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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR015993 | 15,993 | CDP-diacylglycerol pyrophosphatase, proteobacterial | CDP-diacylglyc_Pase_proteobac | Family | 928 | false | false | The CDP-diacylglycerol pyrophosphatases play a role in the regulation of phospholipid metabolism by inositol, as well as regulating the cellular levels of phosphatidylinositol [ ]. This entry is specific for the proteobacterial enzymes. | [
"GO:0008715",
"GO:0008654",
"GO:0016020"
] | [
"CDP-diacylglycerol diphosphatase activity",
"phospholipid biosynthetic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00672"
] | [
"cdh"
] | [
928
] | 1 | [
"EC"
] | [
"3.6.1.26"
] | [
"EC:3.6.1.26"
] | 1 | [
"2pof"
] | 1 | [
"PUB00008242"
] | [
"11016943"
] | [
"Regulation of the DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase by inositol and growth phase. Inhibition of DGPP phosphatase activity by CDP-diacylglyceron and activation of phosphatidylserine synthase activity by DGPP."
] | [
2000
] | 1 | [
"IPR003763"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Callosobruchus maculatus"
] | [
927,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | CDP-diacylglycerol pyrophosphatase, proteobacterial | CDP-diacylglycerol pyrophosphatase, proteobacterial | CDP-diacylglyc_Pase_proteobac | 9 |
IPR015994 | 15,994 | Phosphoenolpyruvate carboxykinase (ATP), conserved site | PEPCK_ATP_CS | Conserved_site | 12,537 | false | false | Phosphoenolpyruvate carboxykinase (ATP) ( ) (PEPCK) [ ] catalyses the formation of phosphoenolpyruvate by decarboxylation of oxaloacetate while hydrolysing ATP, a rate limiting step in gluconeogenesis (the biosynthesis of glucose). | [
"GO:0004612",
"GO:0005524",
"GO:0006094"
] | [
"phosphoenolpyruvate carboxykinase (ATP) activity",
"ATP binding",
"gluconeogenesis"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00532"
] | [
"PEPCK_ATP"
] | [
12537
] | 1 | [
"EC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"4.1.1.49",
"PWY-561",
"PWY-7117",
"PDOC00460"
] | [
"EC:4.1.1.49",
"METACYC:PWY-561",
"METACYC:PWY-7117",
"PROSITEDOC:PDOC00460"
] | 4 | [
"1aq2",
"1ayl",
"1ii2",
"1j3b",
"1k3c",
"1k3d",
"1oen",
"1os1",
"1xkv",
"1ygg",
"1ylh",
"1ytm",
"1yvy",
"2olq",
"2olr",
"2pc9",
"2pxz",
"2py7",
"6asi",
"6asm",
"6asn",
"6at2",
"6at3",
"6at4",
"6crt",
"6v2l",
"6v2n"
] | 27 | [
"PUB00002126",
"PUB00003355"
] | [
"1701430",
"8609605"
] | [
"Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae.",
"Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new str... | [
1990,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
39,
8574,
3796,
4,
124
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
15,
1,
1,
10,
1,
13
] | 6 | true | Conserved_site | Phosphoenolpyruvate carboxykinase (ATP), conserved site | Phosphoenolpyruvate carboxykinase (ATP), conserved site | PEPCK_ATP_CS | 1 |
IPR015995 | 15,995 | Microcystin LR degradation protein MlrC, N-terminal | MlrC_N | Domain | 6,750 | false | false | Proteins in this entry are involved in degradation of the cyanobacterial heptapeptide hepatotoxin microcystin LR, and are encoded in the mlr gene cluster [ ]. MlrC from Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273) is believed to mediate the last step of peptidolytic degradation of the tetrapeptide. It is ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07364"
] | [
"DUF1485"
] | [
6750
] | 1 | [] | [] | [] | 0 | [
"3iuu",
"7ylq"
] | 2 | [
"PUB00036077"
] | [
"11769251"
] | [
"Characterisation of a gene cluster involved in bacterial degradation of the cyanobacterial toxin microcystin LR."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
37,
6134,
369,
210
] | 4 | [] | [] | 0 | true | Domain | Microcystin LR degradation protein MlrC, N-terminal | Microcystin LR degradation protein MlrC, N-terminal | MlrC_N | 1 |
IPR015996 | 15,996 | Uncharacterised conserved protein UCP028451 | UCP028451 | Family | 6,640 | false | false | Members of this family are widely (though sparsely) distributed bacterial proteins, about 230 residues in length. All members have a motif RxxRDxRFxxx[DN]KxxY. The function of this protein family is unknown. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF028451"
] | [
"UCP028451"
] | [
6640
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR012808"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Fungi",
"metagenomes"
] | [
6501,
30,
109
] | 3 | [] | [] | 0 | true | Family | Uncharacterised conserved protein UCP028451 | Uncharacterised conserved protein UCP028451 | UCP028451 | 2 |
IPR016002 | 16,002 | Succinate dehydrogenase cytochrome b558 subunit, Firmicute | Succ_DH_cyt_b558_Firmicute | Family | 1,776 | false | false | This family contains succinate dehydrogenase (also known as succinate:quinone oxidoreductase, SQR) subunit C of Bacillus subtilis, designated cytochrome b-558, and related sequences that include a fumarate reductase subunit C. This family is only weakly similar to the main group of succinate dehydrogenase cytochrome b ... | [] | [] | [] | 0 | [
"PIRSF",
"CDD"
] | [
"PIRSF000170",
"cd03497"
] | [
"Succ_dh_cyt_b558",
"SQR_TypeB_1_TM"
] | [
1661,
1748
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015564",
"PUB00015643",
"PUB00015715",
"PUB00080558",
"PUB00080947",
"PUB00080948",
"PUB00080949",
"PUB00080952",
"PUB00080953"
] | [
"3086287",
"11004459",
"15078221",
"12788489",
"2120540",
"9799121",
"2176107",
"1324713",
"11803013"
] | [
"Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex.",
"Succinate: quinone oxidoreductases: new insights from X-ray crystal structures.",
"Complex II from a structural perspective.",
"Variation in proton donor/acceptor pathways in succinate:quinone oxi... | [
1986,
2000,
2004,
2003,
1990,
1998,
1990,
1992,
2002
] | 9 | [
"IPR011138"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"ecological metagenomes"
] | [
1774,
2
] | 2 | [] | [] | 0 | true | Family | Succinate dehydrogenase cytochrome b558 subunit, Firmicute | Succinate dehydrogenase cytochrome b558 subunit, Firmicute | Succ_DH_cyt_b558_Firmicute | 6 |
IPR016003 | 16,003 | Photosystem II extrinsic protein V, cytochrome c-550 precursor-like | PsbV_cyt_c550-like | Family | 872 | false | false | This entry represents a family of cytochrome c550 proteins mainly found in cyanobacteria and red algae. 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 resid... | [
"GO:0005506",
"GO:0020037",
"GO:0015979",
"GO:0022904",
"GO:0009523"
] | [
"iron ion binding",
"heme binding",
"photosynthesis",
"respiratory electron transport chain",
"photosystem II"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PIRSF"
] | [
"PIRSF005890"
] | [
"Phot_II_cyt_c550"
] | [
872
] | 1 | [] | [] | [] | 0 | [
"1e29",
"1f1c",
"1izl",
"1mz4",
"1s5l",
"1w5c",
"2axt",
"3a0b",
"3a0h",
"3kzi",
"3wu2",
"4fby",
"4il6",
"4ixq",
"4ixr",
"4lji",
"4pbu",
"4pj0",
"4rvy",
"4tnh",
"4tni",
"4tnj",
"4tnk",
"4ub6",
"4ub8",
"4v62",
"4v82",
"4yuu",
"5b5e",
"5b66",
"5e79",
"5e7c"... | 127 | [
"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 | [] | [
"IPR017851"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota"
] | [
414,
458
] | 2 | [] | [] | 0 | true | Family | Photosystem II extrinsic protein V, cytochrome c-550 precursor-like | Photosystem II extrinsic protein V, cytochrome c-550 precursor-like | PsbV_cyt_c550-like | 8 |
IPR016005 | 16,005 | Phosphomevalonate kinase Erg8 | Erg8 | Family | 2,390 | false | false | This entry includes phosphomevalonate kinase Erg8 from fungi and plants. Budding yeast Erg8 is involved in step 2 of the subpathway that synthesizes isopentenyl diphosphate from (R)-mevalonate [ , ]. Arabidopsis Erg8 (AT1G31910, also known as PMK) is involved in the mevalonic acid pathway [ ]. | [
"GO:0004631"
] | [
"phosphomevalonate kinase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF017288",
"TIGR01219"
] | [
"PMK_GHMP_euk",
"Pmev_kin_ERG8"
] | [
2352,
827
] | 2 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC"
] | [
"2.7.4.2",
"GenProp0047",
"GenProp1432",
"PWY-7391",
"PWY-922"
] | [
"EC:2.7.4.2",
"GP:GenProp0047",
"GP:GenProp1432",
"METACYC:PWY-7391",
"METACYC:PWY-922"
] | 5 | [] | 0 | [
"PUB00003676",
"PUB00078853",
"PUB00078854"
] | [
"1846667",
"200835",
"21655959"
] | [
"Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase.",
"Ertosterol biosynthesis in Saccharomyces cerevisiae: mutants deficient in the early steps of the pathway.",
"Peroxisomal localisation of the final steps of the mevalonic acid pathway in... | [
1991,
1977,
2011
] | 3 | [
"IPR035102"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2390
] | 1 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
1,
3,
1,
1,
16
] | 6 | true | Family | Phosphomevalonate kinase Erg8 | Phosphomevalonate kinase Erg8 | Erg8 | 8 |
IPR016008 | 16,008 | Amine dehydrogenase light chain | Amine_DH_Ltc | Family | 681 | false | false | This entry represents a group of bacterial amine dehydrogenase light chains. They include methylamine and arylamine dehydrogenase light chains, which form heterotetramers with their respective heavy chains, and catalyse the oxidative deamination of amines to their corresponding aldehydes. RCH2NH2 + H2O + acceptor = RCH... | [
"GO:0030058",
"GO:0009308"
] | [
"aliphatic amine dehydrogenase activity",
"amine metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000192"
] | [
"Amine_dh_beta"
] | [
681
] | 1 | [
"EC",
"METACYC"
] | [
"1.4.9.1",
"PWY-6967"
] | [
"EC:1.4.9.1",
"METACYC:PWY-6967"
] | 2 | [
"3c75",
"3l4m",
"3l4o",
"3orv",
"3pxs",
"3pxt",
"3pxw",
"3rlm",
"3rmz",
"3rn0",
"3rn1",
"3sjl",
"3sle",
"3svw",
"3sws",
"3sxt",
"4fa1",
"4fa4",
"4fa5",
"4fa9",
"4fan",
"4fav",
"4fb1",
"4k3i",
"4l1q",
"4l3g",
"4l3h",
"4o1q"
] | 28 | [] | [] | [] | [] | 0 | [] | [
"IPR004229"
] | 0 | 1 | 0 | [
"Bacteria",
"unclassified sequences"
] | [
670,
11
] | 2 | [] | [] | 0 | true | Family | Amine dehydrogenase light chain | Amine dehydrogenase light chain | Amine_DH_Ltc | 3 |
IPR016009 | 16,009 | tRNA methyltransferase TRMD/TRM10-type domain | tRNA_MeTrfase_TRMD/TRM10 | Domain | 26,157 | false | false | This domain is found in tRNA methyltransferases including tRNA (guanine-N(1)-)-methyltransferases (TRMD) and mitochondrial ribonuclease P protein 1. Proteins containing this domain also include tRNA (guanine(9)-N1)-methyltransferase (Trm10) from yeasts and Trmt10A from fruit flies. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01746"
] | [
"tRNA_m1G_MT"
] | [
26157
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.1.1.228",
"PWY-6829",
"PWY-7285",
"PWY-7286"
] | [
"EC:2.1.1.228",
"METACYC:PWY-6829",
"METACYC:PWY-7285",
"METACYC:PWY-7286"
] | 4 | [
"1oy5",
"1p9p",
"1uaj",
"1uak",
"1ual",
"1uam",
"3axz",
"3ief",
"3knu",
"3ky7",
"3quv",
"4h3y",
"4h3z",
"4ig6",
"4mcb",
"4mcc",
"4mcd",
"4ypw",
"4ypx",
"4ypy",
"4ypz",
"4yq0",
"4yq1",
"4yq2",
"4yq3",
"4yq4",
"4yq5",
"4yq6",
"4yq7",
"4yq8",
"4yq9",
"4yqa"... | 140 | [
"PUB00002394",
"PUB00058130"
] | [
"6337136",
"18984158"
] | [
"Purification and characterization of transfer RNA (guanine-1)methyltransferase from Escherichia coli.",
"RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme."
