e2x",
"3e31",
"3e3f",
"3e3g",
"3e3i",
"3eyx",
"3mf3",
"3qy1",
"3ucj",
"3uck",
"3ucm",
"3ucn",
"3uco",
"4o1j",
"4o1k",
"4rxy"... | 56 | [
"PUB00002753",
"PUB00004782"
] | [
"1740425",
"1584776"
] | [
"Carbonic anhydrase in Escherichia coli. A product of the cyn operon.",
"A gene homologous to chloroplast carbonic anhydrase (icfA) is essential to photosynthetic carbon dioxide fixation by Synechococcus PCC7942."
] | [
1992,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Pandoravirus",
"unclassified sequences"
] | [
88,
21691,
6032,
5,
148
] | 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)",
"Zea mays"
] | [
33,
2,
2,
9,
1,
43
] | 6 | true | Conserved_site | Carbonic anhydrase, prokaryotic-like, conserved site | Carbonic anhydrase, prokaryotic-like, conserved site | Carbonic_anhydrase_CS | 2 |
IPR015894 | 15,894 | Guanylate-binding protein, N-terminal | Guanylate-bd_N | Domain | 16,222 | false | false | Guanylate-binding protein is a GTPase that is induced by interferon (IFN)-gamma. GTPases induced by IFN-gamma are key to the protective immunity against microbial and viral pathogens. These GTPases are classified into three groups: the small 47-kd GTPases, the Mx proteins, and the large 65- to 67-kd GTPases. Guanylate-... | [
"GO:0003924",
"GO:0005525"
] | [
"GTPase activity",
"GTP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF02263"
] | [
"GBP"
] | [
16222
] | 1 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"3.6.5.-",
"R-HSA-877300",
"R-HSA-909733"
] | [
"EC:3.6.5.-",
"REACTOME:R-HSA-877300",
"REACTOME:R-HSA-909733"
] | 3 | [
"1dg3",
"1f5n",
"2b8w",
"2b92",
"2bc9",
"2d4h",
"3q5d",
"3q5e",
"3qnu",
"3qof",
"3x1d",
"4idn",
"4ido",
"4idp",
"4idq",
"5vgr",
"6b9d",
"6b9e",
"6b9f",
"6b9g",
"6k1z",
"6k2d",
"6loj",
"6vkj",
"6xjn",
"6xjo",
"7ckf",
"7e58",
"7e59",
"7e5a",
"7m1s",
"7ol3"... | 39 | [
"PUB00035996",
"PUB00035997"
] | [
"17266443",
"16936281"
] | [
"Unique features of different members of the human guanylate-binding protein family.",
"Human guanylate binding protein-1 is a secreted GTPase present in increased concentrations in the cerebrospinal fluid of patients with bacterial meningitis."
] | [
2007,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mimiviridae",
"metagenomes"
] | [
16216,
2,
4
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
15,
7,
49,
2,
58,
49,
14,
41,
48
] | 9 | true | Domain | Guanylate-binding protein, N-terminal | Guanylate-binding protein, N-terminal | Guanylate-bd_N | 7 |
IPR015895 | 15,895 | Glutamyl-tRNA reductase, N-terminal | 4pyrrol_synth_GluRdtase_N | Domain | 20,894 | false | false | This entry represents the N-terminal domain of glutamyl-tRNA reductase ( ), which reduces glutamyl-tRNA to glutamate-1-semialdehyde during the first stage of tetrapyrrole biosynthesis by the C5 pathway [ , ]. The enzyme requires NADPH as a cofactor. This N-terminal domain is the catalytic domain [ ]. | [
"GO:0008883",
"GO:0050661",
"GO:0033014"
] | [
"glutamyl-tRNA reductase activity",
"NADP binding",
"tetrapyrrole biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF05201"
] | [
"GlutR_N"
] | [
20894
] | 1 | [
"EC",
"METACYC",
"PROSITEDOC"
] | [
"1.2.1.70",
"PWY-5188",
"PDOC00608"
] | [
"EC:1.2.1.70",
"METACYC:PWY-5188",
"PROSITEDOC:PDOC00608"
] | 3 | [
"1gpj",
"4n7r",
"5che",
"5yjl"
] | 4 | [
"PUB00005387",
"PUB00009744",
"PUB00075508"
] | [
"1502723",
"11215515",
"24753615"
] | [
"Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis.",
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein."
] | [
1992,
2000,
2014
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
828,
18195,
1574,
297
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
1,
2,
14
] | 4 | true | Domain | Glutamyl-tRNA reductase, N-terminal | Glutamyl-tRNA reductase, N-terminal | 4pyrrol_synth_GluRdtase_N | 9 |
IPR015896 | 15,896 | Tetrapyrrole biosynthesis, glutamyl-tRNA reductase, dimerisation domain | 4pyrrol_synth_GluRdtase_dimer | Domain | 19,748 | false | false | Tetrapyrroles are large macrocyclic compounds derived from a common biosynthetic pathway [ ]. The end-product, uroporphyrinogen III, is used to synthesise a number of important molecules, including vitamin B12, haem, sirohaem, chlorophyll, coenzyme F430 and phytochromobilin [ ]. The first stage in tetrapyrrole synthesi... | [
"GO:0008883",
"GO:0050661",
"GO:0033014"
] | [
"glutamyl-tRNA reductase activity",
"NADP binding",
"tetrapyrrole biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF00745"
] | [
"GlutR_dimer"
] | [
19748
] | 1 | [
"EC",
"METACYC"
] | [
"1.2.1.70",
"PWY-5188"
] | [
"EC:1.2.1.70",
"METACYC:PWY-5188"
] | 2 | [
"1gpj",
"4n7r",
"4yvq",
"5che",
"5yjl"
] | 5 | [
"PUB00005387",
"PUB00009744",
"PUB00025328",
"PUB00035496",
"PUB00035498"
] | [
"1502723",
"11215515",
"11726494",
"17227226",
"16564539"
] | [
"Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis.",
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis.",
"Tetrapyrrole biosynthesis in higher plants.",
"Evolu... | [
1992,
2000,
2001,
2007,
2006
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
850,
17019,
1611,
268
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
14,
1,
3,
14
] | 4 | true | Domain | Tetrapyrrole biosynthesis, glutamyl-tRNA reductase, dimerisation domain | Tetrapyrrole biosynthesis, glutamyl-tRNA reductase, dimerisation domain | 4pyrrol_synth_GluRdtase_dimer | 6 |
IPR015897 | 15,897 | CHK kinase-like | CHK_kinase-like | Domain | 15,035 | false | false | Zinc finger C4 and HLH domain containing kinases domain subfamily of choline kinases. | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00587"
] | [
"CHK"
] | [
15035
] | 1 | [] | [] | [] | 0 | [
"8zic",
"9eto"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Gaeavirus sp.",
"metagenomes"
] | [
2382,
12554,
1,
98
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster"
] | [
32,
1,
113
] | 3 | true | Domain | CHK kinase-like | CHK kinase-like | CHK_kinase-like | 6 |
IPR015898 | 15,898 | G-protein, gamma subunit-like domain | G-protein_gamma-like_dom | Domain | 23,184 | false | false | This entry represents the G protein gamma subunit and the GGL (G protein gamma-like) domain, which are related in sequence and are comprised of an extended α-helical polypeptide. The G protein gamma subunit forms a stable dimer with the beta subunit, but it does not make any contact with the alpha subunit, which contac... | [
"GO:0007186"
] | [
"G protein-coupled receptor signaling pathway"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE",
"SMART",
"SMART",
"CDD"
] | [
"PF00631",
"PS50058",
"SM00224",
"SM01224",
"cd00068"
] | [
"G-gamma",
"G_PROTEIN_GAMMA",
"GGL",
"G_gamma",
"GGL"
] | [
21742,
13189,
18827,
22074,
17660
] | 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-BTA-1296041",
"R-BTA-202040",
"R-BTA-2485179",
"R-BTA-2514859",
"R-BTA-381676",
"R-BTA-392170",
"R-BTA-392451",
"R-BTA-392851",
"R-BTA-400042",
"R-BTA-4086398",
"R-BTA-416476",
"R-BTA-416482",
"R-BTA-418217",
"R-BTA-418555",
"R-BTA-418592",
"R-BTA-418594",
"R-BTA-418597",
"R-BTA... | [
"REACTOME:R-BTA-1296041",
"REACTOME:R-BTA-202040",
"REACTOME:R-BTA-2485179",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-381676",
"REACTOME:R-BTA-392170",
"REACTOME:R-BTA-392451",
"REACTOME:R-BTA-392851",
"REACTOME:R-BTA-400042",
"REACTOME:R-BTA-4086398",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA... | 177 | [
"1a0r",
"1b9x",
"1b9y",
"1gg2",
"1got",
"1gp2",
"1omw",
"1tbg",
"1xhm",
"2bcj",
"2pbi",
"2trc",
"3ah8",
"3cik",
"3krw",
"3krx",
"3psc",
"3pvu",
"3pvw",
"3sn6",
"3uzs",
"3v5w",
"4kfm",
"4mk0",
"4pnk",
"5he0",
"5he1",
"5he2",
"5he3",
"5kdo",
"5tdh",
"5ukk"... | 1,290 | [
"PUB00005142",
"PUB00015166",
"PUB00015168",
"PUB00015169",
"PUB00015170",
"PUB00015171",
"PUB00015172",
"PUB00015235"
] | [
"1902986",
"15294442",
"15119945",
"14762218",
"11313912",
"9278091",
"11882385",
"11331068"
] | [
"Diversity of G proteins in signal transduction.",
"G protein activation by G protein coupled receptors: ternary complex formation or catalyzed reaction?",
"Biochemistry of transmembrane signaling mediated by trimeric G proteins.",
"G protein signaling: insights from new structures.",
"Regulation of G prote... | [
1991,
2004,
2004,
2004,
2001,
1997,
2002,
2001
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Cyprinid herpesvirus 3",
"Eukaryota",
"Halobacteriales",
"marine sediment metagenome"
] | [
99,
4,
23077,
3,
1
] | 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... | [
7,
9,
64,
13,
57,
45,
1,
7,
60,
1,
15
] | 11 | true | Domain | G-protein, gamma subunit-like domain | G-protein, gamma subunit-like domain | G-protein_gamma-like_dom | 6 |
IPR015899 | 15,899 | UDP-galactopyranose mutase, C-terminal | UDP-GalPyranose_mutase_C | Domain | 9,416 | false | false | UDP-galactopyranose mutase ( ) is involved in the conversion of UDP-GALP into UDP-GALF through a 2-keto intermediate, and contains FAD as a cofactor. The gene is known as glf, ceoA, and rfbD. It is known experimentally in Escherichia coli, Mycobacterium tuberculosis, and Klebsiella pneumoniae. | [
"GO:0008767"
] | [
"UDP-galactopyranose mutase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF03275"
] | [
"GLF"
] | [
9416
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.4.99.9",
"PWY-6397",
"PWY-7328",
"PWY-7622"
] | [
"EC:5.4.99.9",
"METACYC:PWY-6397",
"METACYC:PWY-7328",
"METACYC:PWY-7622"
] | 4 | [
"1i8t",
"1v0j",
"1wam",
"2bi7",
"2bi8",
"3gf4",
"3hdq",
"3hdy",
"3he3",
"3inr",
"3int",
"3kyb",
"3mj4",
"4mo2",
"4rpg",
"4rph",
"4rpj",
"4rpk",
"4rpl",
"4xgk",
"5br7",
"5eqd",
"5eqf",
"5er9",
"5f3r",
"6d2e",
"6d2g",
"6d99",
"6d9a",
"6d9b",
"6d9c",
"6d9d"... | 33 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
55,
9057,
168,
29,
107
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | UDP-galactopyranose mutase, C-terminal | UDP-galactopyranose mutase, C-terminal | UDP-GalPyranose_mutase_C | 1 |
IPR015904 | 15,904 | Sulphide quinone-reductase | Sulphide_quinone_reductase | Family | 8,587 | false | false | In photolithouautotrophic and chemolithouautotrophic bacteria that utilise sulphide as a hydrogen source, Sulphide Quinone Reductase (SQR) is critical in the initial oxidation step of sulphide. The electrons generated from the oxidation of sulphide are used to generate NADH. SQR is a member of the disulphide containing... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR10632"
] | [
""
] | [
8587
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME"
] | [
"1.8.5.8",
"PWY-7927",
"R-HSA-1614517",
"R-MMU-1614517"
] | [
"EC:1.8.5.8",
"METACYC:PWY-7927",
"REACTOME:R-HSA-1614517",
"REACTOME:R-MMU-1614517"
] | 4 | [
"6mo6",
"6mp5",
"6oi5",
"6oi6",
"6oib",
"6oic",
"6wh6",
"6ynv",
"6ynx",
"6yny",
"6ynz",
"8dhk"
] | 12 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
4764,
3741,
49,
33
] | 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",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
8,
4,
1,
9,
4,
1,
6,
1
] | 8 | true | Family | Sulphide quinone-reductase | Sulphide quinone-reductase | Sulphide_quinone_reductase | 1 |
IPR015908 | 15,908 | Allantoicase domain | Allantoicase_dom | Domain | 7,345 | false | false | Allantoicase (also known as allantoate amidinohydrolase) is involved in purine degradation, facilitating the utilization of purines as secondary nitrogen sources under nitrogen-limiting conditions. While purine degradation converges to uric acid in all vertebrates, its further degradation varies from species to species... | [
"GO:0004037",
"GO:0000256"
] | [
"allantoicase activity",
"allantoin catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF03561"
] | [
"Allantoicase"
] | [
7345
] | 1 | [
"EC",
"METACYC"
] | [
"3.5.3.4",
"PWY-5697"
] | [
"EC:3.5.3.4",
"METACYC:PWY-5697"
] | 2 | [
"1o59",
"1sg3"
] | 2 | [
"PUB00029326",
"PUB00031044",
"PUB00053905",
"PUB00100275"
] | [
"15229895",
"15020593",
"11054555",
"12036579"
] | [
"Crystal structure of an allantoicase (YIR029W) from Saccharomyces cerevisiae at 2.4 A resolution.",
"Crystal structure of yeast allantoicase reveals a repeated jelly roll motif.",
"Human allantoicase gene: cDNA cloning, genomic organization and chromosome localization.",
"Genomic organization and chromosome ... | [
2004,
2004,
2000,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4362,
2935,
48
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
3,
1,
2,
1,
2,
1,
1
] | 7 | true | Domain | Allantoicase domain | Allantoicase domain | Allantoicase_dom | 6 |
IPR015910 | 15,910 | Inosine/uridine-preferring nucleoside hydrolase, conserved site | I/U_nuclsd_hydro_CS | Conserved_site | 7,316 | false | false | Inosine-uridine preferring nucleoside hydrolase ( ) (IU-nucleoside hydrolase or IUNH) is an enzyme first identified in protozoan [ ] that catalyzes the hydrolysis of all of the commonly occurring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as subst... | [
"GO:0016799"
] | [
"hydrolase activity, hydrolyzing N-glycosyl compounds"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01247"
] | [
"IUNH"
] | [
7316
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00960"
] | [
"PROSITEDOC:PDOC00960"
] | 1 | [
"1ezr",
"1mas",
"1q8f",
"1yoe",
"2mas",
"3b9x",
"3g5i",
"3mkm",
"3mkn",
"3t8i",
"5tsq",
"8ctm",
"8rih"
] | 13 | [
"PUB00000434",
"PUB00000435"
] | [
"8634237",
"8634238"
] | [
"Inosine-uridine nucleoside hydrolase from Crithidia fasciculata. Genetic characterization, crystallization, and identification of histidine 241 as a catalytic site residue.",
"Three-dimensional structure of the inosine-uridine nucleoside N-ribohydrolase from Crithidia fasciculata."
