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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR017830 | 17,830 | Hydroxysqualene dehydroxylase HpnE | SQase_HpnE | Family | 3,634 | false | false | In bacteria, squalene (SQ) is an intermediate in the biosynthesis of hopanoids. The genes for hopanoid biosynthesis are typically located on clusters that consist of four highly conserved genes -hpnC, hpnD, hpnE, and hpnF- for conversion of farnesyl diphosphate (FPP) to hopene or related pentacyclic metabolites. HpnE i... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03467"
] | [
"HpnE"
] | [
3634
] | 1 | [
"EC",
"METACYC"
] | [
"1.17.8.1",
"PWY-7072"
] | [
"EC:1.17.8.1",
"METACYC:PWY-7072"
] | 2 | [] | 0 | [
"PUB00086647"
] | [
"26258173"
] | [
"Biosynthesis of Squalene from Farnesyl Diphosphate in Bacteria: Three Steps Catalyzed by Three Enzymes."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Geodia barretti",
"environmental samples",
"metagenomes"
] | [
3588,
1,
3,
42
] | 4 | [] | [] | 0 | true | Family | Hydroxysqualene dehydroxylase HpnE | Hydroxysqualene dehydroxylase HpnE | SQase_HpnE | 6 |
IPR017831 | 17,831 | Hopanoid-associated phosphorylase HpnG | Hopanoid-assoc_phosphoryl_HpnG | Family | 800 | false | false | These proteins are part of the wider family of phosphorylases that typically act on nucleotide-sugar substrates. The proteins in this entry are generally encoded in the same locus as genes involved in the biosynthesis and elaboration of hopene, the cyclization product of the polyisoprenoid squalene. The gene from Zymom... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03468"
] | [
"HpnG"
] | [
800
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042985"
] | [
"9714766"
] | [
"Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the biosynthesis of hopanoid lipids."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"metagenomes"
] | [
796,
4
] | 2 | [] | [] | 0 | true | Family | Hopanoid-associated phosphorylase HpnG | Hopanoid-associated phosphorylase HpnG | Hopanoid-assoc_phosphoryl_HpnG | 4 |
IPR017832 | 17,832 | Glycosyl transferase, family 2, hopene-associated, HpnB | Glyco_trans_2_hopen-assoc_HpnB | Family | 1,979 | false | false | The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferas... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03469"
] | [
"HpnB"
] | [
1979
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009409",
"PUB00042985"
] | [
"9334165",
"9714766"
] | [
"A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities.",
"Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the biosynthesis of hopanoid lipids."
] | [
1997,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Syncephalis pseudoplumigaleata",
"metagenomes"
] | [
1972,
1,
6
] | 3 | [] | [] | 0 | true | Family | Glycosyl transferase, family 2, hopene-associated, HpnB | Glycosyl transferase, family 2, hopene-associated, HpnB | Glyco_trans_2_hopen-assoc_HpnB | 5 |
IPR017833 | 17,833 | Hopanoid biosynthesis associated radical SAM protein HpnH | Hopanoid_synth-assoc_rSAM_HpnH | Family | 2,929 | false | false | Proteins in this entry are members of the radical SAM superfamily of enzymes that utilise an iron-sulphur redox cluster and S-adenosylmethionine to carry out diverse radical mediated reactions [ ]. This group of proteins are frequently encoded in the same locus as squalene-hopene cyclase (SHC, ) and other proteins asso... | [] | [] | [] | 0 | [
"SFLD",
"NCBIFAM"
] | [
"SFLDF00397",
"TIGR03470"
] | [
"adenosyl-hopene_transferase",
"HpnH"
] | [
2906,
2925
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00010539",
"PUB00042985"
] | [
"11222759",
"9714766"
] | [
"Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods.",
"Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the... | [
2001,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2890,
7,
32
] | 3 | [] | [] | 0 | true | Family | Hopanoid biosynthesis associated radical SAM protein HpnH | Hopanoid biosynthesis associated radical SAM protein HpnH | Hopanoid_synth-assoc_rSAM_HpnH | 4 |
IPR017835 | 17,835 | Hopanoid biosynthesis associated glycosyltransferase, HpnI | Hopen-assoc_HpnI | Family | 1,235 | false | false | Proteins in this entry contain glycosyl transferase family 2 domains which are responsible, generally, for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The Acidithiobacillus ferrooxidans ATCC 23270 protein (AFE_0974) is encoded in the same locus as the genes for squale... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03472"
] | [
"HpnI"
] | [
1235
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034422",
"PUB00042985"
] | [
"16930487",
"9714766"
] | [
"Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic.",
"Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the biosynthesis of hopanoid lipids."
] | [
2006,
1998
] | 2 | [
"IPR025993"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"mine drainage metagenome"
] | [
1228,
2,
5
] | 3 | [] | [] | 0 | true | Family | Hopanoid biosynthesis associated glycosyltransferase, HpnI | Hopanoid biosynthesis associated glycosyltransferase, HpnI | Hopen-assoc_HpnI | 9 |
IPR017836 | 17,836 | Hopanoid biosynthesis associated protein HpnK | Hopanoid_biosynth-assoc_HpnK | Family | 899 | false | false | This entry represents a subset of the YdjC-like family of uncharacterised proteins. The Acidithiobacillus ferrooxidans ATCC 23270 protein (AFE_0976) is encoded in the same locus as the genes for squalene-hopene cyclase (SHC, ) and other proteins associated with the biosynthesis of hopanoid natural products. Similarly, ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03473"
] | [
"HpnK"
] | [
899
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034422",
"PUB00042985"
] | [
"16930487",
"9714766"
] | [
"Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic.",
"Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the biosynthesis of hopanoid lipids."
] | [
2006,
1998
] | 2 | [
"IPR006879"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"ecological metagenomes"
] | [
892,
7
] | 2 | [] | [] | 0 | true | Family | Hopanoid biosynthesis associated protein HpnK | Hopanoid biosynthesis associated protein HpnK | Hopanoid_biosynth-assoc_HpnK | 6 |
IPR017837 | 17,837 | Plasmid replication initiator, RepA, IncFII type | Plasmid_rep_init_RepA_IncFII | Family | 847 | false | false | This entry represents plasmid replication initiator RepA from the incFII (plasmid incompatibility group F-II) plasmids. This group of plasmids includes R1 and R100. Immediately upstream of repA is found tap, which encodes a leader peptide of about 24 amino acids, often not assigned as a gene in annotated plasmid sequen... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03474"
] | [
"incFII_RepA"
] | [
847
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR003446"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Callosobruchus maculatus",
"human gut metagenome",
"plasmids"
] | [
839,
4,
1,
3
] | 4 | [] | [] | 0 | true | Family | Plasmid replication initiator, RepA, IncFII type | Plasmid replication initiator, RepA, IncFII type | Plasmid_rep_init_RepA_IncFII | 5 |
IPR017839 | 17,839 | DMSO reductase family, type II, iron-sulphur subunit | DMSO_Rdtase_II_Fe-S_su | Family | 202 | false | false | The DMSO reductase family is a large and rapidly expanding group of enzymes found in bacteria and archaea that share a common form of molybdenum cofactor known as bis(molybdopterin guanine dinucleotide)Mo [ ]. This entry represents the iron-sulphur subunit, typically called the beta subunit, found in various type II DM... | [
"GO:0051536",
"GO:0009061",
"GO:0042597"
] | [
"iron-sulfur cluster binding",
"anaerobic respiration",
"periplasmic space"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM",
"CDD"
] | [
"TIGR03478",
"cd10555"
] | [
"DMSO_red_II_bet",
"EBDH_beta"
] | [
199,
188
] | 2 | [
"GP"
] | [
"GenProp0764"
] | [
"GP:GenProp0764"
] | 1 | [
"2ivf",
"4ydd",
"5ch7",
"5chc",
"5e7o"
] | 5 | [
"PUB00042991",
"PUB00042992",
"PUB00042993",
"PUB00042994"
] | [
"15866716",
"11294876",
"12067345",
"15311335"
] | [
"The C subunit of Ideonella dechloratans chlorate reductase: expression, purification, refolding, and heme reconstitution.",
"Ethylbenzene dehydrogenase, a novel hydrocarbon-oxidizing molybdenum/iron-sulfur/heme enzyme.",
"Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its ... | [
2005,
2001,
2002,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halobacteriales",
"ecological metagenomes"
] | [
106,
90,
6
] | 3 | [] | [] | 0 | true | Family | DMSO reductase family, type II, iron-sulphur subunit | DMSO reductase family, type II, iron-sulphur subunit | DMSO_Rdtase_II_Fe-S_su | 4 |
IPR017840 | 17,840 | DMSO reductase family, type II, molybdopterin subunit | DMSO_Rdtase_II_Mopterin_su | Family | 166 | false | false | The DMSO reductase family is a large and rapidly expanding group of enzymes found in bacteria and archaea that share a common form of molybdenum cofactor known as bis(molybdopterin guanine dinucleotide)Mo [ ]. This entry represents the molybdopterin subunit, typically called the alpha subunit, found in various type II ... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR03479"
] | [
"DMSO_red_II_alp"
] | [
166
] | 1 | [
"GP"
] | [
"GenProp0764"
] | [
"GP:GenProp0764"
] | 1 | [
"2ivf",
"4ydd",
"5ch7",
"5chc",
"5e7o"
] | 5 | [
"PUB00042991",
"PUB00042992",
"PUB00042993",
"PUB00042994"
] | [
"15866716",
"11294876",
"12067345",
"15311335"
] | [
"The C subunit of Ideonella dechloratans chlorate reductase: expression, purification, refolding, and heme reconstitution.",
"Ethylbenzene dehydrogenase, a novel hydrocarbon-oxidizing molybdenum/iron-sulfur/heme enzyme.",
"Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its ... | [
2005,
2001,
2002,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Effrenium voratum",
"Halobacteriales"
] | [
76,
1,
89
] | 3 | [] | [] | 0 | true | Family | DMSO reductase family, type II, molybdopterin subunit | DMSO reductase family, type II, molybdopterin subunit | DMSO_Rdtase_II_Mopterin_su | 2 |
IPR017841 | 17,841 | Hopanoid transporter HpnN | Hopanoid_biosynth_HpnN | Family | 1,278 | false | false | This family includes Hopanoid transporter HpnN which is essential for hopanoid transport from the cytoplasmic to the outer membrane [ ]. It is capable of shuttling hopanoid lipids from the inner membrane to the periplasm, where they probably spontaneously insert to the inner leaflet of the outer membrane, strengthening... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03480"
] | [
"HpnN"
] | [
1278
] | 1 | [] | [] | [] | 0 | [
"5khn",
"5khs",
"6wu0"
] | 3 | [
"PUB00101889",
"PUB00101890"
] | [
"28584102",
"2858410"
] | [
"Crystal structures of the <i>Burkholderia multivorans</i> hopanoid transporter HpnN.",
"Insulin processing and action in adipocytes: evidence for generation of insulin-containing vesicles by leupeptin and monensin."
] | [
2017,
1985
] | 2 | [] | [] | 0 | 0 | null | [
"Opisthokonta",
"Pseudomonadati",
"metagenomes"
] | [
2,
1268,
8
] | 3 | [] | [] | 0 | true | Family | Hopanoid transporter HpnN | Hopanoid transporter HpnN | Hopanoid_biosynth_HpnN | 1 |
IPR017842 | 17,842 | Hopanoid biosynthesis-associated membrane protein HpnM | Hopanoid_biosyn-assoc_HpnM | Family | 338 | false | false | The genes encoding the proteins in this entry are all found in bacteria containing the machinery necessary for biosynthesis of hopanoid lipids. Furthermore, these genes are usually located proximal to other components of this biological process. The proteins are members of a family of putative transporters known as "to... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03481"
] | [
"HpnM"
] | [
338
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR008869"
] | [] | 1 | 0 | 1 | [
"Pseudomonadati",
"metagenomes"
] | [
331,
7
] | 2 | [] | [] | 0 | true | Family | Hopanoid biosynthesis-associated membrane protein HpnM | Hopanoid biosynthesis-associated membrane protein HpnM | Hopanoid_biosyn-assoc_HpnM | 4 |
IPR017843 | 17,843 | DMSO reductase family, type II, chaperone | DMSO_Rdtase_II_chaperone | Family | 108 | false | false | The DMSO reductase family is a large and rapidly expanding group of enzymes found in bacteria and archaea that share a common form of molybdenum cofactor known as bis(molybdopterin guanine dinucleotide)Mo [ ]. Type II members of the DMSO reductase family are heterotrimeric proteins with bis(molybdopterin guanine dinucl... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03482"
] | [
"DMSO_red_II_cha"
] | [
108
] | 1 | [
"GP"
] | [
"GenProp0764"
] | [
"GP:GenProp0764"
] | 1 | [] | 0 | [
"PUB00042992",
"PUB00042993",
"PUB00042994"
] | [
"11294876",
"12067345",
"15311335"
] | [
"Ethylbenzene dehydrogenase, a novel hydrocarbon-oxidizing molybdenum/iron-sulfur/heme enzyme.",
"Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes.",
"Mo and W bis-MGD enzymes:... | [
2001,
2002,
2004
] | 3 | [
"IPR020945"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Halobacteriales"
] | [
29,
79
] | 2 | [] | [] | 0 | true | Family | DMSO reductase family, type II, chaperone | DMSO reductase family, type II, chaperone | DMSO_Rdtase_II_chaperone | 5 |
IPR017844 | 17,844 | Cell division protein FtsZ, C-terminal extension | Cell_div_FtsZ_C | Domain | 1,016 | false | false | This entry describes a domain found as a C-terminal extension to the cell division protein FtsZ in many, but not all, members of the alphaproteobacteria. | [
"GO:0005525",
"GO:0051301",
"GO:0005737"
] | [
"GTP binding",
"cell division",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03483"
] | [
"FtsZ_alphas_C"
] | [
1016
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"marine sediment metagenome"
] | [
1015,
1
] | 2 | [] | [] | 0 | true | Domain | Cell division protein FtsZ, C-terminal extension | Cell division protein FtsZ, C-terminal extension | Cell_div_FtsZ_C | 3 |
IPR017845 | 17,845 | Chlorosome envelope protein H, CsmH | Chlorosome_envelope_CsmH | Repeat | 17 | false | false | This entry contains proteins with a repeated sequence element that is restricted to species of the Chlorobiaceae. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03058"
] | [
"rpt_csmH"
] | [
17
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Chlorobiaceae"
] | [
17
] | 1 | [] | [] | 0 | true | Repeat | Chlorosome envelope protein H, CsmH | Chlorosome envelope protein H, CsmH | Chlorosome_envelope_CsmH | 9 |
IPR017846 | 17,846 | Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase, bacterial type | Nict_dMeBzImd_PRibTrfase_bact | Family | 14,491 | false | false | This entry represents bacterial-type nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase enzymes involved in dimethylbenzimidazole synthesis [ ]. This enzyme catalyses the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). This function ... | [
"GO:0008939",
"GO:0009236"
] | [
"nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity",
"cobalamin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00230",
"TIGR03160"
] | [
"CobT",
"cobT_DBIPRT"
] | [
13076,
14388
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.4.2.21",
"GenProp0269",
"GenProp1349",
"GenProp1366",
"GenProp1378",
"GenProp1454",
"PWY-5509",
"PWY-6269",
"PWY-7964",
"PWY-7965",
"PWY-7966",
"PWY-7967",
"PWY-7968",
"PWY-7969",
"PWY-7970"
] | [
"EC:2.4.2.21",
"GP:GenProp0269",
"GP:GenProp1349",
"GP:GenProp1366",
"GP:GenProp1378",
"GP:GenProp1454",
"METACYC:PWY-5509",
"METACYC:PWY-6269",
"METACYC:PWY-7964",
"METACYC:PWY-7965",
"METACYC:PWY-7966",
"METACYC:PWY-7967",
"METACYC:PWY-7968",
"METACYC:PWY-7969",
"METACYC:PWY-7970"
] | 15 | [
"1d0s",
"1d0v",
"1j33",
"1jh8",
"1jha",
"1jhm",
"1jho",
"1jhp",
"1jhq",
"1jhr",
"1jhu",
"1jhv",
"1jhx",
"1jhy",
"1l4b",
"1l4e",
"1l4f",
"1l4g",
"1l4h",
"1l4k",
"1l4l",
"1l4m",
"1l4n",
"1l5f",
"1l5k",
"1l5l",
"1l5m",
"1l5n",
"1l5o",
"1wx1",
"4hdk",
"4hdm"... | 42 | [
"PUB00009745",
"PUB00014667",
"PUB00014670",
"PUB00014672",
"PUB00015874",
"PUB00015996"
] | [
"7592411",
"12196148",
"8550510",
"11153269",
"12101181",
"8206834"
] | [
"The cobalamin (coenzyme B12) biosynthetic genes of Escherichia coli.",
"Biosynthesis of cobalamin (vitamin B(12)).",
"Salmonella typhimurium cobalamin (vitamin B12) biosynthetic genes: functional studies in S. typhimurium and Escherichia coli.",
"Multiple biosynthetic pathways for vitamin B12: variations on ... | [
1995,
2002,
1996,
2001,
2002,
1994
] | 6 | [
"IPR003200"
] | [
"IPR012176"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
29,
14308,
28,
126
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase, bacterial type | Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase, bacterial type | Nict_dMeBzImd_PRibTrfase_bact | 1 |
IPR017847 | 17,847 | Type VI secretion system, RhsGE-associated Vgr family subset | T6SS_RhsGE_Vgr_subset | Family | 18,704 | false | false | This entry represents a subset of the RhsGE element associated Vgr protein family ( ) found only in genomes with type VI secretion loci. However, members of this entry, although recognisably correlated to type VI secretion according the partial phylogenetic profiling algorithm, are often encoded far from the type VI se... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03361"
] | [
"VI_Rhs_Vgr"
] | [
18704
] | 1 | [
"GP"
] | [
"GenProp0735"
] | [
"GP:GenProp0735"
] | 1 | [
"2p5z",
"4mtk",
"4uhv",
"6h3l",
"6h3n",
"6sjl",
"6sk0",
"6ski",
"7q5p",
"8qja"
] | 10 | [
"PUB00054068",
"PUB00077552"
] | [
"17873062",
"20150509"
] | [
"Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin.",
"In vivo actin cross-linking induced by Vibrio cholerae type VI secretion system is associated with intestinal inflammation."