] | [
1983,
2008
] | 2 | [] | [
"IPR028564"
] | 0 | 1 | 0 | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"candidate division MSBL1 archaeon SCGC-AAA382N08",
"unclassified sequences"
] | [
25438,
2,
91,
1,
625
] | 5 | [
"Escherichia coli (strain K12)",
"Homo sapiens"
] | [
1,
1
] | 2 | true | Domain | tRNA methyltransferase TRMD/TRM10-type domain | tRNA methyltransferase TRMD/TRM10-type domain | tRNA_MeTrfase_TRMD/TRM10 | 6 |
IPR016013 | 16,013 | Binary exotoxin A, clostridial type | Binary_toxinA_clost-typ | Family | 113 | false | false | A large group of bacterial exotoxins are referred to as "A/B toxins", essentially because they are formed from two subunits. The "A" subunit possesses enzyme activity, and is transferred to the host cell following a conformational change in the membrane-bound transport "B" subunit [ ]. Clostridial species are one of th... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR01390"
] | [
"BINARYTOXINA"
] | [
113
] | 1 | [] | [] | [] | 0 | [
"1giq",
"1gir",
"1qs1",
"1qs2",
"2j3v",
"2j3x",
"2j3z",
"2wn4",
"2wn5",
"2wn6",
"2wn7",
"2wn8",
"3buz",
"4gy2",
"4h03",
"4h0t",
"4h0v",
"4h0x",
"4h0y",
"4tr5",
"5dzq",
"5gtt",
"5h03",
"5h04",
"5urp",
"5wtz",
"5wu0",
"6klo",
"6klw",
"6v1s",
"7vnj",
"7vnn"... | 37 | [
"PUB00006620",
"PUB00006643",
"PUB00006658"
] | [
"10802189",
"8225592",
"8645309"
] | [
"Production of actin-specific ADP-ribosyltransferase (binary toxin) by strains of Clostridium difficile.",
"Characterization of Clostridium perfringens iota-toxin genes and expression in Escherichia coli.",
"Characterization of component-I gene of botulinum C2 toxin and PCR detection of its gene in clostridial ... | [
2000,
1993,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Bacillota"
] | [
113
] | 1 | [] | [] | 0 | true | Family | Binary exotoxin A, clostridial type | Binary exotoxin A, clostridial type | Binary_toxinA_clost-typ | 8 |
IPR016014 | 16,014 | Clusterin, N-terminal | Clusterin_N | Domain | 1,790 | false | false | Clusterin is a vertebrate glycoprotein [ ], the exact function of which is not yet clear. Clusterin expression is complex, appearing as different forms in different cell compartments. One set of proteins is directed for secretion, and other clusterin species are expressed in the cytoplasm and nucleus. The secretory for... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00030"
] | [
"CLb"
] | [
1790
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-114608",
"R-BTA-166665",
"R-BTA-6803157",
"R-BTA-977606",
"R-CFA-114608",
"R-CFA-166665",
"R-CFA-977606",
"R-HSA-114608",
"R-HSA-166665",
"R-HSA-6803157",
"R-HSA-977606",
"R-MMU-114608",
"R-MMU-166665",
"R-MMU-6803157",
"R-MMU-977606",
"R-RNO-114608",
"R-RNO-6803157",
"R-RNO... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-166665",
"REACTOME:R-BTA-6803157",
"REACTOME:R-BTA-977606",
"REACTOME:R-CFA-114608",
"REACTOME:R-CFA-166665",
"REACTOME:R-CFA-977606",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-166665",
"REACTOME:R-HSA-6803157",
"REACTOME:R-HSA-977606",
"REACTOME:R-MMU-1... | 22 | [
"7zet",
"7zeu"
] | 2 | [
"PUB00002355",
"PUB00005386",
"PUB00010653"
] | [
"1491011",
"1585460",
"12551933"
] | [
"Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J).",
"Clusterin: the intriguing guises of a widely expressed glycoprotein.",
"Synthesis and functional analyses of nuclear clusterin, a cell death protein."
] | [
1992,
1992,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
1790
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
15,
9,
8
] | 4 | true | Domain | Clusterin, N-terminal | Clusterin, N-terminal | Clusterin_N | 8 |
IPR016015 | 16,015 | Clusterin, C-terminal | Clusterin_C | Domain | 1,778 | false | false | Clusterin is a vertebrate glycoprotein [ ], the exact function of which is not yet clear. Clusterin expression is complex, appearing as different forms in different cell compartments. One set of proteins is directed for secretion, and other clusterin species are expressed in the cytoplasm and nucleus. The secretory for... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00035"
] | [
"CLa"
] | [
1778
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-114608",
"R-BTA-166665",
"R-BTA-6803157",
"R-BTA-977606",
"R-CFA-114608",
"R-CFA-166665",
"R-CFA-977606",
"R-HSA-114608",
"R-HSA-166665",
"R-HSA-6803157",
"R-HSA-977606",
"R-MMU-114608",
"R-MMU-166665",
"R-MMU-6803157",
"R-MMU-977606",
"R-RNO-114608",
"R-RNO-6803157",
"R-RNO... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-166665",
"REACTOME:R-BTA-6803157",
"REACTOME:R-BTA-977606",
"REACTOME:R-CFA-114608",
"REACTOME:R-CFA-166665",
"REACTOME:R-CFA-977606",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-166665",
"REACTOME:R-HSA-6803157",
"REACTOME:R-HSA-977606",
"REACTOME:R-MMU-1... | 22 | [
"7zet",
"7zeu"
] | 2 | [
"PUB00002355",
"PUB00005386",
"PUB00010653"
] | [
"1491011",
"1585460",
"12551933"
] | [
"Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J).",
"Clusterin: the intriguing guises of a widely expressed glycoprotein.",
"Synthesis and functional analyses of nuclear clusterin, a cell death protein."
] | [
1992,
1992,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Bilateria",
"bird metagenome"
] | [
1777,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
11,
4,
9
] | 4 | true | Domain | Clusterin, C-terminal | Clusterin, C-terminal | Clusterin_C | 1 |
IPR016016 | 16,016 | Clusterin | Clusterin | Family | 249 | false | false | Clusterin (Clu), also known as apolipoprotein J, is a vertebrate glycoprotein [ ]. Clusterin expression is complex, appearing as different forms in different cell compartments. One set of proteins is directed for secretion, and other clusterin species are expressed in the cytoplasm and nucleus. The secretory form of th... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF002368"
] | [
"Clusterin"
] | [
249
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-114608",
"R-BTA-166665",
"R-BTA-6803157",
"R-BTA-977606",
"R-CFA-114608",
"R-CFA-166665",
"R-CFA-977606",
"R-HSA-114608",
"R-HSA-166665",
"R-HSA-6803157",
"R-HSA-977606",
"R-MMU-114608",
"R-MMU-166665",
"R-MMU-6803157",
"R-MMU-977606",
"R-RNO-114608",
"R-RNO-6803157",
"R-RNO... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-166665",
"REACTOME:R-BTA-6803157",
"REACTOME:R-BTA-977606",
"REACTOME:R-CFA-114608",
"REACTOME:R-CFA-166665",
"REACTOME:R-CFA-977606",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-166665",
"REACTOME:R-HSA-6803157",
"REACTOME:R-HSA-977606",
"REACTOME:R-MMU-1... | 22 | [
"7zet",
"7zeu"
] | 2 | [
"PUB00005386",
"PUB00010653",
"PUB00081946",
"PUB00081947",
"PUB00081948",
"PUB00081949",
"PUB00081950",
"PUB00081951",
"PUB00081952"
] | [
"1585460",
"12551933",
"21953454",
"22588555",
"21505792",
"19535339",
"22025968",
"11720815",
"27148688"
] | [
"Clusterin: the intriguing guises of a widely expressed glycoprotein.",
"Synthesis and functional analyses of nuclear clusterin, a cell death protein.",
"CRM1 protein-mediated regulation of nuclear clusterin (nCLU), an ionizing radiation-stimulated, Bax-dependent pro-death factor.",
"Clusterin inhibition usin... | [
1992,
2003,
2011,
2012,
2011,
2009,
2011,
2001,
2016
] | 9 | [
"IPR000753"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
249
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
1,
2,
5
] | 4 | true | Family | Clusterin | Clusterin | Clusterin | 2 |
IPR016017 | 16,017 | GDNF/GAS1 | GDNF/GAS1 | Domain | 8,013 | false | false | This cysteine rich domain is found in multiple copies in GNDF and GAS1 proteins. GDNF and neurturin (NTN) receptors are potent survival factors for sympathetic, sensory and central nervous system neurons [ , ]. GDNF and neurturin promote neuronal survival by signalling through similar multicomponent receptors that cons... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF02351",
"SM00907"
] | [
"GDNF",
"GDNF"
] | [
7865,
7697
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-GGA-5673001",
"R-GGA-8853659",
"R-HSA-419037",
"R-HSA-5632681",
"R-HSA-5635838",
"R-HSA-5673001",
"R-HSA-8853659",
"R-HSA-9830674",
"R-MMU-5632681",
"R-MMU-5635838",
"R-MMU-5673001",
"R-MMU-8853659",
"R-RNO-5673001",
"R-RNO-8853659"
] | [
"REACTOME:R-GGA-5673001",
"REACTOME:R-GGA-8853659",
"REACTOME:R-HSA-419037",
"REACTOME:R-HSA-5632681",
"REACTOME:R-HSA-5635838",
"REACTOME:R-HSA-5673001",
"REACTOME:R-HSA-8853659",
"REACTOME:R-HSA-9830674",
"REACTOME:R-MMU-5632681",
"REACTOME:R-MMU-5635838",
"REACTOME:R-MMU-5673001",
"REACTOME... | 14 | [
"1q8d",
"2gh0",
"2v5e",
"3fub",
"4ux8",
"5mr4",
"5mr5",
"5vz4",
"6gl7",
"6q2j",
"6q2n",
"6q2o",
"6q2r",
"6q2s",
"6wmw",
"7ab8",
"7aml",
"7rhq",
"8os6",
"9hyt"
] | 20 | [
"PUB00019606",
"PUB00019607",
"PUB00042818"
] | [
"9192898",
"9192899",
"16551639"
] | [
"A GPI-linked protein that interacts with Ret to form a candidate neurturin receptor.",
"Neurturin responsiveness requires a GPI-linked receptor and the Ret receptor tyrosine kinase.",
"Gas1 is related to the glial cell-derived neurotrophic factor family receptors alpha and regulates Ret signaling."
] | [
1997,
1997,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
8013
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
16,
9,
17,
20,
33
] | 7 | true | Domain | GDNF/GAS1 | GDNF/GAS1 | GDNF/GAS1 | 5 |
IPR016018 | 16,018 | Guanine nucleotide exchange factor SopE, N-terminal domain | SopE_N_dom | Domain | 912 | false | false | The type III secretion system of Gram-negative bacteria is used to transport virulence factors from the pathogen directly into the host cell [ ] and is only triggered when the bacterium comes into close contact with the host. Effector proteins secreted by the type III system do not possess a secretion signal, and are c... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF05364"
] | [
"SecIII_SopE_N"
] | [
912
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00003585",
"PUB00007792",
"PUB00007793"
] | [
"9618447",
"9482928",
"11316807"
] | [
"Type III protein secretion systems in bacterial pathogens of animals and plants.",
"A substrate of the centisome 63 type III protein secretion system of Salmonella typhimurium is encoded by a cryptic bacteriophage.",
"SopE acts as an Rab5-specific nucleotide exchange factor and recruits non-prenylated Rab5 on ... | [
1998,
1998,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Salmonella"
] | [
912
] | 1 | [] | [] | 0 | true | Domain | Guanine nucleotide exchange factor SopE, N-terminal domain | Guanine nucleotide exchange factor SopE, N-terminal domain | SopE_N_dom | 7 |
IPR016020 | 16,020 | Translation initiation factor 3, subunit 12, N-terminal, eukaryotic | Transl_init_fac_sub12_N_euk | Homologous_superfamily | 4,257 | false | false | This superfamily represents the N-terminal domain found in several eukaryotic translation initiation factor 3 subunit 12 (eIF-3 p25; also known as subunit K) proteins. Eukaryotic initiation factor 3 (eIF3) is a multi-subunit complex that is required for binding of mRNA to 40S ribosomal subunits, stabilisation of ternar... | [
"GO:0003743",
"GO:0043022",
"GO:0006446",
"GO:0005852"
] | [
"translation initiation factor activity",
"ribosome binding",
"regulation of translational initiation",
"eukaryotic translation initiation factor 3 complex"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"CATHGENE3D"
] | [
"G3DSA:1.25.40.250"
] | [
""
] | [
4257
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-CEL-156827",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-DDI-156827",
"R-DDI-72689",
"R-DDI-72695",
"R-DDI-72702",
"R-DME-156827",
"R-DME-72649",
"R-DME-72689",
"R-DME-72695",
"R-DME... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-72649",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72695",
"REACTOME:R-CEL-72702",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-72689",
"... | 39 | [
"1rz4",
"3j8b",
"3j8c",
"5a5t",
"6fec",
"6w2s",
"6w2t",
"6yam",
"6ybd",
"6zmw",
"6zon",
"6zp4",
"6zvj",
"7a09",
"7ase",
"7qp6",
"7qp7",
"8oz0",
"8pj1",
"8pj2",
"8pj3",
"8pj4",
"8pj5",
"8pj6",
"8ppl",
"8rg0",
"8xxn",
"9bln",
"9cpa"
] | 29 | [
"PUB00010248"
] | [
"11042177"
] | [
"Plant initiation factor 3 subunit composition resembles mammalian initiation factor 3 and has a novel subunit."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
4256,
1
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
2,
1,
9,
3,
1,
1,
7,
13
] | 10 | true | Homologous_superfamily | Translation initiation factor 3, subunit 12, N-terminal, eukaryotic | Translation initiation factor 3, subunit 12, N-terminal, eukaryotic | Transl_init_fac_sub12_N_euk | 2 |
IPR016024 | 16,024 | Armadillo-type fold | ARM-type_fold | Homologous_superfamily | 1,264,855 | false | false | This entry represents a structural domain with an armadillo (ARM)-like fold, consisting of a multi-helical fold comprised of two curved layers of α-helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis [ ]. These superhelical structures pre... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF48371"
] | [
""
] | [
1264855
] | 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-109704",
"R-BTA-112399",
"R-BTA-114604",
"R-BTA-1169091",
"R-BTA-1222556",
"R-BTA-1234176",
"R-BTA-1236978",
"R-BTA-1250342",
"R-BTA-1257604",
"R-BTA-140342",
"R-BTA-141444",
"R-BTA-1433557",
"R-BTA-156827",
"R-BTA-1660499",
"R-BTA-174084",
"R-BTA-174154",
"R-BTA-174178",
"R... | [
"REACTOME:R-BTA-109704",
"REACTOME:R-BTA-112399",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-1236978",
"REACTOME:R-BTA-1250342",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-140342",
"REACTOME:R-BTA-141444",
"REACTOME:R-B... | 2,033 | [
"1b3u",
"1b89",
"1bk5",
"1bk6",
"1bpo",
"1e7u",
"1e7v",
"1e8w",
"1e8x",
"1e8y",
"1e8z",
"1e90",
"1ee4",
"1ee5",
"1ejl",
"1ejy",
"1f59",
"1g3j",
"1gcj",
"1gw6",
"1h19",
"1h2t",
"1h2u",
"1h2v",
"1h6k",
"1he8",
"1ho8",
"1hs6",
"1hu3",
"1i7w",
"1i7x",
"1ial"... | 2,523 | [
"PUB00015442",
"PUB00015443"
] | [
"10361086",
"11551174"
] | [
"Topological characteristics of helical repeat proteins.",
"Protein repeats: structures, functions, and evolution."