] | [
1996,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Microbacterium phage OscarSo",
"metagenomes"
] | [
86,
6799,
369,
1,
61
] | 5 | [
"Escherichia coli (strain K12)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
3,
1,
1,
1
] | 4 | true | Conserved_site | Inosine/uridine-preferring nucleoside hydrolase, conserved site | Inosine/uridine-preferring nucleoside hydrolase, conserved site | I/U_nuclsd_hydro_CS | 5 |
IPR015911 | 15,911 | Phosphoglycerate kinase, conserved site | Phosphoglycerate_kinase_CS | Conserved_site | 26,754 | false | false | Phosphoglycerate kinase ( ) (PGK) is an enzyme that catalyses the formation of ATP to ADP and vice versa. In the second step of the second phase in glycolysis, 1,3-diphosphoglycerate is converted to 3-phosphoglycerate, forming one molecule of ATP. If the reverse were to occur, one molecule of ADP would be formed. This ... | [
"GO:0004618",
"GO:0006096"
] | [
"phosphoglycerate kinase activity",
"glycolytic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00111"
] | [
"PGLYCERATE_KINASE"
] | [
26754
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REAC... | [
"2.7.2.3",
"PWY-1042",
"PWY-5484",
"PWY-6886",
"PWY-6901",
"PWY-7003",
"PWY-8004",
"PWY-8404",
"PDOC00102",
"R-BTA-70171",
"R-BTA-70263",
"R-CEL-70171",
"R-CEL-70263",
"R-DDI-70171",
"R-DDI-70263",
"R-DME-70171",
"R-DME-70263",
"R-GGA-352875",
"R-GGA-352882",
"R-HSA-70171",
"... | [
"EC:2.7.2.3",
"METACYC:PWY-1042",
"METACYC:PWY-5484",
"METACYC:PWY-6886",
"METACYC:PWY-6901",
"METACYC:PWY-7003",
"METACYC:PWY-8004",
"METACYC:PWY-8404",
"PROSITEDOC:PDOC00102",
"REACTOME:R-BTA-70171",
"REACTOME:R-BTA-70263",
"REACTOME:R-CEL-70171",
"REACTOME:R-CEL-70263",
"REACTOME:R-DDI-... | 34 | [
"13pk",
"16pk",
"1fw8",
"1hdi",
"1kf0",
"1ltk",
"1php",
"1qpg",
"1v6s",
"1vjc",
"1vjd",
"1vpe",
"1zmr",
"2cun",
"2ie8",
"2p9q",
"2p9t",
"2paa",
"2wzb",
"2wzc",
"2wzd",
"2x13",
"2x14",
"2x15",
"2xe6",
"2xe7",
"2xe8",
"2y3i",
"2ybe",
"2zgv",
"3c39",
"3c3a"... | 68 | [
"PUB00006255",
"PUB00006482",
"PUB00006511"
] | [
"2124145",
"6689547",
"10593256"
] | [
"Flexibility and folding of phosphoglycerate kinase.",
"Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects.",
"Folding funnels and conformational transitions via hinge-bending motions."
] | [
1990,
1983,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
519,
19953,
5858,
424
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
5,
1,
1,
6,
1,
7,
4,
1,
9,
5,
1,
1,
15
] | 13 | true | Conserved_site | Phosphoglycerate kinase, conserved site | Phosphoglycerate kinase, conserved site | Phosphoglycerate_kinase_CS | 5 |
IPR015912 | 15,912 | Phosphofructokinase, conserved site | Phosphofructokinase_CS | Conserved_site | 27,820 | false | false | The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes [ ]. One enzyme that utilises this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the... | [
"GO:0003872",
"GO:0006096"
] | [
"6-phosphofructokinase activity",
"glycolytic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00433"
] | [
"PHOSPHOFRUCTOKINASE"
] | [
27820
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.11",
"PWY-1042",
"PWY-1861",
"PWY-5484",
"PWY-7385",
"PDOC00336",
"R-BTA-6798695",
"R-BTA-70171",
"R-CEL-6798695",
"R-CEL-70171",
"R-DME-6798695",
"R-DME-70171",
"R-HSA-6798695",
"R-HSA-70171",
"R-MMU-6798695",
"R-MMU-70171",
"R-RNO-6798695",
"R-RNO-70171",
"R-SCE-6798695"... | [
"EC:2.7.1.11",
"METACYC:PWY-1042",
"METACYC:PWY-1861",
"METACYC:PWY-5484",
"METACYC:PWY-7385",
"PROSITEDOC:PDOC00336",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70171",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-70171",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-70171",
"REACTOME:R-HSA-6798695... | 22 | [
"1mto",
"1pfk",
"1zxx",
"2pfk",
"3o8l",
"3o8n",
"3o8o",
"3opy",
"3pfk",
"3u39",
"4a3s",
"4i36",
"4i4i",
"4i7e",
"4omt",
"4pfk",
"4rh3",
"4u1r",
"4wl0",
"4xyj",
"4xyk",
"4xz2",
"5xoe",
"5xz6",
"5xz7",
"5xz8",
"5xz9",
"5xza",
"6pfk",
"7lw1",
"7tff",
"8w2g"... | 35 | [
"PUB00000020",
"PUB00003237",
"PUB00004002",
"PUB00014238"
] | [
"7825568",
"2975709",
"2953977",
"12023862"
] | [
"Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency.",
"Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products.",
"Mutations in the active site of Escheric... | [
1995,
1988,
1987,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctx254",
"metagenomes"
] | [
53,
17439,
9998,
1,
329
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
... | [
2,
28,
6,
1,
25,
8,
1,
22,
2,
1
] | 10 | true | Conserved_site | Phosphofructokinase, conserved site | Phosphofructokinase, conserved site | Phosphofructokinase_CS | 4 |
IPR015914 | 15,914 | Purple acid phosphatase, N-terminal | PAPs_N | Domain | 23,776 | false | false | This domain is found at the N-terminal of purple acid phosphatase proteins (PAPs) and related acid phosphatase proteins. This typically adopts an immunoglobulin-like β-sandwich fold. Purple acid phosphatases (PAPs) ( ) are a family of binuclear metallohydrolases that break down phosphate esters and anhydrides in acidic... | [
"GO:0003993",
"GO:0046872"
] | [
"acid phosphatase activity",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF16656"
] | [
"Pur_ac_phosph_N"
] | [
23776
] | 1 | [
"EC",
"METACYC"
] | [
"3.1.3.2",
"PWY-6348"
] | [
"EC:3.1.3.2",
"METACYC:PWY-6348"
] | 2 | [
"1kbp",
"1xzw",
"2qfp",
"2qfr",
"3kbp",
"3zk4",
"4dhl",
"4dsy",
"4dt2",
"4kbp",
"6g46",
"6git",
"6giz",
"6gj2",
"6gj9",
"6gja",
"6hwr",
"6of5",
"6ofd",
"6py9",
"6vj7",
"8brn"
] | 22 | [
"PUB00010641",
"PUB00010642",
"PUB00089454",
"PUB00089455",
"PUB00160375"
] | [
"12440878",
"10510276",
"7770774",
"16793224",
"37985663"
] | [
"New insights into the mechanism of purple acid phosphatase through (1)H NMR spectroscopy of the recombinant human enzyme.",
"Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybean.",
"Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn... | [
2002,
1999,
1995,
2006,
2023
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
80,
7720,
15866,
2,
108
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
77,
8,
1,
4,
3,
3,
2,
73,
3,
90
] | 10 | true | Domain | Purple acid phosphatase, N-terminal | Purple acid phosphatase, N-terminal | PAPs_N | 8 |
IPR015917 | 15,917 | Peptidase C14A, caspase catalytic domain | Pept_C14A | Domain | 21,835 | false | false | This entry represents the C-terminal conserved domain found in caspases mostly from animals. This domain includes the core of p45 (45kDa) precursor of caspases, which can be processed to produce the active p20 (20kDa) and p10 (10kDa) subunits. | [
"GO:0008234"
] | [
"cysteine-type peptidase activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS",
"SMART",
"CDD"
] | [
"PR00376",
"SM00115",
"cd00032"
] | [
"IL1BCENZYME",
"CASc",
"CASc"
] | [
19024,
21426,
13122
] | 3 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.22",
"R-BTA-5620971",
"R-CEL-111465",
"R-CEL-140342",
"R-CEL-198323",
"R-CEL-2028269",
"R-CEL-264870",
"R-CEL-351906",
"R-CEL-418889",
"R-CEL-5357905",
"R-DME-111458",
"R-DME-111459",
"R-DME-111465",
"R-DME-111469",
"R-DME-140342",
"R-DME-198323",
"R-DME-2028269",
"R-DME-21439... | [
"EC:3.4.22",
"REACTOME:R-BTA-5620971",
"REACTOME:R-CEL-111465",
"REACTOME:R-CEL-140342",
"REACTOME:R-CEL-198323",
"REACTOME:R-CEL-2028269",
"REACTOME:R-CEL-264870",
"REACTOME:R-CEL-351906",
"REACTOME:R-CEL-418889",
"REACTOME:R-CEL-5357905",
"REACTOME:R-DME-111458",
"REACTOME:R-DME-111459",
"... | 145 | [
"1bmq",
"1cp3",
"1f1j",
"1f9e",
"1gfw",
"1gqf",
"1i3o",
"1i4e",
"1i4o",
"1i51",
"1ibc",
"1ice",
"1jxq",
"1k86",
"1k88",
"1kmc",
"1m72",
"1nme",
"1nmq",
"1nms",
"1nw9",
"1pau",
"1pyo",
"1qdu",
"1qtn",
"1qx3",
"1re1",
"1rhj",
"1rhk",
"1rhm",
"1rhq",
"1rhr"... | 322 | [
"PUB00011704",
"PUB00014747",
"PUB00014748",
"PUB00015006",
"PUB00015008"
] | [
"11517925",
"15077141",
"15066636",
"10578171",
"10872455"
] | [
"Evolutionary lines of cysteine peptidases.",
"Caspase activation - stepping on the gas or releasing the brakes? Lessons from humans and flies.",
"Death without caspases, caspases without death.",
"Caspase structure, proteolytic substrates, and function during apoptotic cell death.",
"Mammalian caspases: st... | [
2001,
2004,
2004,
1999,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Ascovirus",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
6,
944,
20880,
5
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
57,
12,
58,
39,
49
] | 6 | true | Domain | Peptidase C14A, caspase catalytic domain | Peptidase C14A, caspase catalytic domain | Pept_C14A | 3 |
IPR015919 | 15,919 | Cadherin-like superfamily | Cadherin-like_sf | Homologous_superfamily | 160,134 | false | false | This entry represents domains with an immunoglobulin-like β-sandwich fold, consisting of 7 strands in two sheets with a Greek key topology. Such domains are found in cadherin, as well as at the N-terminal of dystroglycan. Dystroglycan is a cell surface receptor consisting of two subunits: alpha-dystroglycan, extracellu... | [
"GO:0005509",
"GO:0016020"
] | [
"calcium ion binding",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"SSF"
] | [
"SSF49313"
] | [
""
] | [
160134
] | 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-418990",
"R-CEL-351906",
"R-CEL-6798695",
"R-CEL-6809371",
"R-CEL-9013404",
"R-CEL-9013408",
"R-CEL-9013423",
"R-CFA-1474228",
"R-CFA-216083",
"R-CFA-351906",
"R-CFA-418990",
"R-CFA-6805567",
"R-CFA-6809371",
"R-CFA-8932504",
"R-CFA-8932505",
"R-CFA-8932506",
"R-CFA-9010553",
... | [
"REACTOME:R-BTA-418990",
"REACTOME:R-CEL-351906",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-6809371",
"REACTOME:R-CEL-9013404",
"REACTOME:R-CEL-9013408",
"REACTOME:R-CEL-9013423",
"REACTOME:R-CFA-1474228",
"REACTOME:R-CFA-216083",
"REACTOME:R-CFA-351906",
"REACTOME:R-CFA-418990",
"REACTOME:R-C... | 167 | [
"1edh",
"1ff5",
"1l3w",
"1ncg",
"1nch",
"1nci",
"1ncj",
"1o6s",
"1op4",
"1q1p",
"1q55",
"1q5a",
"1q5b",
"1q5c",
"1suh",
"1u2c",
"1wuz",
"1wyj",
"1zvn",
"1zxk",
"2a4c",
"2a4e",
"2a62",
"2ee0",
"2kpn",
"2o72",
"2omt",
"2omu",
"2omv",
"2omw",
"2omx",
"2omy"... | 255 | [
"PUB00000071",
"PUB00007174",
"PUB00009704",
"PUB00014193",
"PUB00031647",
"PUB00036004"
] | [
"2197976",
"11736639",
"11909544",
"14570569",