] | [
2007,
2010
] | 2 | [
"IPR006533"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Peduoviridae",
"unclassified sequences"
] | [
18598,
24,
2,
80
] | 4 | [] | [] | 0 | true | Family | Type VI secretion system, RhsGE-associated Vgr family subset | Type VI secretion system, RhsGE-associated Vgr family subset | T6SS_RhsGE_Vgr_subset | 3 |
IPR017848 | 17,848 | RNA polymerase sigma factor, RpoD/SigA, cyanobacteria | RNA_pol_sigma_RpoD/SigA_cyanob | Family | 1,849 | false | false | This family includes a number of closely related sigma-70 ( ) factors in the cyanobacteria. All appear most closely related to the essential sigma-70 factor RpoD, and some are related to the RpoD C-terminal domain model ( ). The bacterial core RNA polymerase complex, which consists of five subunits, is sufficient for t... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02997"
] | [
"Sig70-cyanoRpoD"
] | [
1849
] | 1 | [] | [] | [] | 0 | [
"8gzg",
"8gzh",
"8h3v",
"8h40",
"9dvs",
"9dvt",
"9dvu"
] | 7 | [
"PUB00000061",
"PUB00002181",
"PUB00004340",
"PUB00088319"
] | [
"3052291",
"1597408",
"3092189",
"25596450"
] | [
"Structure and function of bacterial sigma factors.",
"The sigma 70 family: sequence conservation and evolutionary relationships.",
"Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.",
"Plastid sigma factors: Their individual functions and regulation in transcription."... | [
1988,
1992,
1986,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Cyanobacteriota",
"Eukaryota"
] | [
1823,
26
] | 2 | [] | [] | 0 | true | Family | RNA polymerase sigma factor, RpoD/SigA, cyanobacteria | RNA polymerase sigma factor, RpoD/SigA, cyanobacteria | RNA_pol_sigma_RpoD/SigA_cyanob | 4 |
IPR017850 | 17,850 | Alkaline-phosphatase-like, core domain superfamily | Alkaline_phosphatase_core_sf | Homologous_superfamily | 333,992 | false | false | This superfamily represents a structural domain with a core 3-layer α/β/α structure, which can sometimes contain additional subdomains (also covered by this entry). These domains form the core domain of alkaline phosphatases. This structural domain is found in: Alkaline phosphatase ( ); most use zinc and magnesium as c... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.40.720.10",
"SSF53649"
] | [
"",
""
] | [
325151,
317010
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"5.4.2",
"R-BTA-163125",
"R-BTA-1663150",
"R-BTA-6798695",
"R-BTA-6814848",
"R-BTA-9840310",
"R-CEL-196843",
"R-CFA-1663150",
"R-CFA-2022857",
"R-CFA-6798695",
"R-CFA-9840310",
"R-DME-1483166",
"R-DME-6811438",
"R-DME-8935690",
"R-DRE-6798695",
"R-DRE-6814848",
"R-HSA-1483166",
"R-... | [
"EC:5.4.2",
"REACTOME:R-BTA-163125",
"REACTOME:R-BTA-1663150",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6814848",
"REACTOME:R-BTA-9840310",
"REACTOME:R-CEL-196843",
"REACTOME:R-CFA-1663150",
"REACTOME:R-CFA-2022857",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-9840310",
"REACTOME:R-DME-1483166"... | 79 | [
"1aja",
"1ajb",
"1ajc",
"1ajd",
"1alh",
"1ali",
"1alj",
"1alk",
"1ani",
"1anj",
"1auk",
"1b8j",
"1e1z",
"1e2s",
"1e33",
"1e3c",
"1ed8",
"1ed9",
"1ei6",
"1ejj",
"1elx",
"1ely",
"1elz",
"1eqj",
"1ew2",
"1ew8",
"1ew9",
"1fsu",
"1hdh",
"1hjk",
"1hqa",
"1k7h"... | 616 | [
"PUB00000451",
"PUB00029353",
"PUB00029707",
"PUB00038439",
"PUB00038859"
] | [
"9521684",
"12729763",
"12657638",
"15938627",
"15946677"
] | [
"Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis.",
"Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular mode... | [
1998,
2003,
2003,
2005,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
7004,
220444,
100198,
45,
6301
] | 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",... | [
69,
32,
184,
82,
15,
187,
98,
11,
43,
126,
6,
6,
98
] | 13 | true | Homologous_superfamily | Alkaline-phosphatase-like, core domain superfamily | Alkaline-phosphatase-like, core domain superfamily | Alkaline_phosphatase_core_sf | 6 |
IPR017851 | 17,851 | Photosystem II extrinsic protein V, cytochrome c-550 precursor | PsbV_cyt_c550 | Family | 846 | 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 ... | [
"GO:0020037",
"GO:0015979",
"GO:0009523",
"GO:0042651"
] | [
"heme binding",
"photosynthesis",
"photosystem II",
"thylakoid membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01378",
"TIGR03045"
] | [
"PSII_Cyt550",
"PS_II_C550"
] | [
844,
830
] | 2 | [
"GP"
] | [
"GenProp0661"
] | [
"GP:GenProp0661"
] | 1 | [
"1f1c",
"1izl",
"1mz4",
"1s5l",
"1w5c",
"2axt",
"3a0b",
"3a0h",
"3kzi",
"3wu2",
"4fby",
"4il6",
"4ixq",
"4ixr",
"4pbu",
"4pj0",
"4rvy",
"4tnh",
"4tni",
"4tnj",
"4tnk",
"4ub6",
"4ub8",
"4v62",
"4v82",
"4yuu",
"5b5e",
"5b66",
"5e79",
"5e7c",
"5gth",
"5gti"... | 125 | [
"PUB00000610",
"PUB00015369",
"PUB00015381",
"PUB00015382"
] | [
"1646017",
"15258264",
"15233792",
"15474019"
] | [
"Sequence variability in bacterial cytochromes c.",
"Homologs of plant PsbP and PsbQ proteins are necessary for regulation of photosystem ii activity in the cyanobacterium Synechocystis 6803.",
"Structural characterization of photosystem II complex from red alga Porphyridium cruentum retaining extrinsic subunit... | [
1991,
2004,
2004,
2004
] | 4 | [
"IPR016003"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
354,
492
] | 2 | [] | [] | 0 | true | Family | Photosystem II extrinsic protein V, cytochrome c-550 precursor | Photosystem II extrinsic protein V, cytochrome c-550 precursor | PsbV_cyt_c550 | 8 |
IPR017853 | 17,853 | Glycoside hydrolase superfamily | GH_hydrolase_sf | Homologous_superfamily | 1,149,347 | false | false | This entry represents the catalytic TIM β/α barrel common to many different families of glycosyl hydrolases found in all groups of organisms including viruses and Gene Transfer Agents (GTA) [ ]. In the GTA of Rhodobacter capsulatus (Rhodopseudomonas capsulata) a glycosyl hydrolase domain is associated with ORFg15 (RCAP... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51445"
] | [
""
] | [
1149347
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.2.1",
"R-BTA-114608",
"R-BTA-2022857",
"R-BTA-2024101",
"R-BTA-2142845",
"R-BTA-2160916",
"R-BTA-6798695",
"R-BTA-70221",
"R-BTA-975578",
"R-BTA-9840310",
"R-CEL-189085",
"R-CEL-2022857",
"R-CEL-2024101",
"R-CEL-2160916",
"R-CEL-2534343",
"R-CEL-381426",
"R-CEL-6798695",
"R-CEL-... | [
"EC:3.2.1",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-2022857",
"REACTOME:R-BTA-2024101",
"REACTOME:R-BTA-2142845",
"REACTOME:R-BTA-2160916",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70221",
"REACTOME:R-BTA-975578",
"REACTOME:R-BTA-9840310",
"REACTOME:R-CEL-189085",
"REACTOME:R-CEL-2022857",
... | 192 | [
"1a3h",
"1a47",
"1amy",
"1aq0",
"1aqh",
"1aqm",
"1ava",
"1b0i",
"1b1y",
"1b2y",
"1b30",
"1b31",
"1b3v",
"1b3w",
"1b3x",
"1b3y",
"1b3z",
"1b90",
"1b9z",
"1bag",
"1bf2",
"1bfn",
"1bg4",
"1bg9",
"1bga",
"1bgg",
"1bhg",
"1bli",
"1bpl",
"1bqc",
"1bsi",
"1btc"... | 3,796 | [
"PUB00004870",
"PUB00005266",
"PUB00021988",
"PUB00026374",
"PUB00026805",
"PUB00027171",
"PUB00027698",
"PUB00027699",
"PUB00055430",
"PUB00055431"
] | [
"7624375",
"8535779",
"11914097",
"11427528",
"11846790",
"12171933",
"14668328",
"10978344",
"11382219",
"12399927"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carbo... | [
1995,
1995,
2002,
2001,
2002,
2002,
2004,
2000,
2001,
2002
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4932,
676140,
458685,
1025,
8565
] | 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",... | [
1205,
91,
213,
167,
24,
303,
191,
87,
874,
240,
26,
28,
1724
] | 13 | true | Homologous_superfamily | Glycoside hydrolase superfamily | Glycoside hydrolase superfamily | GH_hydrolase_sf | 1 |
IPR017854 | 17,854 | Metallothionein domain superfamily | Metalthion_dom_sf | Homologous_superfamily | 3,499 | false | false | Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , ]. An empirical classification into three classes has been proposed by Fowler and coworkers [ ] and K... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF57868"
] | [
""
] | [
3499
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5661231",
"R-CFA-5661231",
"R-DRE-5661231",
"R-GGA-5661231",
"R-HSA-5661231",
"R-HSA-877300",
"R-MMU-5661231",
"R-RNO-5661231",
"R-SSC-5661231"
] | [
"REACTOME:R-BTA-5661231",
"REACTOME:R-CFA-5661231",
"REACTOME:R-DRE-5661231",
"REACTOME:R-GGA-5661231",
"REACTOME:R-HSA-5661231",
"REACTOME:R-HSA-877300",
"REACTOME:R-MMU-5661231",
"REACTOME:R-RNO-5661231",
"REACTOME:R-SSC-5661231"
] | 9 | [
"1aoo",
"1aqq",
"1aqr",
"1aqs",
"1dfs",
"1dft",
"1dmc",
"1dmd",
"1dme",
"1dmf",
"1fmy",
"1j5l",
"1j5m",
"1ji9",
"1jjd",
"1m0g",
"1m0j",
"1mhu",
"1mrb",
"1mrt",
"1qjk",
"1qjl",
"1rju",
"1t2y",
"2f5h",
"2fj4",
"2fj5",
"2mhu",
"2mrb",
"2mrt",
"4mt2",
"6grv"... | 35 | [
"PUB00001490",
"PUB00003570",
"PUB00003571",
"PUB00005944",
"PUB00026409",
"PUB00078698"
] | [
"2959513",
"1779825",
"1779826",
"2959504",
"11493688",
"21633816"
] | [
"Chemistry and biochemistry of metallothionein.",
"Overview of metallothionein.",
"Definitions and nomenclature of metallothioneins.",
"Nomenclature of metallothionein.",
"A metallothionein containing a zinc finger within a four-metal cluster protects a bacterium from zinc toxicity.",
"Metallothionein pro... | [
1987,
1991,
1991,
1987,
2001,
2011
] | 6 | [] | [] | 0 | 0 | null | [
"Bacillus phage phiCM3",
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Opisthokonta",
"ecological metagenomes"
] | [
1,
896,
1,
2593,
8
] | 5 | [
"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)"
] | [
4,
35,
13,
1,
14,
2
] | 6 | true | Homologous_superfamily | Metallothionein domain superfamily | Metallothionein domain superfamily | Metalthion_dom_sf | 6 |
IPR017855 | 17,855 | SMAD-like domain superfamily | SMAD-like_dom_sf | Homologous_superfamily | 24,005 | false | false | This superfamily represents SMAD (Mothers against decapentaplegic (MAD) homolog) (also called MH2 for MAD homology 2) domains as well as their structural homologues, such as the transactivation domain of interferon regulatory protein 3 (IRF3), both of which have a β-sandwich structural fold. SMAD domains are found at t... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.200.10"
] | [
""
] | [
24005
] | 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-1169408",
"R-BTA-1606341",
"R-BTA-168928",
"R-BTA-201451",
"R-BTA-3134973",
"R-BTA-3270619",
"R-BTA-5689880",
"R-BTA-8941326",
"R-BTA-9013973",
"R-BTA-918233",
"R-BTA-933541",
"R-BTA-936440",
"R-BTA-936964",
"R-CEL-1181150",
"R-CEL-1502540",
"R-CEL-201451",
"R-CEL-2173788",
... | [
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-1606341",
"REACTOME:R-BTA-168928",
"REACTOME:R-BTA-201451",
"REACTOME:R-BTA-3134973",
"REACTOME:R-BTA-3270619",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-8941326",
"REACTOME:R-BTA-9013973",
"REACTOME:R-BTA-918233",
"REACTOME:R-BTA-933541",
"REACTOME:R-... | 147 | [
"1dd1",
"1dev",
"1g88",
"1j2f",
"1khu",
"1khx",
"1mjs",
"1mk2",
"1mr1",
"1qwt",
"1u7f",
"1u7v",
"1ygs",
"1zoq",
"3a77",
"3dit",
"3dsh",
"3gmj",
"4r9p",
"5bvi",
"5c4v",
"5jej",
"5jek",
"5jel",
"5jem",
"5jeo",
"5jer",
"5oem",
"5oen",
"5xoc",
"5xod",
"5zoj"... | 39 | [
"PUB00010680",
"PUB00010681",
"PUB00010682"
] | [
"11779503",
"9214508",
"11483516"
] | [
"Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling.",
"A structural basis for mutational inactivation of the tumour suppressor Smad4.",
"Promoting bone morphogenetic protein signaling through negative regulation of inh... | [
2001,
1997,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Opisthokonta",
"Rhadinovirus",
"bird metagenome"
] | [
23930,
74,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
45,
15,
98,
62,
72
] | 6 | true | Homologous_superfamily | SMAD-like domain superfamily | SMAD-like domain superfamily | SMAD-like_dom_sf | 9 |
IPR017856 | 17,856 | Integrase-like, N-terminal | Integrase-like_N | Homologous_superfamily | 92,330 | false | false | This entry represents a structural domain with an α-helical, orthogonal bundle fold. Domains with this structure are found at the N-terminal (zinc-binding domain) of HIV integrase, and in the following hypothetical proteins: YebC from Escherichia coli, HP0162 from Helicobacter pylori (Campylobacter pylori) and aq1575 f... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.10.200",
"SSF46919"
] | [
"",
""
] | [
92314,
59168
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-162585",
"R-HSA-162588",
"R-HSA-162592",
"R-HSA-162594",
"R-HSA-164516",
"R-HSA-164525",
"R-HSA-164843",
"R-HSA-173107",
"R-HSA-175474",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910",
"R-HSA-9864848"
] | [
"REACTOME:R-HSA-162585",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-162594",
"REACTOME:R-HSA-164516",
"REACTOME:R-HSA-164525",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-175474",
"REACTOME:R-HSA-175567",
"REACTOME:R-HSA-177539",
"REACTOME:R-HSA-180... | 14 | [
"1e0e",
"1k6y",
"1kon",
"1lfp",
"1mw7",
"1wja",
"1wjb",
"1wjc",
"1wjd",
"1wje",
"1wjf",
"3f9k",
"3hpg",
"3hph",
"3jca",
"4f3q",
"4fw2",
"5cz2",
"5ejk",
"5ekz",
"5m0r",
"5u1c",
"6put",
"6puw",
"6puy",
"6puz",
"6rwl",
"6rwm",
"6rwn",
"6rwo",
"6u8q",
"6v3k"... | 65 | [
"PUB00024383",
"PUB00026646",
"PUB00027019"
] | [
"11101216",
"11743009",
"12060744"
] | [
"Refined solution structure of the dimeric N-terminal HHCC domain of HIV-2 integrase.",
"Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein.",
"Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus."
] | [
2000,
2001,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Retroviridae",
"unclassified sequences",
"uncultured marine group II/III euryarchaeote KM3_86_F07"
] | [
28697,
6374,
56673,
585,
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",... | [
4,
1,
3,
3,
2,
17,
17,
1,
2,
3,
1,
1,
7
] | 13 | true | Homologous_superfamily | Integrase-like, N-terminal | Integrase-like, N-terminal | Integrase-like_N | 5 |
IPR017857 | 17,857 | Coagulation factor-like, Gla domain superfamily | Coagulation_fac-like_Gla_dom | Homologous_superfamily | 11,696 | false | false | This superfamily represents the Gla domain found in a subset of coagulation factors (VII, IX and X), related blood regulators (such as vitamin K), and gla-containing proteins. Venom prothrombin activator D found in snakes, also represented in this entry, is functionally similar to blood coagulation factor Xa [ ]. This ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:4.10.740.10"
] | [
""
] | [
11696
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.21",
"R-BTA-114608",
"R-BTA-140834",
"R-BTA-140837",
"R-BTA-140875",
"R-BTA-159740",
"R-BTA-159763",
"R-BTA-159782",
"R-BTA-202733",
"R-CFA-140875",
"R-CFA-159740",
"R-CFA-159763",
"R-CFA-159782",
"R-CFA-202733",
"R-CFA-381426",
"R-CFA-8957275",
"R-GGA-140834",
"R-GGA-140837",... | [
"EC:3.4.21",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-140834",
"REACTOME:R-BTA-140837",
"REACTOME:R-BTA-140875",
"REACTOME:R-BTA-159740",
"REACTOME:R-BTA-159763",
"REACTOME:R-BTA-159782",
"REACTOME:R-BTA-202733",
"REACTOME:R-CFA-140875",
"REACTOME:R-CFA-159740",
"REACTOME:R-CFA-159763",
"REA... | 60 | [
"1cfh",
"1cfi",
"1dan",
"1ezq",
"1f0r",
"1f0s",
"1fak",
"1iod",
"1j34",
"1j35",
"1ksn",
"1lpg",
"1lpk",
"1lpz",
"1lqd",
"1lqv",
"1mgx",
"1nfu",
"1nfw",
"1nfx",
"1nfy",
"1nl0",
"1o5d",
"1p0s",
"1pfx",
"1w0y",
"1w2k",
"1whe",
"1whf",
"1wqv",
"1wss",
"1wtg"... | 111 | [
"PUB00004648",
"PUB00015411",
"PUB00015412",
"PUB00044565",
"PUB00044566",
"PUB00044567",
"PUB00160398",
"PUB00160399"
] | [
"3317405",
"7713897",
"8663165",
"18374189",
"11818531",
"18374194",
"10397729",
"2706986"
] | [
"Molecular cloning of matrix Gla protein: implications for substrate recognition by the vitamin K-dependent gamma-carboxylase.",
"Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.",
"Identification of the phospholipid binding si... | [
1987,
1995,
1996,
2008,
2002,
2008,
1999,
1989
] | 8 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
11696
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
22,
62,
38,
47
] | 4 | true | Homologous_superfamily | Coagulation factor-like, Gla domain superfamily | Coagulation factor-like, Gla domain superfamily | Coagulation_fac-like_Gla_dom | 7 |
IPR017859 | 17,859 | Treacle protein | Treacle | Family | 1,139 | false | false | Treacher Collins Syndrome (TCS) is an autosomal dominant disorder of craniofacial development, the features of which include conductive hearing loss and cleft palate [ , ]; it is the most common of the human mandibulo-facial dysostosis disorders [ ]. The TCS locus has been mapped to human chromosome 5q31.3-32 and the m... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR20787"
] | [
""
] | [
1139
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007652",
"PUB00007653"
] | [
"9096354",
"9042910"
] | [
"TCOF1 gene encodes a putative nucleolar phosphoprotein that exhibits mutations in Treacher Collins Syndrome throughout its coding region.",
"The mutational spectrum in Treacher Collins syndrome reveals a predominance of mutations that create a premature-termination codon."
] | [
1997,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Euteleostomi"
] | [
1139
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
10,
10
] | 3 | true | Family | Treacle protein | Treacle protein | Treacle | 4 |
IPR017860 | 17,860 | Peptidase M22, conserved site | Peptidase_M22_CS | Conserved_site | 19,977 | false | false | Glycoprotease (Gcp) ( ) [ ], or o-syaloglycoprotein endopeptidase, is a metalloprotease secreted by Pasteurella haemolytica which specifically cleaves O-sialoglycoproteins such as glycophorin A. It belongs to the peptidase family M22. The sequence of Gcp is highly similar to uncharacterised orthologues in most complete... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01016"
] | [
"GLYCOPROTEASE"
] | [
19977
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME"
] | [
"2.3.1.234",
"PDOC00779",
"R-HSA-6782315"
] | [
"EC:2.3.1.234",
"PROSITEDOC:PDOC00779",
"REACTOME:R-HSA-6782315"
] | 3 | [
"2ivn",
"2ivo",
"2ivp",
"2vwb",
"3en9",
"3enh",
"3wuh",
"3zet",
"3zeu",
"4k25",
"4wq4",
"4wq5",
"4ydu",
"5jmv",
"6gwj",
"6nbj",
"6z81",
"8iey",
"8ifx",
"8unk",
"8up5",
"9d85"
] | 22 | [
"PUB00002152"
] | [
"1885539"
] | [
"Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Peduoviridae",
"unclassified sequences"
] | [
597,
15179,
3906,
2,
293
] | 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",... | [
1,
1,
3,
1,
1,
3,
7,
1,
2,
3,
2,
1,
3
] | 13 | true | Conserved_site | Peptidase M22, conserved site | Peptidase M22, conserved site | Peptidase_M22_CS | 6 |
IPR017861 | 17,861 | Kae1/TsaD family | KAE1/TsaD | Family | 37,147 | false | false | The first characterised member of the Kae1/TsaD family was annotated as Gcp for O-sialoglycoprotein endopeptidase [ ], but this activity could not be confirmed [ ]. Later, its homologue, Kae1 from Pyrococcus abyssi, has been shown to have DNA-binding properties and apurinic-endonuclease activity [ ]. Members of this fa... | [] | [] | [] | 0 | [
"PRINTS",
"NCBIFAM"
] | [
"PR00789",
"TIGR00329"
] | [
"OSIALOPTASE",
"gcp_kae1"
] | [
36868,
33286
] | 2 | [
"EC",
"GP",
"REACTOME",
"REACTOME"
] | [
"2.3.1.234",
"GenProp1570",
"R-HSA-6782315",
"R-HSA-6787450"
] | [
"EC:2.3.1.234",
"GP:GenProp1570",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-6787450"
] | 4 | [
"2ivn",
"2ivo",
"2ivp",
"2vwb",
"3en9",
"3enh",
"3eno",
"3wuh",
"3zet",
"3zeu",
"4k25",
"4wq4",
"4wq5",
"4ydu",
"5jmv",
"6gwj",
"6n9a",
"6nak",
"6nbj",
"6s84",
"6z81",
"8ide",
"8iey",
"8ifx",
"8k20",
"8unk",
"8up5",
"9d85"
] | 28 | [
"PUB00002152",
"PUB00035406",
"PUB00035445",
"PUB00047751",
"PUB00059911",
"PUB00059916",
"PUB00101388"
] | [
"1885539",
"16564010",
"16874308",
"17766251",
"21285948",
"19578062",
"32047918"
] | [
"Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene.",
"A genome-wide screen identifies the evolutionarily conserved KEOPS complex as a telomere regulator.",
"Yeast homolog of a cancer-testis antigen defines a new transcription complex.",
"An archaeal orthologue ... | [
1991,
2006,
2006,
2007,
2011,
2009,
2020
] | 7 | [] | [
"IPR022450",
"IPR034680"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
938,
27227,
8314,
9,
659
] | 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",... | [
5,
2,
5,
3,
1,
8,
9,
2,
10,
7,
2,
2,
13
] | 13 | true | Family | Kae1/TsaD family | Kae1/TsaD family | KAE1/TsaD | 7 |
IPR017862 | 17,862 | SKI-interacting protein, SKIP | SKI-int_prot_SKIP | Family | 5,594 | false | false | SKIP (SKI-interacting protein) is an essential spliceosomal component and transcriptional coregulator, which may provide regulatory coupling of transcription initiation and splicing [ ]. SKIP was identified in a yeast 2-hybrid screen, where it was shown to interact with both the cellular and viral forms of SKI through ... | [
"GO:0000398",
"GO:0005681"
] | [
"mRNA splicing, via spliceosome",
"spliceosomal complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PANTHER"
] | [
"PTHR12096"
] | [
""
] | [
5594
] | 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-2173795",
"R-BTA-350054",
"R-BTA-72163",
"R-BTA-8941856",
"R-CEL-2173795",
"R-CEL-72163",
"R-DDI-72163",
"R-DME-2173795",
"R-DME-350054",
"R-DME-72163",
"R-HSA-1912408",
"R-HSA-210744",
"R-HSA-2122947",
"R-HSA-2173795",
"R-HSA-2644606",
"R-HSA-2894862",
"R-HSA-350054",
"R-HS... | [
"REACTOME:R-BTA-2173795",
"REACTOME:R-BTA-350054",
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-8941856",
"REACTOME:R-CEL-2173795",
"REACTOME:R-CEL-72163",
"REACTOME:R-DDI-72163",
"REACTOME:R-DME-2173795",
"REACTOME:R-DME-350054",
"REACTOME:R-DME-72163",
"REACTOME:R-HSA-1912408",
"REACTOME:R-HSA-21... | 28 | [
"3jb9",
"5gm6",
"5gmk",
"5lj3",
"5lj5",
"5lqw",
"5mps",
"5mq0",
"5mqf",
"5wsg",
"5xjc",
"5y88",
"5ylz",
"5yzg",
"5z56",
"5z57",
"5z58",
"6bk8",
"6exn",
"6ff4",
"6ff7",
"6icz",
"6id0",
"6id1",
"6j6g",
"6j6h",
"6j6n",
"6j6q",
"6qdv",
"6zym",
"7a5p",
"7aav"... | 62 | [
"PUB00043556",
"PUB00043557",
"PUB00043558"
] | [
"15052407",
"11522815",
"10644367"
] | [
"Transcriptional coregulator SNW/SKIP: the concealed tie of dissimilar pathways.",
"Ski interacts with the evolutionarily conserved SNW domain of Skip.",
"A role for SKIP in EBNA2 activation of CBF1-repressed promoters."
] | [
2004,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5594
] | 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,
1,
1,
2,
11,
5,
1,
6,
2,
1,
1,
6
] | 12 | true | Family | SKI-interacting protein, SKIP | SKI-interacting protein, SKIP | SKI-int_prot_SKIP | 2 |
IPR017864 | 17,864 | Arrestin, conserved site | Arrestin_CS | Conserved_site | 6,735 | false | false | G protein-coupled receptors are a large family of signalling molecules that respond to a wide variety of extracellular stimuli. The receptors relay the information encoded by the ligand through the activation of heterotrimeric G proteins and intracellular effector molecules. To ensure the appropriate regulation of the ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00295"
] | [
"ARRESTINS"
] | [
6735
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00267",
"R-BTA-2514859",
"R-BTA-418555",
"R-BTA-432720",
"R-BTA-432722",
"R-BTA-456926",
"R-BTA-5635838",
"R-BTA-5674135",
"R-BTA-5689880",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-9839389",
"R-CEL-2514859",
"R-CEL-432720",
"R-CEL-432722",
"R-CEL-456926",
"R-CEL-5099900",
"R-C... | [
"PROSITEDOC:PDOC00267",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-432722",
"REACTOME:R-BTA-456926",
"REACTOME:R-BTA-5635838",
"REACTOME:R-BTA-5674135",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BT... | 73 | [
"1ayr",
"1cf1",
"1g4m",
"1g4r",
"1jsy",
"1suj",
"1zsh",
"2wtr",
"3gc3",
"3gd1",
"3p2d",
"3ugu",
"3ugx",
"4j2q",
"4jqi",
"4zrg",
"4zwj",
"5dgy",
"5tv1",
"5w0p",
"6k3f",
"6kl7",
"6ni2",
"6pwc",
"6tko",
"6u1n",
"6up7",
"7df9",
"7dfa",
"7dfb",
"7dfc",
"7f1w"... | 95 | [
"PUB00000986",
"PUB00001029",
"PUB00001684",
"PUB00002739",
"PUB00004275",
"PUB00005126"
] | [
"8452755",
"15335861",
"7720881",
"1517224",
"9495348",
"2158671"
] | [
"Arrestin-subtypes in insect antennae.",
"Arresting G-protein coupled receptor activity.",
"The arrestin superfamily: cone arrestins are a fourth family.",
"Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family.",
"X-ray crystal structure of arrestin from bovine rod outer segments.",
"A... | [
1993,
1993,
1995,
1992,
1998,
1990
] | 6 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
6735
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
16,
8,
12,
18,
22
] | 6 | true | Conserved_site | Arrestin, conserved site | Arrestin, conserved site | Arrestin_CS | 4 |
IPR017865 | 17,865 | F-actin capping protein, alpha subunit, conserved site | F-actin_cap_asu_CS | Conserved_site | 5,582 | false | false | The actin filament system, a prominent part of the cytoskeleton in eukaryotic cells, is both a static structure and a dynamic network that can undergo rearrangements: it is thought to be involved in processes such as cell movement and phagocytosis [ ], as well as muscle contraction. The F-actin capping protein binds in... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00748",
"PS00749"
] | [
"F_ACTIN_CAPPING_A_1",
"F_ACTIN_CAPPING_A_2"
] | [
5227,
4847
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00609",
"R-BTA-2132295",
"R-BTA-3371497",
"R-BTA-6807878",
"R-BTA-6811436",
"R-BTA-879415",
"R-BTA-983231",
"R-CEL-6807878",
"R-CEL-6811436",
"R-CEL-983231",
"R-DDI-6807878",
"R-DDI-983231",
"R-DME-3371497",
"R-DME-6807878",
"R-DME-6811436",
"R-DME-983231",
"R-GGA-3371497",
"R... | [
"PROSITEDOC:PDOC00609",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-6807878",
"REACTOME:R-BTA-6811436",
"REACTOME:R-BTA-879415",
"REACTOME:R-BTA-983231",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811436",
"REACTOME:R-CEL-983231",
"REACTOME:R-DDI-6807878",
"REACTOME:R-D... | 48 | [
"1izn",
"2kxp",
"2kz7",
"3aa0",
"3aa1",
"3aa6",
"3aa7",
"3aaa",
"3aae",
"3lk2",
"3lk3",
"3lk4",
"4akr",
"5adx",
"5afu",
"5nw4",
"6f1t",
"6f1u",
"6f38",
"6f3a",
"6znl",
"7ccc",
"7ds2",
"7ds3",
"7ds4",
"7ds6",
"7ds8",
"7dsa",
"7dsb",
"7pdz",
"7t5q",
"7z8f"... | 44 | [
"PUB00000981",
"PUB00002626"
] | [
"1711931",
"2341404"
] | [
"Variant cDNAs encoding proteins similar to the alpha subunit of chicken CapZ.",
"Beta-actinin is equivalent to Cap Z protein."