] | [
1999,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3885,
90420,
1167098,
1258,
2194
] | 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",... | [
1942,
287,
1918,
559,
1,
1852,
1170,
143,
1247,
1552,
110,
131,
4509
] | 13 | true | Homologous_superfamily | Armadillo-type fold | Armadillo-type fold | ARM-type_fold | 8 |
IPR016025 | 16,025 | Clathrin heavy chain, N-terminal | Clathrin_H-chain_N | Homologous_superfamily | 8,984 | false | false | Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are ... | [
"GO:0005198",
"GO:0006886",
"GO:0016192",
"GO:0030130",
"GO:0030132"
] | [
"structural molecule activity",
"intracellular protein transport",
"vesicle-mediated transport",
"clathrin coat of trans-Golgi network vesicle",
"clathrin coat of coated pit"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component",
"cellular_component"
] | 5 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.130.10.110",
"SSF50989"
] | [
"",
""
] | [
8827,
8910
] | 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-177504",
"R-BTA-190873",
"R-BTA-196025",
"R-BTA-2132295",
"R-BTA-432720",
"R-BTA-432722",
"R-BTA-437239",
"R-BTA-5099900",
"R-BTA-5140745",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-8866427",
"R-BTA-8964038",
"R-BTA-9013420",
"R-BTA-9013424",
"R-CEL-190873",
"R-CEL-196025",
"... | [
"REACTOME:R-BTA-177504",
"REACTOME:R-BTA-190873",
"REACTOME:R-BTA-196025",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-432722",
"REACTOME:R-BTA-437239",
"REACTOME:R-BTA-5099900",
"REACTOME:R-BTA-5140745",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BT... | 114 | [
"1bpo",
"1c9i",
"1c9l",
"1utc",
"1xi4",
"1xi5",
"2xzg",
"3gc3",
"3gd1",
"3iyv",
"4g55",
"5m5r",
"5m5s",
"5m5t",
"5m5u",
"5m5v",
"5m61",
"5ods",
"6e4l",
"6qnn",
"6qnp",
"6sct",
"6wcj",
"6yai",
"7bn1",
"7bn2",
"7om8",
"7zx4",
"9c0y",
"9c0z",
"9ex5",
"9exf"... | 36 | [
"PUB00000964",
"PUB00035753",
"PUB00035765",
"PUB00035769",
"PUB00035906",
"PUB00035907",
"PUB00035908",
"PUB00035909"
] | [
"9827808",
"17449236",
"11598180",
"15261670",
"15752139",
"16806884",
"16734666",
"16699812"
] | [
"Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker.",
"Do different endocytic pathways make different synaptic vesicles?",
"Adaptins: the final recount.",
"COP and clathrin-coated vesicle budding: different pathways, common approaches.",
"New faces of the familiar c... | [
1998,
2007,
2001,
2004,
2005,
2006,
2006,
2006
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Cuniculiplasma divulgatum",
"Eukaryota"
] | [
2,
2,
8980
] | 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... | [
6,
1,
9,
2,
24,
6,
1,
6,
7,
1,
1,
142
] | 12 | true | Homologous_superfamily | Clathrin heavy chain, N-terminal | Clathrin heavy chain, N-terminal | Clathrin_H-chain_N | 8 |
IPR016029 | 16,029 | Inner layer core protein VP3, Reovirus | Inner_layer_core_VP3_Reovir | Homologous_superfamily | 963 | false | false | This entry represents the inner layer core protein VP3 from various Reoviruses, including Orbiviruses and Phytoreviruses, Reoviruses have dsRNA genomes of 10-12 linear segments [ ]. VP3 proteins and their homologues are found in the Orbiviruses Epizootic hemorrhagic disease virus and Bluetongue virus (BTV) [ ], while t... | [
"GO:0005198"
] | [
"structural molecule activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF56831"
] | [
""
] | [
963
] | 1 | [] | [] | [] | 0 | [
"1uf2",
"2btv",
"6pns",
"6po2",
"8w12",
"8w19",
"8w1c",
"8w1i",
"8w1o",
"8w1r",
"8w1s"
] | 11 | [
"PUB00003147",
"PUB00004287",
"PUB00031754"
] | [
"1328474",
"9774103",
"14527391"
] | [
"Comparison of the major structural core proteins of tick-borne and Culicoides-borne orbiviruses.",
"The atomic structure of the bluetongue virus core.",
"The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins."
] | [
1992,
1998,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria",
"Neoptera",
"Riboviria"
] | [
7,
10,
946
] | 3 | [] | [] | 0 | true | Homologous_superfamily | Inner layer core protein VP3, Reovirus | Inner layer core protein VP3, Reovirus | Inner_layer_core_VP3_Reovir | 8 |
IPR016030 | 16,030 | Cobalamin adenosyltransferase-like | CblAdoTrfase-like | Domain | 22,239 | false | false | ATP:cob(I)alamin (or ATP:corrinoid) adenosyltransferases ( ), catalyse the conversion of cobalamin (vitamin B12) into its coenzyme form, adenosylcobalamin (AdoCbl)or coenzyme B12 [ ]. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond. AdoCbl is required as a cofactor fo... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01923"
] | [
"Cob_adeno_trans"
] | [
22239
] | 1 | [
"EC",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.5.1",
"GenProp0269",
"GenProp0292",
"R-HSA-3359471",
"R-HSA-9759218",
"R-MMU-9759218"
] | [
"EC:2.5.1",
"GP:GenProp0269",
"GP:GenProp0292",
"REACTOME:R-HSA-3359471",
"REACTOME:R-HSA-9759218",
"REACTOME:R-MMU-9759218"
] | 6 | [
"1nog",
"1rty",
"1woz",
"1wvt",
"1wy1",
"2ah6",
"2g2d",
"2idx",
"2nt8",
"2r6t",
"2r6x",
"2zhy",
"2zhz",
"3ci1",
"3ci3",
"3ci4",
"3gah",
"3gai",
"3gaj",
"3ke4",
"3ke5",
"4nwp",
"4nwq",
"5cy5",
"5im6",
"5vl4",
"6c9i",
"6c9k",
"6d5k",
"6d5x",
"6nht",
"6nhv"... | 52 | [
"PUB00006386",
"PUB00013593",
"PUB00015064",
"PUB00035323",
"PUB00035324",
"PUB00035325",
"PUB00035391"
] | [
"9311132",
"11160088",
"15317775",
"16672609",
"15516577",
"16636051",
"15704011"
] | [
"Glycerol conversion to 1,3-propanediol by Clostridium pasteurianum: cloning and expression of the gene encoding 1,3-propanediol dehydrogenase.",
"Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene.",
"The eutT gene of Salmonel... | [
1997,
2001,
2004,
2006,
2004,
2006,
2004
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
647,
19097,
2032,
10,
453
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
1,
7,
3,
5
] | 6 | true | Domain | Cobalamin adenosyltransferase-like | Cobalamin adenosyltransferase-like | CblAdoTrfase-like | 5 |
IPR016032 | 16,032 | Signal transduction response regulator, C-terminal effector | Sig_transdc_resp-reg_C-effctor | Homologous_superfamily | 634,971 | false | false | This entry represents a structural domain usually found at the C-terminal of bipartite response regulators. These proteins are known to bind to DNA and RNA polymerases, and their N-terminal receiver domain belongs to the CheY family. The C-terminal effector domain consists of a 3-helical bundle in an up-an-down arrange... | [
"GO:0003677",
"GO:0006355"
] | [
"DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF46894"
] | [
""
] | [
634971
] | 1 | [] | [] | [] | 0 | [
"1a04",
"1fc3",
"1fse",
"1gxp",
"1gxq",
"1h0m",
"1je8",
"1l3l",
"1lq1",
"1odd",
"1opc",
"1p2f",
"1p4w",
"1qqi",
"1rnl",
"1x3u",
"1zg1",
"1zg5",
"1zlj",
"1zlk",
"2d1v",
"2fez",
"2ff4",
"2hqn",
"2hqr",
"2hwv",
"2jpb",
"2jpc",
"2jzy",
"2k4j",
"2krf",
"2m1b"... | 170 | [
"PUB00010651",
"PUB00011096",
"PUB00013308",
"PUB00014650",
"PUB00016941",
"PUB00016947",
"PUB00016950",
"PUB00022327",
"PUB00022388",
"PUB00036081",
"PUB00042804",
"PUB00042805",
"PUB00042806",
"PUB00042807"
] | [
"12372152",
"10966457",
"12015152",
"11069648",
"11243786",
"12740396",
"12198141",
"8989318",
"12837793",
"9521685",
"16176121",
"18076326",
"11934609",
"11489844"
] | [
"Histidine protein kinases: key signal transducers outside the animal kingdom.",
"Two-component signal transduction.",
"Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator.",
"The trans-activation domain of the sporulation response regulator Spo0A revealed by X-ray cr... | [
2002,
2000,
2002,
2000,
2001,
2003,
2002,
1997,
2003,
1998,
2005,
2007,
2002,
2001
] | 14 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid R64",
"Viruses",
"unclassified sequences"
] | [
247,
627873,
1009,
1,
274,
5567
] | 6 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
35
] | 2 | true | Homologous_superfamily | Signal transduction response regulator, C-terminal effector | Signal transduction response regulator, C-terminal effector | Sig_transdc_resp-reg_C-effctor | 8 |
IPR016033 | 16,033 | DNA polymerase II large subunit DP2, N-terminal | PolC_DP2_N | Domain | 869 | false | false | This entry represents the N-terminal domain of the DNA polymerase II large subunit. This domain adopts an α/β structure. DP2 is the large subunit of a two-subunit novel archaebacterial replicative DNA polymerase first characterised for Pyrococcus furiosus. The structure of DP2 appears to be organised as a ~950 residue ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03833"
] | [
"PolC_DP2_N"
] | [
869
] | 1 | [
"EC",
"EC"
] | [
"2.7.7.7",
"3.1.11.1"
] | [
"EC:2.7.7.7",
"EC:3.1.11.1"
] | 2 | [
"3o59",
"5ijl",
"6hms",
"6knb",
"6knc",
"6t8h",
"8ppt",
"8ppu",
"8ppv",
"9f29",
"9f2a"
] | 11 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Geodia barretti",
"ecological metagenomes",
"uncultured marine bacterium MedDCM-OCT-S05-C222"
] | [
824,
1,
43,
1
] | 4 | [] | [] | 0 | true | Domain | DNA polymerase II large subunit DP2, N-terminal | DNA polymerase II large subunit DP2, N-terminal | PolC_DP2_N | 6 |
IPR016035 | 16,035 | Acyl transferase/acyl hydrolase/lysophospholipase | Acyl_Trfase/lysoPLipase | Homologous_superfamily | 238,521 | false | false | This superfamily represents a structural domain with a 3-layer α/β/α topology. This domain can be found in acyl transferases such as bacterial malonyl-CoA ACP transacylase (FabD) and the homologous domain from eukaryotic fatty acid synthase [ ]. This domain is also found in lysophospholipases such as cytosolic phosphol... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF52151"
] | [
""
] | [
238521
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.3.1",
"R-BTA-111995",
"R-BTA-1482788",
"R-BTA-1482798",
"R-BTA-1482801",
"R-BTA-1482839",
"R-BTA-1482922",
"R-BTA-1482925",
"R-BTA-1483115",
"R-BTA-1483166",
"R-BTA-2142753",
"R-BTA-418592",
"R-BTA-432142",
"R-BTA-6811436",
"R-CEL-1482883",
"R-CEL-163560",
"R-CEL-381426",
"R-CEL... | [
"EC:2.3.1",
"REACTOME:R-BTA-111995",
"REACTOME:R-BTA-1482788",
"REACTOME:R-BTA-1482798",
"REACTOME:R-BTA-1482801",
"REACTOME:R-BTA-1482839",
"REACTOME:R-BTA-1482922",
"REACTOME:R-BTA-1482925",
"REACTOME:R-BTA-1483115",
"REACTOME:R-BTA-1483166",
"REACTOME:R-BTA-2142753",
"REACTOME:R-BTA-418592"... | 165 | [
"1cjy",
"1mla",
"1nm2",
"1oxw",
"2c2n",
"2cdh",
"2cf2",
"2cuy",
"2g1h",
"2g2o",
"2g2y",
"2g2z",
"2h1y",
"2hg4",
"2jfd",
"2jfk",
"2pff",
"2qc3",
"2qj3",
"2qo3",
"2uv8",
"2vkz",
"2vz8",
"2vz9",
"3ezo",
"3g87",
"3h0p",
"3hhd",
"3hjv",
"3hmj",
"3im8",
"3im9"... | 240 | [
"PUB00021333",
"PUB00029120",
"PUB00029641"
] | [
"10319815",
"12575934",
"12779324"
] | [
"Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism.",
"Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase.",
"The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrol... | [
1999,
2003,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
259,
136074,
100006,
232,
1950
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
62,
21,
80,
17,
4,
62,
53,
21,
70,
68,
11,
13,
135
] | 13 | true | Homologous_superfamily | Acyl transferase/acyl hydrolase/lysophospholipase | Acyl transferase/acyl hydrolase/lysophospholipase | Acyl_Trfase/lysoPLipase | 7 |
IPR016036 | 16,036 | Malonyl-CoA ACP transacylase, ACP-binding | Malonyl_transacylase_ACP-bd | Homologous_superfamily | 95,201 | false | false | This entry represents a structural domain with an α/β sandwich topology with anti-parallel β-sheets: (β/α/β)2. This domain is believed to be the ACP (acyl carrier protein) binding region of the malonyl-CoA ACP transacylase enzyme (FabD) found in bacteria, or in the homologous domain from eukaryotic fatty acid synthase ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF55048"
] | [
""
] | [
95201
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"... | [
"2.3.1",
"2.3.1.-",
"PWY-3602",
"PWY-361",
"PWY-4801",
"PWY-4922",
"PWY-5048",
"PWY-5139",
"PWY-5268",
"PWY-5284",
"PWY-5292",
"PWY-5307",
"PWY-5313",
"PWY-5317",
"PWY-5318",
"PWY-5353",
"PWY-5400",
"PWY-5473",
"PWY-5475",
"PWY-5477",
"PWY-5660",
"PWY-5679",
"PWY-5710",
... | [
"EC:2.3.1",
"EC:2.3.1.-",
"METACYC:PWY-3602",
"METACYC:PWY-361",
"METACYC:PWY-4801",
"METACYC:PWY-4922",
"METACYC:PWY-5048",
"METACYC:PWY-5139",
"METACYC:PWY-5268",
"METACYC:PWY-5284",
"METACYC:PWY-5292",
"METACYC:PWY-5307",
"METACYC:PWY-5313",
"METACYC:PWY-5317",
"METACYC:PWY-5318",
"... | 236 | [
"1mla",
"1nm2",
"2c2n",
"2cdh",
"2cf2",
"2cuy",
"2g1h",
"2g2o",
"2g2y",
"2g2z",
"2h1y",
"2hg4",
"2jfd",
"2jfk",
"2qc3",
"2qj3",
"2qo3",
"2vz8",
"2vz9",
"3ezo",
"3g87",
"3h0p",
"3hhd",
"3hjv",
"3im8",
"3im9",
"3k89",
"3ptw",
"3qat",
"3r97",
"3rgi",
"3sbm"... | 165 | [
"PUB00029120"
] | [
"12575934"
] | [
"Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
27,
65219,
29388,
567
] | 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",... | [
6,
3,
10,
7,
1,
3,
6,
9,
3,
3,
1,
3
] | 12 | true | Homologous_superfamily | Malonyl-CoA ACP transacylase, ACP-binding | Malonyl-CoA ACP transacylase, ACP-binding | Malonyl_transacylase_ACP-bd | 1 |
IPR016037 | 16,037 | 3-dehydroquinate synthase AroB | DHQ_synth_AroB | Family | 26,554 | false | false | The 3-dehydroquinate synthase (DHQS) domain can exist in isolation or as a domain in the pentafunctional AROM polypeptide ( ) [ ]. 3-dehydroquinate synthase catalyses the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate [ ]. This reaction is part of the shikimate path... | [
"GO:0003856",
"GO:0009073",
"GO:0005737"
] | [
"3-dehydroquinate synthase activity",
"aromatic amino acid family biosynthetic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00110",
"TIGR01357"
] | [
"DHQ_synthase",
"aroB"
] | [
21375,
26467
] | 2 | [
"EC",
"GP",
"METACYC",
"REACTOME"
] | [
"4.2.3.4",
"GenProp0001",
"PWY-6164",
"R-MTU-964903"
] | [
"EC:4.2.3.4",
"GP:GenProp0001",
"METACYC:PWY-6164",
"REACTOME:R-MTU-964903"
] | 4 | [
"1dqs",
"1nr5",
"1nrx",
"1nua",
"1nva",
"1nvb",
"1nvd",
"1nve",
"1nvf",
"1sg6",
"1ujn",
"1xag",
"1xah",
"1xai",
"1xaj",
"1xal",
"3clh",
"3okf",
"3qbd",
"3qbe",
"3zok",
"5eks",
"5hvn",
"6c5c",
"6hqv",
"6lk2",
"6lla",
"7u5s",
"7u5t",
"7u5u"
] | 30 | [
"PUB00001459",
"PUB00003775"
] | [
"7556173",
"9613570"
] | [
"The molecular biology of multidomain proteins. Selected examples.",
"Cloning and characterisation of the Neisseria gonorrhoeae aroB gene."