"15326183",
"16410545"
] | [
"Cadherins: a molecular family important in selective cell-cell adhesion.",
"Structure and functions of classical cadherins.",
"Cadherin-like domains in alpha-dystroglycan, alpha/epsilon-sarcoglycan and yeast and bacterial proteins.",
"Cadherins as modulators of cellular phenotype.",
"The structure of the N... | [
1990,
2001,
2002,
2003,
2004,
2006
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
254,
19081,
140119,
73,
607
] | 5 | [
"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)"
] | [
31,
463,
54,
440,
379,
1,
400,
1
] | 8 | true | Homologous_superfamily | Cadherin-like superfamily | Cadherin-like superfamily | Cadherin-like_sf | 9 |
IPR015920 | 15,920 | Cellobiose dehydrogenase-like, cytochrome domain | Cellobiose_DH-like_cyt | Domain | 6,590 | false | false | Cellobiose dehydrogenase (CHD; ) is found in a variety of fungi, including white rot, brown rot and plant pathogen fungi. The enzyme is extracellular flavocytochrome that degrades both cellulose and lignin. Specifically, CDHs oxidize cellobiose, cellodextrins, and lactose to corresponding lactones, utilizing a variety ... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF16010",
"cd09630"
] | [
"CDH-cyt",
"CDH_like_cytochrome"
] | [
6531,
6385
] | 2 | [] | [] | [] | 0 | [
"1d7b",
"1d7c",
"1d7d",
"1pl3",
"4qi3",
"4qi6",
"4qi7",
"6jt6"
] | 8 | [
"PUB00016255",
"PUB00036005",
"PUB00044228",
"PUB00080637",
"PUB00154975"
] | [
"10673428",
"9920875",
"17878204",
"16787264",
"27338639"
] | [
"A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase.",
"Cellobiose dehydrogenase from the fungi Phanerochaete chrysosporium and Humicola insolens. A flavohemoprotein from Humicola insolens contains 6-hydroxy-FAD as the dominant active cofactor.",... | [
2000,
1999,
2007,
2006,
2016
] | 5 | [
"IPR005018"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
6590
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
8
] | 1 | true | Domain | Cellobiose dehydrogenase-like, cytochrome domain | Cellobiose dehydrogenase-like, cytochrome domain | Cellobiose_DH-like_cyt | 3 |
IPR015925 | 15,925 | Ryanodine/Inositol 1,4,5-trisphosphate receptor | Ryanodine_IP3_receptor | Family | 23,595 | false | false | The ryanodine and inositol 1,4,5-triphosphate (IP3) receptors are intracellular Ca2+ release channels characterised by their large size and 4-fold symmetry [ ]. In excitation-contraction coupling of skeletal and heart muscle, the ryanodine receptor serves as a Ca2+ release channel of sarcoplasmic reticulum (SR) and is ... | [
"GO:0006816"
] | [
"calcium ion transport"
] | [
"biological_process"
] | 1 | [
"PANTHER",
"PANTHER",
"PANTHER"
] | [
"PTHR13715",
"PTHR45816",
"PTHR46399"
] | [
"",
"",
""
] | [
3093,
8177,
12325
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-114508",
"R-CEL-139853",
"R-CEL-381676",
"R-CEL-5578775",
"R-CEL-9717207",
"R-CEL-983695",
"R-DDI-114508",
"R-DDI-139853",
"R-DDI-5578775",
"R-DDI-9717207",
"R-DME-114508",
"R-DME-139853",
"R-DME-381676",
"R-DME-5578775",
"R-DME-9717207",
"R-DME-983695",
"R-HSA-112043",
"R-H... | [
"REACTOME:R-CEL-114508",
"REACTOME:R-CEL-139853",
"REACTOME:R-CEL-381676",
"REACTOME:R-CEL-5578775",
"REACTOME:R-CEL-9717207",
"REACTOME:R-CEL-983695",
"REACTOME:R-DDI-114508",
"REACTOME:R-DDI-139853",
"REACTOME:R-DDI-5578775",
"REACTOME:R-DDI-9717207",
"REACTOME:R-DME-114508",
"REACTOME:R-DME... | 49 | [
"1n4k",
"1xzz",
"2bcx",
"2mc2",
"2xoa",
"3hsm",
"3ila",
"3im5",
"3im6",
"3im7",
"3j8h",
"3jav",
"3jrr",
"3nrt",
"3qr5",
"3rqr",
"3t8s",
"3uj0",
"3uj4",
"4ert",
"4erv",
"4esu",
"4ett",
"4etu",
"4etv",
"4i0y",
"4i1e",
"4i2s",
"4i37",
"4i3n",
"4i6i",
"4i7i"... | 284 | [
"PUB00035217",
"PUB00035218",
"PUB00035219",
"PUB00035220",
"PUB00035221",
"PUB00035222",
"PUB00035223"
] | [
"2660829",
"12765683",
"8010750",
"1426638",
"1562172",
"1648106",
"2455801"
] | [
"Biochemistry and biophysics of excitation-contraction coupling.",
"Retrograde activation of store-operated calcium channel.",
"Structure and development of E-C coupling units in skeletal muscle.",
"Structural analysis of muscle development: transverse tubules, sarcoplasmic reticulum, and the triad.",
"Char... | [
1989,
2003,
1994,
1992,
1992,
1991,
1988
] | 7 | [] | [
"IPR000493"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
154,
23426,
3,
12
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
18,
108,
11,
65,
40,
53
] | 6 | true | Family | Ryanodine/Inositol 1,4,5-trisphosphate receptor | Ryanodine/Inositol 1,4,5-trisphosphate receptor | Ryanodine_IP3_receptor | 8 |
IPR015926 | 15,926 | Cytolysin/lectin | Cytolysin/lectin | Homologous_superfamily | 2,551 | false | false | This entry represents a β-sandwich domain consisting of 10 strands in two sheets that is found in anemone pore-forming cytolysin, in fungal fruit body lectin and in similar eucaryotic sequences. Sea anemones are a rich source of lethal pore-forming peptides and proteins, known collectively as cytolysins or actinoporins... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.60.270.20",
"SSF63724"
] | [
"",
""
] | [
2458,
2484
] | 2 | [] | [] | [] | 0 | [
"1gwy",
"1iaz",
"1kd6",
"1o71",
"1o72",
"1tzq",
"1x99",
"1xi0",
"1y2t",
"1y2u",
"1y2v",
"1y2w",
"1y2x",
"2ks4",
"2l2b",
"2l38",
"2ofc",
"2ofd",
"2ofe",
"3lim",
"3qds",
"3qdt",
"3qdu",
"3qdv",
"3qdw",
"3qdx",
"3qdy",
"3vwi",
"3w9p",
"3zwg",
"3zwj",
"4jox"... | 59 | [
"PUB00013118",
"PUB00013268",
"PUB00013454",
"PUB00015244",
"PUB00015246",
"PUB00032353",
"PUB00076863"
] | [
"12450118",
"11827489",
"12787928",
"11689232",
"14604522",
"15561152",
"19674339"
] | [
"Two genes encoding fruit body lectins of Pleurotus cornucopiae: sequence similarity with the lectin of a nematode-trapping fungus.",
"Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: implications for pore formation.",
"Xerocomus chrysenteron lectin: identification of a new pesticidal... | [
2002,
2002,
2003,
2002,
2003,
2004,
2009
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"virus sp. ctiha2"
] | [
15,
2535,
1
] | 3 | [
"Danio rerio",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
5,
1
] | 2 | true | Homologous_superfamily | Cytolysin/lectin | Cytolysin/lectin | Cytolysin/lectin | 9 |
IPR015931 | 15,931 | Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomain 1/3 | Acnase/IPM_dHydase_lsu_aba_1/3 | Homologous_superfamily | 87,314 | 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 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.499.10"
] | [
""
] | [
87314
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"4.2.1",
"4.2.1.33",
"R-BTA-71403",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-389542",
"R-CEL-71403",
"R-CEL-917937",
"R-CEL-9837999",
"R-CEL-9854311",
"R-DDI-389542",
"R-DDI-71403",
"R-DDI-917937",
"R-DDI-9837999",
"R-DDI-9854311",
"R-HSA-1268020",
"R-HSA-389542",
"R-HSA-71403",
... | [
"EC:4.2.1",
"EC:4.2.1.33",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-389542",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-917937",
"REACTOME:R-CEL-9837999",
"REACTOME:R-CEL-9854311",
"REACTOME:R-DDI-389542",
"REACTOME:R-DDI-71403",
"REACTOME:R-DD... | 39 | [
"1aco",
"1ami",
"1amj",
"1b0j",
"1b0k",
"1b0m",
"1c96",
"1c97",
"1fgh",
"1l5j",
"1nis",
"1nit",
"2b3x",
"2b3y",
"3sn2",
"3snp",
"4kp1",
"4kp2",
"4nqy",
"5acn",
"6acn",
"6vcd",
"7acn",
"8acn"
] | 24 | [
"PUB00005471",
"PUB00016210",
"PUB00032014",
"PUB00033924",
"PUB00036012",
"PUB00036013",
"PUB00036014",
"PUB00036015",
"PUB00036016",
"PUB00036017",
"PUB00036018",
"PUB00036019",
"PUB00036021",
"PUB00036023",
"PUB00082326"
] | [
"9020582",
"9813279",
"15522288",
"1400210",
"16850017",
"10087914",
"15877277",
"17513696",
"15882410",
"15009904",
"17185597",
"16407072",
"15604397",
"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,
1999,
2005,
2007,
2005,
2004,
2006,
2006,
2004,
2006,
2010
] | 15 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2147,
63885,
19659,
1623
] | 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",... | [
19,
2,
5,
11,
4,
31,
7,
4,
12,
15,
4,
5,
105
] | 13 | true | Homologous_superfamily | Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomain 1/3 | Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomain 1/3 | Acnase/IPM_dHydase_lsu_aba_1/3 | 1 |
IPR015932 | 15,932 | Aconitase, domain 2 | Aconitase_dom2 | Homologous_superfamily | 19,336 | 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 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.1060.10"
] | [
""
] | [
19336
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"4.2.1",
"4.2.1.3",
"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-9837999",
"R-MMU-9854311",
... | [
"EC:4.2.1",
"EC:4.2.1.3",
"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-HSA-1268020",
"REACTOME:R-... | 27 | [
"1aco",
"1ami",
"1amj",
"1b0j",
"1b0k",
"1b0m",
"1c96",
"1c97",
"1fgh",
"1l5j",
"1nis",
"1nit",
"5acn",
"6acn",
"7acn",
"8acn"
] | 16 | [
"PUB00005471",
"PUB00016210",
"PUB00032014",
"PUB00033924",
"PUB00036012",
"PUB00036013",
"PUB00036014",
"PUB00036015",
"PUB00036016",
"PUB00036017",
"PUB00036018",
"PUB00036019",
"PUB00036021",
"PUB00036023",
"PUB00082326"
] | [
"9020582",
"9813279",
"15522288",
"1400210",
"16850017",
"10087914",
"15877277",
"17513696",
"15882410",
"15009904",
"17185597",
"16407072",
"15604397",
"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,
1999,
2005,
2007,
2005,
2004,
2006,
2006,
2004,
2006,
2010
] | 15 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
97,
12060,
7009,
170
] | 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,
2,
2,
20,
2,
2,
4,
2,
2
] | 10 | true | Homologous_superfamily | Aconitase, domain 2 | Aconitase, domain 2 | Aconitase_dom2 | 6 |
IPR015933 | 15,933 | Aconitase B, HEAT-like domain | Aconitase_B_HEAT-like_dom | Domain | 8,564 | 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... | [
"GO:0003994",
"GO:0006099"
] | [
"aconitate hydratase activity",
"tricarboxylic acid cycle"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF11791"
] | [
"Aconitase_B_N"
] | [
8564
] | 1 | [
"EC",
"EC",
"METACYC"
] | [
"4.2.1.3",
"4.2.1.99",
"PWY-5747"
] | [
"EC:4.2.1.3",
"EC:4.2.1.99",
"METACYC:PWY-5747"
] | 3 | [
"1l5j"
] | 1 | [
"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 | [
"Bacteria",
"Eukaryota",