] | [
1991,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Faunusvirus sp."
] | [
4,
5577,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
9,
1,
2,
1,
10,
12,
1,
4,
16,
1,
1,
11
] | 12 | true | Conserved_site | F-actin capping protein, alpha subunit, conserved site | F-actin capping protein, alpha subunit, conserved site | F-actin_cap_asu_CS | 2 |
IPR017866 | 17,866 | Succinyl-CoA synthetase, beta subunit, conserved site | Succ-CoA_synthase_bsu_CS | Conserved_site | 32,173 | false | false | There are four different enzymes that share a similar catalytic mechanism which involves the phosphorylation by ATP (or GTP) of a specific histidine residue in the active site. These enzymes are: ATP citrate-lyase ( ) [ ], the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues, catalyz... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01217"
] | [
"SUCCINYL_COA_LIG_3"
] | [
32173
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"6.2.1",
"6.2.1.5",
"PWY-5392",
"PWY-5537",
"PWY-5538",
"PWY-5690",
"PWY-6728",
"PWY-6969",
"PWY-7384",
"PWY-8347",
"PWY-8354",
"PDOC00335",
"R-BTA-6798695",
"R-BTA-71403",
"R-BTA-75105",
"R-BTA-9837999",
"R-CEL-6798695",
"R-CEL-71403",
"R-CEL-75105",
"R-CEL-9837999",
"R-DDI-... | [
"EC:6.2.1",
"EC:6.2.1.5",
"METACYC:PWY-5392",
"METACYC:PWY-5537",
"METACYC:PWY-5538",
"METACYC:PWY-5690",
"METACYC:PWY-6728",
"METACYC:PWY-6969",
"METACYC:PWY-7384",
"METACYC:PWY-8347",
"METACYC:PWY-8354",
"PROSITEDOC:PDOC00335",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-71403",
"REACTOM... | 38 | [
"1cqi",
"1cqj",
"1euc",
"1eud",
"1jkj",
"1jll",
"1scu",
"2fp4",
"2fpg",
"2fpi",
"2fpp",
"2nu6",
"2nu7",
"2nu8",
"2nu9",
"2nua",
"2scu",
"3mwd",
"3mwe",
"3pff",
"3ufx",
"4xx0",
"5cae",
"5tde",
"5tdf",
"5tdm",
"5tdz",
"5te1",
"5teq",
"5tes",
"5tet",
"6g4q"... | 68 | [
"PUB00000280",
"PUB00001411",
"PUB00002257",
"PUB00005004"
] | [
"3002435",
"1371749",
"7961516",
"8401211"
] | [
"Primary structure of the succinyl-CoA synthetase of Escherichia coli.",
"Cloning and expression of a human ATP-citrate lyase cDNA.",
"Genetics of the serine cycle in Methylobacterium extorquens AM1: identification, sequence, and mutation of three new genes involved in C1 assimilation, orf4, mtkA, and mtkB.",
... | [
1985,
1992,
1994,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
697,
18475,
12566,
435
] | 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",... | [
10,
4,
11,
10,
1,
20,
10,
2,
4,
19,
1,
3,
17
] | 13 | true | Conserved_site | Succinyl-CoA synthetase, beta subunit, conserved site | Succinyl-CoA synthetase, beta subunit, conserved site | Succ-CoA_synthase_bsu_CS | 7 |
IPR017867 | 17,867 | Protein-tyrosine phosphatase, low molecular weight | Tyr_phospatase_low_mol_wt | Family | 29,293 | false | false | This entry represents the low molecular weight (LMW) protein-tyrosine phosphatases (or acid phosphatase), which act on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates [ , ]. The structure of a LMW PTPase has been solved by X-ray crystallography [ ] and is found to form... | [
"GO:0004725",
"GO:0006470"
] | [
"protein tyrosine phosphatase activity",
"protein dephosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00719"
] | [
"LMWPTPASE"
] | [
29293
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3.48",
"R-HSA-9635465",
"R-HSA-9636383",
"R-HSA-9636467",
"R-HSA-9637628"
] | [
"EC:3.1.3.48",
"REACTOME:R-HSA-9635465",
"REACTOME:R-HSA-9636383",
"REACTOME:R-HSA-9636467",
"REACTOME:R-HSA-9637628"
] | 5 | [
"1bvh",
"1c0e",
"1d1p",
"1d1q",
"1d2a",
"1dg9",
"1p8a",
"1phr",
"1pnt",
"1u2p",
"1u2q",
"1xww",
"1z12",
"1z13",
"1zgg",
"2cwd",
"2fek",
"2luo",
"2p4u",
"2wja",
"2wmy",
"3ido",
"3ily",
"3js5",
"3jvi",
"3n8i",
"3rof",
"4d74",
"4egs",
"4eti",
"4etm",
"4etn"... | 63 | [
"PUB00002706",
"PUB00004186",
"PUB00005003",
"PUB00035793",
"PUB00035794",
"PUB00035795",
"PUB00035796",
"PUB00035797",
"PUB00035798"
] | [
"1587862",
"8052313",
"1304913",
"9818190",
"14625689",
"12678841",
"16672235",
"8948575",
"9646865"
] | [
"Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase.",
"The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase.",
"Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase.",
... | [
1992,
1994,
1992,
1998,
2003,
2003,
2006,
1996,
1998
] | 9 | [] | [
"IPR002115"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
31,
24433,
4530,
2,
297
] | 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",... | [
7,
1,
2,
8,
2,
5,
4,
1,
3,
13,
1,
1,
6
] | 13 | true | Family | Protein-tyrosine phosphatase, low molecular weight | Protein-tyrosine phosphatase, low molecular weight | Tyr_phospatase_low_mol_wt | 6 |
IPR017868 | 17,868 | Filamin/ABP280 repeat-like | Filamin/ABP280_rpt-like | Repeat | 30,716 | false | false | The many different actin cross-linking proteins share a common architecture, consisting of a globular actin-binding domain and an extended rod. Whereas their actin-binding domains consist of two calponin homology domains (see ), their rods fall into three families. The rod domain of the family including the Dictyosteli... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00630",
"PS50194"
] | [
"Filamin",
"FILAMIN_REPEAT"
] | [
23858,
30252
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50194",
"R-CEL-6798695",
"R-DDI-114608",
"R-DDI-1169408",
"R-DDI-446353",
"R-DDI-5627123",
"R-DDI-5673000",
"R-DDI-5675221",
"R-DME-114608",
"R-DME-1169408",
"R-DME-446353",
"R-DME-5627123",
"R-DRE-983168",
"R-HSA-114608",
"R-HSA-1169408",
"R-HSA-430116",
"R-HSA-446353",
"R-HS... | [
"PROSITEDOC:PDOC50194",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DDI-114608",
"REACTOME:R-DDI-1169408",
"REACTOME:R-DDI-446353",
"REACTOME:R-DDI-5627123",
"REACTOME:R-DDI-5673000",
"REACTOME:R-DDI-5675221",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-1169408",
"REACTOME:R-DME-446353",
"REACTOME:R-DM... | 29 | [
"1ksr",
"1qfh",
"1v05",
"1wlh",
"2aav",
"2bp3",
"2brq",
"2d7m",
"2d7n",
"2d7o",
"2d7p",
"2d7q",
"2di7",
"2di8",
"2di9",
"2dia",
"2dib",
"2dic",
"2dj4",
"2dlg",
"2dmb",
"2dmc",
"2ds4",
"2e9i",
"2e9j",
"2ee6",
"2ee9",
"2eea",
"2eeb",
"2eec",
"2eed",
"2j3s"... | 80 | [
"PUB00003939",
"PUB00010567"
] | [
"9164464",
"10467095"
] | [
"The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold.",
"Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod."
] | [
1997,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
244,
2005,
28409,
22,
36
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
20,
48,
99,
35,
90,
40,
5,
45,
23
] | 9 | true | Repeat | Filamin/ABP280 repeat-like | Filamin/ABP280 repeat-like | Filamin/ABP280_rpt-like | 2 |
IPR017870 | 17,870 | FeS cluster insertion, C-terminal, conserved site | FeS_cluster_insertion_CS | Conserved_site | 32,655 | false | false | This entry represents a conserved site at the C-terminal in ATAP proteins during FeS cluster formation and iron-binding proteins. A-type assembly protein (ATAP) is a conserved and essential member of the ISC, SUF, and NIF systems and plays an indispensable role in the FeS cluster assembly and the transfer process. The ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01152"
] | [
"HESB"
] | [
32655
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-1362409",
"R-BTA-9854311",
"R-DDI-1362409",
"R-DME-1362409",
"R-HSA-1362409",
"R-HSA-9854311",
"R-MMU-1362409",
"R-MMU-9854311",
"R-RNO-1362409",
"R-SCE-1362409",
"R-SPO-1362409"
] | [
"REACTOME:R-BTA-1362409",
"REACTOME:R-BTA-9854311",
"REACTOME:R-DDI-1362409",
"REACTOME:R-DME-1362409",
"REACTOME:R-HSA-1362409",
"REACTOME:R-HSA-9854311",
"REACTOME:R-MMU-1362409",
"REACTOME:R-MMU-9854311",
"REACTOME:R-RNO-1362409",
"REACTOME:R-SCE-1362409",
"REACTOME:R-SPO-1362409"
] | 11 | [
"1nwb",
"1r94",
"1r95",
"1s98",
"2apn",
"2d2a"
] | 6 | [
"PUB00003442",
"PUB00003602",
"PUB00010345",
"PUB00017348",
"PUB00017349",
"PUB00030961",
"PUB00058194",
"PUB00160404",
"PUB00160405",
"PUB00160406"
] | [
"8875867",
"10217509",
"10322040",
"12207230",
"9582371",
"15050828",
"17698959",
"23586717",
"32108236",
"33007329"
] | [
"A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.",
"Organization and expression of nitrogen-fixation genes in the aerobic nitrogen-fixing unicellular cyanobacterium Synechococcus sp. strain RF-1.",
"SufS is a NifS-like protein, and SufD is necessary for stability... | [
1996,
1999,
1999,
2002,
1998,
2004,
2007,
2013,
2020,
2021
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
414,
26008,
5712,
16,
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",... | [
7,
2,
3,
1,
3,
3,
4,
1,
6,
6,
2,
2,
15
] | 13 | true | Conserved_site | FeS cluster insertion, C-terminal, conserved site | FeS cluster insertion, C-terminal, conserved site | FeS_cluster_insertion_CS | 7 |
IPR017871 | 17,871 | ABC transporter-like, conserved site | ABC_transporter-like_CS | Conserved_site | 1,854,037 | false | false | This entry represents a conserved region found in a group of related ATP-binding proteins and is associated with ATP-binding [ , , , , ]. The proteins belonging to this group also contain one or two copies of the 'A' consensus sequence [ ] or the 'P-loop' sequence motif [ ]. ABC transporters belong to the ATP-Binding C... | [
"GO:0005524",
"GO:0016887"
] | [
"ATP binding",
"ATP hydrolysis activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00211"
] | [
"ABC_TRANSPORTER_1"
] | [
1854037
] | 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-1660661",
"R-BTA-189483",
"R-BTA-2142691",
"R-BTA-382556",
"R-BTA-9707564",
"R-BTA-9753281",
"R-BTA-9758890",
"R-CEL-1369007",
"R-CEL-159418",
"R-CEL-189483",
"R-CEL-2142845",
"R-CEL-382556",
"R-CEL-9748787",
"R-CEL-9749641",
"R-CEL-9753281",
"R-CEL-9754706",
"R-CFA-159418",
... | [
"REACTOME:R-BTA-1660661",
"REACTOME:R-BTA-189483",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-382556",
"REACTOME:R-BTA-9707564",
"REACTOME:R-BTA-9753281",
"REACTOME:R-BTA-9758890",
"REACTOME:R-CEL-1369007",
"REACTOME:R-CEL-159418",
"REACTOME:R-CEL-189483",
"REACTOME:R-CEL-2142845",
"REACTOME:R-... | 279 | [
"1b0u",
"1f3o",
"1g29",
"1g6h",
"1g9x",
"1gaj",
"1ji0",
"1jj7",
"1l2t",
"1l7v",
"1mt0",
"1mv5",
"1oxs",
"1oxt",
"1oxu",
"1oxv",
"1q12",
"1q1b",
"1q1e",
"1q3h",
"1r0w",
"1r0x",
"1r0y",
"1r0z",
"1r10",
"1v43",
"1vci",
"1xef",
"1xf9",
"1xfa",
"1xmi",
"1yqt"... | 1,054 | [
"PUB00000705",
"PUB00001131",
"PUB00002368",
"PUB00003805",
"PUB00003995",
"PUB00003996",
"PUB00004290",
"PUB00005361",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654"
] | [
"3288195",
"6329717",
"2229036",
"1977073",
"3762694",
"3762695",
"9872322",
"2126155",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270"
] | [
"A family of closely related ATP-binding subunits from prokaryotic and eukaryotic cells.",
"Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.",
"Binding protein-dependent transport systems.",
"Stru... | [
1988,
1982,
1990,
1990,
1986,
1986,
1998,
1990,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
2001
] | 18 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
29276,
1562132,
245313,
76,
3,
17237
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
451,
80,
172,
119,
75,
206,
134,
33,
315,
223,
27,
16,
568
] | 13 | true | Conserved_site | ABC transporter-like, conserved site | ABC transporter-like, conserved site | ABC_transporter-like_CS | 8 |
IPR017872 | 17,872 | Pyrimidine-nucleoside phosphorylase, conserved site | Pyrmidine_PPase_CS | Conserved_site | 15,880 | false | false | Two highly similar activities are represented in this group: thymidine phosphorylase (TP, gene deoA, ) and pyrimidine-nucleoside phosphorylase (PyNP, gene pdp, ). Both are dimeric enzymes that function in the salvage pathway to catalyse the reversible phosphorolysis of pyrimidine nucleosides to the free base and sugar ... | [
"GO:0006206"
] | [
"pyrimidine nucleobase metabolic process"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS00647"
] | [
"THYMID_PHOSPHORYLASE"
] | [
15880
] | 1 | [
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME"
] | [
"2.4.2",
"2.4.2.4",
"PWY-7181",
"R-HSA-73614",
"R-HSA-73621"
] | [
"EC:2.4.2",
"EC:2.4.2.4",
"METACYC:PWY-7181",
"REACTOME:R-HSA-73614",
"REACTOME:R-HSA-73621"
] | 5 | [
"1azy",
"1brw",
"1otp",
"1tpt",
"1uou",
"2dsj",
"2j0f",
"2tpt",
"2wk5",
"2wk6",
"3h5q",
"4ead",
"4eaf",
"4ga4",
"4ga5",
"4ga6",
"4lhm",
"4x46",
"4xr5",
"4yek",
"4yyy",
"5ep8",
"5ey3",
"5oln",
"7m7k"
] | 25 | [
"PUB00010722",
"PUB00010723",
"PUB00010724"
] | [
"9310231",
"9698549",
"9817849"
] | [
"Platelet-derived endothelial cell growth factor thymidine phosphorylase in tumour growth and response to therapy.",
"Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase.",
"The crystal structure of pyrimidine nucleoside phosphorylase in a closed... | [
1997,
1998,
1998
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
372,
14462,
824,
222
] | 4 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens"
] | [
2,
1,
5
] | 3 | true | Conserved_site | Pyrimidine-nucleoside phosphorylase, conserved site | Pyrimidine-nucleoside phosphorylase, conserved site | Pyrmidine_PPase_CS | 1 |
IPR017873 | 17,873 | Cysteine-rich Golgi apparatus protein 1 repeat, eukaryote | Cys-rich_GLG1_repeat_euk | Repeat | 3,372 | false | false | This entry is found in Golgi apparatus protein 1 (GLG1, ) and related proteins in the metazoa. GLG1 is located in Golgi cisterns of various cell types, can bind fibroblast growth factor and E-selectin. Sixteen cysteine-rich GLG1 repeats form the core of the protein and are located in the lumen. The C-terminal part of G... | [
"GO:0000139"
] | [
"Golgi membrane"
] | [
"cellular_component"
] | 1 | [
"PROFILE"
] | [
"PS51289"
] | [
"GLG1_C_RICH"
] | [
3372
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-202733",
"R-HSA-202733",
"R-MMU-202733",
"R-RNO-202733"
] | [
"REACTOME:R-CEL-202733",
"REACTOME:R-HSA-202733",
"REACTOME:R-MMU-202733",
"REACTOME:R-RNO-202733"
] | 4 | [] | 0 | [
"PUB00003683",
"PUB00043660"
] | [
"1448090",
"12029485"
] | [
"Identification of a cysteine-rich receptor for fibroblast growth factors.",
"Identification and characterization of an insect homologue of the vertebrate Golgi apparatus protein 1 (MG-160/cysteine-rich fibroblast growth factor receptor/E-selectin ligand-1/latent transforming growth factor-beta complex protein-1)... | [
1992,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Nocardia cerradoensis"
] | [
3371,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
2,
4,
6,
4
] | 6 | true | Repeat | Cysteine-rich Golgi apparatus protein 1 repeat, eukaryote | Cysteine-rich Golgi apparatus protein 1 repeat, eukaryote | Cys-rich_GLG1_repeat_euk | 7 |
IPR017874 | 17,874 | CRIC domain | CRIC_domain | Domain | 5,719 | false | false | The multi-domain protein Connector enhancer of kinase suppressor of ras (Connector enhancer of KSR) (CNK) functions as a scaffold in several signal cascades and acts on proliferation, differentiation and apoptosis. CNK connects upstream activators and downstream targets of Ras- and Rho-dependent signalling pathways and... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF10534",
"PS51290"
] | [
"CRIC_ras_sig",
"CRIC"
] | [
5679,
5603
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-5674135",
"R-HSA-5674135",
"R-HSA-6802946",
"R-HSA-6802948",
"R-HSA-6802952",
"R-HSA-6802955",
"R-HSA-9649948",
"R-HSA-9656223",
"R-MMU-5674135",
"R-RNO-5674135"
] | [
"REACTOME:R-CEL-5674135",
"REACTOME:R-HSA-5674135",
"REACTOME:R-HSA-6802946",
"REACTOME:R-HSA-6802948",
"REACTOME:R-HSA-6802952",
"REACTOME:R-HSA-6802955",
"REACTOME:R-HSA-9649948",
"REACTOME:R-HSA-9656223",
"REACTOME:R-MMU-5674135",
"REACTOME:R-RNO-5674135"
] | 10 | [
"8bw8",
"8bw9",
"9k1l"
] | 3 | [
"PUB00043661",
"PUB00043662"
] | [
"12028359",
"16289034"
] | [
"Synaptic localization of membrane-associated guanylate kinase-interacting protein mediated by the pleckstrin homology domain.",
"The scaffold protein CNK1 interacts with the angiotensin II type 2 receptor."
] | [
2002,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
4,
5715
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
57,
1,
23,
8,
15
] | 6 | true | Domain | CRIC domain | CRIC domain | CRIC_domain | 5 |
IPR017878 | 17,878 | TB domain | TB_dom | Domain | 12,245 | false | false | The transforming growth factor beta family of cytokines, are potent and multifunctional signalling molecules. Prior to ligand receptor binding there exist extracellular regulators that target these cytokines and facilitate the formation of morphogen gradients that control developmental processes. Some of these proteins... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00683",
"PS51364"
] | [
"TB",
"TB"
] | [
10020,
12228
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1474228",
"R-BTA-1566948",
"R-BTA-2129379",
"R-BTA-216083",
"R-BTA-2173789",
"R-BTA-2473224",
"R-BTA-381426",
"R-BTA-8957275",
"R-DRE-2473224",
"R-HSA-1474228",
"R-HSA-1566948",
"R-HSA-2129379",
"R-HSA-216083",
"R-HSA-2173789",
"R-HSA-2473224",
"R-HSA-381426",
"R-HSA-8957275",... | [
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1566948",
"REACTOME:R-BTA-2129379",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-2173789",
"REACTOME:R-BTA-2473224",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-DRE-2473224",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-1566948",
"REACTOME:... | 31 | [
"1apj",
"1ksq",
"1uzj",
"1uzk",
"1uzp",
"1uzq",
"2b0u",
"2p6a",
"2w86",
"3b4v",
"3hh2",
"3sek",
"5jhw",
"5ms9"
] | 14 | [
"PUB00001310",
"PUB00022024",
"PUB00031953",
"PUB00039476"
] | [
"9362480",
"14607119",
"15062093",
"16198295"
] | [
"Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils.",
"Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta.",
"Structure of the integrin bindin... | [
1997,
2003,
2004,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Burkholderia",
"Eukaryota",
"bird metagenome"
] | [
4,
12240,
1
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
36,
57,
33,
42
] | 4 | true | Domain | TB domain | TB domain | TB_dom | 9 |
IPR017879 | 17,879 | PotA, ATP-binding domain | PotA_ATP-bd | Domain | 9,791 | false | false | PotA is a bacterial protein that imports putrescine and spermidine [ , , ]. Spermidine is a polyamine involved in cellular metabolism that can be used to stimulate the enzyme the RNA polymerase, T7 RNA polymerase. Putrescine attacks s-adenosyl methionine and converts it to spermidine. PotA has two domains with the N-te... | [
"GO:0015417",
"GO:0015594",
"GO:0015846",
"GO:0016020"
] | [
"ABC-type polyamine transporter activity",
"ABC-type putrescine transporter activity",
"polyamine transport",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"CDD"
] | [
"cd03300"
] | [
"ABC_PotA_N"
] | [
9791
] | 1 | [
"EC"
] | [
"7.6.2.11"
] | [
"EC:7.6.2.11"
] | 1 | [
"8y5f",
"8y5g",
"8y5h",
"8y5i",
"8zx1"
] | 5 | [
"PUB00002665",
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654",
"PUB00060280",
"PUB00060281"
] | [
"1939142",
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270",
"21318881",
"11976340"
] | [
"Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome.",
"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 cas... | [
1991,
1998,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
2001,
2011,
2002
] | 14 | [
"IPR003439"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Hadarchaeum yellowstonense",
"metagenomes"
] | [
9685,
7,
1,
98
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | PotA, ATP-binding domain | PotA, ATP-binding domain | PotA_ATP-bd | 9 |
IPR017881 | 17,881 | Nitrite reductase (NADH) small subunit | NirD | Family | 6,697 | false | false | In Proteobacteria and Actinobacteria the main nitrite reductase activity is contributed by the NADH-dependent nitrite reductase, which detoxifies the nitrite formed as the product of nitrate reduction. The NADH-nitrite reductase operon consists of 4 genes: nirB, nirD, nirC and cysG. The enzyme is formed by the two subu... | [
"GO:0008942"
] | [
"nitrite reductase [NAD(P)H] activity"
] | [
"molecular_function"
] | 1 | [
"PANTHER"
] | [
"PTHR40562"
] | [
""
] | [
6697
] | 1 | [
"EC"
] | [
"1.7.1.15"
] | [
"EC:1.7.1.15"
] | 1 | [
"2jo6",
"2jza",
"3c0d",
"4aiv"
] | 4 | [
"PUB00043673",
"PUB00043674",
"PUB00043837",
"PUB00080966"
] | [
"8919448",
"2200672",
"16271700",
"11460929"
] | [
"Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen starvation?",
"Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome.",
"Multiple Rieske proteins in prokaryotes: w... | [
1996,
1990,
2005,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
6655,
15,
27
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Nitrite reductase (NADH) small subunit | Nitrite reductase (NADH) small subunit | NirD | 1 |
IPR017884 | 17,884 | SANT domain | SANT_dom | Domain | 87,314 | false | false | The SANT domain is a motif of ~50 amino acids present in proteins involved in chromatin-remodelling and transcription regulation. This eukaryotic domain was identified in nuclear receptor co-repressors and named after switching-defective protein 3 (Swi3), adaptor 2 (Ada2), nuclear receptor co-repressor (N-CoR) and tran... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51293"
] | [
"SANT"
] | [
87314
] | 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-3371453",
"R-BTA-9772755",
"R-CEL-381340",
"R-CEL-383280",
"R-CEL-5250924",
"R-DDI-5689901",
"R-DME-3214815",
"R-DME-5689880",
"R-DME-983231",
"R-DRE-3371453",
"R-DRE-5689880",
"R-DRE-5689901",
"R-HSA-1251985",
"R-HSA-1989781",
"R-HSA-2122947",
"R-HSA-2151201",
"R-HSA-2173795"... | [
"REACTOME:R-BTA-3371453",
"REACTOME:R-BTA-9772755",
"REACTOME:R-CEL-381340",
"REACTOME:R-CEL-383280",
"REACTOME:R-CEL-5250924",
"REACTOME:R-DDI-5689901",
"REACTOME:R-DME-3214815",
"REACTOME:R-DME-5689880",
"REACTOME:R-DME-983231",
"REACTOME:R-DRE-3371453",
"REACTOME:R-DRE-5689880",
"REACTOME:R... | 123 | [
"1guu",
"1mbe",
"1mbf",
"1ofc",
"1wgx",
"1x41",
"1xc5",
"2cjj",
"2cqr",
"2crg",
"2cu7",
"2elk",
"2eqr",
"2iw5",
"2ltp",
"2m2e",
"2nog",
"2uxn",
"2uxx",
"2v1d",
"2x0l",
"2xaf",
"2xag",
"2xah",
"2xaj",
"2xaq",
"2xas",
"2y48",
"2y9y",
"2y9z",
"2yqk",
"2yus"... | 199 | [
"PUB00005459",
"PUB00029414",
"PUB00043689"
] | [
"8882580",
"14536084",
"15040448"
] | [
"The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB.",
"Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.",
"The SANT domain: a unique histone-tail-binding module?"