] | [
1995,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
123,
23403,
2609,
419
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
4,
1,
1,
2,
1,
1,
17
] | 7 | true | Family | 3-dehydroquinate synthase AroB | 3-dehydroquinate synthase AroB | DHQ_synth_AroB | 7 |
IPR016039 | 16,039 | Thiolase-like | Thiolase-like | Homologous_superfamily | 438,639 | false | false | This superfamily represents a structural domain with a thiolase-like 3-layer α/β/α topology. This domain usually occurs in two similar copies that are related by a pseudo-dyad, and which arose through duplication. The proteins in this entry can be split into two groups: those related to thiolase, and those related to c... | [
"GO:0016746"
] | [
"acyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.40.47.10",
"SSF53901"
] | [
"",
""
] | [
433552,
436982
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.3.1",
"R-BTA-1482798",
"R-BTA-70895",
"R-BTA-77108",
"R-BTA-77111",
"R-BTA-77285",
"R-BTA-77289",
"R-BTA-77305",
"R-BTA-77310",
"R-BTA-77346",
"R-BTA-77348",
"R-BTA-77350",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-1482798",
"R-CEL-191273",
"R-CEL-70895",
"R-CEL-77108",
"R-CEL-... | [
"EC:2.3.1",
"REACTOME:R-BTA-1482798",
"REACTOME:R-BTA-70895",
"REACTOME:R-BTA-77108",
"REACTOME:R-BTA-77111",
"REACTOME:R-BTA-77285",
"REACTOME:R-BTA-77289",
"REACTOME:R-BTA-77305",
"REACTOME:R-BTA-77310",
"REACTOME:R-BTA-77346",
"REACTOME:R-BTA-77348",
"REACTOME:R-BTA-77350",
"REACTOME:R-BT... | 129 | [
"1afw",
"1b3n",
"1bi5",
"1bq6",
"1cgk",
"1cgz",
"1chw",
"1cml",
"1d6f",
"1d6h",
"1d6i",
"1dd8",
"1dlu",
"1dlv",
"1dm3",
"1e5m",
"1ebl",
"1ee0",
"1ek4",
"1f91",
"1fj4",
"1fj8",
"1g5x",
"1h4f",
"1hn9",
"1hnd",
"1hnh",
"1hnj",
"1hnk",
"1hzp",
"1i86",
"1i88"... | 836 | [
"PUB00014381",
"PUB00016103",
"PUB00019762",
"PUB00020434",
"PUB00025721",
"PUB00031426",
"PUB00031547",
"PUB00031633",
"PUB00032244",
"PUB00036842"
] | [
"11732902",
"15292254",
"9482715",
"9402066",
"11243824",
"15286723",
"15286722",
"15380179",
"15229654",
"16441657"
] | [
"Structure-guided programming of polyketide chain-length determination in chalcone synthase.",
"Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase: crystal structure and mechanism.",
"Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of... | [
2001,
2004,
1998,
1997,
2001,
2004,
2004,
2004,
2004,
2006
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
4800,
318484,
109798,
1,
13,
5543
] | 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",... | [
186,
12,
26,
24,
8,
66,
43,
17,
210,
67,
5,
4,
357
] | 13 | true | Homologous_superfamily | Thiolase-like | Thiolase-like | Thiolase-like | 5 |
IPR016040 | 16,040 | NAD(P)-binding domain | NAD(P)-bd_dom | Domain | 190,002 | false | false | This entry represents NAD- and NADP-binding domains with a core Rossmann-type fold, which consists of 3-layers α/β/α, where the six β-strands are parallel in the order 321456. Many different enzymes contain an NAD/NADP-binding domain, including: C-terminal domain of alcohol dehydrogenases [ ] Tyrosine-dependent oxidore... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF13460",
"PF16363"
] | [
"NAD_binding_10",
"GDP_Man_Dehyd"
] | [
101266,
88737
] | 2 | [
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1260",
"GenProp1355",
"GenProp1724",
"R-BTA-189483",
"R-BTA-9707564",
"R-CEL-6787639",
"R-DDI-6787639",
"R-DDI-70370",
"R-DME-6787639",
"R-DME-70370",
"R-DRE-173599",
"R-DRE-1971475",
"R-HSA-173599",
"R-HSA-189483",
"R-HSA-1971475",
"R-HSA-5609977",
"R-HSA-6787639",
"R-HSA-... | [
"GP:GenProp1260",
"GP:GenProp1355",
"GP:GenProp1724",
"REACTOME:R-BTA-189483",
"REACTOME:R-BTA-9707564",
"REACTOME:R-CEL-6787639",
"REACTOME:R-DDI-6787639",
"REACTOME:R-DDI-70370",
"REACTOME:R-DME-6787639",
"REACTOME:R-DME-70370",
"REACTOME:R-DRE-173599",
"REACTOME:R-DRE-1971475",
"REACTOME:... | 32 | [
"1bxk",
"1db3",
"1ek5",
"1ek6",
"1g1a",
"1hdo",
"1he2",
"1he3",
"1he4",
"1he5",
"1hzj",
"1i3k",
"1i3l",
"1i3m",
"1i3n",
"1kep",
"1ker",
"1ket",
"1keu",
"1kew",
"1n7g",
"1n7h",
"1oc2",
"1orr",
"1r66",
"1r6d",
"1rkx",
"1rpn",
"1t2a",
"1wvg",
"1xq6",
"1ybm"... | 117 | [
"PUB00000446",
"PUB00015984",
"PUB00023536",
"PUB00025375",
"PUB00025866",
"PUB00025981",
"PUB00029889",
"PUB00031657",
"PUB00031693",
"PUB00032388",
"PUB00032846",
"PUB00041823"
] | [
"9174344",
"9917402",
"10448043",
"8591026",
"11276087",
"11301020",
"14595395",
"15449945",
"15518536",
"15642260",
"8114093",
"17222187"
] | [
"Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli.",
"A detailed structural description of Escherichia coli succinyl-CoA synthetase.",
"Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.",
"T... | [
1997,
1999,
1999,
1995,
2001,
2001,
2003,
2004,
2004,
2005,
1994,
2007
] | 12 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2238,
135214,
49724,
140,
2686
] | 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",... | [
144,
8,
8,
8,
5,
18,
16,
3,
94,
35,
2,
4,
220
] | 13 | true | Domain | NAD(P)-binding domain | NAD(P)-binding domain | NAD(P)-bd_dom | 2 |
IPR016041 | 16,041 | CO dehydrogenase/acetyl-CoA synthase delta subunit, TIM barrel | Ac-CoA_synth_d_su_TIM-brl | Domain | 1,900 | false | false | This entry represents a conserved region predicted to form a TIM α/β barrel, and is found in the delta subunit of a number of CO dehydrogenase/acetyl-CoA synthase enzymes. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03599"
] | [
"CdhD"
] | [
1900
] | 1 | [] | [] | [] | 0 | [
"2h9a",
"2ycl",
"4c1n",
"4djd",
"4dje",
"4djf",
"9fzy",
"9fzz",
"9g00"
] | 9 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
559,
1116,
3,
222
] | 4 | [] | [] | 0 | true | Domain | CO dehydrogenase/acetyl-CoA synthase delta subunit, TIM barrel | CO dehydrogenase/acetyl-CoA synthase delta subunit, TIM barrel | Ac-CoA_synth_d_su_TIM-brl | 7 |
IPR016045 | 16,045 | Tyrosine-protein kinase, non-receptor, TYK2, N-terminal | Tyr_kinase_non-rcpt_TYK2_N | Domain | 908 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR01827"
] | [
"YKINASETYK2"
] | [
908
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-HSA-1059683",
"R-HSA-110056",
"R-HSA-112411",
"R-HSA-449836",
"R-HSA-6783783",
"R-HSA-6785807",
"R-HSA-6788467",
"R-HSA-8854691",
"R-HSA-8984722",
"R-HSA-9020591",
"R-HSA-9020933",
"R-HSA-9020956",
"R-HSA-909733",
"R-HSA-912694",
"R-HSA-9674555",
"R-HSA-9679191",
"R-HSA-9705462",
... | [
"REACTOME:R-HSA-1059683",
"REACTOME:R-HSA-110056",
"REACTOME:R-HSA-112411",
"REACTOME:R-HSA-449836",
"REACTOME:R-HSA-6783783",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6788467",
"REACTOME:R-HSA-8854691",
"REACTOME:R-HSA-8984722",
"REACTOME:R-HSA-9020591",
"REACTOME:R-HSA-9020933",
"REACTOME:R... | 35 | [
"4po6"
] | 1 | [
"PUB00005115",
"PUB00013872",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412"
] | [
"3291115",
"2156206",
"12368087",
"12471243",
"15078142",
"15320712",
"19275641",
"16700535",
"15845350"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Identification and chromosomal mapping of new human tyrosine kinase genes.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput st... | [
1988,
1990,
2002,
2002,
2004,
2004,
2009,
2006,
2005
] | 9 | [] | [] | 0 | 0 | null | [
"Euteleostomi"
] | [
908
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
11,
6,
5
] | 4 | true | Domain | Tyrosine-protein kinase, non-receptor, TYK2, N-terminal | Tyrosine-protein kinase, non-receptor, TYK2, N-terminal | Tyr_kinase_non-rcpt_TYK2_N | 6 |
IPR016047 | 16,047 | M23ase, beta-sheet core domain | M23ase_b-sheet_dom | Domain | 123,669 | false | false | This entry represents the duplicated hybrid domain found in the M23 peptidase family in bacteria, which includes various peptidoglycan hydrolases with diverse specificities. Many members, such as Lysostaphin , are Gly-Gly endopeptidases, while others like Protease LasA have broader substrate specificity. The duplicated... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01551"
] | [
"Peptidase_M23"
] | [
123669
] | 1 | [] | [] | [] | 0 | [
"1qwy",
"2b0p",
"2b13",
"2b44",
"2gu1",
"2hsi",
"3it5",
"3it7",
"3nyy",
"3slu",
"3tuf",
"3uz0",
"4bh5",
"4lxc",
"4qp5",
"4qpb",
"4rny",
"4rnz",
"4zyb",
"5b0h",
"5gt1",
"5j1k",
"5j1l",
"5j1m",
"5kqb",
"5kqc",
"5kvp",
"5nmy",
"6ik4",
"6jmx",
"6jmy",
"6jmz"... | 67 | [
"PUB00014245",
"PUB00075514",
"PUB00075515",
"PUB00160315",
"PUB00160316"
] | [
"9705652",
"23352894",
"24478397",
"34281200",
"36386627"
] | [
"A promiscuous binding surface: crystal structure of the IIA domain of the glucose-specific permease from Mycoplasma capricolum.",
"Leukocyte cell-derived chemotaxin 2 is a zinc-binding protein.",
"LECT2 functions as a hepatokine that links obesity to skeletal muscle insulin resistance.",
"Structural Characte... | [
1998,
2013,
2014,
2021,
2022
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
206,
119925,
824,
783,
1931
] | 5 | [
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Homo sapiens"
] | [
1,
4,
1
] | 3 | true | Domain | M23ase, beta-sheet core domain | M23ase, beta-sheet core domain | M23ase_b-sheet_dom | 7 |
IPR016049 | 16,049 | RNA polymerase Rpc34-like | RNA_pol_Rpc34-like | Family | 4,748 | false | false | The entry represents a subunit specific of RNA Pol III, the tRNA specific polymerase. The C34 subunit of Saccharomyces cerevisiae RNA Pol III is part of a subcomplex of three subunits which have no counterpart in the other two nuclear RNA polymerases. This subunit interacts with TFIIIB70 and therefore participates in P... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR12780"
] | [
""
] | [
4748
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-76061",
"R-DDI-76066",
"R-DME-76061",
"R-DME-76066",
"R-HSA-1834949",
"R-HSA-73780",
"R-HSA-73980",
"R-HSA-749476",
"R-HSA-76061",
"R-HSA-76066",
"R-HSA-76071",
"R-MMU-76061",
"R-MMU-76066",
"R-MMU-76071",
"R-SCE-76066",
"R-SPO-76061",
"R-SPO-76066"
] | [
"REACTOME:R-DDI-76061",
"REACTOME:R-DDI-76066",
"REACTOME:R-DME-76061",
"REACTOME:R-DME-76066",
"REACTOME:R-HSA-1834949",
"REACTOME:R-HSA-73780",
"REACTOME:R-HSA-73980",
"REACTOME:R-HSA-749476",
"REACTOME:R-HSA-76061",
"REACTOME:R-HSA-76066",
"REACTOME:R-HSA-76071",
"REACTOME:R-MMU-76061",
"... | 17 | [
"2dk5",
"2yu3",
"5fj8",
"5fj9",
"5fja",
"6cnb",
"6cnc",
"6cnd",
"6cnf",
"6eu0",
"6eu1",
"6eu2",
"6eu3",
"6f40",
"6f41",
"6f42",
"6f44",
"6tut",
"7a6h",
"7ae1",
"7ae3",
"7aea",
"7ast",
"7d58",
"7d59",
"7dn3",
"7du2",
"7fji",
"7fjj",
"7z0h",
"7z1l",
"7z1m"... | 56 | [
"PUB00010211"
] | [
"9312031"
] | [
"Dual role of the C34 subunit of RNA polymerase III in transcription initiation."