"Methanosarcinales",
"metagenomes"
] | [
8347,
129,
8,
80
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Aconitase B, HEAT-like domain | Aconitase B, HEAT-like domain | Aconitase_B_HEAT-like_dom | 1 |
IPR015938 | 15,938 | Glycine N-acyltransferase, N-terminal | Glycine_N-acyltransferase_N | Domain | 2,420 | false | false | This entry represents glycine N-acyltransferase (also called aralkyl acyl-CoA:amino acid N-acyltransferase; ). Mitochondrial acyltransferases catalyse the transfer of an acyl group from acyl-CoA to the N terminus of glycine to produce N-acylglycine. These enzymes can conjugate a multitude of substrates to form a variet... | [
"GO:0047961",
"GO:0005739"
] | [
"glycine N-acyltransferase activity",
"mitochondrion"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF06021"
] | [
"Gly_acyl_tr_N"
] | [
2420
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1.13",
"R-HSA-177128",
"R-HSA-177135",
"R-HSA-9749641",
"R-MMU-177128",
"R-MMU-177135",
"R-MMU-9749641",
"R-RNO-177128",
"R-RNO-177135",
"R-RNO-9749641"
] | [
"EC:2.3.1.13",
"REACTOME:R-HSA-177128",
"REACTOME:R-HSA-177135",
"REACTOME:R-HSA-9749641",
"REACTOME:R-MMU-177128",
"REACTOME:R-MMU-177135",
"REACTOME:R-MMU-9749641",
"REACTOME:R-RNO-177128",
"REACTOME:R-RNO-177135",
"REACTOME:R-RNO-9749641"
] | 10 | [
"7pk0",
"7pk1",
"7pk2"
] | 3 | [
"PUB00036032",
"PUB00036033"
] | [
"10630424",
"8660675"
] | [
"The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase.",
"Fatty acid amide biosynthesis: a possible new role for peptidylglycine alpha-amidating enzyme and acyl-coenzyme A: glycine N-acyltransferase."
] | [
2000,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
2420
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
15,
7,
9
] | 4 | true | Domain | Glycine N-acyltransferase, N-terminal | Glycine N-acyltransferase, N-terminal | Glycine_N-acyltransferase_N | 4 |
IPR015939 | 15,939 | Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal | Fum_Rdtase/Succ_DH_flav-like_C | Domain | 56,940 | false | false | This entry represents a domain with a spectrin-repeat-like fold consisting of three helices in a closed bundle with a left-handed twist. This domain is found in the succinate dehydrogenase/fumarate reductase oxidoreductase family of proteins, such as: L-aspartate oxidase ( ), a flavoenzyme component of the bacterial qu... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02910"
] | [
"Succ_DH_flav_C"
] | [
56940
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-71403",
"R-CEL-9854311",
"R-DDI-71403",
"R-DDI-9854311",
"R-DME-71403",
"R-DME-9854311",
"R-DRE-71403",
"R-DRE-9854311",
"R-GGA-372987",
"R-HSA-611105",
"R-HSA-71403",
"R-HSA-9854311",
"R-MMU-71403",
"R-MMU-9854311",
"R-RNO-71403",
"R-RNO-9854311",
"R-SCE-71403",
"R-SCE-9854... | [
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-9854311",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-9854311",
"REACTOME:R-DME-71403",
"REACTOME:R-DME-9854311",
"REACTOME:R-DRE-71403",
"REACTOME:R-DRE-9854311",
"REACTOME:R-GGA-372987",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-71403",
"REACTOME:R-HSA-9854... | 24 | [
"1chu",
"1e7p",
"1jnr",
"1jnz",
"1kf6",
"1kfy",
"1knp",
"1knr",
"1l0v",
"1nek",
"1nen",
"1qlb",
"1yq3",
"1yq4",
"1zoy",
"1zp0",
"2acz",
"2b76",
"2bs2",
"2bs3",
"2bs4",
"2e5v",
"2fbw",
"2fja",
"2fjb",
"2fjd",
"2fje",
"2h88",
"2h89",
"2wdq",
"2wdr",
"2wdv"... | 115 | [
"PUB00013184",
"PUB00015752",
"PUB00023955",
"PUB00026455",
"PUB00026780"
] | [
"11850430",
"12560550",
"10425677",
"11842205",
"11863440"
] | [
"Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.",
"Architecture of succinate dehydrogenase and reactive oxygen species generation.",
"Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase ox... | [
2002,
2003,
1999,
2002,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
1156,
47932,
6817,
1034,
1
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
9,
2,
3,
2,
3,
7,
1,
1,
5,
4,
2,
1,
20
] | 13 | true | Domain | Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal | Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal | Fum_Rdtase/Succ_DH_flav-like_C | 5 |
IPR015940 | 15,940 | Ubiquitin-associated domain | UBA | Domain | 106,179 | false | false | UBA domains are a commonly occurring sequence motif of approximately 45 amino acid residues that are found in diverse proteins involved in the ubiquitin/proteasome pathway, DNA excision-repair, and cell signalling via protein kinases [ ]. The human homologue of yeast Rad23A is one example of a nucleotide excision-repai... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00627",
"PF22562",
"PF22567",
"PS50030",
"SM00165"
] | [
"UBA",
"UBA_7",
"UBA_9",
"UBA",
"UBA"
] | [
46838,
15989,
1094,
102002,
73987
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50030",
"R-BTA-532668",
"R-BTA-5689877",
"R-BTA-5689880",
"R-BTA-5693565",
"R-BTA-5696394",
"R-BTA-5696395",
"R-BTA-8866652",
"R-BTA-8948751",
"R-BTA-983168",
"R-CEL-5673000",
"R-CEL-5674135",
"R-CEL-5675221",
"R-CEL-5689880",
"R-CEL-8856825",
"R-CEL-9856649",
"R-DDI-5689880",
... | [
"PROSITEDOC:PDOC50030",
"REACTOME:R-BTA-532668",
"REACTOME:R-BTA-5689877",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-5693565",
"REACTOME:R-BTA-5696394",
"REACTOME:R-BTA-5696395",
"REACTOME:R-BTA-8866652",
"REACTOME:R-BTA-8948751",
"REACTOME:R-BTA-983168",
"REACTOME:R-CEL-5673000",
"REACTOME:R-... | 205 | [
"1dv0",
"1f4i",
"1ify",
"1oqy",
"1q02",
"1qze",
"1veg",
"1vej",
"1vek",
"1vg5",
"1wgn",
"1whc",
"1wiv",
"1wj7",
"1wji",
"1wr1",
"1y8g",
"1yla",
"1z96",
"1zmu",
"1zmv",
"1zmw",
"2bwb",
"2bwe",
"2cos",
"2cp8",
"2cpw",
"2crn",
"2cwb",
"2d9s",
"2dag",
"2dah"... | 136 | [
"PUB00003958",
"PUB00005450",
"PUB00006344",
"PUB00007089",
"PUB00024785",
"PUB00029556",
"PUB00032304",
"PUB00061440",
"PUB00065904"
] | [
"9846873",
"8871400",
"8596629",
"12079361",
"11087358",
"14557549",
"15837191",
"20826778",
"22405001"
] | [
"Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr.",
"The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway.",
"The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.",
"Solution structures of UBA domains revea... | [
1998,
1996,
1996,
2002,
2000,
2003,
2005,
2010,
2012
] | 9 | [] | [
"IPR033382",
"IPR033741",
"IPR033864",
"IPR035467",
"IPR041811",
"IPR041812",
"IPR041915",
"IPR041917",
"IPR041918",
"IPR041923",
"IPR041926",
"IPR041927",
"IPR041928",
"IPR041969",
"IPR041970",
"IPR041971",
"IPR041974",
"IPR042599",
"IPR042614",
"IPR042615",
"IPR047878",
"... | 0 | 24 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
7,
568,
105564,
13,
27
] | 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... | [
159,
33,
289,
75,
196,
146,
10,
81,
238,
8,
10,
239
] | 12 | true | Domain | Ubiquitin-associated domain | Ubiquitin-associated domain | UBA | 8 |
IPR015942 | 15,942 | Asp/Glu/hydantoin racemase | Asp/Glu/hydantoin_racemase | Family | 53,703 | false | false | This entry represents a group of related proteins that includes aspartate racemase, glutamate racemase, hydantoin racemase and arylmalonate decarboxylase. Two conserved cysteines are present in the sequence of these enzymes. They play a role in catalytic activity by acting as bases in proton abstraction from the substr... | [
"GO:0047661"
] | [
"amino-acid racemase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01177"
] | [
"Asp_Glu_race"
] | [
53703
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC"
] | [
"5.1.1.3",
"GenProp1448",
"PWY-6386",
"PWY-6387"
] | [
"EC:5.1.1.3",
"GP:GenProp1448",
"METACYC:PWY-6386",
"METACYC:PWY-6387"
] | 4 | [
"1b73",
"1b74",
"1iu9",
"1jfl",
"1zuw",
"2dwu",
"2dx7",
"2eq5",
"2gzm",
"2jfn",
"2jfo",
"2jfp",
"2jfq",
"2jfu",
"2jfv",
"2jfw",
"2jfx",
"2jfy",
"2jfz",
"2ohg",
"2oho",
"2ohv",
"2vvt",
"2w4i",
"2zsk",
"3hfr",
"3ist",
"3isv",
"3ojc",
"3out",
"3qvj",
"3qvk"... | 64 | [
"PUB00000380",
"PUB00055747",
"PUB00083212",
"PUB00094355"
] | [
"8385993",
"21616082",
"17132860",
"26555188"
] | [
"Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus.",
"Characterization of the Structure and Function of Klebsiella pneumoniae Allantoin Racemase.",
"Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from ... | [
1993,
2011,
2006,
2015
] | 4 | [] | [
"IPR004380",
"IPR004391"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctjdk2",
"unclassified sequences"
] | [
324,
49055,
3588,
1,
735
] | 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"
] | [
5,
2,
1,
3,
1,
2,
6
] | 7 | true | Family | Asp/Glu/hydantoin racemase | Asp/Glu/hydantoin racemase | Asp/Glu/hydantoin_racemase | 8 |
IPR015943 | 15,943 | WD40/YVTN repeat-like-containing domain superfamily | WD40/YVTN_repeat-like_dom_sf | Homologous_superfamily | 1,418,655 | false | false | This superfamily represents a WD40/YVTN repeat-like domain. Both the WD40 and the YVTN repeated motifs consist of about 40 residues, and although they consist of distinct sequences, they do share a similar structure. Structurally, both the WD40 and the YVTN repeated motifs form seven-bladed propellers (although some me... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:2.130.10.10"
] | [
""
] | [
1418655
] | 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-1296041",
"R-BTA-141430",
"R-BTA-141444",
"R-BTA-1538133",
"R-BTA-156827",
"R-BTA-159227",
"R-BTA-159230",
"R-BTA-159231",
"R-BTA-159236",
"R-BTA-1632852",
"R-BTA-165159",
"R-BTA-166208",
"R-BTA-168638",
"R-BTA-170822",
"R-BTA-174184",
"R-BTA-176409",
"R-BTA-177929",
"R-BTA-... | [
"REACTOME:R-BTA-1296041",
"REACTOME:R-BTA-141430",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-1538133",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-159227",
"REACTOME:R-BTA-159230",
"REACTOME:R-BTA-159231",
"REACTOME:R-BTA-159236",
"REACTOME:R-BTA-1632852",
"REACTOME:R-BTA-165159",
"REACTOME:R-BTA-... | 1,643 | [
"1a0r",
"1b9x",
"1b9y",
"1erj",
"1fwx",
"1gg2",
"1got",
"1gp2",
"1gxr",
"1jju",
"1jmx",
"1jmz",
"1jof",
"1k32",
"1k8k",
"1l0q",
"1mae",
"1maf",
"1mda",
"1mg2",
"1mg3",
"1n6d",
"1n6e",
"1n6f",
"1nex",
"1nr0",
"1olz",
"1omw",
"1p22",
"1pby",
"1pev",
"1pgu"... | 3,980 | [
"PUB00012384",
"PUB00014157",
"PUB00022422",
"PUB00023573",
"PUB00024645",
"PUB00025413",
"PUB00029039",
"PUB00029204"
] | [
"9514722",
"12377130",
"12925784",
"10360181",
"10856245",