] | [
1996,
2003,
2004
] | 3 | [
"IPR001005"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
5,
87308,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
210,
37,
199,
44,
105,
94,
6,
141,
122,
8,
5,
371
] | 12 | true | Domain | SANT domain | SANT domain | SANT_dom | 3 |
IPR017887 | 17,887 | Transcription factor TCP subgroup | TF_TCP_subgr | Domain | 15,920 | false | false | The TCP domain has been named after its first characterised members (TB1, CYC and PCFs). So far, members of the TCP family have only been found in plants and function in processes related to cell proliferation. The TCP domain is probably involved in DNA-binding and protein-protein interactions [ ]. The TCP domain is pr... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF03634",
"PS51369"
] | [
"TCP",
"TCP"
] | [
15878,
15457
] | 2 | [] | [] | [] | 0 | [
"5zkt",
"7vp1",
"7vp2",
"7vp3",
"7vp4",
"7vp5",
"7vp6",
"7vp7"
] | 8 | [
"PUB00008402"
] | [
"10363373"
] | [
"The TCP domain: a motif found in proteins regulating plant growth and development."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"marine sediment metagenome"
] | [
15919,
1
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
96,
62,
1,
114
] | 4 | true | Domain | Transcription factor TCP subgroup | Transcription factor TCP subgroup | TF_TCP_subgr | 7 |
IPR017888 | 17,888 | CYC/TB1, R domain | CYC/TB1_R_domain | Domain | 4,793 | false | false | Members of the TCP family of transcription factors have so far only been found in plants, where they are implicated in processes related to cell proliferation. It appears that TCP domain (see ) protein have been recruited during evolution to control cell division and growth in various developmental processes. The TCP p... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51370"
] | [
"R"
] | [
4793
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00008402",
"PUB00043685"
] | [
"10363373",
"14990618"
] | [
"The TCP domain: a motif found in proteins regulating plant growth and development.",
"Regulated expression of a novel TCP domain transcription factor indicates an involvement in the control of meristem activation processes in Solanum tuberosum."
] | [
1999,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halopenitus persicus"
] | [
11,
4781,
1
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
21,
4,
10
] | 3 | true | Domain | CYC/TB1, R domain | CYC/TB1, R domain | CYC/TB1_R_domain | 4 |
IPR017889 | 17,889 | Avidin-like, conserved site | Avidin-like_CS | Conserved_site | 258 | false | false | Avidin [ ] is a minor constituent of egg white in several groups of oviparous vertebrates. Avidin, which was discovered in the 1920's, takes its name from the avidity with which it binds biotin. These two molecules bind so strongly that is extremely difficult to separate them. Streptavidin is a protein produced by Stre... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00577"
] | [
"AVIDIN_1"
] | [
258
] | 1 | [] | [] | [] | 0 | [
"1avd",
"1ave",
"1df8",
"1hqq",
"1hxl",
"1hxz",
"1hy2",
"1i9h",
"1ij8",
"1kff",
"1kl3",
"1kl4",
"1kl5",
"1lcv",
"1lcw",
"1lcz",
"1ldo",
"1ldq",
"1lel",
"1luq",
"1mk5",
"1mm9",
"1moy",
"1n43",
"1n4j",
"1n7y",
"1n9m",
"1n9y",
"1nbx",
"1nc9",
"1ndj",
"1nqm"... | 292 | [
"PUB00001099",
"PUB00001496",
"PUB00003308",
"PUB00003567",
"PUB00004675"
] | [
"8500658",
"2784773",
"8515446",
"2388586",
"2928324"
] | [
"The SpEGF III gene encodes a member of the fibropellins: EGF repeat-containing proteins that form the apical lamina of the sea urchin embryo.",
"Avidin-like domain in an epidermal growth factor homolog from a sea urchin.",
"Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its f... | [
1993,
1989,
1993,
1990,
1989
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Deuterostomia"
] | [
10,
248
] | 2 | [] | [] | 0 | true | Conserved_site | Avidin-like, conserved site | Avidin-like, conserved site | Avidin-like_CS | 9 |
IPR017891 | 17,891 | Insulin-like growth factor binding protein, N-terminal, Cys-rich conserved site | Insulin_GF-bd_Cys-rich_CS | Conserved_site | 8,310 | false | false | The insulin-like growth factors (IGF-I and IGF-II) bind to specific binding proteins in extracellular fluids with high affinity [ , ]. These IGF-binding proteins (IGFBP) prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cells culture. They s... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00222"
] | [
"IGFBP_N_1"
] | [
8310
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-381426",
"R-BTA-6803211",
"R-BTA-8957275",
"R-DRE-381426",
"R-GGA-381426",
"R-GGA-8957275",
"R-HSA-2032785",
"R-HSA-380994",
"R-HSA-381426",
"R-HSA-6803211",
"R-HSA-8951671",
"R-HSA-8957275",
"R-HSA-9615017",
"R-MMU-381426",
"R-MMU-6803211",
"R-MMU-8957275",
"R-RNO-381426",
... | [
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-6803211",
"REACTOME:R-BTA-8957275",
"REACTOME:R-DRE-381426",
"REACTOME:R-GGA-381426",
"REACTOME:R-GGA-8957275",
"REACTOME:R-HSA-2032785",
"REACTOME:R-HSA-380994",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-6803211",
"REACTOME:R-HSA-8951671",
"REACTOME:R-H... | 21 | [
"1wqj",
"2dsp",
"2dsq",
"2dsr",
"7ufg",
"7wrq"
] | 6 | [
"PUB00003068",
"PUB00003677",
"PUB00004938",
"PUB00005642",
"PUB00013536",
"PUB00032303"
] | [
"1654338",
"1309586",
"1725860",
"7680510",
"9822601",
"15642270"
] | [
"Connective tissue growth factor: a cysteine-rich mitogen secreted by human vascular endothelial cells is related to the SRC-induced immediate early gene product CEF-10.",
"Proviral rearrangements and overexpression of a new cellular gene (nov) in myeloblastosis-associated virus type 1-induced nephroblastomas.",
... | [
1991,
1992,
1991,
1993,
1998,
2005
] | 6 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Metazoa"
] | [
10,
8300
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
35,
21,
36
] | 4 | true | Conserved_site | Insulin-like growth factor binding protein, N-terminal, Cys-rich conserved site | Insulin-like growth factor binding protein, N-terminal, Cys-rich conserved site | Insulin_GF-bd_Cys-rich_CS | 4 |
IPR017892 | 17,892 | Protein kinase, C-terminal | Pkinase_C | Domain | 72,649 | false | false | This domain is found in a large variety of protein kinases with different functions and dependencies. Protein kinase C, for example, is a calcium-activated, phospholipid-dependent serine- and threonine-specific enzyme. It is activated by diacylglycerol which, in turn, phosphorylates a range of cellular proteins. This d... | [
"GO:0004674",
"GO:0005524",
"GO:0006468"
] | [
"protein serine/threonine kinase activity",
"ATP binding",
"protein phosphorylation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF00433"
] | [
"Pkinase_C"
] | [
72649
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11",
"R-BTA-114516",
"R-BTA-1169091",
"R-BTA-416993",
"R-BTA-4419969",
"R-BTA-5099900",
"R-BTA-5218921",
"R-BTA-5625740",
"R-BTA-5625886",
"R-BTA-5668599",
"R-BTA-76005",
"R-BTA-8980692",
"R-BTA-9013106",
"R-BTA-9013149",
"R-BTA-9013418",
"R-BTA-9013422",
"R-CEL-111465",
"R-CE... | [
"EC:2.7.11",
"REACTOME:R-BTA-114516",
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-416993",
"REACTOME:R-BTA-4419969",
"REACTOME:R-BTA-5099900",
"REACTOME:R-BTA-5218921",
"REACTOME:R-BTA-5625740",
"REACTOME:R-BTA-5625886",
"REACTOME:R-BTA-5668599",
"REACTOME:R-BTA-76005",
"REACTOME:R-BTA-8980692",... | 617 | [
"1gzk",
"1gzn",
"1gzo",
"1mrv",
"1mry",
"1o6k",
"1o6l",
"1xjd",
"1zrz",
"2i0e",
"2jdo",
"2jdr",
"2jed",
"2r5t",
"2uw9",
"2x39",
"2xh5",
"3a60",
"3a61",
"3a62",
"3a8w",
"3a8x",
"3cqu",
"3cqw",
"3d0e",
"3e87",
"3e88",
"3e8d",
"3hdm",
"3hdn",
"3iw4",
"3mv5"... | 114 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004
] | 5 | [
"IPR000961"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Gammaretrovirus"
] | [
72644,
5
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
44,
26,
173,
54,
124,
113,
6,
18,
172,
7,
7,
57
] | 12 | true | Domain | Protein kinase, C-terminal | Protein kinase, C-terminal | Pkinase_C | 5 |
IPR017894 | 17,894 | HTH domain, IS21 transposase-type | HTH_IS21_transposase_type | Domain | 6,539 | false | false | This entry represents the IS21 transposase-type HTH domain. Autonomous mobile genetic elements such as transposons or insertion sequences (IS) encode an enzyme, called transposase, required for excising and inserting the mobile element. The IS21 is among the largest of bacterial IS elements and encodes a transposase de... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50531"
] | [
"HTH_IS21"
] | [
6539
] | 1 | [] | [] | [] | 0 | [
"8b4h",
"8q4d"
] | 2 | [
"PUB00007262"
] | [
"11315188"
] | [
"Transposase and cointegrase: specialized transposition proteins of the bacterial insertion sequence IS21 and related elements."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Enterobacteria phage fiAA91-ss",
"Eukaryota",
"Methanobacteriati",
"plasmids",
"unclassified sequences"
] | [
6370,
1,
11,
94,
8,
55
] | 6 | [] | [] | 0 | true | Domain | HTH domain, IS21 transposase-type | HTH domain, IS21 transposase-type | HTH_IS21_transposase_type | 4 |
IPR017895 | 17,895 | Helix-turn-helix, IS408/IS1162 transposase-type | HTH_IS408/IS1162_type | Domain | 2,455 | false | false | This entry represents the IS408/IS1162 transposase-type HTH domain. Autonomous mobile genetic elements such as transposons or insertion sequences (IS) encode an enzyme, called transposase, required for excising and inserting the mobile element. The IS21 is among the largest of bacterial IS elements and encodes a transp... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50532"
] | [
"HTH_IS408"
] | [
2455
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007262"
] | [
"11315188"
] | [
"Transposase and cointegrase: specialized transposition proteins of the bacterial insertion sequence IS21 and related elements."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2400,
6,
49
] | 3 | [] | [] | 0 | true | Domain | Helix-turn-helix, IS408/IS1162 transposase-type | Helix-turn-helix, IS408/IS1162 transposase-type | HTH_IS408/IS1162_type | 7 |
IPR017896 | 17,896 | 4Fe-4S ferredoxin-type, iron-sulphur binding domain | 4Fe4S_Fe-S-bd | Domain | 463,802 | false | false | Ferredoxins are a group of iron-sulphur proteins which mediate electron transfer in a wide variety of metabolic reactions. Ferredoxins can be divided into several subgroups depending upon the physiological nature of the iron-sulphur cluster(s). One of these subgroups are the 4Fe-4S ferredoxins, which are found in bacte... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF00037",
"PF12797",
"PF12798",
"PF12800",
"PF12801",
"PF12837",
"PF12838",
"PF13183",
"PF13187",
"PF13237",
"PF13247",
"PF13746",
"PF17179",
"PS51379"
] | [
"Fer4",
"Fer4_2",
"Fer4_3",
"Fer4_4",
"Fer4_5",
"Fer4_6",
"Fer4_7",
"Fer4_8",
"Fer4_9",
"Fer4_10",
"Fer4_11",
"Fer4_18",
"Fer4_22",
"4FE4S_FER_2"
] | [
61255,
4503,
516,
10507,
22400,
3211,
96807,
59786,
27316,
26390,
44837,
10415,
3737,
445079
] | 14 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"GenProp0839",
"GenProp0842",
"R-BTA-611105",
"R-BTA-6799198",
"R-CEL-611105",
"R-CEL-6799198",
"R-CEL-71403",
"R-CEL-73621",
"R-DDI-71403",
"R-DDI-73621",
"R-DME-611105",
"R-DME-6799198",
"R-DME-71403",
"R-DRE-71403",
"R-DRE-73621",
"R-GGA-372987",
"R-HSA-611105",
"R-HSA-6799198",... | [
"GP:GenProp0839",
"GP:GenProp0842",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-CEL-611105",
"REACTOME:R-CEL-6799198",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-73621",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-73621",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-6799198",
"REACTO... | 40 | [
"1a6l",
"1axq",
"1b0p",
"1b0t",
"1b0v",
"1bc6",
"1bd6",
"1blu",
"1bqx",
"1bwe",
"1c4a",
"1c4c",
"1clf",
"1d3w",
"1dax",
"1dfd",
"1dur",
"1dwl",
"1e08",
"1e7p",
"1f2g",
"1f5b",
"1f5c",
"1fca",
"1fd2",
"1fda",
"1fdb",
"1fdd",
"1fdn",
"1feh",
"1fer",
"1ff2"... | 972 | [
"PUB00001503",
"PUB00003332",
"PUB00003399"
] | [
"2185975",
"7966291",
"3129571"
] | [
"Recent developments in the field of iron-sulfur proteins.",
"Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 A resolution.",
"Examination of protein sequence homologies: IV. Twenty-seven bacterial ferredoxins."
] | [
1990,
1994,
1987
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
22764,
374793,
55016,
1,
317,
10911
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
36,
7,
10,
11,
42,
31,
24,
4,
43,
22,
3,
3,
76
] | 13 | true | Domain | 4Fe-4S ferredoxin-type, iron-sulphur binding domain | 4Fe-4S ferredoxin-type, iron-sulphur binding domain | 4Fe4S_Fe-S-bd | 8 |
IPR017897 | 17,897 | Thrombospondin, type 3 repeat | Thrombospondin_3_rpt | Repeat | 10,068 | false | false | Thrombospondins are multimeric multidomain glycoproteins that function at cell surfaces and in the extracellular matrix milieu. They act as regulators of cell interactions in vertebrates. They are divided into two subfamilies, A and B, according to their overall molecular organisation. The subgroup A proteins TSP-1 and... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51234"
] | [
"TSP3"
] | [
10068
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-216083",
"R-BTA-3000178",
"R-HSA-114608",
"R-HSA-186797",
"R-HSA-216083",
"R-HSA-3000170",
"R-HSA-3000178",
"R-HSA-5083635",
"R-HSA-5173214",
"R-HSA-8936459",
"R-MMU-114608",
"R-MMU-186797",
"R-MMU-216083",
"R-MMU-3000178",
"R-MMU-5173214",
"R-RNO-186797",
"R-RNO-216083",
"R... | [
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-3000178",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-186797",
"REACTOME:R-HSA-216083",
"REACTOME:R-HSA-3000170",
"REACTOME:R-HSA-3000178",
"REACTOME:R-HSA-5083635",
"REACTOME:R-HSA-5173214",
"REACTOME:R-HSA-8936459",
"REACTOME:R-MMU-114608",
"REACTOME:R-M... | 18 | [
"1ux6",
"1yo8",
"2rhp",
"3fby"
] | 4 | [
"PUB00037903",
"PUB00038581",
"PUB00043707"
] | [
"15014436",
"16186819",
"11687483"
] | [
"Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats.",
"Structure of the calcium-rich signature domain of human thrombospondin-2.",
"Thrombospondins: multifunctional regulators of cell interactions."
] | [
2004,
2005,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
6,
671,
9361,
30
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
18,
4,
23,
17,
15
] | 5 | true | Repeat | Thrombospondin, type 3 repeat | Thrombospondin, type 3 repeat | Thrombospondin_3_rpt | 7 |
IPR017898 | 17,898 | Vacuolar protein sorting-associated, VPS28, N-terminal | VPS28_N | Domain | 4,141 | false | false | The Endosomal Sorting Complex Required for Transport (ESCRT) complexes form the machinery driving protein sorting from endosomes to lysosomes. ESCRT complexes are central to receptor down-regulation, lysosome biogenesis, and budding of HIV. Yeast ESCRT-I consists of three protein subunits, Vps23, Vps28, and Vps37. In h... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51313"
] | [
"VPS28_N"
] | [
4141
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-917729",
"R-CEL-917729",
"R-DDI-917729",
"R-DME-917729",
"R-HSA-162588",
"R-HSA-174490",
"R-HSA-917729",
"R-HSA-9610379",
"R-HSA-9615710",
"R-MMU-917729",
"R-RNO-917729",
"R-SCE-917729"
] | [
"REACTOME:R-BTA-917729",
"REACTOME:R-CEL-917729",
"REACTOME:R-DDI-917729",
"REACTOME:R-DME-917729",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-917729",
"REACTOME:R-HSA-9610379",
"REACTOME:R-HSA-9615710",
"REACTOME:R-MMU-917729",
"REACTOME:R-RNO-917729",
"REACTOME:R-SCE-9... | 12 | [
"2caz",
"2f66",
"2f6m",
"2p22",
"6vme"
] | 5 | [
"PUB00039953",
"PUB00040552"
] | [
"16615893",
"16615894"
] | [
"ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes.",
"Structural and functional organization of the ESCRT-I trafficking complex."
] | [
2006,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
4,
4137
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
1,
1,
2,
6,
3,
1,
2,
7,
1,
1,
4
] | 12 | true | Domain | Vacuolar protein sorting-associated, VPS28, N-terminal | Vacuolar protein sorting-associated, VPS28, N-terminal | VPS28_N | 5 |
IPR017899 | 17,899 | Vacuolar protein sorting-associated, VPS28, C-terminal | VPS28_C | Domain | 4,221 | false | false | The Endosomal Sorting Complex Required for Transport (ESCRT) complexes form the machinery driving protein sorting from endosomes to lysosomes. ESCRT complexes are central to receptor down-regulation, lysosome biogenesis, and budding of HIV. Yeast ESCRT-I consists of three protein subunits, Vps23, Vps28, and Vps37. In h... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51310"
] | [
"VPS28_C"
] | [
4221
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-917729",
"R-CEL-917729",
"R-DDI-917729",
"R-DME-917729",
"R-HSA-162588",
"R-HSA-174490",
"R-HSA-917729",
"R-HSA-9610379",
"R-HSA-9615710",
"R-MMU-917729",
"R-RNO-917729",
"R-SCE-917729"
] | [
"REACTOME:R-BTA-917729",
"REACTOME:R-CEL-917729",
"REACTOME:R-DDI-917729",
"REACTOME:R-DME-917729",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-917729",
"REACTOME:R-HSA-9610379",
"REACTOME:R-HSA-9615710",
"REACTOME:R-MMU-917729",
"REACTOME:R-RNO-917729",
"REACTOME:R-SCE-9... | 12 | [
"2g3k",
"2j9u",
"2j9v",
"2j9w"
] | 4 | [
"PUB00039953",
"PUB00040552"
] | [
"16615893",
"16615894"
] | [
"ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes.",
"Structural and functional organization of the ESCRT-I trafficking complex."
] | [
2006,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanomassiliicoccus intestinalis",
"Eukaryota",
"marine sediment metagenome"
] | [
14,
2,
4203,
2
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
8,
1,
1,
2,
6,
3,
1,
2,
6,
1,
1,
5
] | 12 | true | Domain | Vacuolar protein sorting-associated, VPS28, C-terminal | Vacuolar protein sorting-associated, VPS28, C-terminal | VPS28_C | 3 |
IPR017900 | 17,900 | 4Fe-4S ferredoxin, iron-sulphur binding, conserved site | 4Fe4S_Fe_S_CS | Conserved_site | 378,588 | false | false | This entry represents a conserved site of Fe-4S ferredoxin, iron-sulphur binding domain Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s) [ , ]. One group, originally found in ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00198"
] | [
"4FE4S_FER_1"
] | [
378588
] | 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-611105",
"R-BTA-6799198",
"R-CEL-6799198",
"R-CEL-71403",
"R-CEL-73621",
"R-DDI-71403",
"R-DDI-73621",
"R-DME-611105",
"R-DME-6799198",
"R-DME-71403",
"R-DRE-71403",
"R-DRE-73621",
"R-GGA-372987",
"R-HSA-611105",
"R-HSA-6799198",
"R-HSA-71403",
"R-HSA-73621",
"R-HSA-8983711"... | [
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-CEL-6799198",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-73621",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-73621",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-6799198",
"REACTOME:R-DME-71403",
"REACTOME:R-DRE-71403",
"REACTOME:R-DRE-73621"... | 33 | [
"1a6l",
"1axq",
"1b0p",
"1b0t",
"1b0v",
"1bc6",
"1bd6",
"1blu",
"1bqx",
"1bwe",
"1c4a",
"1c4c",
"1clf",
"1d3w",
"1dur",
"1dwl",
"1e08",
"1e7p",
"1f2g",
"1f5b",
"1f5c",
"1fca",
"1fd2",
"1fda",
"1fdb",
"1fdd",
"1fdn",
"1feh",
"1fer",
"1frh",
"1fri",
"1frj"... | 893 | [
"PUB00003253",
"PUB00003332",
"PUB00003397",
"PUB00003406"
] | [
"2600971",
"7966291",
"3932661",
"2506358"
] | [
"Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 A resolution. Structural comparisons of bacterial ferredoxins.",
"Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 A resolution.",
"New perspectives on bacterial ferredoxin evolution.",
"... | [
1989,
1994,
1985,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
19452,
304185,
46244,
1,
41,
8665
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
32,
5,
9,
10,
37,
19,
18,
2,
36,
17,
2,
2,
61
] | 13 | true | Conserved_site | 4Fe-4S ferredoxin, iron-sulphur binding, conserved site | 4Fe-4S ferredoxin, iron-sulphur binding, conserved site | 4Fe4S_Fe_S_CS | 4 |
IPR017901 | 17,901 | C-CAP/cofactor C-like domain | C-CAP_CF_C-like | Domain | 15,289 | false | false | The C-CAP/cofactor C-like domain is present in several cytoskeleton-related proteins, which also contain a number of additional domains [ , , , ]: Eukaryotic cyclase-associated protein (CAP or SRV2), a modular actin monomer binding that directly regulates filament dynamics and has been implicated in a number of complex... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51329"
] | [
"C_CAP_COFACTOR_C"
] | [
15289
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-6798695",
"R-DRE-5624138",
"R-GGA-5624138",
"R-HSA-114608",
"R-HSA-389977",
"R-HSA-428890",
"R-HSA-5624138",
"R-HSA-6798695",
"R-MMU-5624138",
"R-MMU-6798695",
"R-RNO-6798695",
"R-SCE-6798695",
"R-SPO-6798695"
] | [
"REACTOME:R-DDI-6798695",
"REACTOME:R-DRE-5624138",
"REACTOME:R-GGA-5624138",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-389977",
"REACTOME:R-HSA-428890",
"REACTOME:R-HSA-5624138",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-5624138",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-6798695",
"REACTOME:R... | 13 | [
"1k4z",
"1k8f",
"1kq5",
"2b0r",
"2bx6",
"2yuh",
"3bh6",
"3bh7",
"5aj8",
"5cya",
"6fm2",
"9m1m",
"9m1n"
] | 13 | [
"PUB00026629",
"PUB00039797",
"PUB00043710",
"PUB00043711"
] | [
"15311924",
"16472755",
"17645436",
"14536023"
] | [
"Crystal structure of the actin binding domain of the cyclase-associated protein.",
"Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3.",
"An essential quality control mechanism at the eukaryotic basal body prior to intraflagellar transport.",
"Domain analysis of the ... | [
2004,
2006,
2007,
2003
] | 4 | [] | [
"IPR013912"
] | 0 | 1 | 0 | [
"Algisphaera agarilytica",
"Eukaryota",
"Megaviricetes",
"Methanobrevibacter gottschalkii",
"seawater metagenome"
] | [
1,
15283,
2,
2,
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... | [
23,
8,
9,
4,
18,
13,
3,
14,
22,
2,
2,
44
] | 12 | true | Domain | C-CAP/cofactor C-like domain | C-CAP/cofactor C-like domain | C-CAP_CF_C-like | 7 |
IPR017903 | 17,903 | COS domain | COS_domain | Domain | 13,615 | false | false | N-terminal RING finger/B-box/coiled coil (RBCC) or tripartite motif (TRIM) proteins, which are found in metazoa, are involved in a vast array of intracellular functions. They appear to function as part of large protein complexes and possess ubiquitin-protein isopeptide ligase activity. The following RBCC proteins conta... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51262"
] | [
"COS"
] | [
13615
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-983168",
"R-DME-983168",
"R-HSA-877300",
"R-HSA-9615017",
"R-HSA-983168",
"R-MMU-983168",
"R-RNO-983168"
] | [
"REACTOME:R-BTA-983168",
"REACTOME:R-DME-983168",
"REACTOME:R-HSA-877300",
"REACTOME:R-HSA-9615017",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-983168",
"REACTOME:R-RNO-983168"
] | 7 | [
"5im8"
] | 1 | [
"PUB00042940"
] | [
"16434393"
] | [
"Subclassification of the RBCC/TRIM superfamily reveals a novel motif necessary for microtubule binding."