] | [
1997
] | 1 | [] | [
"IPR007832"
] | 0 | 1 | 0 | [
"Eukaryota",
"Thermoproteati"
] | [
4732,
16
] | 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... | [
5,
1,
2,
2,
12,
3,
1,
4,
5,
1,
1,
7
] | 12 | true | Family | RNA polymerase Rpc34-like | RNA polymerase Rpc34-like | RNA_pol_Rpc34-like | 1 |
IPR016050 | 16,050 | Proteasome beta-type subunit, conserved site | Proteasome_bsu_CS | Conserved_site | 32,211 | false | false | The proteasome (or macropain) ( ) [ , , , , ] is a multicatalytic proteinase complex in eukaryotes and archaea, and in some bacteria, that seems to be involved in an ATP/ubiquitin-dependent nonlysosomal proteolytic pathway. In eukaryotes the proteasome is composed of 28 distinct subunits which form a highly ordered rin... | [
"GO:0030163",
"GO:0005839"
] | [
"protein catabolic process",
"proteasome core complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00854"
] | [
"PROTEASOME_BETA_1"
] | [
32211
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.25.1",
"PDOC00668",
"R-BTA-1169091",
"R-BTA-1234176",
"R-BTA-1236974",
"R-BTA-1236978",
"R-BTA-174084",
"R-BTA-174154",
"R-BTA-174178",
"R-BTA-174184",
"R-BTA-187577",
"R-BTA-195253",
"R-BTA-202424",
"R-BTA-2467813",
"R-BTA-2871837",
"R-BTA-349425",
"R-BTA-350562",
"R-BTA-3825... | [
"EC:3.4.25.1",
"PROSITEDOC:PDOC00668",
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-1236974",
"REACTOME:R-BTA-1236978",
"REACTOME:R-BTA-174084",
"REACTOME:R-BTA-174154",
"REACTOME:R-BTA-174178",
"REACTOME:R-BTA-174184",
"REACTOME:R-BTA-187577",
"REACTOME:R-BTA-195253",
... | 459 | [
"1fnt",
"1g0u",
"1g65",
"1iru",
"1j2q",
"1jd2",
"1pma",
"1ryp",
"1ya7",
"1yar",
"1yau",
"1z7q",
"2f16",
"2fak",
"2gpl",
"2zcy",
"3bdm",
"3c91",
"3c92",
"3d29",
"3dy3",
"3dy4",
"3e47",
"3gpj",
"3gpt",
"3gpw",
"3h4p",
"3hye",
"3ipm",
"3j9i",
"3jco",
"3jcp"... | 573 | [
"PUB00000148",
"PUB00000524",
"PUB00001329",
"PUB00004123",
"PUB00005460",
"PUB00030848",
"PUB00065662"
] | [
"2643381",
"7682410",
"7697118",
"1317508",
"8882582",
"9087403",
"22341445"
] | [
"The multicatalytic proteinase of mammalian cells.",
"Proteasomes: multicatalytic proteinase complexes.",
"Proteasomes. Multicatalytic proteinase complexes.",
"Proteolysis, proteasomes and antigen presentation.",
"Proteasomes: destruction as a programme.",
"Structure of 20S proteasome from yeast at 2.4 A ... | [
1989,
1993,
1993,
1992,
1996,
1997,
2012
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
722,
6,
31444,
39
] | 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... | [
32,
4,
20,
25,
51,
31,
6,
23,
45,
9,
8,
62
] | 12 | true | Conserved_site | Proteasome beta-type subunit, conserved site | Proteasome beta-type subunit, conserved site | Proteasome_bsu_CS | 4 |
IPR016052 | 16,052 | YgiW/YdeI | YgiW/YdeI | Family | 1,990 | false | false | This entry represents certain OB fold proteins involved in stress tolerance, including YgiW and YdeI from Escherichia coli [ , , , , ]. This family includes putative periplasmic proteins. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00156"
] | [
""
] | [
1990
] | 1 | [] | [] | [] | 0 | [
"1nnx"
] | 1 | [
"PUB00016305",
"PUB00054160",
"PUB00061993",
"PUB00099706",
"PUB00100116"
] | [
"15178340",
"19919618",
"19767429",
"33106344",
"22990488"
] | [
"BOF: a novel family of bacterial OB-fold proteins.",
"Identification of stress-related proteins in Escherichia coli using the pollutant cis-dichloroethylene.",
"A protein important for antimicrobial peptide resistance, YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC.",
"Role of OB-Fold Protein Yd... | [
2004,
2010,
2009,
2020,
2012
] | 5 | [
"IPR005220"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta",
"Traversvirus",
"metagenomes"
] | [
1955,
2,
30,
3
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | YgiW/YdeI | YgiW/YdeI | YgiW/YdeI | 4 |
IPR016054 | 16,054 | Ly-6 antigen/uPA receptor-like | LY6_UPA_recep-like | Domain | 15,007 | false | false | This entry represents a three-fold repeated domain that is found in a number of venomous neuro- and cytotoxins from snakes [ ] as well as in cell receptors such as urokinase-type plasminogen activator receptor (uPAR) that occurs singly in other GPI-linked cell-surface glycoproteins (Ly-6 family, CD59). A variety of GPI... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00021",
"SM00134"
] | [
"UPAR_LY6",
"LU"
] | [
9984,
7790
] | 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-162791",
"R-BTA-163125",
"R-BTA-6798695",
"R-BTA-75205",
"R-HSA-140875",
"R-HSA-162791",
"R-HSA-163125",
"R-HSA-202733",
"R-HSA-204005",
"R-HSA-5694530",
"R-HSA-6798695",
"R-HSA-6807878",
"R-HSA-75205",
"R-HSA-977606",
"R-MMU-140875",
"R-MMU-162791",
"R-MMU-163125",
"R-MMU-2... | [
"REACTOME:R-BTA-162791",
"REACTOME:R-BTA-163125",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-75205",
"REACTOME:R-HSA-140875",
"REACTOME:R-HSA-162791",
"REACTOME:R-HSA-163125",
"REACTOME:R-HSA-202733",
"REACTOME:R-HSA-204005",
"REACTOME:R-HSA-5694530",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6... | 36 | [
"1cdq",
"1cdr",
"1cds",
"1erg",
"1erh",
"1ywh",
"2fd6",
"2i9b",
"2j8b",
"2n99",
"2ofs",
"2uwr",
"2ux2",
"3bt1",
"3bt2",
"3laq",
"3u73",
"3u74",
"4bik",
"4k24",
"4qti",
"5imt",
"5imy",
"6aex",
"6iom",
"6ion",
"6zd0",
"6zss",
"6zze",
"6zzf",
"7bpr",
"7bps"... | 38 | [
"PUB00002692",
"PUB00002796",
"PUB00085048"
] | [
"1850423",
"8394346",
"23881252"
] | [
"The ligand-binding domain of the cell surface receptor for urokinase-type plasminogen activator.",
"Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator. A domain structure belonging to a novel superfamily of glycolipid-anchored me... | [
1991,
1993,
2013
] | 3 | [] | [
"IPR059168"
] | 0 | 1 | 0 | [
"Eukaryota",
"Gammaherpesvirinae"
] | [
15003,
4
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
26,
86,
95,
129
] | 5 | true | Domain | Ly-6 antigen/uPA receptor-like | Ly-6 antigen/uPA receptor-like | LY6_UPA_recep-like | 9 |
IPR016055 | 16,055 | Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III | A-D-PHexomutase_a/b/a-I/II/III | Homologous_superfamily | 99,150 | false | false | This superfamily represents domains I, II and III found in alpha-D-phosphohexomutase enzymes. All three domains share a 3-layer α/β/α topology. The alpha-D-phosphohexomutase superfamily is composed of four related enzymes, each of which catalyses a phosphoryl transfer on their sugar substrates: phosphoglucomutase (PGM)... | [
"GO:0016868",
"GO:0005975"
] | [
"intramolecular phosphotransferase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF53738"
] | [
""
] | [
99150
] | 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... | [
"5.4.2",
"5.4.2.10",
"PWY-6749",
"R-DDI-3322077",
"R-DDI-6798695",
"R-DDI-70171",
"R-DDI-70221",
"R-DDI-70370",
"R-DDI-71336",
"R-DME-3322077",
"R-DME-6798695",
"R-DME-70221",
"R-DME-70370",
"R-HSA-3322077",
"R-HSA-446210",
"R-HSA-5609974",
"R-HSA-6798695",
"R-HSA-70171",
"R-HSA-... | [
"EC:5.4.2",
"EC:5.4.2.10",
"METACYC:PWY-6749",
"REACTOME:R-DDI-3322077",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-70171",
"REACTOME:R-DDI-70221",
"REACTOME:R-DDI-70370",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-3322077",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-70221",
"REACTOME:R-DME-70370... | 47 | [
"1c47",
"1c4g",
"1jdy",
"1k2y",
"1k35",
"1kfi",
"1kfq",
"1lxt",
"1p5d",
"1p5g",
"1pcj",
"1pcm",
"1tuo",
"1vkl",
"1wqa",
"2dka",
"2dkc",
"2dkd",
"2f7l",
"2fkf",
"2fkm",
"2fuv",
"2h4l",
"2h5a",
"2z0f",
"3bkq",
"3c04",
"3i3w",
"3na5",
"3olp",
"3pdk",
"3pmg"... | 97 | [
"PUB00022429",
"PUB00037156",
"PUB00040705",
"PUB00042561",
"PUB00042562",
"PUB00042563",
"PUB00042564"
] | [
"14725765",
"15299905",
"16595672",
"10506283",
"10913078",
"11004509",
"15238632"
] | [
"Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.",
"Structure of rabbit muscle phosphoglucomutase refined at 2.4 A resolution.",
"The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme.",
"Functional divers... | [
2004,
1997,
2006,
1999,
2000,
2000,
2004
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2584,
74761,
19865,
6,
1934
] | 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",... | [
34,
4,
7,
10,
3,
38,
22,
2,
15,
26,
4,
4,
45
] | 13 | true | Homologous_superfamily | Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III | Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III | A-D-PHexomutase_a/b/a-I/II/III | 1 |
IPR016057 | 16,057 | Pheromone Er-2/Er-23, protozoan | Pheromone_Er2/Er23_protoz | Homologous_superfamily | 4 | false | false | Protozoan pheromones are cell-type specific protein signals. This entry represents the mating ciliate pheromones (or gamones) Er-2 and Er-23 from the protozoan Euplotes raikovi. These pheromones are diffusible extracellular communication signals that distinguishes different intra-specific classes of cells commonly refe... | [
"GO:0000772"
] | [
"mating pheromone activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.10.190"
] | [
""
] | [
4
] | 1 | [] | [] | [] | 0 | [
"1erd",
"1ha8"
] | 2 | [
"PUB00013212",
"PUB00024644",
"PUB00028612"
] | [
"12681291",
"7833811",
"11700049"
] | [
"Cross-talk between the autocrine (mitogenic) pheromone loop of the ciliate Euplotes raikovi and the intracellular cyclic AMP concentration.",
"The NMR solution structure of the pheromone Er-2 from the ciliated protozoan Euplotes raikovi.",
"NMR structure of the Euplotes raikovi pheromone Er-23 and identificati... | [
2003,
1994,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Euplotes raikovi"
] | [
4
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Pheromone Er-2/Er-23, protozoan | Pheromone Er-2/Er-23, protozoan | Pheromone_Er2/Er23_protoz | 7 |
IPR016058 | 16,058 | Pheromone Er-1, protozoan | Pheromone_Er1_protoz | Homologous_superfamily | 5 | false | false | Protozoan pheromones are cell-type specific protein signals. This entry represents the mating ciliate pheromone (or gamone) Er-1 from the protozoan Euplotes raikovi. Er-1 is a diffusible extracellular communication signal that distinguishes different intra-specific classes of cells commonly referred to as 'mating types... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.20.50.10"
] | [
""
] | [
5
] | 1 | [] | [] | [] | 0 | [
"1erc",
"1erp",
"2erl",
"6e6o"
] | 4 | [
"PUB00013212",
"PUB00013310",
"PUB00040415"
] | [
"12681291",
"7833812",
"15299668"
] | [
"Cross-talk between the autocrine (mitogenic) pheromone loop of the ciliate Euplotes raikovi and the intracellular cyclic AMP concentration.",
"The NMR solution structure of the pheromone Er-1 from the ciliated protozoan Euplotes raikovi.",
"A challenging case for protein crystal structure determination: the ma... | [
2003,
1994,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Euplotes raikovi"
] | [
5
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Pheromone Er-1, protozoan | Pheromone Er-1, protozoan | Pheromone_Er1_protoz | 1 |
IPR016059 | 16,059 | DNA ligase, ATP-dependent, conserved site | DNA_ligase_ATP-dep_CS | Conserved_site | 31,547 | false | false | DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalysing the formation of an internucleotide ester bond between phosphate and deoxyribose. It is active during DNA replication, DNA repair and DNA recombination. There are two forms of DNA ligase, one requires ATP ( ), the oth... | [
"GO:0003909"
] | [
"DNA ligase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00333",
"PS00697"
] | [
"DNA_LIGASE_A2",
"DNA_LIGASE_A1"
] | [
13973,
27864
] | 2 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"6.5.1",
"6.5.1.1",
"PDOC00295",
"R-CEL-5358565",
"R-CEL-5358606",
"R-CEL-5651801",
"R-CEL-6782210",
"R-CEL-69183",
"R-DDI-110362",
"R-DDI-110381",
"R-DDI-5358565",
"R-DDI-5358606",
"R-DDI-5649702",
"R-DDI-5651801",
"R-DDI-6782210",
"R-DDI-69183",
"R-DME-5358565",
"R-DME-5358606",
... | [
"EC:6.5.1",
"EC:6.5.1.1",
"PROSITEDOC:PDOC00295",
"REACTOME:R-CEL-5358565",
"REACTOME:R-CEL-5358606",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-69183",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-110381",
"REACTOME:R-DDI-5358565",
"REACTOME:R-DDI-5358606",
"REACTOME:R-... | 65 | [
"1a0i",
"1fvi",
"1p8l",
"1x9n",
"2cfm",
"2hiv",
"2hix",
"2q2t",
"2q2u",
"3gde",
"3l2p",
"3rr5",
"3vnn",
"3w1b",
"3w1g",
"3w5o",
"4eq5",
"6bkf",
"6bkg",
"6dt1",
"6imj",
"6imk",
"6iml",
"6imn",
"6p09",
"6p0a",
"6p0b",
"6p0c",
"6p0d",
"6p0e",
"6q1v",
"6rar"... | 77 | [
"PUB00000083",
"PUB00004409",
"PUB00004738",
"PUB00010654"
] | [
"1497311",
"1437556",
"1988940",
"11983065"
] | [
"Mammalian DNA ligases.",
"Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases.",
"Location of the active site for enzyme-adenylate formation in DNA ligases.",
"ATP-dependent DNA ligases."