"12057191",
"12553912",
"15150269"
] | [
"Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution.",
"Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins.",
"Structure of the phenylhydrazine adduct of the quinohemoprotein... | [
1998,
2002,
2003,
1999,
2000,
2002,
2003,
2004
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
6685,
238586,
1166619,
648,
6117
] | 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",... | [
1432,
257,
1563,
546,
3,
1921,
1180,
151,
850,
1518,
126,
146,
2884
] | 13 | true | Homologous_superfamily | WD40/YVTN repeat-like-containing domain superfamily | WD40/YVTN repeat-like-containing domain superfamily | WD40/YVTN_repeat-like_dom_sf | 7 |
IPR015944 | 15,944 | Glycine-tRNA ligase, beta subunit | Gly-tRNA-synth_bsu | Family | 16,992 | false | false | This entry represents the beta subunit of glycine-tRNA ligase. The aminoacyl-tRNA synthetases ( ) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology [ ]. The 2... | [
"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 | [
"HAMAP",
"PFAM",
"PRINTS",
"NCBIFAM"
] | [
"MF_00255",
"PF02092",
"PR01045",
"TIGR00211"
] | [
"Gly_tRNA_synth_beta",
"tRNA_synt_2f",
"TRNASYNTHGB",
"glyS"
] | [
15923,
16991,
15316,
16333
] | 4 | [
"EC",
"GP"
] | [
"6.1.1.14",
"GenProp0258"
] | [
"EC:6.1.1.14",
"GP:GenProp0258"
] | 2 | [
"7eiv",
"7lu4",
"7xjy",
"7xjz",
"7xk0",
"7xk1",
"7xof",
"7yse",
"8h1c",
"8ie2"
] | 10 | [
"PUB00000386",
"PUB00002277",
"PUB00002392",
"PUB00002880",
"PUB00007191"
] | [
"8364025",
"7665503",
"6309809",
"7962006",
"2203971"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The glycyl-tRNA synthetase of Chlamydia trachomatis.",
"Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase.",
"Human glycyl-tRNA synthetase. Wide divergence of primary structure fro... | [
1993,
1995,
1983,
1994,
1990
] | 5 | [
"IPR006194"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3,
15710,
1003,
276
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
1,
3,
7
] | 4 | true | Family | Glycine-tRNA ligase, beta subunit | Glycine-tRNA ligase, beta subunit | Gly-tRNA-synth_bsu | 6 |
IPR015946 | 15,946 | K homology domain-like, alpha/beta | KH_dom-like_a/b | Homologous_superfamily | 245,338 | false | false | The K homology domain is a common RNA-binding motif present in one or multiple copies in both prokaryotic and eukaryotic regulatory proteins. The KH motifs may act cooperatively to bind RNA in the case of multiple motifs, or independently in the case of single KH motif proteins. Prokaryotic (pKH) and eukaryotic (eKH) K... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.300.20"
] | [
""
] | [
245338
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-9759... | 128 | [
"1ega",
"1fjg",
"1hh2",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1jos",
"1k0r",
"1kkg",
"1l2f",
"1lql",
"1mky",
"1ml5",
"1ml8",
"1n2f",
"1n32",
"1n33",
"1n34",
"1n36",
"1nye"... | 1,868 | [
"PUB00011737",
"PUB00011738",
"PUB00011739"
] | [
"11014182",
"10411886",
"11430821"
] | [
"Structure of the 30S ribosomal subunit.",
"Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif.",
"An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA."
] | [
2000,
1999,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
4281,
206063,
6,
30841,
4147
] | 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,
4,
5,
5,
7,
19,
15,
1,
19,
30,
1,
1,
51
] | 13 | true | Homologous_superfamily | K homology domain-like, alpha/beta | K homology domain-like, alpha/beta | KH_dom-like_a/b | 9 |
IPR015947 | 15,947 | PUA-like superfamily | PUA-like_sf | Homologous_superfamily | 211,818 | false | false | This superfamily represents domains with a PUA-like structure, consisting of a pseudo-barrel composed of mixed folded sheets of five strands. This structural motif is found in: PUA-containing proteins. The N-terminal of ATP sulphurylases, which contains extra structures, some similar to the PK β-barrel domain [ ]. Seve... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF88697"
] | [
""
] | [
211818
] | 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-9033241",
"R-CEL-171319",
"R-CEL-174362",
"R-CEL-9837999",
"R-DDI-171319",
"R-DME-171319",
"R-DME-9837999",
"R-GGA-417076",
"R-HSA-171319",
"R-HSA-174362",
"R-HSA-2408550",
"R-HSA-3560796",
"R-HSA-3899300",
"R-HSA-390471",
"R-HSA-5334118",
"R-HSA-6782315",
"R-HSA-6790901",
"... | [
"REACTOME:R-BTA-9033241",
"REACTOME:R-CEL-171319",
"REACTOME:R-CEL-174362",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-171319",
"REACTOME:R-DME-171319",
"REACTOME:R-DME-9837999",
"REACTOME:R-GGA-417076",
"REACTOME:R-HSA-171319",
"REACTOME:R-HSA-174362",
"REACTOME:R-HSA-2408550",
"REACTOME:R-HSA... | 42 | [
"1g8f",
"1g8g",
"1g8h",
"1i2d",
"1iq8",
"1it7",
"1it8",
"1j2b",
"1j70",
"1jec",
"1jed",
"1jee",
"1jhd",
"1k8w",
"1m8p",
"1nxz",
"1q7h",
"1r3e",
"1r3f",
"1r6x",
"1s04",
"1sgv",
"1sqw",
"1t5y",
"1t62",
"1te7",
"1v47",
"1v6z",
"1vhk",
"1vhy",
"1wk2",
"1wmm"... | 337 | [
"PUB00003444",
"PUB00014132",
"PUB00029267",
"PUB00036063",
"PUB00036064",
"PUB00036065",
"PUB00036066"
] | [
"10093218",
"11157739",
"14517985",
"17803682",
"16793063",
"16407303",
"16943774"
] | [
"Novel predicted RNA-binding domains associated with the translation machinery.",
"Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation.",
"Functional assignment based on structural analysis: crystal structure of the yggJ protein (HI0303) of Haemophilus influenz... | [
1999,
2001,
2003,
2007,
2006,
2006,
2006
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5685,
129382,
73770,
368,
2613
] | 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",... | [
221,
6,
41,
23,
6,
73,
39,
9,
116,
75,
8,
8,
241
] | 13 | true | Homologous_superfamily | PUA-like superfamily | PUA-like superfamily | PUA-like_sf | 3 |
IPR015948 | 15,948 | Bacteriophage PRD1, P2, C-terminal | Phage_PRD1_P2_C | Homologous_superfamily | 9 | false | false | The absorption protein P2 (synonym: receptor-binding protein P2) from the bacteriophage PRD1 is a multi-β-sheet protein whose complicated topology forms an elongated seahorse-shaped molecule with a distinct head, containing a pseudo-β propeller structure with approximate 6-fold symmetry, and a tail (β-sandwich). It is ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.105.10.10"
] | [
""
] | [
9
] | 1 | [] | [] | [] | 0 | [
"1n7u",
"1n7v"
] | 2 | [
"PUB00029009"
] | [
"12623018"
] | [
"The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Alphatectivirus",
"Streptomyces cavernicola"
] | [
8,
1
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Bacteriophage PRD1, P2, C-terminal | Bacteriophage PRD1, P2, C-terminal | Phage_PRD1_P2_C | 4 |
IPR015949 | 15,949 | Bacteriophage PRD1, P2, N-terminal | Phage_PRD1_P2_N | Homologous_superfamily | 8 | false | false | The absorption protein P2 (synonym: receptor-binding protein P2) from the bacteriophage PRD1 is a multi-β-sheet protein whose complicated topology forms an elongated seahorse-shaped molecule with a distinct head, containing a pseudo-β propeller structure with approximate 6-fold symmetry, and a tail (β-sandwich). It is ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.70.250.10"
] | [
""
] | [
8
] | 1 | [] | [] | [] | 0 | [
"1n7u",
"1n7v"
] | 2 | [
"PUB00029009"
] | [
"12623018"
] | [
"The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Alphatectivirus"
] | [
8
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Bacteriophage PRD1, P2, N-terminal | Bacteriophage PRD1, P2, N-terminal | Phage_PRD1_P2_N | 6 |
IPR015950 | 15,950 | Chemokine-binding M3, subdomain 1, viral | Chemokine-bd_M3_sub1_vir | Homologous_superfamily | 7 | false | false | This entry represents a β-sandwich domain found in a group of viral chemokine binding proteins. These proteins bind with CC-chemokine MCP-1, acting as cytokine decoy receptors [ ]. For example, the murine herpesvirus decoy receptor M3 acts as an immune system saboteur by altering host anti-viral inflammatory repsonses.... | [
"GO:0019956"
] | [
"chemokine binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.40.1330"
] | [
""
] | [
7
] | 1 | [] | [] | [] | 0 | [
"1mkf",
"1ml0",
"2nyz",
"2nz1"
] | 4 | [
"PUB00027380"
] | [
"12419245"
] | [
"Structural basis of chemokine sequestration by a herpesvirus decoy receptor."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Rhadinovirus"
] | [
7
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Chemokine-binding M3, subdomain 1, viral | Chemokine-binding M3, subdomain 1, viral | Chemokine-bd_M3_sub1_vir | 7 |
IPR015951 | 15,951 | Chemokine-binding M3, subdomain 2, viral | Chemokine-bd_M3_sub2_vir | Homologous_superfamily | 8 | false | false | This entry represents the C-terminal of a β-sandwich domain found in a group of viral chemokine binding proteins. These proteins bind with CC-chemokine MCP-1, acting as cytokine decoy receptors [ ]. For example, the murine herpesvirus decoy receptor M3 acts as an immune system saboteur by altering host anti-viral infla... | [
"GO:0019956"
] | [
"chemokine binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.40.1340"
] | [
""
] | [
8
] | 1 | [] | [] | [] | 0 | [
"1mkf",
"1ml0",
"2nyz",
"2nz1"
] | 4 | [
"PUB00027380"
] | [
"12419245"
] | [
"Structural basis of chemokine sequestration by a herpesvirus decoy receptor."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Rhadinovirus"
] | [
8
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Chemokine-binding M3, subdomain 2, viral | Chemokine-binding M3, subdomain 2, viral | Chemokine-bd_M3_sub2_vir | 9 |
IPR015952 | 15,952 | Methane monooxygenase, gamma chain, domain 1 | Me_mOase_g_dom1 | Homologous_superfamily | 60 | false | false | Methane monooxygenases ( ) catalyse the oxidation of methane to methanol in the presence of oxygen and NADH in methanotrophs. It has a broad specificity, hydroxylating many alkanes, and converting alkenes into the corresponding epoxides. In additional reactions, CO is oxidized to CO2, ammonia is oxidized to hydroxylami... | [
"GO:0015049",
"GO:0015947"
] | [
"methane monooxygenase [NAD(P)H] activity",
"methane metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:1.20.1280.10"
] | [
""
] | [
60
] | 1 | [] | [] | [] | 0 | [
"1fyz",
"1fz0",
"1fz1",
"1fz2",
"1fz3",
"1fz4",
"1fz5",
"1fz6",