] | [
2006
] | 1 | [] | [
"IPR040859"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
3,
13611,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
38,
1,
42,
39,
50
] | 6 | true | Domain | COS domain | COS domain | COS_domain | 3 |
IPR017904 | 17,904 | ADF/Cofilin | ADF/Cofilin | Family | 12,707 | false | false | Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subu... | [
"GO:0030042",
"GO:0015629"
] | [
"actin filament depolymerization",
"actin cytoskeleton"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS",
"PANTHER",
"CDD"
] | [
"PR00006",
"PTHR11913",
"cd11286"
] | [
"COFILIN",
"",
"ADF_cofilin_like"
] | [
3438,
12245,
11664
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-114608",
"R-HSA-2029482",
"R-HSA-3928662",
"R-HSA-399954",
"R-HSA-5627117",
"R-HSA-8950505"
] | [
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-2029482",
"REACTOME:R-HSA-3928662",
"REACTOME:R-HSA-399954",
"REACTOME:R-HSA-5627117",
"REACTOME:R-HSA-8950505"
] | 6 | [
"1ahq",
"1ak6",
"1ak7",
"1cfy",
"1cnu",
"1cof",
"1f7s",
"1q8g",
"1q8x",
"1qpv",
"1tvj",
"2i2q",
"2kvk",
"2l72",
"2lj8",
"2lxx",
"2mot",
"2mp4",
"2mv2",
"2xf1",
"2xfa",
"3j0s",
"3q2b",
"4bex",
"4ked",
"4kee",
"4kef",
"5hvk",
"5ivu",
"5l6w",
"5yu8",
"6uby"... | 51 | [
"PUB00041585",
"PUB00080546",
"PUB00080547",
"PUB00080548",
"PUB00080549",
"PUB00080550"
] | [
"17018289",
"11809832",
"10461190",
"24836399",
"23395798",
"20133134"
] | [
"Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin.",
"The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics.",
"Putting a new twist on actin: ADF/cofilins modulate actin dynamics.",
"... | [
2006,
2002,
1999,
2014,
2013,
2010
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
34,
12673
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
44,
1,
3,
3,
16,
9,
1,
20,
10,
1,
1,
69
] | 12 | true | Family | ADF/Cofilin | ADF/Cofilin | ADF/Cofilin | 5 |
IPR017905 | 17,905 | ERV/ALR sulfhydryl oxidase domain | ERV/ALR_sulphydryl_oxidase | Domain | 12,058 | false | false | The ~100-residue ERV/ALR sulphydryl oxidase domain is a versatile module adapted for catalysis of disulphide bond formation in various organelles and biological settings. The ERV/ALR sulphydryl oxidase domain has a Cys-X-X-Cys dithiol/disulphide motif adjacent to a bound FAD cofactor, enabling transfer of electrons fro... | [
"GO:0016972"
] | [
"thiol oxidase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF04777",
"PS51324"
] | [
"Evr1_Alr",
"ERV_ALR"
] | [
11604,
11978
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.8.3.2",
"PWY-7533",
"R-GGA-114608",
"R-GGA-381426",
"R-GGA-6798695",
"R-GGA-8957275",
"R-HSA-114608",
"R-HSA-1268020",
"R-HSA-381426",
"R-HSA-6798695",
"R-HSA-8957275",
"R-MMU-114608",
"R-MMU-381426",
"R-MMU-6798695",
"R-MMU-8957275",
"R-RNO-114608",
"R-RNO-381426",
"R-RNO-67986... | [
"EC:1.8.3.2",
"METACYC:PWY-7533",
"REACTOME:R-GGA-114608",
"REACTOME:R-GGA-381426",
"REACTOME:R-GGA-6798695",
"REACTOME:R-GGA-8957275",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-1268020",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8957275",
"REACTOME:R-MMU-114608",
"RE... | 19 | [
"1jr8",
"1jra",
"1oqc",
"2hj3",
"3gwl",
"3gwn",
"3lli",
"3llk",
"3mbg",
"3o55",
"3qcp",
"3qd9",
"3r7c",
"3t58",
"3t59",
"3td7",
"3tk0",
"3u2l",
"3u2m",
"3u5s",
"3w4y",
"4e0h",
"4e0i",
"4ldk",
"4p2l"
] | 25 | [
"PUB00013604",
"PUB00026507",
"PUB00041418",
"PUB00043720",
"PUB00043721",
"PUB00043722"
] | [
"11035794",
"11740506",
"16893552",
"10542195",
"17298084",
"1174050"
] | [
"A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.",
"A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.",
"Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide.",
"... | [
2000,
2002,
2006,
1999,
2007,
1975
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Nitrosotalea sinensis",
"Viruses",
"unclassified sequences"
] | [
43,
10967,
1,
426,
621
] | 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... | [
15,
7,
3,
10,
13,
6,
2,
3,
8,
2,
2,
15
] | 12 | true | Domain | ERV/ALR sulfhydryl oxidase domain | ERV/ALR sulfhydryl oxidase domain | ERV/ALR_sulphydryl_oxidase | 9 |
IPR017907 | 17,907 | Zinc finger, RING-type, conserved site | Znf_RING_CS | Conserved_site | 321,506 | false | false | A number of eukaryotic and viral proteins contain a conserved cysteine-rich domain of 40 to 60 residues (called C3HC4 zinc-finger or 'RING' finger) [ ] that binds two atoms of zinc. There are two different variants, the C3HC4-type and the C3H2C3-type, which is clearly related despite the different cysteine/histidine pa... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00518"
] | [
"ZF_RING_1"
] | [
321506
] | 1 | [
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTO... | [
"2.3.2",
"2.3.2.27",
"PWY-7511",
"R-BTA-1257604",
"R-BTA-166058",
"R-BTA-193692",
"R-BTA-201681",
"R-BTA-202424",
"R-BTA-205043",
"R-BTA-209543",
"R-BTA-209560",
"R-BTA-2559580",
"R-BTA-2871837",
"R-BTA-3108214",
"R-BTA-3134975",
"R-BTA-3899300",
"R-BTA-450302",
"R-BTA-450321",
"... | [
"EC:2.3.2",
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-166058",
"REACTOME:R-BTA-193692",
"REACTOME:R-BTA-201681",
"REACTOME:R-BTA-202424",
"REACTOME:R-BTA-205043",
"REACTOME:R-BTA-209543",
"REACTOME:R-BTA-209560",
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-28... | 573 | [
"1bor",
"1chc",
"1fbv",
"1g25",
"1jm7",
"1rmd",
"1z6u",
"2ckl",
"2csy",
"2ct2",
"2d8t",
"2djb",
"2ea6",
"2eci",
"2ecj",
"2ecn",
"2ecv",
"2ecw",
"2ecy",
"2egp",
"2h0d",
"2jmd",
"2k4d",
"2ldr",
"2mq1",
"2mwx",
"2xeu",
"2y1m",
"2y1n",
"2y43",
"2ysj",
"2ysl"... | 256 | [
"PUB00001094",
"PUB00014077",
"PUB00017951",
"PUB00017952",
"PUB00017953",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"8804826",
"12665246",
"7729428",
"10500182",
"10531381",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"The RING finger domain: a recent example of a sequence-structure family.",
"Zinc fingers--folds for many occasions.",
"The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML.",
"RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitinat... | [
1996,
2002,
1995,
1999,
1999,
2007,
2005,
2005,
1999,
2001
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
212,
319836,
1146,
312
] | 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... | [
476,
107,
726,
137,
641,
411,
25,
248,
480,
11,
19,
546
] | 12 | true | Conserved_site | Zinc finger, RING-type, conserved site | Zinc finger, RING-type, conserved site | Znf_RING_CS | 2 |
IPR017910 | 17,910 | Zinc finger, large T-antigen D1-type | Znf_lg_T-Ag_D1-typ | Domain | 679 | false | false | Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b... | [
"GO:0003677",
"GO:0005524",
"GO:0006260"
] | [
"DNA binding",
"ATP binding",
"DNA replication"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROFILE"
] | [
"PS51341"
] | [
"ZF_LTAG_D1"
] | [
679
] | 1 | [
"EC"
] | [
"5.6.2.4"
] | [
"EC:5.6.2.4"
] | 1 | [
"1n25",
"1svl",
"1svm",
"1svo",
"2h1l",
"4e2i",
"4gdf",
"5j40",
"5j47",
"5j4v",
"5j4y",
"9evh",
"9evp",
"9exd",
"9f3t",
"9f3u",
"9f5i",
"9f73",
"9f74",
"9f75",
"9f7n",
"9f9n",
"9f9o",
"9f9w",
"9f9x",
"9fa1",
"9fa2",
"9fb0",
"9fb4",
"9fb5",
"9fb6",
"9kae"... | 33 | [
"PUB00014077",
"PUB00027539",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00040814",
"PUB00041759",
"PUB00043699"
] | [
"12665246",
"12774115",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"16611889",
"17139255",
"8824775"
] | [
"Zinc fingers--folds for many occasions.",
"Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
"Zinc finger proteins: getting a grip on RNA.",
"Zi... | [
2002,
2003,
2007,
2005,
2005,
1999,
2001,
2006,
2006,
1995
] | 10 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses"
] | [
30,
649
] | 2 | [
"Mus musculus"
] | [
1
] | 1 | true | Domain | Zinc finger, large T-antigen D1-type | Zinc finger, large T-antigen D1-type | Znf_lg_T-Ag_D1-typ | 7 |
IPR017911 | 17,911 | MacB-like, ATP-binding domain | MacB-like_ATP-bd | Domain | 136,709 | false | false | This entry represents the ATP-binding domain of MacB-like proteins. MacB proteins are ABC transporters involved in the export of macrolide antibiotics [ ]. It is also present in proteins involved in the release of lipoproteins from the cytoplasmic membrane (LolCDE complex) [ ]. ABC transporters belong to the ATP-Bindin... | [] | [] | [] | 0 | [
"CDD"
] | [
"cd03255"
] | [
"ABC_MJ0796_LolCDE_FtsE"
] | [
136709
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.6.2.-",
"R-HSA-9638334",
"R-HSA-9760173",
"R-HSA-9913143"
] | [
"EC:7.6.2.-",
"REACTOME:R-HSA-9638334",
"REACTOME:R-HSA-9760173",
"REACTOME:R-HSA-9913143"
] | 4 | [
"1f3o",
"1l2t",
"2pcj",
"2pcl",
"3tif",
"5gko",
"5lil",
"5lj6",
"5lj7",
"5lj9",
"5lja",
"5nik",
"5nil",
"5ws4",
"5xu1",
"7arh",
"7ari",
"7arj",
"7ark",
"7arl",
"7arm",
"7mdx",
"7mdy",
"7tcg",
"7tch",
"7v8i",
"7v8l",
"7v8m",
"7w78",
"7w79",
"7w7a",
"7w7b"... | 48 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654",
"PUB00043739",
"PUB00097511",
"PUB00097512"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270",
"11544226",
"32873757",
"29339384"
] | [
"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,
2001,
2001,
2020,
2018
] | 14 | [
"IPR003439"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Caudovirales sp. ctqPn17",
"Eukaryota",
"unclassified sequences"
] | [
2148,
132724,
1,
418,
1418
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
3
] | 2 | true | Domain | MacB-like, ATP-binding domain | MacB-like, ATP-binding domain | MacB-like_ATP-bd | 1 |
IPR017913 | 17,913 | Colipase, N-terminal | Colipase_N | Domain | 654 | false | false | This entry represents the N-terminal domain of colipase proteins. Colipase [ , ] is a small protein cofactor needed by pancreatic lipase for efficient dietary lipid hydrolyisis. It also binds to the bile-salt covered triacylglycerol interface, thus allowing the enzyme to anchor itself to the water-lipid interface. Effi... | [
"GO:0008047",
"GO:0007586",
"GO:0016042",
"GO:0005576"
] | [
"enzyme activator activity",
"digestion",
"lipid catabolic process",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF01114"
] | [
"Colipase"
] | [
654
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-192456",
"R-BTA-975634",
"R-HSA-192456",
"R-HSA-975634",
"R-MMU-192456",
"R-MMU-975634",
"R-RNO-192456",
"R-RNO-975634",
"R-SSC-192456",
"R-SSC-975634",
"R-XTR-192456",
"R-XTR-975634"
] | [
"REACTOME:R-BTA-192456",
"REACTOME:R-BTA-975634",
"REACTOME:R-HSA-192456",
"REACTOME:R-HSA-975634",
"REACTOME:R-MMU-192456",
"REACTOME:R-MMU-975634",
"REACTOME:R-RNO-192456",
"REACTOME:R-RNO-975634",
"REACTOME:R-SSC-192456",
"REACTOME:R-SSC-975634",
"REACTOME:R-XTR-192456",
"REACTOME:R-XTR-975... | 12 | [
"1eth",
"1lpa",
"1lpb",
"1n8s",
"1pcn",
"1pco"
] | 6 | [
"PUB00000630",
"PUB00000684",
"PUB00006457",
"PUB00006494"
] | [
"1567900",
"3147715",
"10570245",
"9240923"
] | [
"Pancreatic colipase. Structural and physiological aspects.",
"Minireview on pancreatic lipase and colipase.",
"Colipase: structure and interaction with pancreatic lipase.",
"Structure and function of pancreatic lipase and colipase."
] | [
1992,
1988,
1999,
1997
] | 4 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
654
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
2
] | 3 | true | Domain | Colipase, N-terminal | Colipase, N-terminal | Colipase_N | 1 |
IPR017914 | 17,914 | Colipase, C-terminal | Colipase_C | Domain | 723 | false | false | This entry represents the C-terminal domain of colipase proteins. Colipase [ , ] is a small protein cofactor needed by pancreatic lipase for efficient dietary lipid hydrolyisis. It also binds to the bile-salt covered triacylglycerol interface, thus allowing the enzyme to anchor itself to the water-lipid interface. Effi... | [
"GO:0008047",
"GO:0007586",
"GO:0016042",
"GO:0005576"
] | [
"enzyme activator activity",
"digestion",
"lipid catabolic process",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF02740"
] | [
"Colipase_C"
] | [
723
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-192456",
"R-BTA-975634",
"R-HSA-192456",
"R-HSA-975634",
"R-MMU-192456",
"R-MMU-975634",
"R-RNO-192456",
"R-RNO-975634",
"R-SSC-192456",
"R-SSC-975634",
"R-XTR-192456",
"R-XTR-975634"
] | [
"REACTOME:R-BTA-192456",
"REACTOME:R-BTA-975634",
"REACTOME:R-HSA-192456",
"REACTOME:R-HSA-975634",
"REACTOME:R-MMU-192456",
"REACTOME:R-MMU-975634",
"REACTOME:R-RNO-192456",
"REACTOME:R-RNO-975634",
"REACTOME:R-SSC-192456",
"REACTOME:R-SSC-975634",
"REACTOME:R-XTR-192456",
"REACTOME:R-XTR-975... | 12 | [
"1eth",
"1lpa",
"1lpb",
"1n8s",
"1pcn",
"1pco"
] | 6 | [
"PUB00000630",
"PUB00000684",
"PUB00006457",
"PUB00006494"
] | [
"1567900",
"3147715",
"10570245",
"9240923"
] | [
"Pancreatic colipase. Structural and physiological aspects.",
"Minireview on pancreatic lipase and colipase.",
"Colipase: structure and interaction with pancreatic lipase.",
"Structure and function of pancreatic lipase and colipase."
] | [
1992,
1988,
1999,
1997
] | 4 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
723
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
3,
3
] | 3 | true | Domain | Colipase, C-terminal | Colipase, C-terminal | Colipase_C | 4 |
IPR017915 | 17,915 | Colipase, conserved site | Colipase_CS | Conserved_site | 733 | false | false | Colipase [ , ] is a small protein cofactor needed by pancreatic lipase for efficient dietary lipid hydrolyisis. It also binds to the bile-salt covered triacylglycerol interface, thus allowing the enzyme to anchor itself to the water-lipid interface. Efficient absorption of dietary fats is dependent on the action of pan... | [
"GO:0008047",
"GO:0007586",
"GO:0016042",
"GO:0005576"
] | [
"enzyme activator activity",
"digestion",
"lipid catabolic process",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PROSITE"
] | [
"PS00121"
] | [
"COLIPASE_1"
] | [
733
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-192456",
"R-BTA-975634",
"R-HSA-192456",
"R-HSA-975634",
"R-MMU-192456",
"R-MMU-975634",
"R-RNO-192456",
"R-RNO-975634",
"R-SSC-192456",
"R-SSC-975634",
"R-XTR-192456",
"R-XTR-975634"
] | [
"REACTOME:R-BTA-192456",
"REACTOME:R-BTA-975634",
"REACTOME:R-HSA-192456",
"REACTOME:R-HSA-975634",
"REACTOME:R-MMU-192456",
"REACTOME:R-MMU-975634",
"REACTOME:R-RNO-192456",
"REACTOME:R-RNO-975634",
"REACTOME:R-SSC-192456",
"REACTOME:R-SSC-975634",
"REACTOME:R-XTR-192456",
"REACTOME:R-XTR-975... | 12 | [
"1eth",
"1lpa",
"1lpb",
"1n8s",
"1pcn",
"1pco"
] | 6 | [
"PUB00000630",
"PUB00000684",
"PUB00006457",
"PUB00006494"
] | [
"1567900",
"3147715",
"10570245",
"9240923"
] | [
"Pancreatic colipase. Structural and physiological aspects.",
"Minireview on pancreatic lipase and colipase.",
"Colipase: structure and interaction with pancreatic lipase.",
"Structure and function of pancreatic lipase and colipase."
] | [
1992,
1988,
1999,
1997
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
3,
730
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
3,
3
] | 3 | true | Conserved_site | Colipase, conserved site | Colipase, conserved site | Colipase_CS | 7 |
IPR017916 | 17,916 | Steadiness box (SB) domain | SB_dom | Domain | 5,833 | false | false | The Endosomal Sorting Complex Required for Transport (ESCRT) complexes form the machinery driving protein sorting from endosomes to lysosomes. ESCRT complexes are central to receptor down-regulation, lysosome biogenesis, and budding of HIV. Yeast ESCRT-I consists of three protein subunits, Vps23, Vps28, and Vps37. In h... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF09454",
"PS51312"
] | [
"Vps23_core",
"SB"
] | [
5822,
5548
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-917729",
"R-HSA-162588",
"R-HSA-174490",
"R-HSA-917729",
"R-HSA-9610379",
"R-HSA-9615710",
"R-MMU-917729",
"R-RNO-917729",
"R-SCE-917729"
] | [
"REACTOME:R-DDI-917729",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-917729",
"REACTOME:R-HSA-9610379",
"REACTOME:R-HSA-9615710",
"REACTOME:R-MMU-917729",
"REACTOME:R-RNO-917729",
"REACTOME:R-SCE-917729"
] | 9 | [
"2caz",
"2f66",
"2f6m",
"2p22",
"6vme"
] | 5 | [
"PUB00039953",
"PUB00040552"
] | [
"16615893",
"16615894"
] | [
"ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes.",
"Structural and functional organization of the ESCRT-I trafficking complex."
] | [
2006,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Vitreoscilla filiformis",
"marine sediment metagenome"
] | [
5827,
1,
5
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
9,
1,
2,
1,
4,
4,
1,
3,
5,
1,
1,
7
] | 12 | true | Domain | Steadiness box (SB) domain | Steadiness box (SB) domain | SB_dom | 2 |
IPR017918 | 17,918 | Nitrogen regulatory protein PII, conserved site | N-reg_PII_CS | Conserved_site | 24,104 | false | false | The P-II protein (gene glnB) is a bacterial protein important for the control of glutamine synthetase [ , , ]. In nitrogen-limiting conditions, when the ratio of glutamine to 2-ketoglutarate decreases, P-II is uridylylated on a tyrosine residue to form P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase... | [
"GO:0030234",
"GO:0006808"
] | [
"enzyme regulator activity",
"regulation of nitrogen utilization"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00638"
] | [
"PII_GLNB_CTER"
] | [
24104
] | 1 | [] | [] | [] | 0 | [
"1gnk",
"1hwu",
"1pil",
"1qy7",
"1ufl",
"1ul3",
"1v3r",
"1v3s",
"1v9o",
"1vfj",
"2eg1",
"2eg2",
"2gnk",
"2gw8",
"2j9c",
"2j9d",
"2j9e",
"2jj4",
"2ns1",
"2nuu",
"2o66",
"2o67",
"2pii",
"2rd5",
"2v5h",
"2xbp",
"2xg8",
"2xul",
"2xzw",
"2z0g",
"3bzq",
"3l7p"... | 73 | [
"PUB00000687",
"PUB00001837",
"PUB00002236",
"PUB00003730",
"PUB00005249"
] | [
"2574599",
"7904973",
"8282685",
"2907369",
"7866749"
] | [
"Regulation of transcription of the glnALG operon of Escherichia coli by protein phosphorylation.",
"Cloning and organization of the abc and mdl genes of Escherichia coli: relationship to eukaryotic multidrug resistance.",
"The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane protein and a p... | [
1989,
1993,
1994,
1988,
1994
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
987,
22080,
542,
495
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica"
] | [
6,
2,
1
] | 3 | true | Conserved_site | Nitrogen regulatory protein PII, conserved site | Nitrogen regulatory protein PII, conserved site | N-reg_PII_CS | 9 |
IPR017919 | 17,919 | Transcription factor TFE/TFIIEalpha HTH domain | TFIIE/TFIIEa_HTH | Domain | 5,876 | false | false | Initiation of eukaryotic mRNA transcription requires melting of promoter DNA with the help of the general transcription factors TFIIE and TFIIH. In higher eukaryotes, the general transcription factor TFIIE consists of two subunits: the large alpha subunit ( ) and the small beta ( ). TFIIE beta has been found to bind to... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51344"
] | [
"HTH_TFE_IIE"
] | [
5876
] | 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-674695",
"R-BTA-6807505",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-75953",
"R-BTA-76042",
"R-DDI-674695",
"R-DDI-6807505",
"R-DDI-73776",
"R-DDI-73779",
"R-DDI-75953",
"R-DDI-76042",
"R-HSA-167161",
"R-HSA-167162",
"R-HSA-167172",
"R-HSA-674695",
"R-HSA-6807505",
"R-HSA-73776",
... | [
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-73776",
"REACTOME:R-BTA-73779",
"REACTOME:R-BTA-75953",
"REACTOME:R-BTA-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",
... | 39 | [
"1q1h",
"5fmf",
"5fyw",
"5fz5",
"5gpy",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5iya",
"5iyb",
"5iyc",
"5iyd",
"5oqj",
"5oqm",
"5sva",
"6gyl",
"6gym",
"6kf4",
"6kf9",
"6o9l",
"6pln",
"6xjf",
"7eg9",
"7ega",
"7egb",
"7egc",
"7ena",
"7enc",
"7lbm",
"7ml0",
"7ml1"... | 77 | [
"PUB00006521",
"PUB00022500",
"PUB00043742",
"PUB00043743",
"PUB00043744",
"PUB00043809"
] | [
"10716934",
"13679366",
"9271406",
"11258705",
"11160119",
"3679366"
] | [
"Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface.",
"An extended winged helix domain in general transcription factor E/IIE alpha.",
"Genetic analysis of the large subunit of yeast transcription factor IIE reveals two regions with distinct functions.",
"The ar... | [
2000,
2003,
1997,
2001,
2001,
1987
] | 6 | [
"IPR024550"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
823,
21,
5005,
27
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
20,
1,
3,
1,
5,
4,
1,
9,
2,
1,
1,
16
] | 12 | true | Domain | Transcription factor TFE/TFIIEalpha HTH domain | Transcription factor TFE/TFIIEalpha HTH domain | TFIIE/TFIIEa_HTH | 5 |
IPR017920 | 17,920 | COMM domain | COMM | Domain | 13,511 | false | false | The leucine-rich, 70-85 amino acid long COMM domain is predicted to form a β-sheet [ ]. COMM (copper metabolism gene MURR1) domain proteins constitute a family initially identified as interacting partners of COMMD1 (previously known as MURR1), the prototype member of this protein family. COMMD1 is a multifunctional pro... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF07258",
"PS51269"
] | [
"COMM_domain",
"COMM"
] | [
13228,
12780
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8951664",
"R-DDI-6798695",
"R-DDI-8951664",
"R-DME-8951664",
"R-HSA-6798695",
"R-HSA-8951664",
"R-MMU-6798695",
"R-MMU-8951664",
"R-RNO-6798695",
"R-RNO-8951664",
"R-XTR-8951664"
] | [
"REACTOME:R-BTA-8951664",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-8951664",
"REACTOME:R-DME-8951664",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8951664",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-8951664",
"REACTOME:R-RNO-6798695",
"REACTOME:R-RNO-8951664",
"REACTOME:R-XTR-8951664"
] | 11 | [
"6bp6",
"8esd",
"8f2r",
"8f2u",
"8p0w"
] | 5 | [
"PUB00043133",
"PUB00043745"
] | [
"15799966",
"16573520"
] | [
"COMMD proteins, a novel family of structural and functional homologs of MURR1.",
"Characterization of COMMD protein-protein interactions in NF-kappaB signalling."