... | [
1992,
1992,
1991,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
965,
14210,
14947,
1249,
176
] | 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... | [
21,
1,
6,
3,
19,
12,
3,
9,
15,
2,
3,
25
] | 12 | true | Conserved_site | DNA ligase, ATP-dependent, conserved site | DNA ligase, ATP-dependent, conserved site | DNA_ligase_ATP-dep_CS | 2 |
IPR016061 | 16,061 | Proline-tRNA ligase, class II, C-terminal | Pro-tRNA_ligase_II_C | Domain | 14,505 | false | false | Proline tRNA ligase (also known as Prolyl tRNA synthetase) ( ) exists in two forms, which are loosely related. The first form is present in the majority of eubacteria species. The second one, present in some eubacteria, is essentially present in archaea and eukaryota. Proline-tRNA ligase belongs to class IIa. This doma... | [
"GO:0000166",
"GO:0004827",
"GO:0005524",
"GO:0006433",
"GO:0005737"
] | [
"nucleotide binding",
"proline-tRNA ligase activity",
"ATP binding",
"prolyl-tRNA aminoacylation",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"PFAM",
"SMART"
] | [
"PF09180",
"SM00946"
] | [
"ProRS-C_1",
"ProRS-C_1"
] | [
13338,
14379
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1.15",
"R-DME-9856649",
"R-HSA-2408522",
"R-HSA-379716",
"R-HSA-6782315",
"R-HSA-9856649",
"R-MMU-9856649"
] | [
"EC:6.1.1.15",
"REACTOME:R-DME-9856649",
"REACTOME:R-HSA-2408522",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-9856649"
] | 7 | [
"1h4q",
"1h4s",
"1h4t",
"1hc7",
"1nj1",
"1nj2",
"1nj5",
"1nj6",
"3ial",
"4hvc",
"4k86",
"4k87",
"4k88",
"4ncx",
"4olf",
"4q15",
"4twa",
"4wi1",
"4ydq",
"5f9y",
"5f9z",
"5ifu",
"5v58",
"5vad",
"5xif",
"5xig",
"5xih",
"5xii",
"5xij",
"5xik",
"5xil",
"5xio"... | 89 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
860,
7064,
6436,
11,
134
] | 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... | [
13,
1,
2,
2,
2,
2,
1,
10,
7,
1,
1,
23
] | 12 | true | Domain | Proline-tRNA ligase, class II, C-terminal | Proline-tRNA ligase, class II, C-terminal | Pro-tRNA_ligase_II_C | 3 |
IPR016063 | 16,063 | TM1410 putative glycosidase | TM1410_Glycdase | Family | 147 | false | false | This is a family of uncharacterised proteins. Family members were initially considered to be putative cysteinyl-tRNA synthetases, [ ], but this is no longer thought to be the case. The sequences have a signal peptide. Members of this family occur in Deinococcus radiodurans (bacterial) and Methanococcus jannaschii (arch... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01370"
] | [
""
] | [
147
] | 1 | [] | [] | [] | 0 | [
"2aam",
"9eux",
"9euz"
] | 3 | [
"PUB00017670"
] | [
"11333988"
] | [
"An aminoacyl tRNA synthetase whose sequence fits into neither of the two known classes."
] | [
2001
] | 1 | [
"IPR016062"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Hypsibius exemplaris",
"marine sediment metagenome"
] | [
17,
125,
1,
4
] | 4 | [] | [] | 0 | true | Family | TM1410 putative glycosidase | TM1410 putative glycosidase | TM1410_Glycdase | 5 |
IPR016064 | 16,064 | NAD kinase/diacylglycerol kinase-like domain superfamily | NAD/diacylglycerol_kinase_sf | Homologous_superfamily | 130,566 | false | false | ATP-NAD kinases ( ) catalyse the phosphorylation of NAD to NADP utilizing ATP and other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus. ATP-NAD kinase contains two domains, where domain 1 has an α/β topology that is related in structure to the N-terminal of phosphofructokinase, an... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF111331"
] | [
""
] | [
130566
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"2.7.1",
"2.7.1.23",
"PWY-5083",
"PWY-7268",
"PWY-7269",
"PWY-8148",
"R-BTA-114508",
"R-CEL-114508",
"R-CEL-1483206",
"R-CEL-1660661",
"R-CEL-390471",
"R-CEL-5218921",
"R-CEL-9009391",
"R-CEL-9833482",
"R-CEL-9840309",
"R-DDI-114508",
"R-DDI-1483206",
"R-DDI-1660661",
"R-DDI-3904... | [
"EC:2.7.1",
"EC:2.7.1.23",
"METACYC:PWY-5083",
"METACYC:PWY-7268",
"METACYC:PWY-7269",
"METACYC:PWY-8148",
"REACTOME:R-BTA-114508",
"REACTOME:R-CEL-114508",
"REACTOME:R-CEL-1483206",
"REACTOME:R-CEL-1660661",
"REACTOME:R-CEL-390471",
"REACTOME:R-CEL-5218921",
"REACTOME:R-CEL-9009391",
"REA... | 69 | [
"1suw",
"1u0r",
"1u0t",
"1y3h",
"1y3i",
"1yt5",
"1z0s",
"1z0u",
"1z0z",
"2an1",
"2bon",
"2i1w",
"2i29",
"2i2a",
"2i2b",
"2i2c",
"2i2d",
"2i2f",
"2jgr",
"2p1r",
"2q5f",
"2qv7",
"2qvl",
"3afo",
"3pfn",
"3s40",
"3t5p",
"3v7u",
"3v7w",
"3v7y",
"3v80",
"3v8m"... | 134 | [
"PUB00031631",
"PUB00037645"
] | [
"15269221",
"16242716"
] | [
"A novel fold revealed by Mycobacterium tuberculosis NAD kinase, a key allosteric enzyme in NADP biosynthesis.",
"Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP."
] | [
2004,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2368,
68883,
57745,
5,
1565
] | 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",... | [
83,
22,
187,
53,
2,
90,
78,
6,
62,
92,
5,
5,
166
] | 13 | true | Homologous_superfamily | NAD kinase/diacylglycerol kinase-like domain superfamily | NAD kinase/diacylglycerol kinase-like domain superfamily | NAD/diacylglycerol_kinase_sf | 4 |
IPR016066 | 16,066 | Alpha-D-phosphohexomutase, conserved site | A-D-PHexomutase_CS | Conserved_site | 74,652 | false | false | The alpha-D-phosphohexomutase superfamily is composed of four related enzymes, each of which catalyses a phosphoryl transfer on their sugar substrates: phosphoglucomutase (PGM), phosphoglucomutase/phosphomannomutase (PGM/PMM), phosphoglucosamine mutase (PNGM), and phosphoacetylglucosamine mutase (PAGM) [ ]. PGM ( ) con... | [
"GO:0000287"
] | [
"magnesium ion binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00710"
] | [
"PGM_PMM"
] | [
74652
] | 1 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REAC... | [
"5.4.2",
"5.4.2.10",
"PWY-6749",
"PDOC00589",
"R-DDI-3322077",
"R-DDI-6798695",
"R-DDI-70171",
"R-DDI-70221",
"R-DDI-70370",
"R-DDI-71336",
"R-DME-3322077",
"R-DME-6798695",
"R-DME-70221",
"R-DME-70370",
"R-HSA-3322077",
"R-HSA-446210",
"R-HSA-5609974",
"R-HSA-6798695",
"R-HSA-70... | [
"EC:5.4.2",
"EC:5.4.2.10",
"METACYC:PWY-6749",
"PROSITEDOC:PDOC00589",
"REACTOME:R-DDI-3322077",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-70171",
"REACTOME:R-DDI-70221",
"REACTOME:R-DDI-70370",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-3322077",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-70221... | 43 | [
"1c47",
"1c4g",
"1jdy",
"1k35",
"1kfi",
"1kfq",
"1lxt",
"1p5d",
"1p5g",
"1pcj",
"1pcm",
"1vkl",
"2dka",
"2dkc",
"2dkd",
"2f7l",
"2fkf",
"2fuv",
"2h4l",
"2h5a",
"2z0f",
"3bkq",
"3c04",
"3na5",
"3olp",
"3pdk",
"3pmg",
"4bju",
"4hjh",
"4il8",
"4mrq",
"4qg5"... | 85 | [
"PUB00022429",
"PUB00037156",
"PUB00040705",
"PUB00042561",
"PUB00042562",
"PUB00042563",
"PUB00042564"
] | [
"14725765",
"15299905",
"16595672",
"10506283",
"10913078",
"11004509",
"15238632"
] | [
"Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.",
"Structure of rabbit muscle phosphoglucomutase refined at 2.4 A resolution.",
"The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme.",
"Functional divers... | [
2004,
1997,
2006,
1999,
2000,
2000,
2004
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1954,
57723,
13969,
4,
1002
] | 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",... | [
16,
4,
3,
6,
3,
26,
18,
2,
7,
19,
4,
2,
32
] | 13 | true | Conserved_site | Alpha-D-phosphohexomutase, conserved site | Alpha-D-phosphohexomutase, conserved site | A-D-PHexomutase_CS | 3 |
IPR016067 | 16,067 | S-adenosylmethionine decarboxylase, core | S-AdoMet_deCO2ase_core | Homologous_superfamily | 18,075 | false | false | S-adenosylmethionine decarboxylase (AdoMetDC) [ ] catalyses the removal of the carboxylate group of S-adenosylmethionine to form S-adenosyl-5'-3-methylpropylamine which then acts as the n-propylamine group donor in the synthesis of the polyamines spermidine and spermine from putrescine. The catalytic mechanism of AdoMe... | [
"GO:0004014",
"GO:0008295"
] | [
"adenosylmethionine decarboxylase activity",
"spermidine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF56276"
] | [
""
] | [
18075
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1.50",
"PWY-6834",
"R-BTA-351202",
"R-CEL-351202",
"R-DDI-351202",
"R-DME-351202",
"R-HSA-351202",
"R-MMU-351202",
"R-RNO-351202",
"R-SCE-351202",
"R-SPO-351202"
] | [
"EC:4.1.1.50",
"METACYC:PWY-6834",
"REACTOME:R-BTA-351202",
"REACTOME:R-CEL-351202",
"REACTOME:R-DDI-351202",
"REACTOME:R-DME-351202",
"REACTOME:R-HSA-351202",
"REACTOME:R-MMU-351202",
"REACTOME:R-RNO-351202",
"REACTOME:R-SCE-351202",
"REACTOME:R-SPO-351202"
] | 11 | [
"1i72",
"1i79",
"1i7b",
"1i7c",
"1i7m",
"1jen",
"1jl0",
"1mhm",
"1msv",
"1tlu",
"1tmi",
"1vr7",
"2iii",
"3dz2",
"3dz3",
"3dz4",
"3dz5",
"3dz6",
"3dz7",
"3ep3",
"3ep4",
"3ep5",
"3ep6",
"3ep7",
"3ep8",
"3ep9",
"3epa",
"3epb",
"3h0v",
"3h0w",
"3iwb",
"3iwc"... | 40 | [
"PUB00006224"
] | [
"10378277"
] | [
"The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
471,
10012,
7273,
68,
251
] | 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",... | [
19,
1,
1,
2,
1,
8,
5,
1,
14,
5,
1,
1,
21
] | 13 | true | Homologous_superfamily | S-adenosylmethionine decarboxylase, core | S-adenosylmethionine decarboxylase, core | S-AdoMet_deCO2ase_core | 7 |
IPR016068 | 16,068 | Translin, N-terminal | Translin_N | Homologous_superfamily | 7,502 | false | false | Translins are DNA-binding proteins that specifically recognise consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. They seem to recognise single-sranded DNA ends generated by staggered breaks occuring at recombination hot spo... | [
"GO:0043565"
] | [
"sequence-specific DNA binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:1.20.58.190"
] | [
""
] | [
7502
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-426486",
"R-HSA-426486",
"R-MMU-426486",
"R-RNO-426486",
"R-SPO-426486"
] | [
"REACTOME:R-BTA-426486",
"REACTOME:R-HSA-426486",
"REACTOME:R-MMU-426486",
"REACTOME:R-RNO-426486",
"REACTOME:R-SPO-426486"
] | 5 | [
"1j1j",
"1key",
"2qrx",
"2qva",
"3axj",
"3pja",
"3qb5",
"3riu",
"4dg7",
"4wyv",
"8z7a"
] | 11 | [
"PUB00005776",
"PUB00028825",
"PUB00037000"
] | [
"9013868",
"12079346",
"15039555"
] | [
"Isolation and characterization of a cDNA encoding a Translin-like protein, TRAX.",
"Crystal structure of TB-RBP, a novel RNA-binding and regulating protein.",
"Structure of human translin at 2.2 A resolution."