"1fz7",
"1fz8",
"1fz9",
"1fzh",
"1fzi",
"1mhy",
"1mhz",
"1mmo",
"1mty",
"1xmf",
"1xmg",
"1xmh",
"1xu3",
"1xu5",
"1xvb",
"1xvc",
"1xvd",
"1xve",
"1xvf",
"1xvg",
"4gam",
"6d7k",
"6vk4",
"6vk5"... | 43 | [
"PUB00021642",
"PUB00036067"
] | [
"11456616",
"9329079"
] | [
"Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site.",
"Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating ... | [
2001,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
60
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Methane monooxygenase, gamma chain, domain 1 | Methane monooxygenase, gamma chain, domain 1 | Me_mOase_g_dom1 | 5 |
IPR015955 | 15,955 | Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal | Lactate_DH/Glyco_Ohase_4_C | Homologous_superfamily | 83,913 | false | false | This entry represents a structural motif found at the C-terminal of lactate dehydrogenase ( )and malate dehydrogenases ( ), as well as at the C-terminal of family 4 glycoside hydrolases ( ). These domains have an unusual fold consisting of segregated α-helical and β-sheet regions, although they contain predominantly an... | [
"GO:0003824",
"GO:0016616"
] | [
"catalytic activity",
"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.90.110.10",
"SSF56327"
] | [
"",
""
] | [
78072,
83708
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"1.1.1",
"1.1.1.37",
"PWY-1622",
"PWY-5392",
"PWY-561",
"PWY-5690",
"PWY-6728",
"PWY-6969",
"PWY-7115",
"PWY-7383",
"PWY-8086",
"R-BTA-70268",
"R-BTA-71403",
"R-BTA-9837999",
"R-BTA-9856872",
"R-BTA-9861718",
"R-CEL-70268",
"R-CEL-71403",
"R-CEL-9837999",
"R-CEL-9856872",
"R-... | [
"EC:1.1.1",
"EC:1.1.1.37",
"METACYC:PWY-1622",
"METACYC:PWY-5392",
"METACYC:PWY-561",
"METACYC:PWY-5690",
"METACYC:PWY-6728",
"METACYC:PWY-6969",
"METACYC:PWY-7115",
"METACYC:PWY-7383",
"METACYC:PWY-8086",
"REACTOME:R-BTA-70268",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-9837999",
"REACTOM... | 53 | [
"1a5z",
"1b8p",
"1b8u",
"1b8v",
"1bdm",
"1bmd",
"1ceq",
"1cet",
"1civ",
"1d3a",
"1emd",
"1ez4",
"1guy",
"1guz",
"1gv0",
"1gv1",
"1hlp",
"1hye",
"1hyg",
"1hyh",
"1i0z",
"1i10",
"1ib6",
"1ie3",
"1iz9",
"1ldb",
"1ldg",
"1ldm",
"1ldn",
"1llc",
"1lld",
"1lth"... | 346 | [
"PUB00004870",
"PUB00005266",
"PUB00025866",
"PUB00027386",
"PUB00029383"
] | [
"7624375",
"8535779",
"11276087",
"8117664",
"12588867"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase.",
"Refined crystal structure of mitochondrial ... | [
1995,
1995,
2001,
1994,
2003
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
1058,
48780,
33268,
2,
805
] | 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",... | [
57,
4,
35,
13,
5,
44,
31,
3,
33,
41,
3,
2,
72
] | 13 | true | Homologous_superfamily | Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal | Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal | Lactate_DH/Glyco_Ohase_4_C | 4 |
IPR015956 | 15,956 | Penicillin-binding protein, C-terminal domain superfamily | Peniciliin-bd_prot_C_sf | Homologous_superfamily | 20,874 | false | false | This superfamily represents a structural motif found at the C-terminal of penicillin-binding proteins 4 (PBP4) and 5 (PBP5), as well as at the C-terminal of D-Ala-D-Ala carboxypeptidase A, a member of the MEROPS S11 peptidase family (PBP4 and PBP5 also belong to this peptidase family). These domains share a similar str... | [
"GO:0004180",
"GO:0006508"
] | [
"carboxypeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF69189"
] | [
""
] | [
20874
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.4.16.4",
"PWY-5265",
"PWY-6471"
] | [
"EC:3.4.16.4",
"METACYC:PWY-5265",
"METACYC:PWY-6471"
] | 3 | [
"1hd8",
"1nj4",
"1nzo",
"1nzu",
"1sdn",
"1tvf",
"1xp4",
"1z6f",
"3a3j",
"3beb",
"3bec",
"3hum",
"3hun",
"3it9",
"3ita",
"3itb",
"3mzd",
"3mze",
"3mzf",
"4drt",
"5fsr",
"5j8x",
"5tr7",
"5tw4",
"5tw8",
"5tx9",
"5txi",
"5ty2",
"5ty7",
"6c39",
"6c3k",
"6dz8"... | 35 | [
"PUB00022291",
"PUB00032485",
"PUB00035543"
] | [
"14555648",
"15596446",
"16411754"
] | [
"Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex.",
"Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae.",
"Crystal structure of penicillin binding protein 4 (dacB) from ... | [
2003,
2005,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stx2-converting phage 1717",
"unclassified sequences"
] | [
20641,
38,
1,
194
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Homologous_superfamily | Penicillin-binding protein, C-terminal domain superfamily | Penicillin-binding protein, C-terminal domain superfamily | Peniciliin-bd_prot_C_sf | 6 |
IPR015957 | 15,957 | Cytolethal distending toxin A | CDtoxinA | Family | 286 | false | false | null | [] | [] | [] | 0 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF036516",
"PR01387"
] | [
"CDT_A",
"CDTOXINA"
] | [
171,
252
] | 2 | [] | [] | [] | 0 | [
"1sr4",
"2f2f"
] | 2 | [
"PUB00006618",
"PUB00006646",
"PUB00006675"
] | [
"10777111",
"8112838",
"10203548"
] | [
"Sequence of lethal events in HeLa cells exposed to the G2 blocking cytolethal distending toxin.",
"Cloning, sequencing, and expression of the Escherichia coli cytolethal distending toxin genes.",
"Cytolethal distending toxin genes in Campylobacter jejuni and Campylobacter coli isolates: detection and analysis ... | [
2000,
1994,
1999
] | 3 | [
"IPR003558"
] | [] | 1 | 0 | 1 | [
"Pseudomonadati",
"Viruses"
] | [
283,
3
] | 2 | [] | [] | 0 | true | Family | Cytolethal distending toxin A | Cytolethal distending toxin A | CDtoxinA | 6 |
IPR015958 | 15,958 | Potassium transporter Trk1, fungi | Trk1_fungi | Family | 3,009 | false | false | Trk1 (also known as Trk) transporters play a crucial roles in K(+) transport in yeasts and filamentous fungi [ , , ]. | [
"GO:0015079",
"GO:0030007",
"GO:0071805",
"GO:0005886"
] | [
"potassium ion transmembrane transporter activity",
"intracellular potassium ion homeostasis",
"potassium ion transmembrane transport",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PIRSF"
] | [
"PIRSF002450"
] | [
"K+_transpter_TRK"
] | [
3009
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00073540",
"PUB00073541",
"PUB00153147"
] | [
"24021239",
"17626012",
"15485849"
] | [
"Role of Saccharomyces cerevisiae Trk1 in stabilization of intracellular potassium content upon changes in external potassium levels.",
"Molecular and functional characterization of a Na(+)-K(+) transporter from the Trk family in the ectomycorrhizal fungus Hebeloma cylindrosporum.",
"The TRK1 potassium transpor... | [
2014,
2007,
2004
] | 3 | [
"IPR004773"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
3009
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
2,
2
] | 3 | true | Family | Potassium transporter Trk1, fungi | Potassium transporter Trk1, fungi | Trk1_fungi | 4 |
IPR015960 | 15,960 | Mu1 membrane penetration protein, domain IV | Mu1_membr_pen_domIV | Homologous_superfamily | 281 | false | false | Mu1 is an outer capsid protein that acts as a reoviral penetration agent. Non-enveloped animal reoviruses must enter host cells by membrane penetration that does not involve membrane fusion, as they lack a viral membrane. Reoviruses are activated by proteolytic cleavage in the intestinal lumen, leading to infectious su... | [
"GO:0046718"
] | [
"symbiont entry into host cell"
] | [
"biological_process"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.120.420"
] | [
""
] | [
281
] | 1 | [] | [] | [] | 0 | [
"1jmu",
"2cse",
"3iyl",
"3k1q",
"5zvt",
"6xf8",
"6zty",
"6ztz",
"7ell",
"9cyt",
"9cyy"
] | 11 | [
"PUB00013280",
"PUB00036074"
] | [
"11832217",
"1548757"
] | [
"Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3.",
"Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu 1 are required for site-specific cleavage to mu 1C in transfected cells."
] | [
2002,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Spinareoviridae"
] | [
281
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Mu1 membrane penetration protein, domain IV | Mu1 membrane penetration protein, domain IV | Mu1_membr_pen_domIV | 5 |
IPR015961 | 15,961 | Mu1 membrane penetration protein, domain I | Mu1_membr_pen_domI | Homologous_superfamily | 259 | false | false | Mu1 is an outer capsid protein that acts as a reoviral penetration agent. Non-enveloped animal reoviruses must enter host cells by membrane penetration that does not involve membrane fusion, as they lack a viral membrane. Reoviruses are activated by proteolytic cleavage in the intestinal lumen, leading to infectious su... | [
"GO:0046718"
] | [
"symbiont entry into host cell"
] | [
"biological_process"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.1370.10"
] | [
""
] | [
259
] | 1 | [] | [] | [] | 0 | [
"1jmu",
"2cse",
"6xf8",
"6zty",
"6ztz",
"7ell",
"9cyt",
"9cyy"
] | 8 | [
"PUB00013280",
"PUB00036074"
] | [
"11832217",
"1548757"
] | [
"Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3.",
"Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu 1 are required for site-specific cleavage to mu 1C in transfected cells."
] | [
2002,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Spinareoviridae"
] | [
259
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Mu1 membrane penetration protein, domain I | Mu1 membrane penetration protein, domain I | Mu1_membr_pen_domI | 5 |
IPR015962 | 15,962 | Mu1 membrane penetration protein, domain II | Mu1_membr_pen_domII | Homologous_superfamily | 282 | false | false | Mu1 is an outer capsid protein that acts as a reoviral penetration agent. Non-enveloped animal reoviruses must enter host cells by membrane penetration that does not involve membrane fusion, as they lack a viral membrane. Reoviruses are activated by proteolytic cleavage in the intestinal lumen, leading to infectious su... | [
"GO:0046718"
] | [
"symbiont entry into host cell"
] | [
"biological_process"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.2040.10"
] | [
""
] | [
282
] | 1 | [] | [] | [] | 0 | [
"1jmu",
"2cse",
"3iyl",
"3k1q",
"5zvt",
"6xf8",
"6zty",
"6ztz",
"7ell",
"9cyt",
"9cyy"
] | 11 | [
"PUB00013280",
"PUB00036074"
] | [
"11832217",
"1548757"
] | [
"Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3.",
"Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu 1 are required for site-specific cleavage to mu 1C in transfected cells."