] | [
2005,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
27,
13484
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
11,
10,
27,
36,
59
] | 6 | true | Domain | COMM domain | COMM domain | COMM | 2 |
IPR017921 | 17,921 | Zinc finger, CTCHY-type | Znf_CTCHY | Domain | 9,192 | false | false | Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51270"
] | [
"ZF_CTCHY"
] | [
9192
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.2.27",
"PWY-7511",
"R-HSA-110320",
"R-HSA-983168",
"R-MMU-110320",
"R-MMU-983168"
] | [
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-HSA-110320",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-110320",
"REACTOME:R-MMU-983168"
] | 6 | [
"2dkt",
"2k2c",
"7ynx"
] | 3 | [
"PUB00014077",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00043738"
] | [
"12665246",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"12654245"
] | [
"Zinc fingers--folds for many occasions.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
"Zinc finger proteins: getting a grip on RNA.",
"Zinc finger peptides for the regulation of gene expression.",
"Zinc finger proteins: new ... | [
2002,
2007,
2005,
2005,
1999,
2001,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
15,
9152,
17,
8
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Ze... | [
35,
4,
5,
6,
3,
1,
25,
4,
1,
65
] | 10 | true | Domain | Zinc finger, CTCHY-type | Zinc finger, CTCHY-type | Znf_CTCHY | 8 |
IPR017923 | 17,923 | Transcription factor IIS, N-terminal | TFIIS_N | Domain | 27,238 | false | false | Transcription factor IIS (TFIIS) is a transcription elongation factor that increases the overall transcription rate of RNA polymerase II by reactivating transcription elongation complexes that have arrested transcription. The three structural domains of TFIIS are conserved from yeast to human. The 80 or so N-terminal r... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF08711",
"PS51319"
] | [
"Med26",
"TFIIS_N"
] | [
26224,
25567
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-75955",
"R-CEL-112382",
"R-CEL-674695",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-6796648",
"R-CEL-75955",
"R-DDI-6781823",
"R-DDI-6782135",
"R-DDI-6782210",
"R-DDI-6796648",
... | [
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-75955",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6781823",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-C... | 70 | [
"1eo0",
"1pqv",
"1wjt",
"2xpl",
"2xpn",
"2xpo",
"2xpp",
"3nfq",
"3o8z",
"3oak",
"5iy6",
"5iy7",
"5iy8",
"5iya",
"5iyb",
"5iyc",
"5odd",
"6nzo",
"6o9l",
"6px3",
"6vti",
"6zuy",
"6zuz",
"6zv1",
"6zv2",
"6zv3",
"6zv4",
"7cnf",
"7emf",
"7ena",
"7enc",
"7enj"... | 72 | [
"PUB00014034",
"PUB00042913"
] | [
"10811649",
"16648364"
] | [
"Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70.",
"A sequence motif conserved in diverse nuclear proteins identifies a protein interaction domain utilised for nuclear targeting by human TFIIS."
] | [
2000,
2006
] | 2 | [] | [
"IPR003617"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
6,
27231,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
89,
3,
74,
14,
42,
23,
3,
63,
38,
2,
3,
114
] | 12 | true | Domain | Transcription factor IIS, N-terminal | Transcription factor IIS, N-terminal | TFIIS_N | 5 |
IPR017924 | 17,924 | RNA-binding protein YhbY | RNA-binding_YhbY | Family | 7,697 | false | false | The YhbY family of proteins are predicted to bind RNA on the basis of structural similarity to known RNA-binding proteins [ ]. The Escherichia coli YhbY protein cosediments with free 50S ribosomal subunits, implying a role in ribosome assembly. | [
"GO:0003723"
] | [
"RNA binding"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00253"
] | [
"RNA_bind_YhbY"
] | [
7697
] | 1 | [] | [] | [] | 0 | [
"1jo0",
"1ln4",
"1rq8"
] | 3 | [
"PUB00019352"
] | [
"12429100"
] | [
"Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomada group",
"unclassified sequences"
] | [
7590,
7,
33,
67
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | RNA-binding protein YhbY | RNA-binding protein YhbY | RNA-binding_YhbY | 9 |
IPR017925 | 17,925 | Dihydrofolate reductase conserved site | DHFR_CS | Conserved_site | 20,563 | false | false | Dihydrofolate reductase (DHFR) ( ) catalyses the NADPH-dependent reduction of dihydrofolate to tetrahydrofolate, an essential step in de novo synthesis both of glycine and of purines and deoxythymidine phosphate (the precursors of DNA synthesis) [ ], and important also in the conversion of deoxyuridine monophosphate to... | [
"GO:0004146"
] | [
"dihydrofolate reductase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00075"
] | [
"DHFR_1"
] | [
20563
] | 1 | [
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.5.1.3",
"PWY-3841",
"PWY-6614",
"R-CEL-196757",
"R-DME-196757",
"R-HSA-1474151",
"R-HSA-196757",
"R-HSA-69205",
"R-MMU-196757",
"R-RNO-196757",
"R-SCE-196757",
"R-SPO-196757"
] | [
"EC:1.5.1.3",
"METACYC:PWY-3841",
"METACYC:PWY-6614",
"REACTOME:R-CEL-196757",
"REACTOME:R-DME-196757",
"REACTOME:R-HSA-1474151",
"REACTOME:R-HSA-196757",
"REACTOME:R-HSA-69205",
"REACTOME:R-MMU-196757",
"REACTOME:R-RNO-196757",
"REACTOME:R-SCE-196757",
"REACTOME:R-SPO-196757"
] | 12 | [
"1ai9",
"1ao8",
"1aoe",
"1boz",
"1bzf",
"1cd2",
"1daj",
"1ddr",
"1dds",
"1df7",
"1dg5",
"1dg7",
"1dg8",
"1dhf",
"1dis",
"1diu",
"1dlr",
"1dr1",
"1dr2",
"1dr3",
"1dr4",
"1dr5",
"1dr6",
"1dr7",
"1dra",
"1dre",
"1drf",
"1drh",
"1dyh",
"1dyi",
"1dyj",
"1dyr"... | 647 | [
"PUB00001361",
"PUB00002379",
"PUB00002387",
"PUB00003657",
"PUB00005107",
"PUB00017878"
] | [
"3383852",
"500653",
"6815178",
"2601715",
"2830673",
"3880743"
] | [
"Crystal structure of human dihydrofolate reductase complexed with folate.",
"Porcine liver dihydrofolate reductase. Purification, properties, and amino acid sequence.",
"Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and b... | [
1988,
1979,
1982,
1989,
1988,
1985
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid R483",
"Viruses",
"unclassified sequences"
] | [
348,
14673,
4971,
1,
395,
175
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces... | [
18,
1,
2,
1,
3,
2,
1,
6,
3,
1,
1,
19
] | 12 | true | Conserved_site | Dihydrofolate reductase conserved site | Dihydrofolate reductase conserved site | DHFR_CS | 8 |
IPR017926 | 17,926 | Glutamine amidotransferase | GATASE | Domain | 204,411 | false | false | Glutamine amidotransferase (GATase) enzymes catalyse the removal of the ammonia group from glutamine and then transfer this group to a substrate to form a new carbon-nitrogen group [ ]. The GATase domain exists either as a separate polypeptidic subunit or as part of a larger polypeptide fused in different ways to a syn... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00117"
] | [
"GATase"
] | [
204411
] | 1 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1650",
"R-BTA-499943",
"R-CEL-500753",
"R-CEL-73817",
"R-CEL-9748787",
"R-DDI-499943",
"R-DDI-500753",
"R-DDI-73817",
"R-DDI-9748787",
"R-DME-499943",
"R-DME-500753",
"R-DRE-499943",
"R-GGA-499943",
"R-HSA-499943",
"R-HSA-500753",
"R-HSA-70635",
"R-HSA-73817",
"R-HSA-974878... | [
"GP:GenProp1650",
"REACTOME:R-BTA-499943",
"REACTOME:R-CEL-500753",
"REACTOME:R-CEL-73817",
"REACTOME:R-CEL-9748787",
"REACTOME:R-DDI-499943",
"REACTOME:R-DDI-500753",
"REACTOME:R-DDI-73817",
"REACTOME:R-DDI-9748787",
"REACTOME:R-DME-499943",
"REACTOME:R-DME-500753",
"REACTOME:R-DRE-499943",
... | 37 | [
"1a9x",
"1bxr",
"1c30",
"1c3o",
"1ce8",
"1cs0",
"1gpm",
"1gpw",
"1i1q",
"1i7q",
"1i7s",
"1jdb",
"1jvn",
"1k9v",
"1ka9",
"1kee",
"1kxj",
"1m6v",
"1o1y",
"1ox4",
"1ox5",
"1ox6",
"1qdl",
"1s1m",
"1t36",
"1vcm",
"1vcn",
"1vco",
"1wl8",
"2a9v",
"2ad5",
"2d7j"... | 144 | [
"PUB00000003",
"PUB00000116",
"PUB00000720",
"PUB00002062",
"PUB00002406",
"PUB00002413",
"PUB00003933",
"PUB00014421",
"PUB00016818",
"PUB00043761"
] | [
"4355768",
"2679363",
"8098212",
"3298209",
"6086650",
"2982857",
"8548458",
"10449718",
"15301531",
"9575335"
] | [
"The amidotransferases.",
"Evolution of a biosynthetic pathway: the tryptophan paradigm.",
"The evolutionary history of the first three enzymes in pyrimidine biosynthesis.",
"Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain.",
"Sequence of the small subunit of yea... | [
1973,
1989,
1993,
1987,
1984,
1985,
1996,
1999,
2004,
1998
] | 10 | [] | [
"IPR004739",
"IPR006221",
"IPR033828",
"IPR035686"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5484,
150407,
44867,
57,
3596
] | 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",... | [
81,
4,
13,
7,
6,
26,
11,
10,
49,
26,
9,
8,
152
] | 13 | true | Domain | Glutamine amidotransferase | Glutamine amidotransferase | GATASE | 9 |
IPR017927 | 17,927 | FAD-binding domain, ferredoxin reductase-type | FAD-bd_FR_type | Domain | 231,004 | false | false | Flavoenzymes have the ability to catalyse a wide range of biochemical reactions. They are involved in the dehydrogenation of a variety of metabolites, in electron transfer from and to redox centres, in light emission, in the activation of oxygen for oxidation and hydroxylation reactions [ ]. About 1% of all eukaryotic ... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PROFILE"
] | [
"PS51384"
] | [
"FAD_FR"
] | [
231004
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-1222556",
"R-BTA-1236973",
"R-BTA-1237044",
"R-BTA-196836",
"R-BTA-211945",
"R-BTA-3299685",
"R-BTA-4420097",
"R-BTA-5668599",
"R-BTA-6798695",
"R-BTA-9013149",
"R-BTA-9013404",
"R-BTA-9013423",
"R-CEL-156581",
"R-CEL-1614635",
"R-CEL-209968",
"R-CEL-9759218",
... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-1236973",
"REACTOME:R-BTA-1237044",
"REACTOME:R-BTA-196836",
"REACTOME:R-BTA-211945",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-5668599",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9013149",
"REACTOME:R... | 174 | [
"1a8p",
"1amo",
"1b2r",
"1bjk",
"1bqe",
"1bx0",
"1bx1",
"1cne",
"1cnf",
"1cqx",
"1ddg",
"1ddi",
"1e62",
"1e63",
"1e64",
"1ep1",
"1ep2",
"1ep3",
"1ewy",
"1f20",
"1fdr",
"1fnb",
"1fnc",
"1fnd",
"1frn",
"1frq",
"1gaq",
"1gaw",
"1gjr",
"1go2",
"1gr1",
"1gvh"... | 307 | [
"PUB00019097",
"PUB00036241",
"PUB00043766",
"PUB00043767"
] | [
"11514662",
"9865948",
"10694883",
"16600599"
] | [
"Sequence-structure analysis of FAD-containing proteins.",
"The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii.",
"Flavoenzymes: diverse catalysts with recurrent features.",
"To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes."
] | [
2001,
1998,
2000,
2006
] | 4 | [] | [
"IPR003097",
"IPR008333",
"IPR013112",
"IPR013113"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Vibrio phage VP-HS15",
"plasmids",
"unclassified sequences"
] | [
1456,
138408,
89869,
1,
3,
1267
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
150,
11,
70,
29,
8,
83,
45,
25,
76,
94,
16,
10,
203
] | 13 | true | Domain | FAD-binding domain, ferredoxin reductase-type | FAD-binding domain, ferredoxin reductase-type | FAD-bd_FR_type | 8 |
IPR017932 | 17,932 | Glutamine amidotransferase type 2 domain | GATase_2_dom | Domain | 156,413 | false | false | A large group of biosynthetic enzymes are able to catalyse the removal of the ammonia group from glutamine and then to transfer this group to a substrate to form a new carbon-nitrogen group. This catalytic activity is known as glutamine amidotransferase (GATase) [ ]. The GATase domain exists either as a separate polype... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF00310",
"PF13537",
"PS51278"
] | [
"GATase_2",
"GATase_7",
"GATASE_TYPE_2"
] | [
28718,
47179,
153668
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8963693",
"R-DDI-8963693",
"R-DME-73817",
"R-GGA-419140",
"R-HSA-380994",
"R-HSA-381038",
"R-HSA-4085023",
"R-HSA-446210",
"R-HSA-73817",
"R-HSA-8963693",
"R-HSA-9633012",
"R-HSA-9648895",
"R-MMU-446210",
"R-MMU-73817",
"R-MMU-8963693",
"R-RNO-446210",
"R-RNO-73817",
"R-RNO-... | [
"REACTOME:R-BTA-8963693",
"REACTOME:R-DDI-8963693",
"REACTOME:R-DME-73817",
"REACTOME:R-GGA-419140",
"REACTOME:R-HSA-380994",
"REACTOME:R-HSA-381038",
"REACTOME:R-HSA-4085023",
"REACTOME:R-HSA-446210",
"REACTOME:R-HSA-73817",
"REACTOME:R-HSA-8963693",
"REACTOME:R-HSA-9633012",
"REACTOME:R-HSA-... | 22 | [
"1ao0",
"1ct9",
"1ea0",
"1ecb",
"1ecc",
"1ecf",
"1ecg",
"1ecj",
"1gph",
"1jgt",
"1jxa",
"1llw",
"1llz",
"1lm1",
"1m1z",
"1mb9",
"1mbz",
"1mc1",
"1ofd",
"1ofe",
"1te5",
"1xff",
"1xfg",
"2j6h",
"2vdc",
"2vf4",
"2vf5",
"3mdn",
"3ooj",
"4amv",
"6czf",
"6gq3"... | 57 | [
"PUB00000003",
"PUB00002062",
"PUB00002391",
"PUB00002406",
"PUB00009386",
"PUB00043761",
"PUB00043790",
"PUB00043791"
] | [
"4355768",
"3298209",
"6411716",
"6086650",
"10357231",
"9575335",
"2573597",
"15052410"
] | [
"The amidotransferases.",
"Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain.",
"The glutamine-utilizing site of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase.",
"Sequence of the small subunit of yeast carbamyl phosphate synthetase and iden... | [
1973,
1987,
1983,
1984,
1999,
1998,
1989,
2004
] | 8 | [] | [
"IPR033738",
"IPR035584",
"IPR047084"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3770,
119318,
30333,
231,
2761
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
46,
8,
8,
20,
5,
25,
14,
6,
24,
24,
8,
5,
142
] | 13 | true | Domain | Glutamine amidotransferase type 2 domain | Glutamine amidotransferase type 2 domain | GATase_2_dom | 3 |
IPR017937 | 17,937 | Thioredoxin, conserved site | Thioredoxin_CS | Conserved_site | 178,536 | false | false | This entry represents a conserved site found in the thioredoxin domain. This site contains two cysteines that form the redox-active disulphide bond. Thioredoxins [ , , , ] are small disulphide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00194"
] | [
"THIOREDOXIN_1"
] | [
178536
] | 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-1614558",
"R-BTA-2559580",
"R-BTA-3299685",
"R-BTA-499943",
"R-BTA-5628897",
"R-BTA-5676934",
"R-BTA-844456",
"R-CEL-1614558",
"R-CEL-1650814",
"R-CEL-2559580",
"R-CEL-264876",
"R-CEL-3299685",
"R-CEL-381426",
"R-CEL-499943",
"R-CEL-532668",
"R-CEL-5628897",
"R-CEL-5676934",
... | [
"REACTOME:R-BTA-1614558",
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-499943",
"REACTOME:R-BTA-5628897",
"REACTOME:R-BTA-5676934",
"REACTOME:R-BTA-844456",
"REACTOME:R-CEL-1614558",
"REACTOME:R-CEL-1650814",
"REACTOME:R-CEL-2559580",
"REACTOME:R-CEL-264876",
"REACTOME:R... | 167 | [
"1a23",
"1a24",
"1a2j",
"1a2l",
"1a2m",
"1acv",
"1aiu",
"1auc",
"1bed",
"1bq7",
"1dby",
"1dsb",
"1eej",
"1ep7",
"1ep8",
"1ert",
"1eru",
"1erv",
"1f9m",
"1faa",
"1fb0",
"1fb6",
"1fvj",
"1fvk",
"1gh2",
"1gl8",
"1jfu",
"1keb",
"1kng",
"1m7t",
"1mek",
"1nsw"... | 581 | [
"PUB00000038",
"PUB00000561",
"PUB00001458",
"PUB00001495",
"PUB00002504",
"PUB00002862",
"PUB00002883",
"PUB00005250",
"PUB00005258",
"PUB00005259",
"PUB00005423"
] | [
"3896121",
"3371540",
"7635143",
"2537773",
"2668278",
"7913469",
"7983029",
"8590004",
"7788289",
"7788290",
"7940678"
] | [
"Thioredoxin.",
"Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins.",
"Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese.",
"Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multif... | [
1985,
1988,
1995,
1989,
1989,
1994,
1994,
1995,
1995,
1995,
1994
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1657,
113096,
61483,
137,
2163
] | 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",... | [
122,
21,
36,
25,
6,
110,
57,
7,
47,
73,
6,
5,
175
] | 13 | true | Conserved_site | Thioredoxin, conserved site | Thioredoxin, conserved site | Thioredoxin_CS | 1 |
IPR017938 | 17,938 | Riboflavin synthase-like beta-barrel | Riboflavin_synthase-like_b-brl | Homologous_superfamily | 256,179 | false | false | This superfamily represents a structural domain with a closed β-barrel fold with greek-key topology. Domains with this structure can be found in the following proteins: Riboflavin synthase, which contains two homologous domains of this structure [ ]. The FAD-binding (N-terminal) domain of ferredoxin reductase (flavodox... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF63380"
] | [
""
] | [
256179
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-1222556",
"R-BTA-1236973",
"R-BTA-1237044",
"R-BTA-196836",
"R-BTA-211945",
"R-BTA-3299685",
"R-BTA-4420097",
"R-BTA-5668599",
"R-BTA-6798695",
"R-BTA-9013149",
"R-BTA-9013404",
"R-BTA-9013423",
"R-CEL-156581",
"R-CEL-1614635",
"R-CEL-209968",
"R-CEL-9759218",
... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-1236973",
"REACTOME:R-BTA-1237044",
"REACTOME:R-BTA-196836",
"REACTOME:R-BTA-211945",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-5668599",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9013149",
"REACTOME:R... | 174 | [
"1a8p",
"1amo",
"1b2r",
"1bjk",
"1bqe",
"1bx0",
"1bx1",
"1cne",
"1cnf",
"1cqx",
"1ddg",
"1ddi",
"1e62",
"1e63",
"1e64",
"1ep1",
"1ep2",
"1ep3",
"1ewy",
"1f20",
"1fdr",
"1fnb",
"1fnc",
"1fnd",
"1frn",
"1frq",
"1gaq",
"1gaw",
"1gjr",
"1go2",
"1gr1",
"1gvh"... | 322 | [
"PUB00004914",
"PUB00005157",
"PUB00014352",
"PUB00016237",
"PUB00022011",
"PUB00022784",
"PUB00024613",
"PUB00024750",
"PUB00025941",
"PUB00030235",
"PUB00036526",
"PUB00036699",
"PUB00036827",
"PUB00043427",
"PUB00043814"
] | [
"9237990",
"1280857",
"10860732",
"15379538",
"12051836",
"15502298",
"11188687",
"11473123",
"11377200",
"10353815",
"7760334",
"9149148",
"11964402",
"18298940",
"18602927"
] | [
"Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.",
"Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S].",
"Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reduct... | [
1997,
1992,
2000,
2004,
2002,
2004,
2000,
2001,
2001,
1999,
1995,
1997,
2002,
2008,
2008
] | 15 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
2043,
162971,
89207,
4,
3,
1951
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
147,
11,
73,
29,
9,
92,
48,
22,
81,
95,
15,
11,
226
] | 13 | true | Homologous_superfamily | Riboflavin synthase-like beta-barrel | Riboflavin synthase-like beta-barrel | Riboflavin_synthase-like_b-brl | 5 |
IPR017939 | 17,939 | Gamma-glutamylcyclotransferase | G-Glutamylcylcotransferase | Family | 10,538 | false | false | This entry contains the human protein C7orf24 ( ) which has been used as a cancer marker with a potential role in cell proliferation. It has been characterised as gamma-glutamyl cyclotransferase (GGCT), a homodimer of two 21kDa subunits, that catalyses the formation of 5-oxoproline (2-pyrrolidone-5-carboxylic acid, pyr... | [
"GO:0003839"
] | [
"gamma-glutamylcyclotransferase activity"
] | [
"molecular_function"
] | 1 | [
"PANTHER"
] | [
"PTHR12935"
] | [
""
] | [
10538
] | 1 | [
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.3.2.9",
"PWY-4041",
"PWY-7533",
"R-BTA-174403",
"R-HSA-174403",
"R-MMU-174403"
] | [
"EC:4.3.2.9",
"METACYC:PWY-4041",
"METACYC:PWY-7533",
"REACTOME:R-BTA-174403",
"REACTOME:R-HSA-174403",
"REACTOME:R-MMU-174403"
] | 6 | [
"2i5t",
"2pn7",
"2q53",
"2rbh",
"3cry"
] | 5 | [
"PUB00043815",
"PUB00083161",
"PUB00083162",
"PUB00094237",
"PUB00094238"
] | [
"18515354",
"15979823",
"21612254",
"28376389",
"25302411"
] | [
"The identification and structural characterization of C7orf24 as gamma-glutamyl cyclotransferase. An essential enzyme in the gamma-glutamyl cycle.",
"Bioinformatic and expression analysis of the putative gliotoxin biosynthetic gene cluster of Aspergillus fumigatus.",
"Identification of cryptic products of the ... | [
2008,
2005,
2011,
2017,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
20,
5130,
5263,
24,
101
] | 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"
] | [
1,
7,
5,
7,
3,
1,
5
] | 7 | true | Family | Gamma-glutamylcyclotransferase | Gamma-glutamylcyclotransferase | G-Glutamylcylcotransferase | 7 |
IPR017941 | 17,941 | Rieske [2Fe-2S] iron-sulphur domain | Rieske_2Fe-2S | Domain | 142,574 | false | false | This entry represents the Rieske [2Fe-2S] iron-sulphur domain. The structure of several Rieske domains has been solved [ ]. It contains three layers of antiparallel β-sheets forming two β-sandwiches. Both β-sandwiches share the central sheet 2. The metal-binding site is at the top of the β-sandwich formed by the sheets... | [
"GO:0051537"
] | [
"2 iron, 2 sulfur cluster binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF00355",
"PS51296"
] | [
"Rieske",
"RIESKE"
] | [
128436,
142395
] | 2 | [
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp0613",
"GenProp1554",
"GenProp1746",
"R-BTA-611105",
"R-BTA-9865881",
"R-CEL-9865881",
"R-DME-611105",
"R-DME-9865881",
"R-DRE-9865881",
"R-GGA-611105",
"R-GGA-9865881",
"R-HSA-611105",
"R-HSA-9865881",
"R-MMU-611105",
"R-MMU-9865881",
"R-RNO-611105",
"R-RNO-9865881",
"R-SC... | [
"GP:GenProp0613",
"GP:GenProp1554",
"GP:GenProp1746",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-9865881",
"REACTOME:R-CEL-9865881",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-9865881",
"REACTOME:R-DRE-9865881",
"REACTOME:R-GGA-611105",
"REACTOME:R-GGA-9865881",
"REACTOME:R-HSA-611105",
"REACTOM... | 23 | [
"1bcc",
"1be3",
"1bgy",
"1eg9",
"1ezv",
"1fqt",
"1g8j",
"1g8k",
"1jm1",
"1kb9",
"1kyo",
"1l0l",
"1l0n",
"1ndo",
"1ntk",
"1ntm",
"1ntz",
"1nu1",
"1nyk",
"1o7g",
"1o7h",
"1o7m",
"1o7n",
"1o7p",
"1o7w",
"1p84",
"1pp9",
"1ppj",
"1q90",
"1qcr",
"1rfs",
"1rie"... | 436 | [
"PUB00005280",
"PUB00043836",
"PUB00043837"
] | [
"8736555",
"16168954",
"16271700"
] | [
"Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution.",
"Rieske business: structure-function of Rieske non-heme oxygenases.",
"Multiple Rieske proteins in prokaryotes: where and why?"