] | [
1997,
2002,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Eubacteriales",
"Eukaryota"
] | [
2,
7500
] | 2 | [
"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... | [
16,
2,
5,
13,
5,
2,
8,
7,
2,
22
] | 10 | true | Homologous_superfamily | Translin, N-terminal | Translin, N-terminal | Translin_N | 7 |
IPR016069 | 16,069 | Translin, C-terminal | Translin_C | Homologous_superfamily | 7,146 | false | false | Translins are DNA-binding proteins that specifically recognise consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. They seem to recognise single-sranded DNA ends generated by staggered breaks occuring at recombination hot spo... | [
"GO:0043565"
] | [
"sequence-specific DNA binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:1.20.58.200"
] | [
""
] | [
7146
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-426486",
"R-HSA-426486",
"R-MMU-426486",
"R-RNO-426486",
"R-SPO-426486"
] | [
"REACTOME:R-BTA-426486",
"REACTOME:R-HSA-426486",
"REACTOME:R-MMU-426486",
"REACTOME:R-RNO-426486",
"REACTOME:R-SPO-426486"
] | 5 | [
"1j1j",
"1key",
"2qrx",
"2qva",
"3axj",
"3pja",
"3qb5",
"3riu",
"4dg7",
"4wyv",
"8z7a"
] | 11 | [
"PUB00005776",
"PUB00028825",
"PUB00037000"
] | [
"9013868",
"12079346",
"15039555"
] | [
"Isolation and characterization of a cDNA encoding a Translin-like protein, TRAX.",
"Crystal structure of TB-RBP, a novel RNA-binding and regulating protein.",
"Structure of human translin at 2.2 A resolution."
] | [
1997,
2002,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
2,
7143,
1
] | 3 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Ze... | [
13,
2,
4,
6,
4,
2,
8,
8,
2,
14
] | 10 | true | Homologous_superfamily | Translin, C-terminal | Translin, C-terminal | Translin_C | 5 |
IPR016071 | 16,071 | Staphylococcal nuclease (SNase-like), OB-fold | Staphylococal_nuclease_OB-fold | Domain | 28,776 | false | false | Staphylococcus aureus nuclease (SNase) homologues, previously thought to be restricted to bacteria and archaea, are also in eukaryotes. Staphylococcal nuclease has a multi-domain organisation [ ]. The human cellular coactivator p100 contains four repeats, each of which is a SNase homologue. These repeats are unlikely t... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00565",
"PS50830",
"SM00318"
] | [
"SNase",
"TNASE_3",
"SNc"
] | [
28139,
25678,
25567
] | 3 | [
"REACTOME"
] | [
"R-HSA-6802952"
] | [
"REACTOME:R-HSA-6802952"
] | 1 | [
"1a2t",
"1a2u",
"1a3t",
"1a3u",
"1a3v",
"1aex",
"1ena",
"1enc",
"1eqv",
"1ey0",
"1ey4",
"1ey5",
"1ey6",
"1ey7",
"1ey8",
"1ey9",
"1eya",
"1eyc",
"1eyd",
"1ez6",
"1ez8",
"1f2m",
"1f2y",
"1f2z",
"1ihz",
"1ii3",
"1jok",
"1joo",
"1joq",
"1jor",
"1kaa",
"1kab"... | 328 | [
"PUB00000546",
"PUB00005048",
"PUB00031199"
] | [
"9003410",
"9041650",
"8475069"
] | [
"The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development.",
"P100, a transcriptional coactivator, is a human homologue of staphylococcal nuclease.",
"The alpha aneurism: a structural... | [
1997,
1997,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
696,
17973,
9291,
230,
2,
584
] | 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... | [
10,
1,
3,
1,
8,
6,
2,
15,
5,
1,
2,
32
] | 12 | true | Domain | Staphylococcal nuclease (SNase-like), OB-fold | Staphylococcal nuclease (SNase-like), OB-fold | Staphylococal_nuclease_OB-fold | 5 |
IPR016072 | 16,072 | SKP1 component, dimerisation | Skp1_comp_dimer | Domain | 13,453 | false | false | SKP1 (together with SKP2) was identified as an essential component of the cyclin A-CDK2 S phase kinase complex [ ]. It was found to bind several F-box containing proteins (e.g., Cdc4, Skp2, cyclin F) and to be involved in the ubiquitin protein degradation pathway. A yeast homologue of SKP1 (P52286) was identified in th... | [
"GO:0006511"
] | [
"ubiquitin-dependent protein catabolic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01466"
] | [
"Skp1"
] | [
13453
] | 1 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1754",
"R-BTA-1169091",
"R-BTA-174113",
"R-BTA-187577",
"R-BTA-195253",
"R-BTA-202424",
"R-BTA-2565942",
"R-BTA-2871837",
"R-BTA-5607761",
"R-BTA-5607764",
"R-BTA-5610780",
"R-BTA-5610785",
"R-BTA-5676590",
"R-BTA-5684264",
"R-BTA-68949",
"R-BTA-69231",
"R-BTA-69601",
"R-BT... | [
"GP:GenProp1754",
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-174113",
"REACTOME:R-BTA-187577",
"REACTOME:R-BTA-195253",
"REACTOME:R-BTA-202424",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-2871837",
"REACTOME:R-BTA-5607761",
"REACTOME:R-BTA-5607764",
"REACTOME:R-BTA-5610780",
"REACTOME:R-BTA-5610... | 157 | [
"1fqv",
"1fs1",
"1fs2",
"1ldk",
"1nex",
"1p22",
"2ass",
"2ast",
"2e31",
"2e32",
"2ovp",
"2ovq",
"2ovr",
"2p1m",
"2p1n",
"2p1o",
"2p1p",
"2p1q",
"3c6n",
"3c6o",
"3c6p",
"3l2o",
"3mks",
"3ogk",
"3ogl",
"3ogm",
"3v7d",
"3wso",
"4i6j",
"5hyw",
"5hzg",
"5ibk"... | 111 | [
"PUB00005233",
"PUB00006069",
"PUB00006070",
"PUB00006072",
"PUB00010628",
"PUB00029039"
] | [
"10205047",
"8670864",
"7852383",
"9390558",
"11099048",
"12553912"
] | [
"Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function.",
"The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution.",
"Characterization of FP21, a cytosolic glycoprotein from Dictyostelium.",
"Regula... | [
1999,
1996,
1995,
1997,
2000,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
13417,
29,
7
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
64,
20,
1,
16,
5,
4,
1,
66,
4,
1,
1,
91
] | 12 | true | Domain | SKP1 component, dimerisation | SKP1 component, dimerisation | Skp1_comp_dimer | 3 |
IPR016073 | 16,073 | SKP1 component, POZ domain | Skp1_comp_POZ | Domain | 17,223 | false | false | SKP1 (together with SKP2) was identified as an essential component of the cyclin A-CDK2 S phase kinase complex [ ]. It was found to bind several F-box containing proteins (e.g., Cdc4, Skp2, cyclin F) and to be involved in the ubiquitin protein degradation pathway. A yeast homologue of SKP1 (P52286) was identified in th... | [
"GO:0006511"
] | [
"ubiquitin-dependent protein catabolic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF03931"
] | [
"Skp1_POZ"
] | [
17223
] | 1 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1754",
"R-BTA-1169091",
"R-BTA-1234176",
"R-BTA-174113",
"R-BTA-187577",
"R-BTA-195253",
"R-BTA-202424",
"R-BTA-2565942",
"R-BTA-2871837",
"R-BTA-5607761",
"R-BTA-5607764",
"R-BTA-5610780",
"R-BTA-5610785",
"R-BTA-5676590",
"R-BTA-5684264",
"R-BTA-674695",
"R-BTA-6796648",
... | [
"GP:GenProp1754",
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-174113",
"REACTOME:R-BTA-187577",
"REACTOME:R-BTA-195253",
"REACTOME:R-BTA-202424",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-2871837",
"REACTOME:R-BTA-5607761",
"REACTOME:R-BTA-5607764",
"REACTOME:R-BTA-5610... | 193 | [
"1fqv",
"1fs1",
"1fs2",
"1hv2",
"1ldk",
"1lm8",
"1lqb",
"1nex",
"1p22",
"1vcb",
"2ass",
"2ast",
"2c9w",
"2e31",
"2e32",
"2fnj",
"2izv",
"2jz3",
"2ma9",
"2ovp",
"2ovq",
"2ovr",
"2p1m",
"2p1n",
"2p1o",
"2p1p",
"2p1q",
"3c6n",
"3c6o",
"3c6p",
"3dcg",
"3l2o"... | 328 | [
"PUB00005233",
"PUB00006069",
"PUB00006070",
"PUB00006072",
"PUB00010628",
"PUB00029039"
] | [
"10205047",
"8670864",
"7852383",
"9390558",
"11099048",
"12553912"
] | [
"Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function.",
"The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution.",
"Characterization of FP21, a cytosolic glycoprotein from Dictyostelium.",
"Regula... | [
1999,
1996,
1995,
1997,
2000,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
17195,
21,
7
] | 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... | [
58,
25,
4,
19,
14,
10,
3,
54,
14,
2,
2,
61
] | 12 | true | Domain | SKP1 component, POZ domain | SKP1 component, POZ domain | Skp1_comp_POZ | 7 |
IPR016075 | 16,075 | RNA polymerase, phosphoprotein P, C-terminal XD, paramyxovirinae | RNA_pol_Pprot-P_XD_paramyxovir | Homologous_superfamily | 1,303 | false | false | Paramyxovirinae has a negative-sense ssRNA genome that is packaged by the viral nucleoprotein (N) within a helical nucleocapsid. The N-RNA (nucleoprotein-RNA) complex is used as a template for both transcription and replication. During viral genome replication, the synthesis of viral RNA and its encapsidation by N are ... | [
"GO:0003723",
"GO:0003968",
"GO:0006351",
"GO:0019079"
] | [
"RNA binding",
"RNA-directed RNA polymerase activity",
"DNA-templated transcription",
"viral genome replication"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"SSF"
] | [
"SSF101089"
] | [
""
] | [
1303
] | 1 | [] | [] | [] | 0 | [
"1oks",
"1r4g",
"1t6o",
"2k9d",
"5lxj",
"8kdb",
"8kdc",
"9dus",
"9dut",
"9knq",
"9knt",
"9knv",
"9oce",
"9ocf"
] | 14 | [
"PUB00003548",
"PUB00020838",
"PUB00030518",
"PUB00031362",
"PUB00042566"
] | [
"10400742",
"12944395",
"14980481",
"15159535",
"17459940"
] | [
"Dissection of individual functions of the Sendai virus phosphoprotein in transcription.",
"Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein.",
"Structure and dynamics of the nucleocapsid-binding domain of the Sendai v... | [
1999,
2003,
2004,
2004,
2007
] | 5 | [] | [] | 0 | 0 | null | [
"Paramyxoviridae"
] | [
1303
] | 1 | [] | [] | 0 | true | Homologous_superfamily | RNA polymerase, phosphoprotein P, C-terminal XD, paramyxovirinae | RNA polymerase, phosphoprotein P, C-terminal XD, paramyxovirinae | RNA_pol_Pprot-P_XD_paramyxovir | 1 |
IPR016082 | 16,082 | Large ribosomal subunit protein uL30-like, ferredoxin-like fold domain | Ribosomal_uL30_ferredoxin-like | Domain | 33,817 | false | false | Ribosomal protein uL30 is one of the proteins from the large ribosomal subunit. uL30 belongs to a family of ribosomal proteins which, on the basis of sequence similarities [ ], groups bacteria and archaea uL30, yeast mitochondrial L33, and Drosophila melanogaster, Dictyostelium discoideum (Slime mold), fungal and mamma... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00327"
] | [
"Ribosomal_L30"
] | [
33817
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",
"R-DDI-97595... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-9759... | 79 | [
"1bxy",
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk"... | 1,895 | [
"PUB00004400",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00059243",
"PUB00059244",
"PUB00059245",
"PUB00095412",
"PUB00095413"
] | [
"1549461",
"11297922",
"11290319",
"11114498",
"8256515",
"11087857",
"15100437",
"23002217",
"26083755"
] | [
"Yeast ribosomal proteins: XIII. Saccharomyces cerevisiae YL8A gene, interrupted with two introns, encodes a homolog of mammalian L7.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Two distinct yeast pro... | [
1992,
2001,
2001,
2000,
1993,
2000,
2004,
2012,
2015
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
935,
20291,
12207,
384
] | 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",... | [
15,
1,
3,
4,
1,
10,
11,
2,
15,
14,
4,
4,
37
] | 13 | true | Domain | Large ribosomal subunit protein uL30-like, ferredoxin-like fold domain | Large ribosomal subunit protein uL30-like, ferredoxin-like fold domain | Ribosomal_uL30_ferredoxin-like | 7 |