] | [
2002,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Reovirales"
] | [
282
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Mu1 membrane penetration protein, domain II | Mu1 membrane penetration protein, domain II | Mu1_membr_pen_domII | 2 |
IPR015963 | 15,963 | Uridylate kinase, bacteria | Uridylate_kinase_bac | Family | 26,154 | false | false | Uridylate kinases (also known as UMP kinases) are key enzymes in the synthesis of nucleoside triphosphates. They catalyse the reversible transfer of the gamma-phosphoryl group from an ATP donor to UMP, yielding UDP, which is the starting point for the synthesis of all other pyrimidine nucleotides. The eukaryotic enzyme... | [
"GO:0033862",
"GO:0006221",
"GO:0005737"
] | [
"UMP kinase activity",
"pyrimidine nucleotide biosynthetic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_01220_B",
"TIGR02075",
"cd04254"
] | [
"PyrH_B",
"pyrH_bact",
"AAK_UMPK-PyrH-Ec"
] | [
24817,
24898,
26108
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP"
] | [
"2.7.4.22",
"GenProp1262",
"GenProp1307",
"GenProp1318",
"GenProp1369",
"GenProp1635"
] | [
"EC:2.7.4.22",
"GP:GenProp1262",
"GP:GenProp1307",
"GP:GenProp1318",
"GP:GenProp1369",
"GP:GenProp1635"
] | 6 | [
"1ybd",
"1z9d",
"2a1f",
"2bnd",
"2bne",
"2bnf",
"2jjx",
"2v4y",
"2va1",
"3ek5",
"3ek6",
"3nwy",
"4a7w",
"4a7x",
"7bes",
"7bix",
"7bl7",
"8yh1"
] | 18 | [
"PUB00039683",
"PUB00039689",
"PUB00042653",
"PUB00042654",
"PUB00100341",
"PUB00100342"
] | [
"16095620",
"15857829",
"7711027",
"8679525",
"30409856",
"19037728"
] | [
"The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis.",
"Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation.",
"Escherichi... | [
2005,
2005,
1995,
1996,
2019,
2009
] | 6 | [
"IPR011817"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"candidate division MSBL1 archaeon SCGC-AAA382M17",
"unclassified sequences"
] | [
24272,
1425,
1,
456
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
9,
1,
6,
13
] | 4 | true | Family | Uridylate kinase, bacteria | Uridylate kinase, bacteria | Uridylate_kinase_bac | 5 |
IPR015965 | 15,965 | tRNA ligase, phosphodiesterase | tRNA_lig_PDEase | Domain | 2,374 | false | false | This entry represents a phosphodiesterase domain found in tRNA ligases [ ]. | [
"GO:0003972",
"GO:0005524",
"GO:0006388"
] | [
"RNA ligase (ATP) activity",
"ATP binding",
"tRNA splicing, via endonucleolytic cleavage and ligation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF08302"
] | [
"tRNA_lig_CPD"
] | [
2374
] | 1 | [
"EC"
] | [
"6.5.1.3"
] | [
"EC:6.5.1.3"
] | 1 | [
"5u32",
"6tzm",
"6tzo",
"6tzx",
"6u00",
"6u03",
"6u05",
"9r3w"
] | 8 | [
"PUB00017112"
] | [
"12933796"
] | [
"Genetic and biochemical analysis of the functional domains of yeast tRNA ligase."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
10,
2358,
6
] | 3 | [
"Arabidopsis thaliana",
"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)",
"Zea mays"
] | [
6,
1,
1,
1,
2
] | 5 | true | Domain | tRNA ligase, phosphodiesterase | tRNA ligase, phosphodiesterase | tRNA_lig_PDEase | 4 |
IPR015966 | 15,966 | tRNA ligase, kinase domain, fungi | tRNA_lig_kin_fungi | Domain | 1,904 | false | false | This entry represents a kinase domain found in fungal tRNA ligases [ ]. tRNA ligases are enzymes required for the splicing of precursor tRNA molecules containing introns. This domain contains a P-loop motif. | [
"GO:0003972",
"GO:0005524",
"GO:0006388"
] | [
"RNA ligase (ATP) activity",
"ATP binding",
"tRNA splicing, via endonucleolytic cleavage and ligation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF08303"
] | [
"tRNA_lig_kinase"
] | [
1904
] | 1 | [
"EC"
] | [
"6.5.1.3"
] | [
"EC:6.5.1.3"
] | 1 | [
"5u32",
"6tzm",
"6tzo",
"6tzx",
"6u00",
"6u03",
"6u05",
"9r3w"
] | 8 | [
"PUB00017112"
] | [
"12933796"
] | [
"Genetic and biochemical analysis of the functional domains of yeast tRNA ligase."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Homavirus sp."
] | [
1903,
1
] | 2 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Domain | tRNA ligase, kinase domain, fungi | tRNA ligase, kinase domain, fungi | tRNA_lig_kin_fungi | 9 |
IPR015967 | 15,967 | Recombination protein RecR, zinc finger domain | Rcmb_RecR_Znf | Domain | 23,488 | false | false | This conserved site represents the C4-type zinc finger which contains four strictly conserved cysteine residues that coordinates a zinc ion [ , ]. Mutations in this domain affects bacterial survival suggesting that it plays an important role, likely in DNA binding [ ]. The bacterial protein RecR is an important regulat... | [
"GO:0046872",
"GO:0006281",
"GO:0006310"
] | [
"metal ion binding",
"DNA repair",
"DNA recombination"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PFAM",
"PROSITE"
] | [
"PF02132",
"PS01300"
] | [
"RecR_ZnF",
"RECR"
] | [
22335,
19684
] | 2 | [
"PROSITEDOC"
] | [
"PDOC01004"
] | [
"PROSITEDOC:PDOC01004"
] | 1 | [
"1vdd",
"2v1c",
"3vdp",
"3vdu",
"3ve5",
"4jcv",
"4o6o",
"5z2v",
"5zvq",
"8a93",
"8ab0",
"8bpr",
"8k3f"
] | 13 | [
"PUB00004365",
"PUB00032061",
"PUB00064122",
"PUB00101156",
"PUB00101157"
] | [
"2674903",
"15116069",
"23019218",
"29633970",
"25460918"
] | [
"The recR locus of Escherichia coli K-12: molecular cloning, DNA sequencing and identification of the gene product.",
"Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair.",
"RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssD... | [
1989,
2004,
2012,
2018,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
9,
22861,
158,
1,
459
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Recombination protein RecR, zinc finger domain | Recombination protein RecR, zinc finger domain | Rcmb_RecR_Znf | 1 |
IPR015969 | 15,969 | P40 nucleoprotein, subdomain 1, Borna disease virus | P40_nucleoprot_sub1_BD-vir | Homologous_superfamily | 398 | false | false | This entry represents P40 nucleoproteins from several Borna disease virus (BDV) strains. BDV is an RNA virus that is a member of the Mononegavirales family, which includes such members as Measles virus and Ebola virus sp.. BDV causes an infection of the central nervous system in a wide range of vertebrates, which can p... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.3040.10"
] | [
""
] | [
398
] | 1 | [] | [] | [] | 0 | [
"1n93",
"1pp1"
] | 2 | [
"PUB00012372",
"PUB00029014"
] | [
"9882386",
"14527390"
] | [
"Borna disease virus nucleoprotein (p40) is a major target for CD8(+)-T-cell-mediated immune response.",
"Crystal structure of the borna disease virus nucleoprotein."
] | [
1999,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Amniota",
"Bornaviridae"
] | [
39,
359
] | 2 | [
"Homo sapiens"
] | [
2
] | 1 | true | Homologous_superfamily | P40 nucleoprotein, subdomain 1, Borna disease virus | P40 nucleoprotein, subdomain 1, Borna disease virus | P40_nucleoprot_sub1_BD-vir | 2 |
IPR015970 | 15,970 | P40 nucleoprotein, subdomain 2, Borna disease virus | P40_nucleoprot_sub2_BD-vir | Homologous_superfamily | 579 | false | false | This entry represents P40 nucleoproteins from several Borna disease virus (BDV) strains. BDV is an RNA virus that is a member of the Mononegavirales family, which includes such members as Measles virus and Ebola virus sp.. BDV causes an infection of the central nervous system in a wide range of vertebrates, which can p... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.3050.10"
] | [
""
] | [
579
] | 1 | [] | [] | [] | 0 | [
"1n93",
"1pp1",
"4ypi",
"5z9w",
"6c54",
"6nut"
] | 6 | [
"PUB00012372",
"PUB00029014"
] | [
"9882386",
"14527390"
] | [
"Borna disease virus nucleoprotein (p40) is a major target for CD8(+)-T-cell-mediated immune response.",
"Crystal structure of the borna disease virus nucleoprotein."
] | [
1999,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Riboviria"
] | [
75,
504
] | 2 | [
"Homo sapiens"
] | [
1
] | 1 | true | Homologous_superfamily | P40 nucleoprotein, subdomain 2, Borna disease virus | P40 nucleoprotein, subdomain 2, Borna disease virus | P40_nucleoprot_sub2_BD-vir | 4 |
IPR015971 | 15,971 | Nucleocapsid, Phlebovirus | Nucleocapsid_Phlebovirus | Family | 541 | false | false | This family consists of several Phlebovirus nucleocapsid proteins. | [
"GO:0003723",
"GO:0019013"
] | [
"RNA binding",
"viral nucleocapsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PIRSF"
] | [
"PIRSF003953"
] | [
"N_PhelboV"
] | [
541
] | 1 | [] | [] | [] | 0 | [
"3lyf",
"3ouo",
"3ov9",
"4csf",
"4csg",
"4h5l",
"4h5m",
"4h5o",
"4h5p",
"4h5q",
"4j4r",
"4j4s",
"4j4u",
"4j4v",
"4j4w",
"4j4x",
"4j4y",
"4v9e",
"5fva",
"8rcq",
"9umz"
] | 21 | [] | [] | [] | [] | 0 | [
"IPR009522"
] | [] | 1 | 0 | 1 | [
"Arthropoda",
"Viruses"
] | [
12,
529
] | 2 | [] | [] | 0 | true | Family | Nucleocapsid, Phlebovirus | Nucleocapsid, Phlebovirus | Nucleocapsid_Phlebovirus | 2 |
IPR015972 | 15,972 | Large ribosomal subunit protein eL19, domain 1 | Ribosomal_eL19_dom1 | Homologous_superfamily | 7,140 | false | false | This entry represents the N-terminal domain of the large ribosomal subunit protein eL19 found in eukaryotes and archaea [ ]. eL19 is part of the large ribosomal subunit, whose structure has been determined in a number of eukaryotic and archaeal species [ ]. eL19 is a multi-helical protein consisting of two different 3-... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.1650.10"
] | [
""
] | [
7140
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-CFA-156827",
"R-CFA-1799339",
"R-CFA-6791226",
"R-CFA-72689",
"R-CFA-727... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-9759... | 76 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 656 | [
"PUB00006505",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00030943"
] | [
"10381320",
"11297922",
"11290319",
"11114498",
"15184028"
] | [
"The structure and evolution of the ribosomal proteins encoded in the spc operon of the archaeon (Crenarchaeota) Sulfolobus acidocaldarius.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The roles of rib... | [
1999,
2001,
2001,
2000,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
940,
3,
6162,
35
] | 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... | [
9,
1,
1,
1,
10,
3,
1,
4,
6,
2,
2,
17
] | 12 | true | Homologous_superfamily | Large ribosomal subunit protein eL19, domain 1 | Large ribosomal subunit protein eL19, domain 1 | Ribosomal_eL19_dom1 | 4 |
IPR015973 | 15,973 | Large ribosomal subunit protein eL19, domain 2 | Ribosomal_eL19_dom2 | Homologous_superfamily | 563 | false | false | Ribosomal protein eL19 from eukaryotes and eL19 (known as L19e) from archaea [ ] form part of the large ribosomal subunit, whose structure has been determined in a number of eukaryotic and archaeal species [ ]. eL19 is a multi-helical protein consisting of two different 3-helical domains connected by a long, partly hel... | [
"GO:0003735",
"GO:0006412"
] | [
"structural constituent of ribosome",
"translation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:1.20.5.560"
] | [
""
] | [
563
] | 1 | [] | [] | [] | 0 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 72 | [
"PUB00006505",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00030943"
] | [
"10381320",
"11297922",
"11290319",
"11114498",
"15184028"
] | [
"The structure and evolution of the ribosomal proteins encoded in the spc operon of the archaeon (Crenarchaeota) Sulfolobus acidocaldarius.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The roles of rib... | [
1999,
2001,
2001,
2000,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
552,
11
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Large ribosomal subunit protein eL19, domain 2 | Large ribosomal subunit protein eL19, domain 2 | Ribosomal_eL19_dom2 | 2 |
IPR015974 | 15,974 | Large ribosomal subunit protein eL19, domain 3 | Ribosomal_eL19_dom3 | Homologous_superfamily | 586 | false | false | Ribosomal protein eL19 from eukaryotes and eL19 (known as L19e) from archaea [ ] form part of the large ribosomal subunit, whose structure has been determined in a number of eukaryotic and archaeal species [ ]. eL19 is a multi-helical protein consisting of two different 3-helical domains connected by a long, partly hel... | [
"GO:0003735",
"GO:0006412"
] | [
"structural constituent of ribosome",
"translation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.1200.60"
] | [
""
] | [
586
] | 1 | [] | [] | [] | 0 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 72 | [
"PUB00006505",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00030943"
] | [
"10381320",
"11297922",
"11290319",
"11114498",
"15184028"
] | [
"The structure and evolution of the ribosomal proteins encoded in the spc operon of the archaeon (Crenarchaeota) Sulfolobus acidocaldarius.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The roles of rib... | [
1999,
2001,
2001,
2000,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"ecological metagenomes"
] | [
560,
10,
16
] | 3 | [] | [] | 0 | true | Homologous_superfamily | Large ribosomal subunit protein eL19, domain 3 | Large ribosomal subunit protein eL19, domain 3 | Ribosomal_eL19_dom3 | 2 |
IPR015976 | 15,976 | Bacteriophage T4, Gp11, C-terminal finger domain | Phage_T4_Gp11_C | Homologous_superfamily | 321 | false | false | This superfamily includes the middle finger domain, which is a seven-stranded, antiparallel, skewed β-roll with one α-helix [ ]. The bacteriophage baseplate controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. The baseplate is a multi-subunit assembly at the distal end of the tail... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.1160.10"
] | [
""
] | [
321
] | 1 | [] | [] | [] | 0 | [
"1el6",
"1pdf",
"1tja",
"5iv5",
"5iv7",
"9f4b"
] | 6 | [
"PUB00029807",
"PUB00036076"
] | [
"12923574",
"10966799"
] | [
"Three-dimensional structure of bacteriophage T4 baseplate.",
"Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers."