] | [
1996,
2005,
2005
] | 3 | [] | [
"IPR005805",
"IPR037338",
"IPR037339",
"IPR043257",
"IPR054716"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
2673,
110829,
26831,
5,
6,
2230
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
84,
3,
22,
12,
3,
11,
6,
4,
41,
10,
1,
2,
68
] | 13 | true | Domain | Rieske [2Fe-2S] iron-sulphur domain | Rieske [2Fe-2S] iron-sulphur domain | Rieske_2Fe-2S | 3 |
IPR017942 | 17,942 | Lipid-binding serum glycoprotein, N-terminal | Lipid-bd_serum_glycop_N | Domain | 9,832 | false | false | This entry represents the N-terminal domain found in several lipid-binding serum glycoproteins. The N- and C-terminal domains share a similar two-layer α/β structure, but they show little sequence identity. Proteins containing this N-terminal domain include: Bactericidal permeability-increasing protein (BPI) Lipopolysa... | [
"GO:0008289"
] | [
"lipid binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF01273",
"SM00328"
] | [
"LBP_BPI_CETP",
"BPI1"
] | [
9585,
6950
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-166016",
"R-BTA-6798695",
"R-BTA-6803157",
"R-CEL-166016",
"R-CEL-5686938",
"R-HSA-166016",
"R-HSA-166020",
"R-HSA-381426",
"R-HSA-5686938",
"R-HSA-6785807",
"R-HSA-6798695",
"R-HSA-6803157",
"R-HSA-8957275",
"R-HSA-8964041",
"R-HSA-8964058",
"R-HSA-9029569",
"R-MMU-166016",
... | [
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6803157",
"REACTOME:R-CEL-166016",
"REACTOME:R-CEL-5686938",
"REACTOME:R-HSA-166016",
"REACTOME:R-HSA-166020",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-5686938",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6798695",
"REACTOME:R-H... | 29 | [
"1bp1",
"1ewf",
"2obd",
"3zpm",
"4ews",
"4f2a",
"4keg",
"4kgh",
"4kgo",
"4m4d",
"4n4x",
"5i7j",
"5i7k",
"5i7l",
"5wd6",
"6baq",
"6o1t"
] | 17 | [
"PUB00005225",
"PUB00021529",
"PUB00043816",
"PUB00043817",
"PUB00043818",
"PUB00043819",
"PUB00043820"
] | [
"9188532",
"10843855",
"12887306",
"17277799",
"18245229",
"16364440",
"12693940"
] | [
"Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.",
"The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold.",
"Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): structure... | [
1997,
2000,
2003,
2007,
2008,
2006,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9832
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
15,
9,
5,
34,
32,
4,
49,
7
] | 8 | true | Domain | Lipid-binding serum glycoprotein, N-terminal | Lipid-binding serum glycoprotein, N-terminal | Lipid-bd_serum_glycop_N | 8 |
IPR017943 | 17,943 | Bactericidal permeability-increasing protein, alpha/beta domain superfamily | Bactericidal_perm-incr_a/b_dom | Homologous_superfamily | 16,152 | false | false | This superfamily represents a structural domain with a core structure consisting of two layers, alpha/beta. These homologous structural domains can show little sequence identity with each other. A number of mammalian lipid-binding serum glycoproteins contain one or more such structural domains, including: Bactericidal ... | [
"GO:0008289"
] | [
"lipid binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF55394"
] | [
""
] | [
16152
] | 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-166016",
"R-BTA-6798695",
"R-BTA-6803157",
"R-CEL-166016",
"R-CEL-5686938",
"R-DDI-166016",
"R-DDI-5686938",
"R-DDI-6798695",
"R-DDI-6803157",
"R-HSA-166016",
"R-HSA-166020",
"R-HSA-381426",
"R-HSA-5686938",
"R-HSA-6785807",
"R-HSA-6798695",
"R-HSA-6803157",
"R-HSA-8957275",
... | [
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6803157",
"REACTOME:R-CEL-166016",
"REACTOME:R-CEL-5686938",
"REACTOME:R-DDI-166016",
"REACTOME:R-DDI-5686938",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-6803157",
"REACTOME:R-HSA-166016",
"REACTOME:R-HSA-166020",
"REACTOME:R-H... | 33 | [
"1bp1",
"1ewf",
"2obd",
"3zpm",
"4ews",
"4f2a",
"4keg",
"4kgh",
"4kgo",
"4m4d",
"4n4x",
"5i7j",
"5i7k",
"5i7l",
"5wd6",
"6baq",
"6o1t"
] | 17 | [
"PUB00005225",
"PUB00021529",
"PUB00043816",
"PUB00043817",
"PUB00043818",
"PUB00043819",
"PUB00043820"
] | [
"9188532",
"10843855",
"12887306",
"17277799",
"18245229",
"16364440",
"12693940"
] | [
"Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.",
"The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold.",
"Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): structure... | [
1997,
2000,
2003,
2007,
2008,
2006,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"hydrothermal vent metagenome"
] | [
52,
16099,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
15,
15,
5,
2,
36,
34,
1,
6,
52,
8
] | 10 | true | Homologous_superfamily | Bactericidal permeability-increasing protein, alpha/beta domain superfamily | Bactericidal permeability-increasing protein, alpha/beta domain superfamily | Bactericidal_perm-incr_a/b_dom | 1 |
IPR017944 | 17,944 | KaiA/RbsU helical domain superfamily | KaiA/RbsU_helical_domain_sf | Homologous_superfamily | 1,876 | false | false | This superfamily represents a structural domain consisting of four helices in a bundle with a right-handed superhelix. Homologous structural domains can be found in: The C-terminal domain of the circadian clock protein KaiA The N-terminal domain of the phosphoserine phosphatase protein RsbU The cyanobacterial clock pro... | [
"GO:0006468"
] | [
"protein phosphorylation"
] | [
"biological_process"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.1240.30",
"SSF101215"
] | [
"",
""
] | [
1873,
1505
] | 2 | [] | [] | [] | 0 | [
"1q6a",
"1q6b",
"1r5q",
"1r8j",
"1suy",
"1sv1",
"1v2z",
"1w53",
"2j6y",
"2j6z",
"2j70",
"4g86",
"5c5e",
"5jwr",
"5n8y"
] | 15 | [
"PUB00031979",
"PUB00032184"
] | [
"15170179",
"15263010"
] | [
"Crystal structure of the C-terminal clock-oscillator domain of the cyanobacterial KaiA protein.",
"Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C."
] | [
2004,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanosarcinales",
"Rhizophagus irregularis"
] | [
1857,
18,
1
] | 3 | [] | [] | 0 | true | Homologous_superfamily | KaiA/RbsU helical domain superfamily | KaiA/RbsU helical domain superfamily | KaiA/RbsU_helical_domain_sf | 7 |
IPR017945 | 17,945 | DHBP synthase RibB-like alpha/beta domain superfamily | DHBP_synth_RibB-like_a/b_dom | Homologous_superfamily | 87,854 | false | false | This superfamily represents a structural domain consisting of segregated alpha and beta regions in 3-layers. Homologous domains with this structure are found in: 3,4-dihydroxy-2-butanone 4-phosphate synthase ( ) (DHBP synthase) (RibB) A family of eukaryotic and prokaryotic hypothetical proteins that includes YrdC and Y... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF55821"
] | [
""
] | [
87854
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6787450",
"R-HSA-6787450",
"R-MMU-6787450",
"R-RNO-6787450"
] | [
"REACTOME:R-BTA-6787450",
"REACTOME:R-HSA-6787450",
"REACTOME:R-MMU-6787450",
"REACTOME:R-RNO-6787450"
] | 4 | [
"1g57",
"1g58",
"1hru",
"1iez",
"1jcu",
"1k49",
"1k4i",
"1k4l",
"1k4o",
"1k4p",
"1k7j",
"1kk9",
"1pvw",
"1pvy",
"1snn",
"1tks",
"1tku",
"2eqa",
"2mx1",
"2ris",
"2riu",
"3aje",
"3h07",
"3l7v",
"3lqu",
"3lrj",
"3ls6",
"3mgz",
"3mio",
"3mk5",
"3tsp",
"3tsq"... | 65 | [
"PUB00003582",
"PUB00011084",
"PUB00015683",
"PUB00043824",
"PUB00043825",
"PUB00043826",
"PUB00054278"
] | [
"9211332",
"12377778",
"12211024",
"11396941",
"15716138",
"18004774",
"19287007"
] | [
"Biosynthesis of riboflavin: 3,4-dihydroxy-2-butanone-4-phosphate synthase.",
"HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation.",
"Crystal structure of the YciO protein from Escherichia coli.",
"Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon ... | [
1997,
2002,
2002,
2001,
2005,
2008,
2009
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2202,
72781,
11185,
9,
1677
] | 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",... | [
26,
3,
16,
1,
4,
1,
2,
2,
13,
5,
2,
2,
44
] | 13 | true | Homologous_superfamily | DHBP synthase RibB-like alpha/beta domain superfamily | DHBP synthase RibB-like alpha/beta domain superfamily | DHBP_synth_RibB-like_a/b_dom | 4 |
IPR017946 | 17,946 | PLC-like phosphodiesterase, TIM beta/alpha-barrel domain superfamily | PLC-like_Pdiesterase_TIM-brl | Homologous_superfamily | 154,832 | false | false | This superfamily represents a structural domain consisting of a TIM β/α-barrel. These domains are found in several phospholipase C (PLC) like phosphodiesterases, including: Mammalian phospholipase C isozyme D1 [ ]. Bacterial phosphatidylinositol-specific phospholipase C [ ]. Glycerophosphodiester phosphodiesterases, su... | [
"GO:0008081",
"GO:0006629"
] | [
"phosphoric diester hydrolase activity",
"lipid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.20.20.190",
"SSF51695"
] | [
"",
""
] | [
150684,
154028
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-112043",
"R-BTA-1855204",
"R-BTA-399997",
"R-BTA-4086398",
"R-BTA-416476",
"R-BTA-418217",
"R-BTA-434316",
"R-BTA-500657",
"R-BTA-6814848",
"R-CEL-112043",
"R-CEL-1855204",
"R-CEL-416476",
"R-DDI-112043",
"R-DDI-114604",
"R-DDI-1169408",
"R-DDI-1855204",
"R-DDI-202433",
"R-D... | [
"REACTOME:R-BTA-112043",
"REACTOME:R-BTA-1855204",
"REACTOME:R-BTA-399997",
"REACTOME:R-BTA-4086398",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418217",
"REACTOME:R-BTA-434316",
"REACTOME:R-BTA-500657",
"REACTOME:R-BTA-6814848",
"REACTOME:R-CEL-112043",
"REACTOME:R-CEL-1855204",
"REACTOME:R-CEL... | 168 | [
"1aod",
"1djg",
"1djh",
"1dji",
"1djw",
"1djx",
"1djy",
"1djz",
"1gym",
"1o1z",
"1ptd",
"1ptg",
"1qas",
"1qat",
"1t6m",
"1t8q",
"1v8e",
"1vd6",
"1xx1",
"1ydy",
"1zcc",
"2f9r",
"2fju",
"2isd",
"2o55",
"2oog",
"2or2",
"2otd",
"2p76",
"2plc",
"2ptd",
"2pz0"... | 124 | [
"PUB00023203",
"PUB00030187",
"PUB00038838",
"PUB00043827"
] | [
"9335537",
"8784353",
"16909422",
"18691970"
] | [
"Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis.",
"C2 domain conformational changes in phospholipase C-delta 1.",
"Crystal structure of glycerophosphodiester phosphodiesterase from Agrobacterium tumefaciens by SAD wit... | [
1997,
1996,
2006,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
906,
64783,
87811,
141,
1191
] | 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",... | [
141,
44,
197,
30,
2,
120,
71,
14,
73,
123,
5,
3,
210
] | 13 | true | Homologous_superfamily | PLC-like phosphodiesterase, TIM beta/alpha-barrel domain superfamily | PLC-like phosphodiesterase, TIM beta/alpha-barrel domain superfamily | PLC-like_Pdiesterase_TIM-brl | 3 |
IPR017947 | 17,947 | Aryldialkylphosphatase, zinc-binding site | AryldialkylPase_Zn-BS | Binding_site | 3,674 | false | false | Synonym(s): Paraoxonase, A-esterase, Aryltriphosphatase, Phosphotriesterase, Paraoxon hydrolase Bacteria such as Brevundimonas diminuta (Pseudomonas diminuta) harbour a plasmid that carries the gene for aryldialkylphosphatase ( ) (PTE) (also known as parathion hydrolase). This enzyme has attracted interest because of i... | [
"GO:0008270",
"GO:0016788",
"GO:0009056"
] | [
"zinc ion binding",
"hydrolase activity, acting on ester bonds",
"catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS01322"
] | [
"PHOSPHOTRIESTERASE_1"
] | [
3674
] | 1 | [] | [] | [] | 0 | [
"1bf6",
"1dpm",
"1eyw",
"1ez2",
"1hzy",
"1i0b",
"1i0d",
"1jgm",
"1p6b",
"1p6c",
"1psc",
"1pta",
"1qw7",
"2d2g",
"2d2h",
"2d2j",
"2o4m",
"2o4q",
"2ob3",
"2oql",
"2r1k",
"2r1l",
"2r1m",
"2r1n",
"2r1p",
"2vc5",
"2vc7",
"2zc1",
"3a3w",
"3a3x",
"3a4j",
"3c86"... | 150 | [
"PUB00000454",
"PUB00000987"
] | [
"9548740",
"9383406"
] | [
"Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family.",
"Evolution in action."
] | [
1998,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
33,
2550,
1038,
53
] | 4 | [
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
1,
3,
4
] | 5 | true | Binding_site | Aryldialkylphosphatase, zinc-binding site | Aryldialkylphosphatase, zinc-binding site | AryldialkylPase_Zn-BS | 9 |
IPR017948 | 17,948 | Transforming growth factor beta, conserved site | TGFb_CS | Conserved_site | 33,772 | false | false | This entry represents a a region which includes two of the conserved cysteines. Transforming growth factor-beta (TGF-beta) is a multifunctional peptide that controls proliferation, differentiation and other functions in many cell types. TGF-beta-1 is a peptide of 112 amino acid residues derived by proteolytic cleavage ... | [
"GO:0008083"
] | [
"growth factor activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00250"
] | [
"TGF_BETA_1"
] | [
33772
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-1502540",
"R-BTA-201451",
"R-BTA-209822",
"R-BTA-2129379",
"R-BTA-2173789",
"R-BTA-2473224",
"R-BTA-381426",
"R-BTA-8957275",
"R-BTA-9839389",
"R-BTA-9839406",
"R-CEL-114608",
"R-CEL-201451",
"R-CEL-2129379",
"R-CEL-2173788",
"R-CEL-2173789",
"R-CEL-2173791",
... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1502540",
"REACTOME:R-BTA-201451",
"REACTOME:R-BTA-209822",
"REACTOME:R-BTA-2129379",
"REACTOME:R-BTA-2173789",
"REACTOME:R-BTA-2473224",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-9839389",
"REACTOME:R-BTA-9839406",
"REACTOME:R-... | 135 | [
"1bmp",
"1es7",
"1kla",
"1klc",
"1kld",
"1ktz",
"1lx5",
"1lxi",
"1m4u",
"1nys",
"1nyu",
"1reu",
"1rew",
"1s4y",
"1tfg",
"1tgj",
"1tgk",
"1waq",
"1zkz",
"2arp",
"2arv",
"2b0u",
"2bhk",
"2goo",
"2h62",
"2h64",
"2p6a",
"2pjy",
"2qcq",
"2qcw",
"2qj9",
"2qja"... | 150 | [
"PUB00000211",
"PUB00004939",
"PUB00005153",
"PUB00007614",
"PUB00043835"
] | [
"1575734",
"8199356",
"1631557",
"8679613",
"18662538"
] | [
"Evolutionary grouping of the transforming growth factor-beta superfamily.",
"Evolution of the transforming growth factor-beta superfamily.",
"Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.",
"Transforming growth factor beta 1: three-dimensional structure in solut... | [
1992,
1994,
1992,
1996,
2008
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Chordopoxvirinae",
"Eukaryota",
"organismal metagenomes"
] | [
4,
6,
33760,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
95,
11,
103,
77,
85
] | 6 | true | Conserved_site | Transforming growth factor beta, conserved site | Transforming growth factor beta, conserved site | TGFb_CS | 5 |
IPR017949 | 17,949 | Thaumatin, conserved site | Thaumatin_CS | Conserved_site | 8,865 | false | false | Thaumatin [ ] is an intensely sweet-tasting protein, 100,000 times sweeter than sucrose on a molar basis [ ] found in berries from Thaumatococcus daniellii, a tropical flowering plant known as Katemfe, it is induced by attack by viroids, which are single-stranded unencapsulated RNA molecules that do not code for protei... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00316"
] | [
"THAUMATIN_1"
] | [
8865
] | 1 | [] | [] | [] | 0 | [
"1aun",
"1du5",
"1lr2",
"1lr3",
"1lxz",
"1ly0",
"1pcv",
"1pp3",
"1rqw",
"1thi",
"1thu",
"1thv",
"1thw",
"1z3q",
"2a7i",
"2ahn",
"2blr",
"2blu",
"2d8o",
"2d8p",
"2g4y",
"2i0w",
"2oqn",
"2pe7",
"2vhk",
"2vhr",
"2vi1",
"2vi2",
"2vi3",
"2vi4",
"2vu6",
"2vu7"... | 212 | [
"PUB00001747",
"PUB00004543",
"PUB00004556",
"PUB00004580",
"PUB00004582",
"PUB00043682"
] | [
"7049841",
"1650615",
"1463856",
"7846159",
"7630973",
"16666857"
] | [
"Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli.",
"A wheat glutathione-S-transferase gene with transposon-like sequences in the promoter region.",
"Nucleotide sequence of an osmotin-like cDNA induced in tomato during viroid infection.",
"Characteriza... | [
1982,
1991,
1992,
1994,
1995,
1989
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
29,
8836
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
82,
47,
66
] | 3 | true | Conserved_site | Thaumatin, conserved site | Thaumatin, conserved site | Thaumatin_CS | 8 |
IPR017950 | 17,950 | Urease active site | Urease_AS | Active_site | 13,983 | false | false | Urease (urea amidohydrolase, ) is a nickel-binding enzyme that catalyses the hydrolysis of urea to carbon dioxide and ammonia [ ]. Historically, it was the first enzyme to be crystallized (in 1926). It is mainly found in plant seeds, microorganisms and invertebrates. In plants, urease is a hexamer of identical chains. ... | [
"GO:0009039"
] | [
"urease activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00145"
] | [
"UREASE_2"
] | [
13983
] | 1 | [
"EC",
"METACYC"
] | [
"3.5.1.5",
"PWY-5704"
] | [
"EC:3.5.1.5",
"METACYC:PWY-5704"
] | 2 | [
"1a5k",
"1a5l",
"1a5m",
"1a5n",
"1a5o",
"1e9z",
"1ef2",
"1ejr",
"1ejs",
"1ejt",
"1ejw",
"1ejx",
"1fwi",
"1fwj",
"1ie7",
"1kra",
"1krb",
"1s3t",
"1ubp",
"2kau",
"2ubp",
"3la4",
"3ubp",
"4ac7",
"4ceu",
"4cex",
"4ep8",
"4epb",
"4epd",
"4epe",
"4g7e",
"4goa"... | 70 | [
"PUB00001363",
"PUB00003605",
"PUB00005206"
] | [
"3402446",
"2651866",
"7754395"
] | [
"The structure of jack bean urease. The complete amino acid sequence, limited proteolysis and reactive cysteine residues.",
"Microbial ureases: significance, regulation, and molecular characterization.",
"The crystal structure of urease from Klebsiella aerogenes."
] | [
1988,
1989,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
608,
10311,
2375,
689
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
2,
1,
1,
9
] | 5 | true | Active_site | Urease active site | Urease active site | Urease_AS | 9 |
IPR017951 | 17,951 | Urease alpha subunit, C-terminal | Urease_asu_c | Domain | 23,805 | false | false | This entry describes the C-terminal domain of urease alpha subunit UreC (designated beta or UreB in Helicobacter species). Urease ( ) belongs to MEROPS peptidase family M38 (clan MJ). Urease (urea amidohydrolase, ) a nickel-binding enzyme that catalyses the hydrolysis of urea to form ammonia and carbamate [ ]. It is ma... | [
"GO:0009039",
"GO:0016151"
] | [
"urease activity",
"nickel cation binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROFILE"
] | [
"PS51368"
] | [
"UREASE_3"
] | [
23805
] | 1 | [
"EC",
"METACYC"
] | [
"3.5.1.5",
"PWY-5704"
] | [
"EC:3.5.1.5",
"METACYC:PWY-5704"
] | 2 | [
"1a5k",
"1a5l",
"1a5m",
"1a5n",
"1a5o",
"1e9y",
"1e9z",
"1ef2",
"1ejr",
"1ejs",
"1ejt",
"1eju",
"1ejv",
"1ejw",
"1ejx",
"1fwa",
"1fwb",
"1fwc",
"1fwd",
"1fwe",
"1fwf",
"1fwg",
"1fwh",
"1fwi",
"1fwj",
"1ie7",
"1kra",
"1krb",
"1krc",
"1s3t",
"1ubp",
"2kau"... | 84 | [
"PUB00001363",
"PUB00003605",
"PUB00005206",
"PUB00010725"
] | [
"3402446",
"2651866",
"7754395",
"7565414"
] | [
"The structure of jack bean urease. The complete amino acid sequence, limited proteolysis and reactive cysteine residues.",
"Microbial ureases: significance, regulation, and molecular characterization.",
"The crystal structure of urease from Klebsiella aerogenes.",
"Molecular biology of microbial ureases."