] | [
2003,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Flagellimonas marina",
"Viruses"
] | [
1,
320
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Bacteriophage T4, Gp11, C-terminal finger domain | Bacteriophage T4, Gp11, C-terminal finger domain | Phage_T4_Gp11_C | 9 |
IPR015982 | 15,982 | Baseplate structural protein Gp11, N-terminal domain superfamily | Baseplate_struct_Gp11_N_sf | Homologous_superfamily | 306 | false | false | This superfamily represents the N-terminal domain of Gp11, which has an α-helical structure that assumes an orthogonal bundle topology. The bacteriophage baseplate controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. The baseplate is a multi-subunit assembly at the distal end of t... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.286.30"
] | [
""
] | [
306
] | 1 | [] | [] | [] | 0 | [
"1el6",
"1pdf",
"1tja",
"5iv5",
"5iv7",
"9f4b"
] | 6 | [
"PUB00029807",
"PUB00036076"
] | [
"12923574",
"10966799"
] | [
"Three-dimensional structure of bacteriophage T4 baseplate.",
"Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers."
] | [
2003,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Flagellimonas marina",
"Viruses"
] | [
1,
305
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Baseplate structural protein Gp11, N-terminal domain superfamily | Baseplate structural protein Gp11, N-terminal domain superfamily | Baseplate_struct_Gp11_N_sf | 2 |
IPR015984 | 15,984 | Cytochrome c prime, subgroup | Cyt_c_prime_subgr | Family | 2,037 | false | false | Cytochromes c (cytC) can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide range of ... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00608"
] | [
"CYTCHROMECII"
] | [
2037
] | 1 | [] | [] | [] | 0 | [
"1bbh",
"1cgn",
"1cgo",
"1cpq",
"1cpr",
"1e83",
"1e84",
"1e85",
"1e86",
"1eky",
"1gqa",
"1jaf",
"1nbb",
"1rcp",
"2ccy",
"2j8w",
"2j9b",
"2xl6",
"2xl8",
"2xld",
"2xle",
"2xlh",
"2xlm",
"2xlo",
"2xlv",
"2xlw",
"2xm0",
"2xm4",
"2ykz",
"2yl0",
"2yl1",
"2yl3"... | 69 | [
"PUB00000609",
"PUB00000610",
"PUB00000611",
"PUB00003313"
] | [
"1646016",
"1646017",
"1646027",
"8230224"
] | [
"Bacterial 4-alpha-helical bundle cytochromes.",
"Sequence variability in bacterial cytochromes c.",
"Ligand binding properties of cytochromes c'.",
"Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 A resolution."
] | [
1991,
1991,
1991,
1993
] | 4 | [
"IPR012127"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"metagenomes"
] | [
2013,
24
] | 2 | [] | [] | 0 | true | Family | Cytochrome c prime, subgroup | Cytochrome c prime, subgroup | Cyt_c_prime_subgr | 4 |
IPR015985 | 15,985 | Tellurite resistance methyltransferase TehB-like domain | TehB-like_dom | Domain | 3,384 | false | false | Tellurite resistance protein TehB is part of a tellurite-reducing operon tehA and tehB. When present in high copy number, TehB is responsible for potassium tellurite resistance, probably by increasing the reduction rate of tellurite to metallic tellurium within the bacterium. TehB is a cytoplasmic protein which possess... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03848"
] | [
"TehB"
] | [
3384
] | 1 | [] | [] | [] | 0 | [
"2i6g",
"2xva",
"2xvm",
"3m70",
"4dq0"
] | 5 | [
"PUB00014885"
] | [
"11053398"
] | [
"Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
3269,
38,
34,
43
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Tellurite resistance methyltransferase TehB-like domain | Tellurite resistance methyltransferase TehB-like domain | TehB-like_dom | 7 |
IPR015986 | 15,986 | Sortase B, Firmicutes | SrtB_Firmicute | Family | 410 | false | false | Members of this transpeptidase family are, in most cases, designated sortase B, product of the srtB gene. This protein shows only distant similarity to the sortase A family, for which there may be several members in a single bacterial genome. Typical SrtB substrate motifs include NAKTN, NPKSS, etc, and otherwise resemb... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF030150"
] | [
"UCP030150"
] | [
410
] | 1 | [] | [] | [] | 0 | [
"1ng5",
"1qwz",
"1qx6",
"1qxa",
"1rz2",
"2oqw",
"2oqz",
"4lfd"
] | 8 | [
"PUB00014494",
"PUB00029054",
"PUB00030423",
"PUB00045370",
"PUB00081158",
"PUB00081159",
"PUB00081160",
"PUB00081162",
"PUB00081163",
"PUB00081164"
] | [
"11401711",
"15242591",
"14725770",
"17012401",
"15718231",
"16524923",
"15808931",
"17200112",
"16041044",
"15028680"
] | [
"Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus.",
"Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site.",
"The structure of sortase B, a cysteine transpeptidase that tethers surface protein to ... | [
2001,
2004,
2004,
2006,
2005,
2006,
2005,
2007,
2005,
2004
] | 10 | [
"IPR009835"
] | [] | 1 | 0 | 1 | [
"Bacillota",
"human gut metagenome"
] | [
409,
1
] | 2 | [] | [] | 0 | true | Family | Sortase B, Firmicutes | Sortase B, Firmicutes | SrtB_Firmicute | 7 |
IPR015987 | 15,987 | Uncharacterised conserved protein UCP022704 | UCP022704 | Family | 3,390 | false | false | This family consists of several hypothetical bacterial proteins but contains one sequence Ree1 ( ) from Saccharomyces cerevisiae [ ]. Members of this family are typically around 200 residues in length. The function of this family is unknown. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF022704"
] | [
"UCP022704"
] | [
3390
] | 1 | [] | [] | [] | 0 | [
"3mep",
"3o12"
] | 2 | [
"PUB00086893"
] | [
"18851946"
] | [
"Novel Ree1 regulates the expression of ENO1 via the Snf1 complex pathway in Saccharomyces cerevisiae."
] | [
2008
] | 1 | [
"IPR009784"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"Siphoviridae sp. ctcfw7",
"metagenomes"
] | [
3266,
109,
7,
1,
7
] | 5 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Uncharacterised conserved protein UCP022704 | Uncharacterised conserved protein UCP022704 | UCP022704 | 8 |
IPR015988 | 15,988 | STAT transcription factor, coiled coil | STAT_TF_CC | Homologous_superfamily | 10,863 | false | false | The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus ... | [
"GO:0006355",
"GO:0007165"
] | [
"regulation of DNA-templated transcription",
"signal transduction"
] | [
"biological_process",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF47655"
] | [
""
] | [
10863
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1251985",
"R-BTA-1266695",
"R-BTA-1433557",
"R-BTA-186763",
"R-BTA-512988",
"R-BTA-8854691",
"R-BTA-8983432",
"R-BTA-8985947",
"R-BTA-9020558",
"R-BTA-9020958",
"R-CEL-1059683",
"R-CEL-1169408",
"R-CEL-1251985",
"R-CEL-186763",
"R-CEL-201556",
"R-CEL-3249367",
"R-CEL-6783783",... | [
"REACTOME:R-BTA-1251985",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-186763",
"REACTOME:R-BTA-512988",
"REACTOME:R-BTA-8854691",
"REACTOME:R-BTA-8983432",
"REACTOME:R-BTA-8985947",
"REACTOME:R-BTA-9020558",
"REACTOME:R-BTA-9020958",
"REACTOME:R-CEL-1059683",
"REACTOME:... | 234 | [
"1bf5",
"1bg1",
"1uur",
"1uus",
"1y1u",
"1yvl",
"3cwg",
"4e68",
"4y5u",
"4y5w",
"5d39",
"5oen",
"6mbw",
"6mbz",
"6njs",
"6nuq",
"6qhd",
"6tlc",
"6ux2",
"6wcz",
"7nuf",
"7tva",
"7tvb",
"7ubt",
"7uc6",
"7uc7",
"7zn7",
"7znn",
"8d3f",
"8t12",
"8t13",
"8yyu"... | 34 | [
"PUB00007134",
"PUB00011807",
"PUB00032712",
"PUB00051157"
] | [
"12039028",
"9630226",
"15780933",
"18433722"
] | [
"Signaling through the JAK/STAT pathway, recent advances and future challenges.",
"Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.",
"Structural bases of unphosphorylated STAT1 association and receptor binding.",
"Crystal structure of unphosphorylated STAT3 core fragment."
] | [
2002,
1998,
2005,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
36,
10826,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
29,
6,
108,
33,
31
] | 6 | true | Homologous_superfamily | STAT transcription factor, coiled coil | STAT transcription factor, coiled coil | STAT_TF_CC | 8 |
IPR015990 | 15,990 | ADP-specific phosphofructokinase/glucokinase, archaeal | ADP_PFK/GK_arc | Family | 181 | false | false | Proteins in this entry show high ADP-dependent activities for both glucokinase and /or phosphofructokinase [ ]. They act in a modified Embden-Meyerhof sugar metabolism pathway that is present in some archaea [ , ]. | [
"GO:0000287",
"GO:0016773",
"GO:0006096"
] | [
"magnesium ion binding",
"phosphotransferase activity, alcohol group as acceptor",
"glycolytic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF015883"
] | [
"ADP-Pfk_glckin"
] | [
181
] | 1 | [
"EC",
"EC",
"METACYC"
] | [
"2.7.1",
"2.7.1.146",
"PWY-6142"
] | [
"EC:2.7.1",
"EC:2.7.1.146",
"METACYC:PWY-6142"
] | 3 | [
"1l2l",
"1u2x",
"1ua4",
"3drw",
"4b8r",
"4b8s",
"5k27",
"5kkg",
"5o0i",
"5o0j",
"5od2",
"6c8z",
"6xio"
] | 13 | [
"PUB00015898",
"PUB00016086",
"PUB00016171"
] | [
"12832801",
"14762828",
"11856730"
] | [
"Archaeal ADP-dependent phosphofructokinase: expression, purification, crystallization and preliminary crystallographic analysis.",
"Unique sugar metabolism and novel enzymes of hyperthermophilic archaea.",
"ADP-dependent glucokinase/phosphofructokinase, a novel bifunctional enzyme from the hyperthermophilic ar... | [
2003,
2004,
2002
] | 3 | [
"IPR007666"
] | [
"IPR011790",
"IPR031299"
] | 1 | 2 | 0 | [
"Methanobacteriota"
] | [
181
] | 1 | [] | [] | 0 | true | Family | ADP-specific phosphofructokinase/glucokinase, archaeal | ADP-specific phosphofructokinase/glucokinase, archaeal | ADP_PFK/GK_arc | 3 |
IPR015991 | 15,991 | Hydrolase TatD/YcfH-like | TatD/YcfH-like | Family | 24,994 | false | false | This entry includes a group of enzymes, including the putative 3'-5' ssDNA/RNA exonuclease TatD from Enterobacter sp., the uncharacterised metal-dependent hydrolase YcfH from Escherichia coli, the D-aminoacyl-tRNA deacylase Dtd3 from Synechocystis sp. and some uncharacterised proteins. YchF has D-tyrosyl-tRNA deacylase... | [
"GO:0004536"
] | [
"DNA nuclease activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00010"
] | [
""
] | [
24994
] | 1 | [] | [] | [] | 0 | [
"1j6o",
"1yix",
"2gzx",
"6l25"
] | 4 | [
"PUB00077548"
] | [
"19332551"
] | [
"Widespread distribution of cell defense against D-aminoacyl-tRNAs."
] | [
2009
] | 1 | [
"IPR001130"
] | [
"IPR033665"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
232,
24232,
63,
2,
465
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Hydrolase TatD/YcfH-like | Hydrolase TatD/YcfH-like | TatD/YcfH-like | 3 |
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