] | [
1988,
1989,
1995,
1995
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
688,
12133,
2936,
8048
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
2,
1,
1,
15
] | 5 | true | Domain | Urease alpha subunit, C-terminal | Urease alpha subunit, C-terminal | Urease_asu_c | 4 |
IPR017953 | 17,953 | Carbohydrate kinase, predicted, conserved site | Carbohydrate_kinase_pred_CS | Conserved_site | 20,687 | false | false | Proteins in this entry are related to Hydroxyethylthiazole kinase ( ) and PfkB carbohydrate kinase implying they are also carbohydrate kinases. Several uncharacterised proteins have been shown to share regions of similarities, including yeast chromosome XI hypothetical protein YKL151c; Caenorhabditis elegans hypothetic... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS01049",
"PS01050"
] | [
"YJEF_C_1",
"YJEF_C_2"
] | [
4498,
19146
] | 2 | [
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.2.1.136",
"PWY-6938",
"PWY-8136",
"R-CEL-196807",
"R-DME-196807",
"R-DRE-196807",
"R-SCE-196807",
"R-SPO-196807"
] | [
"EC:4.2.1.136",
"METACYC:PWY-6938",
"METACYC:PWY-8136",
"REACTOME:R-CEL-196807",
"REACTOME:R-DME-196807",
"REACTOME:R-DRE-196807",
"REACTOME:R-SCE-196807",
"REACTOME:R-SPO-196807"
] | 8 | [
"1kyh",
"2ax3",
"2r3b",
"2r3e",
"3bgk",
"3k5w",
"3rph",
"3rpz",
"3rq2",
"3rq5",
"3rq6",
"3rq8",
"3rqh",
"3rqq",
"3rqx",
"3rrb",
"3rre",
"3rrf",
"3rrj",
"3rs8",
"3rs9",
"3rsf",
"3rsg",
"3rsq",
"3rss",
"3rt7",
"3rt9",
"3rta",
"3rtb",
"3rtc",
"3rtd",
"3rte"... | 35 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
411,
17488,
2385,
403
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
13,
1,
1,
1,
1,
1
] | 7 | true | Conserved_site | Carbohydrate kinase, predicted, conserved site | Carbohydrate kinase, predicted, conserved site | Carbohydrate_kinase_pred_CS | 2 |
IPR017954 | 17,954 | Lipid-binding serum glycoprotein, conserved site | Lipid-bd_serum_glycop_CS | Conserved_site | 1,279 | false | false | This entry represents a conserved sequence region found in the N-terminal domain of several lipid-binding serum glycoproteins. The N- and C-terminal domains of these proteins share a similar two-layer α/β structure, but they show little sequence identity. Proteins containing this N-terminal domain include: Bactericidal... | [
"GO:0008289"
] | [
"lipid binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00400"
] | [
"LBP_BPI_CETP"
] | [
1279
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-166016",
"R-BTA-6798695",
"R-BTA-6803157",
"R-HSA-166016",
"R-HSA-166020",
"R-HSA-5686938",
"R-HSA-6785807",
"R-HSA-6798695",
"R-HSA-6803157",
"R-HSA-8964041",
"R-HSA-8964058",
"R-HSA-9029569",
"R-MMU-166016",
"R-MMU-166020",
"R-MMU-5686938",
"R-MMU-8964058",
"R-RNO-166016",
... | [
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6803157",
"REACTOME:R-HSA-166016",
"REACTOME:R-HSA-166020",
"REACTOME:R-HSA-5686938",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6803157",
"REACTOME:R-HSA-8964041",
"REACTOME:R-HSA-8964058",
"REACTOME:R... | 19 | [
"1bp1",
"1ewf",
"2obd",
"4ews",
"4f2a",
"4m4d"
] | 6 | [
"PUB00005225",
"PUB00021529",
"PUB00043816",
"PUB00043817",
"PUB00043818",
"PUB00043819",
"PUB00043820"
] | [
"9188532",
"10843855",
"12887306",
"17277799",
"18245229",
"16364440",
"12693940"
] | [
"Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.",
"The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold.",
"Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): structure... | [
1997,
2000,
2003,
2007,
2008,
2006,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1279
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
18,
11,
10
] | 4 | true | Conserved_site | Lipid-binding serum glycoprotein, conserved site | Lipid-binding serum glycoprotein, conserved site | Lipid-bd_serum_glycop_CS | 4 |
IPR017956 | 17,956 | AT hook, DNA-binding motif | AT_hook_DNA-bd_motif | Conserved_site | 28,077 | false | false | AT hooks are DNA-binding motifs with a preference for A/T rich regions. These motifs are found in a variety of proteins, including the high mobility group (HMG) proteins [ ], in DNA-binding proteins from plants [ ] and in hBRG1 protein, a central ATPase of the human switching/sucrose non-fermenting (SWI/SNF) remodellin... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"SMART"
] | [
"PF02178",
"PR00929",
"SM00384"
] | [
"AT_hook",
"ATHOOK",
"AT_hook"
] | [
5383,
15301,
24381
] | 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-2559584",
"R-CFA-2559584",
"R-DME-674695",
"R-DME-6804756",
"R-DME-73776",
"R-DME-73779",
"R-DME-75953",
"R-DME-76042",
"R-HSA-162592",
"R-HSA-164843",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910",
"R-HSA-2559584",
"R-HSA-3214841",
"R-HSA-427413",
"R-MMU-25... | [
"REACTOME:R-CEL-2559584",
"REACTOME:R-CFA-2559584",
"REACTOME:R-DME-674695",
"REACTOME:R-DME-6804756",
"REACTOME:R-DME-73776",
"REACTOME:R-DME-73779",
"REACTOME:R-DME-75953",
"REACTOME:R-DME-76042",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-175567",
"REACTOME:R-HSA-1775... | 24 | [
"6igm",
"6uxv",
"6uxw",
"7c4j",
"7kif",
"7kim",
"7kuf",
"8x15",
"8x19",
"8x1c",
"9ca7",
"9ca8",
"9ca9",
"9caa",
"9cab"
] | 15 | [
"PUB00044075",
"PUB00044076",
"PUB00044077"
] | [
"11406267",
"8790293",
"17081121"
] | [
"HMGI/Y proteins: flexible regulators of transcription and chromatin structure.",
"Novel members of a family of AT hook-containing DNA-binding proteins from rice are identified through their in vitro interaction with consensus target sites of plant and animal homeodomain proteins.",
"DNA-binding properties of t... | [
2001,
1996,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
818,
27213,
14,
32
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
80,
4,
49,
8,
33,
26,
6,
46,
28,
1,
1,
143
] | 12 | true | Conserved_site | AT hook, DNA-binding motif | AT hook, DNA-binding motif | AT_hook_DNA-bd_motif | 8 |
IPR017957 | 17,957 | P-type trefoil, conserved site | P_trefoil_CS | Conserved_site | 4,376 | false | false | A cysteine-rich domain of approximately forty five amino-acid residues has been found in some extracellular eukaryotic proteins [ , , , ]. It is known as either the 'P', 'trefoil' or 'TFF' domain, and contains six cysteines linked by three disulphide bonds with connectivity 1-5, 2-4, 3-6. The domain has been found in a... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00025"
] | [
"P_TREFOIL_1"
] | [
4376
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-2534343",
"R-BTA-6798695",
"R-BTA-70221",
"R-HSA-189085",
"R-HSA-2534343",
"R-HSA-5357609",
"R-HSA-5659898",
"R-HSA-6798695",
"R-HSA-70221",
"R-HSA-9018519",
"R-MMU-2534343",
"R-MMU-6798695",
"R-MMU-70221",
"R-RNO-189085",
"R-RNO-6798695",
"R-RNO-70221",
"R-SSC-2534343"
] | [
"REACTOME:R-BTA-2534343",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70221",
"REACTOME:R-HSA-189085",
"REACTOME:R-HSA-2534343",
"REACTOME:R-HSA-5357609",
"REACTOME:R-HSA-5659898",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-70221",
"REACTOME:R-HSA-9018519",
"REACTOME:R-MMU-2534343",
"REACTOME:R-M... | 17 | [
"1e9t",
"1hi7",
"1pcp",
"1pe3",
"1pos",
"1ps2",
"1psp",
"2psp",
"2qly",
"2qmj",
"3ctt",
"3l4t",
"3l4u",
"3l4v",
"3l4w",
"3l4x",
"3l4y",
"3l4z",
"3lpo",
"3lpp",
"5kzw",
"5kzx",
"5nn3",
"5nn4",
"5nn5",
"5nn6",
"5nn8",
"6v1c",
"6v1d",
"7p2z",
"7p32",
"8bqu"... | 43 | [
"PUB00001033",
"PUB00001707",
"PUB00005012",
"PUB00005400"
] | [
"7820556",
"9187350",
"8518738",
"8267796"
] | [
"Trefoil peptides. Coming up clover.",
"Rolling in the clover: trefoil factor family (TFF)-domain peptides, cell migration and cancer.",
"A trefoil domain in the major rabbit zona pellucida protein.",
"The P-domain or trefoil motif: a role in renewal and pathology of mucous epithelia?"
] | [
1994,
1997,
1993,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4376
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
18,
13,
23
] | 4 | true | Conserved_site | P-type trefoil, conserved site | P-type trefoil, conserved site | P_trefoil_CS | 8 |
IPR017958 | 17,958 | Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site | Gln-tRNA_amidoTrfase_suB_CS | Conserved_site | 24,891 | false | false | Glutamyl-tRNA(Gln) amidotransferase (Gat; [ec:EC 6.3.5]) provides a means of producing correctly charged Gln-tRNA(Gln) through the transamidation of mis-acylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase [ ]. The reaction takes place in the presence of glutamine and ATP through an activated gamma... | [
"GO:0016884"
] | [
"carbon-nitrogen ligase activity, with glutamine as amido-N-donor"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01234"
] | [
"GATB"
] | [
24891
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"6.3.5.-",
"PWY-5297",
"PWY-7811",
"PWY-8229"
] | [
"EC:6.3.5.-",
"METACYC:PWY-5297",
"METACYC:PWY-7811",
"METACYC:PWY-8229"
] | 4 | [
"1zq1",
"2d6f",
"2df4",
"2dqn",
"2f2a",
"2g5h",
"2g5i",
"3al0",
"3h0l",
"3h0m",
"3h0r",
"3ip4",
"3kfu",
"4n0h",
"4n0i",
"4wj3"
] | 16 | [
"PUB00007932"
] | [
"9342321"
] | [
"Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1653,
19818,
3066,
354
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyce... | [
3,
1,
3,
3,
1,
2,
5,
1,
1,
3
] | 10 | true | Conserved_site | Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site | Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site | Gln-tRNA_amidoTrfase_suB_CS | 3 |
IPR017959 | 17,959 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E | Asn/Gln-tRNA_amidoTrfase_suB/E | Family | 29,935 | false | false | Glutamyl-tRNA(Gln) amidotransferase (Gat; ) provides a means of producing correctly charged Gln-tRNA(Gln) through the transamidation of mis-acylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase [ , ]. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Gl... | [
"GO:0016884"
] | [
"carbon-nitrogen ligase activity, with glutamine as amido-N-donor"
] | [
"molecular_function"
] | 1 | [
"PANTHER"
] | [
"PTHR11659"
] | [
""
] | [
29935
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"6.3.5.-",
"PWY-5297",
"PWY-7811",
"PWY-8229"
] | [
"EC:6.3.5.-",
"METACYC:PWY-5297",
"METACYC:PWY-7811",
"METACYC:PWY-8229"
] | 4 | [
"1zq1",
"2d6f",
"2df4",
"2dqn",
"2f2a",
"2g5h",
"2g5i",
"3al0",
"3h0l",
"3h0m",
"3h0r",
"3ip4",
"3kfu",
"4n0h",
"4n0i",
"4wj3"
] | 16 | [
"PUB00007932",
"PUB00015320",
"PUB00038985",
"PUB00040197",
"PUB00100077"
] | [
"9342321",
"10993083",
"16216574",
"16809540",
"20457752"
] | [
"Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation.",
"Domain-specific recruitment of amide amino acids for protein synthesis.",
"Structural basis for tRNA-dependent amidotransferase function.",
"Structural basis of RNA-dependent r... | [
1997,
2000,
2005,
2006,
2010
] | 5 | [] | [
"IPR004413",
"IPR004414"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1785,
22110,
5357,
683
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
3,
1,
1,
2,
9,
3,
1,
2,
7,
1,
1,
6
] | 12 | true | Family | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E | Asn/Gln-tRNA_amidoTrfase_suB/E | 5 |
IPR017961 | 17,961 | DNA polymerase, Y-family, little finger domain | DNA_pol_Y-fam_little_finger | Domain | 64,057 | false | false | This entry represents the little finger domain found in Y-family (lesion bypass) DNA polymerases. Y-family polymerases were originally known as UmuC/DinB/Rev1/Rad30 after each branch of the family. These enzymes are characterised by their low-fidelity synthesis on undamaged DNA templates and by their ability to travers... | [
"GO:0003684",
"GO:0006281"
] | [
"damaged DNA binding",
"DNA repair"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF11799"
] | [
"IMS_C"
] | [
64057
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.7",
"R-CEL-5655862",
"R-CEL-5696397",
"R-CEL-5696400",
"R-CEL-6782135",
"R-CEL-6782210",
"R-DME-110312",
"R-DME-110320",
"R-DME-5655862",
"R-DME-5656121",
"R-GGA-353503",
"R-HSA-110312",
"R-HSA-110320",
"R-HSA-5655862",
"R-HSA-5656121",
"R-HSA-5656169",
"R-HSA-5685942",
"R-H... | [
"EC:2.7.7.7",
"REACTOME:R-CEL-5655862",
"REACTOME:R-CEL-5696397",
"REACTOME:R-CEL-5696400",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-DME-110312",
"REACTOME:R-DME-110320",
"REACTOME:R-DME-5655862",
"REACTOME:R-DME-5656121",
"REACTOME:R-GGA-353503",
"REACTOME:R-HSA-110312"... | 44 | [
"1jih",
"1jx4",
"1jxl",
"1n48",
"1n56",
"1ryr",
"1rys",
"1s0m",
"1s0n",
"1s0o",
"1s10",
"1s97",
"1s9f",
"1t3n",
"1t94",
"1unn",
"1zet",
"2ago",
"2agp",
"2agq",
"2alz",
"2aq4",
"2asd",
"2asj",
"2asl",
"2atl",
"2au0",
"2bq3",
"2bqr",
"2bqu",
"2br0",
"2c22"... | 508 | [
"PUB00026401",
"PUB00026570",
"PUB00031381",
"PUB00031831",
"PUB00040279",
"PUB00044577",
"PUB00044578"
] | [
"11545743",
"11595188",
"15296733",
"14592985",
"16819516",
"17207624",
"18603483"
] | [
"Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis.",
"Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication.",
"Crystal structure of the catalytic core of human DNA polymerase kappa.",
... | [
2001,
2001,
2004,
2003,
2006,
2007,
2008
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
651,
47868,
14854,
11,
6,
667
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
24,
3,
19,
3,
2,
18,
21,
3,
15,
20,
2,
2,
31
] | 13 | true | Domain | DNA polymerase, Y-family, little finger domain | DNA polymerase, Y-family, little finger domain | DNA_pol_Y-fam_little_finger | 7 |
IPR017964 | 17,964 | DNA-directed DNA polymerase, family B, conserved site | DNA-dir_DNA_pol_B_CS | Conserved_site | 26,282 | false | false | DNA is the biological information that instructs cells how to exist in an ordered fashion: accurate replication is thus one of the most important events in the life cycle of a cell. This function is performed by DNA- directed DNA-polymerases ( ) by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the gro... | [
"GO:0000166",
"GO:0003676"
] | [
"nucleotide binding",
"nucleic acid binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00116"
] | [
"DNA_POLYMERASE_B"
] | [
26282
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.7",
"R-CEL-110314",
"R-CEL-5651801",
"R-CEL-5656169",
"R-CEL-5696397",
"R-CEL-5696400",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-69091",
"R-CEL-69166",
"R-CEL-69183",
"R-DDI-110314",
"R-DDI-113501",
"R-DDI-5651801",
"R-DDI-5656169",
"R-DDI-5696397",
"R-DDI-6782135",
"R-DDI-6... | [
"EC:2.7.7.7",
"REACTOME:R-CEL-110314",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-5656169",
"REACTOME:R-CEL-5696397",
"REACTOME:R-CEL-5696400",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-69091",
"REACTOME:R-CEL-69166",
"REACTOME:R-CEL-69183",
"REACTOME:R-DDI-110314",
... | 134 | [
"1clq",
"1d5a",
"1ig9",
"1ih7",
"1q8i",
"1q9x",
"1q9y",
"1qht",
"1qqc",
"1s5j",
"1tgo",
"1waf",
"1waj",
"1wn7",
"1wns",
"1xhx",
"1xhz",
"1xi1",
"2atq",
"2dtu",
"2dy4",
"2ex3",
"2gv9",
"2jgu",
"2oyq",
"2ozm",
"2ozs",
"2p5g",
"2p5o",
"2py5",
"2pyj",
"2pyl"... | 308 | [
"PUB00000436",
"PUB00004353",
"PUB00010600"
] | [
"8679562",
"2461550",
"9757117"
] | [
"Crystal structures of an NH2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions.",
"A sequence motif in many polymerases.",
"Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon."
] | [
1996,
1988,
1998
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1054,
4458,
16178,
4296,
296
] | 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,
5,
5,
3,
1,
20,
7,
3,
6,
17,
4,
4,
28
] | 13 | true | Conserved_site | DNA-directed DNA polymerase, family B, conserved site | DNA-directed DNA polymerase, family B, conserved site | DNA-dir_DNA_pol_B_CS | 8 |
IPR017967 | 17,967 | HMG box A DNA-binding domain, conserved site | HMG_boxA_CS | Conserved_site | 3,324 | false | false | High mobility group (HMG or HMGB) proteins constitute a family of relatively low molecular weight non-histone components in chromatin. HMG1 and HMG2 are highly similar, and preferentially bind single-stranded DNA and unwind double-stranded DNA. Although they have no sequence specificity, they have a high affinity for b... | [
"GO:0003677",
"GO:0005634"
] | [
"DNA binding",
"nucleus"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00353"
] | [
"HMG_BOX_1"
] | [
3324
] | 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-140342",
"R-BTA-445989",
"R-BTA-5620971",
"R-BTA-5686938",
"R-BTA-6798695",
"R-BTA-879415",
"R-BTA-933542",
"R-CFA-140342",
"R-CFA-445989",
"R-CFA-5620971",
"R-CFA-5686938",
"R-CFA-6798695",
"R-CFA-879415",
"R-CFA-933542",
"R-DME-140342",
"R-DME-209394",
"R-DME-5620971",
"R-... | [
"REACTOME:R-BTA-140342",
"REACTOME:R-BTA-445989",
"REACTOME:R-BTA-5620971",
"REACTOME:R-BTA-5686938",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-879415",
"REACTOME:R-BTA-933542",
"REACTOME:R-CFA-140342",
"REACTOME:R-CFA-445989",
"REACTOME:R-CFA-5620971",
"REACTOME:R-CFA-5686938",
"REACTOME:R-CF... | 49 | [
"1aab",
"1ckt",
"1j3x",
"2eqz",
"2ly4",
"2rtu",
"2yrq",
"4qr9",
"5zdz",
"5ze0",
"5ze1",
"5ze2",
"6cg0",
"6cij",
"6cik",
"6cil",
"6cim",
"6oem",
"6oen",
"6oeo",
"6oer",
"9cg9"
] | 22 | [
"PUB00015133"
] | [
"11497996"
] | [
"HMG1 and 2: architectural DNA-binding proteins."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3324
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
4,
14,
22,
23
] | 5 | true | Conserved_site | HMG box A DNA-binding domain, conserved site | HMG box A DNA-binding domain, conserved site | HMG_boxA_CS | 6 |
IPR017968 | 17,968 | Acylphosphatase, conserved site | Acylphosphatase_CS | Conserved_site | 24,459 | false | false | Acylphosphatase ( ) is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [ ], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [ ]. The enzyme has a mainly β-sheet structure with 2 short α-helical segments.... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00150",
"PS00151"
] | [
"ACYLPHOSPHATASE_1",
"ACYLPHOSPHATASE_2"
] | [
19562,
12364
] | 2 | [
"EC"
] | [
"3.6.1.7"
] | [
"EC:3.6.1.7"
] | 1 | [
"1aps",
"1gxt",
"1gxu",
"1urr",
"1v3z",
"1w2i",
"1y9o",
"2acy",
"2bjd",
"2bje",
"2fhm",
"2gv1",
"2hlt",
"2hlu",
"2k7j",
"2k7k",
"2lxf",
"2vh7",
"2w4c",
"2w4d",
"2w4p",
"3br8",
"3tnv",
"3toq",
"3trg",
"3vth",
"3vti",
"4hi1",
"4hi2",
"4oix",
"4oj1",
"4oj3"... | 38 | [
"PUB00002331",
"PUB00002351",
"PUB00003238",
"PUB00011085",
"PUB00033805"
] | [
"2830253",
"1664426",
"2538623",
"12206761",
"9799289"
] | [
"The primary structure of chicken muscle acylphosphatase isozyme Ch1.",
"The primary structure of two molecular species of porcine organ-common type acylphosphatase.",
"Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy.",
"Cry... | [
1987,
1991,
1989,
2002,
1998
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1155,
18691,
4320,
293
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
4,
10,
2,
12,
5,
5,
10,
9
] | 9 | true | Conserved_site | Acylphosphatase, conserved site | Acylphosphatase, conserved site | Acylphosphatase_CS | 4 |
IPR017972 | 17,972 | Cytochrome P450, conserved site | Cyt_P450_CS | Conserved_site | 410,766 | false | false | This entry represents a conserved site based around a highly conserved cysteine residue involved in binding haem iron in the fifth coordination site, which is found in the C-terminal regions of P450 proteins. Cytochrome P450 enzymes are a superfamily of haem-containing mono-oxygenases that are found in all kingdoms of ... | [
"GO:0005506",
"GO:0016705"
] | [
"iron ion binding",
"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00086"
] | [
"CYTOCHROME_P450"
] | [
410766
] | 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-191273",
"R-BTA-193048",
"R-BTA-193993",
"R-BTA-194002",
"R-BTA-211916",
"R-BTA-211935",
"R-BTA-211958",
"R-BTA-211976",
"R-BTA-211981",
"R-BTA-211999",
"R-BTA-5365859",
"R-BTA-9027307",
"R-BTA-9749641",
"R-CEL-196791",
"R-CEL-211916",
"R-CEL-211935",
"R-CEL-211945",
"R-CEL-... | [
"REACTOME:R-BTA-191273",
"REACTOME:R-BTA-193048",
"REACTOME:R-BTA-193993",
"REACTOME:R-BTA-194002",
"REACTOME:R-BTA-211916",
"REACTOME:R-BTA-211935",
"REACTOME:R-BTA-211958",
"REACTOME:R-BTA-211976",
"REACTOME:R-BTA-211981",
"REACTOME:R-BTA-211999",
"REACTOME:R-BTA-5365859",
"REACTOME:R-BTA-90... | 216 | [
"1akd",
"1bu7",
"1bvy",
"1c8j",
"1cl6",
"1cmj",
"1cmn",
"1cp4",
"1cpt",
"1dt6",
"1dz4",
"1dz6",
"1dz8",
"1dz9",
"1e9x",
"1ea1",
"1egy",
"1ehe",
"1ehf",
"1ehg",
"1eup",
"1f24",
"1f25",
"1f26",
"1f4t",
"1f4u",
"1fag",
"1fah",
"1geb",
"1ged",
"1gei",
"1gej"... | 1,353 | [
"PUB00033965",
"PUB00033966",
"PUB00033967",
"PUB00033969"
] | [
"16042601",
"17023115",
"15128046",
"8637843"
] | [
"Biodiversity of cytochrome P450 redox systems.",
"Cytochrome P450--redox partner fusion enzymes.",
"Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.",
"Structural domains of P450-containi... | [
2005,
2007,
2004,
1995
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
806,
81805,
327145,
2,
57,
951
] | 6 | [
"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... | [
1055,
80,
215,
162,
242,
181,
22,
846,
270,
3,
2,
787
] | 12 | true | Conserved_site | Cytochrome P450, conserved site | Cytochrome P450, conserved site | Cyt_P450_CS | 1 |
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