IPR016084 | 16,084 | Haem oxygenase-like, multi-helical | Haem_Oase-like_multi-hlx | Homologous_superfamily | 52,844 | false | false | This superfamily represents a multi-helical structural domain consisting of two structural repeats (duplication) of a 3-helical motif. This domain can be found in both eukaryotic and prokaryotic haem oxygenases [ , ], in TENA/THI-4 proteins that lack the haem-binding site [ ], and in coenzyme PQQ (pyrrolo-quinoline-qui... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.20.910.10",
"SSF48613"
] | [
"",
""
] | [
52604,
49898
] | 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-189483",
"R-BTA-917937",
"R-BTA-9609523",
"R-BTA-9707564",
"R-BTA-9707587",
"R-HSA-189483",
"R-HSA-6785807",
"R-HSA-6798695",
"R-HSA-844456",
"R-HSA-8980692",
"R-HSA-917937",
"R-HSA-9609523",
"R-HSA-9660826",
"R-HSA-9707564",
"R-HSA-9707587",
"R-HSA-9707616",
"R-HSA-9818027",
... | [
"REACTOME:R-BTA-189483",
"REACTOME:R-BTA-917937",
"REACTOME:R-BTA-9609523",
"REACTOME:R-BTA-9707564",
"REACTOME:R-BTA-9707587",
"REACTOME:R-HSA-189483",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-844456",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-917937",
"REACTOME:R-H... | 36 | [
"1dve",
"1dvg",
"1irm",
"1ivj",
"1iw0",
"1iw1",
"1ix3",
"1ix4",
"1j02",
"1j2c",
"1j77",
"1n3u",
"1n45",
"1ni6",
"1otv",
"1otw",
"1oyk",
"1oyl",
"1oze",
"1ozl",
"1ozr",
"1ozw",
"1p3t",
"1p3u",
"1p3v",
"1rcw",
"1rtw",
"1s13",
"1s8c",
"1sk7",
"1t5p",
"1to9"... | 179 | [
"PUB00022669",
"PUB00026272",
"PUB00029597",
"PUB00030800"
] | [
"15049686",
"11560504",
"15148379",
"15858269"
] | [
"Crystal structure of human heme oxygenase-1 in a complex with biliverdin.",
"Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1.",
"Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production ... | [
2004,
2001,
2004,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
750,
38463,
13303,
27,
301
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
23,
17,
3,
24,
10,
4,
12,
8,
5,
3,
53
] | 11 | true | Homologous_superfamily | Haem oxygenase-like, multi-helical | Haem oxygenase-like, multi-helical | Haem_Oase-like_multi-hlx | 1 |
IPR016085 | 16,085 | Protease inhibitor, beta-barrel domain | Protease_inh_B-barrel_dom | Homologous_superfamily | 2,397 | false | false | This entry represents a β-barrel domain found in the protease inhibitors staphostatin [ ] and metalloprotease inhibitor [ ]. | [
"GO:0004866"
] | [
"endopeptidase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF50882"
] | [
""
] | [
2397
] | 1 | [] | [] | [] | 0 | [
"1jiw",
"1nyc",
"1oh1",
"1pxv",
"1qwx",
"1smp",
"1y4h",
"2rn4",
"6ixx",
"6iy4",
"7mhw"
] | 11 | [
"PUB00006323",
"PUB00029436",
"PUB00032579",
"PUB00034485"
] | [
"7752231",
"14621990",
"15644332",
"15716447"
] | [
"Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi.",
"A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus.",
"A comparison of staphostatin B with standard mechanism serine protease in... | [
1995,
2003,
2005,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
2391,
6
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Protease inhibitor, beta-barrel domain | Protease inhibitor, beta-barrel domain | Protease_inh_B-barrel_dom | 2 |
IPR016087 | 16,087 | Chalcone isomerase | Chalcone_isomerase | Domain | 10,904 | false | false | Chalcone isomerase (CHI, ; also known as chalcone-flavanone isomerase) is a plant enzyme responsible for the isomerisation of chalcone to naringenin, a key step in the biosynthesis of flavonoids. The Petunia hybrida (Petunia) genome contains two genes coding for very similar enzymes, ChiA and ChiB, but only the first s... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM"
] | [
"PF02431",
"PF16035",
"PF16036"
] | [
"Chalcone",
"Chalcone_2",
"Chalcone_3"
] | [
2946,
2897,
5061
] | 3 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.5.1.6",
"PWY-2002",
"PWY-5059",
"PWY-6325",
"PWY-6787",
"PWY-7397",
"PWY-7897"
] | [
"EC:5.5.1.6",
"METACYC:PWY-2002",
"METACYC:PWY-5059",
"METACYC:PWY-6325",
"METACYC:PWY-6787",
"METACYC:PWY-7397",
"METACYC:PWY-7897"
] | 7 | [
"1eyp",
"1eyq",
"1fm7",
"1fm8",
"1jep",
"1jx0",
"1jx1",
"4doi",
"4dok",
"4dol",
"4doo",
"5wkr",
"5wks",
"5wl3",
"5wl4",
"5wl5",
"5wl6",
"5wl7",
"5wl8",
"5yx3",
"5yx4",
"6cjn",
"6cjo",
"6ms8",
"8dlc",
"8dld",
"8ew8",
"8ew9",
"8v8l",
"8v8o",
"8v8p",
"9kah"... | 33 | [
"PUB00024704",
"PUB00103775"
] | [
"10966651",
"36739946"
] | [
"Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase.",
"Aim18p and Aim46p are chalcone isomerase (CHI)-domain-containing mitochondrial hemoproteins in Saccharomyces cerevisiae."
] | [
2000,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4609,
6242,
53
] | 3 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
29,
1,
21,
2,
1,
53
] | 6 | true | Domain | Chalcone isomerase | Chalcone isomerase | Chalcone_isomerase | 5 |
IPR016088 | 16,088 | Chalcone isomerase, 3-layer sandwich | Chalcone_isomerase_3-sand | Homologous_superfamily | 9,297 | false | false | Chalcone isomerase ( ; also known as chalcone-flavanone isomerase or fatty-acid-binding protein) is a plant enzyme responsible for the isomerisation of chalcone to naringenin, a key step in the biosynthesis of flavonoids. The Petunia hybrida (Petunia) genome contains two genes coding for very similar enzymes, ChiA and ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.50.70.10"
] | [
""
] | [
9297
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.5.1.6",
"PWY-2002",
"PWY-5059",
"PWY-6325",
"PWY-6787",
"PWY-7397",
"PWY-7897"
] | [
"EC:5.5.1.6",
"METACYC:PWY-2002",
"METACYC:PWY-5059",
"METACYC:PWY-6325",
"METACYC:PWY-6787",
"METACYC:PWY-7397",
"METACYC:PWY-7897"
] | 7 | [
"1eyp",
"1eyq",
"1fm7",
"1fm8",
"1jep",
"1jx0",
"1jx1",
"4doi",
"4dok",
"4dol",
"4doo",
"5wkr",
"5wks",
"5wl3",
"5wl4",
"5wl5",
"5wl6",
"5wl7",
"5wl8",
"5yx3",
"5yx4",
"6cjn",
"6cjo",
"6ms8",
"8dlc",
"8dld",
"8ew8",
"8ew9",
"8v8l",
"8v8o",
"8v8p",
"9kah"... | 33 | [
"PUB00024704"
] | [
"10966651"
] | [
"Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Geoglobus acetivorans",
"unclassified sequences"
] | [
2430,
6821,
1,
45
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
28,
1,
22,
2,
1,
77
] | 6 | true | Homologous_superfamily | Chalcone isomerase, 3-layer sandwich | Chalcone isomerase, 3-layer sandwich | Chalcone_isomerase_3-sand | 3 |
IPR016089 | 16,089 | Chalcone isomerase, orthogonal bundle domain superfamily | Chalcone_isomerase_bundle_sf | Homologous_superfamily | 4,360 | false | false | Chalcone isomerase ( ; also known as chalcone-flavanone isomerase or fatty-acid-binding protein) is a plant enzyme responsible for the isomerisation of chalcone to naringenin, a key step in the biosynthesis of flavonoids. The Petunia hybrida (Petunia) genome contains two genes coding for very similar enzymes, ChiA and ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.890.20"
] | [
""
] | [
4360
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.5.1.6",
"PWY-2002",
"PWY-5059",
"PWY-6325",
"PWY-6787",
"PWY-7397",
"PWY-7897"
] | [
"EC:5.5.1.6",
"METACYC:PWY-2002",
"METACYC:PWY-5059",
"METACYC:PWY-6325",
"METACYC:PWY-6787",
"METACYC:PWY-7397",
"METACYC:PWY-7897"
] | 7 | [
"1eyp",
"1eyq",
"1fm7",
"1fm8",
"1jep",
"1jx0",
"1jx1",
"4doi",
"4dok",
"4dol",
"4doo",
"5wkr",
"5wks",
"5wl3",
"5wl4",
"5wl5",
"5wl6",
"5wl7",
"5wl8",
"5yx3",
"5yx4",
"6cjn",
"6cjo",
"6ms8",
"8dlc",
"8dld",
"8v8l",
"8v8o",
"8v8p",
"9kah",
"9kai"
] | 31 | [
"PUB00024704"
] | [
"10966651"
] | [
"Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine metagenome"
] | [
6,
4352,
2
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
26,
21,
64
] | 3 | true | Homologous_superfamily | Chalcone isomerase, orthogonal bundle domain superfamily | Chalcone isomerase, orthogonal bundle domain superfamily | Chalcone_isomerase_bundle_sf | 8 |
IPR016090 | 16,090 | Phospholipase A2-like, central domain | PLA2-like_dom | Domain | 14,240 | false | false | Proteins containing this domain include eukaryotic phospholipase A2 enzymes (PLA2; ), small lipolytic enzymes that release fatty acids from the second carbon group of glycerol, usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA) [ ]. The resulting products are either ... | [
"GO:0004623",
"GO:0006644",
"GO:0050482"
] | [
"A2-type glycerophospholipase activity",
"phospholipid metabolic process",
"arachidonate secretion"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PFAM",
"PFAM",
"SMART",
"CDD"
] | [
"PF00068",
"PF05826",
"SM00085",
"cd00125"
] | [
"Phospholip_A2_1",
"Phospholip_A2_2",
"PA2c",
"PLA2c"
] | [
9694,
4489,
9756,
7512
] | 4 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"3.1.1.4",
"PWY-6803",
"PWY-7409",
"PWY-7416",
"PWY-7417",
"PWY-7783",
"PWY-8051",
"PWY-8053",
"PWY-8355",
"PWY-8356",
"PWY-8357",
"PWY-8395",
"PWY-8396",
"PWY-8397",
"PWY-8398",
"PWY-8399",
"PWY-8400",
"PWY-8410",
"PWY-8411",
"PWY-8412",
"PWY-8413",
"R-BTA-1482788",
"R-B... | [
"EC:3.1.1.4",
"METACYC:PWY-6803",
"METACYC:PWY-7409",
"METACYC:PWY-7416",
"METACYC:PWY-7417",
"METACYC:PWY-7783",
"METACYC:PWY-8051",
"METACYC:PWY-8053",
"METACYC:PWY-8355",
"METACYC:PWY-8356",
"METACYC:PWY-8357",
"METACYC:PWY-8395",
"METACYC:PWY-8396",
"METACYC:PWY-8397",
"METACYC:PWY-8... | 56 | [
"1a2a",
"1a3d",
"1a3f",
"1ae7",
"1aok",
"1ayp",
"1b4w",
"1bbc",
"1bjj",
"1bk9",
"1bp2",
"1bpq",
"1bun",
"1bvm",
"1c1j",
"1c74",
"1ceh",
"1cl5",
"1clp",
"1db4",
"1db5",
"1dcy",
"1dpy",
"1fb2",
"1fdk",
"1fe5",
"1fv0",
"1fx9",
"1fxf",
"1g0z",
"1g2x",
"1g4i"... | 324 | [
"PUB00003922",
"PUB00026999",
"PUB00028486",
"PUB00081579",
"PUB00081580",
"PUB00081581",
"PUB00081584",
"PUB00081586",
"PUB00081623",
"PUB00081624",
"PUB00081625",
"PUB00092777",
"PUB00097848",
"PUB00097849"
] | [
"7664098",
"12161451",
"11897785",
"11872155",
"11293116",
"11212293",
"11080675",
"10331081",
"16805767",
"10838563",
"16339444",
"23148443",
"28063838",
"25365526"
] | [
"NMR structures of phospholipase A2 reveal conformational changes during interfacial activation.",
"Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes.",
"The crystal structure of prokaryotic phospholipase A2.",
"Phospholi... | [
1995,
2002,
2002,
2002,
2001,
1999,
2000,
1999,
2006,
2000,
2005,
2012,
2017,
2014
] | 14 | [] | [
"IPR041798"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
121,
14118,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
9,
14,
27,
37,
46
] | 6 | true | Domain | Phospholipase A2-like, central domain | Phospholipase A2-like, central domain | PLA2-like_dom | 1 |
IPR016091 | 16,091 | Superantigen toxin, C-terminal | SuperAg_toxin_C | Homologous_superfamily | 1,311 | false | false | This entry represents superantigen toxins from Staphylococcus aureus and Streptococcus pyogenes, which share a common core structure consisting of β(2)-α-β(2). S. aureus toxins with this fold include: enterotoxins A (SEA) [ ], B (SEB) [ ], C2 (SEC2) [ ], C3 (SEC3) [ ] and H (SEH) [ ], heat shock syndrome toxin-1 [ ], a... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"SSF"
] | [
"SSF54334"
] | [
""
] | [
1311
] | 1 | [] | [] | [] | 0 | [
"1an8",
"1aw7",
"1b1z",
"1bxt",
"1ck1",
"1cqv",
"1d5m",
"1d5x",
"1d5z",
"1d6e",
"1dyq",
"1enf",
"1esf",
"1et6",
"1et9",
"1eu3",
"1eu4",
"1ewc",
"1f77",
"1fnu",
"1fnv",
"1fnw",
"1goz",
"1ha5",
"1hqr",
"1hxy",
"1i4g",
"1i4h",
"1i4p",
"1i4q",
"1i4r",
"1i4x"... | 156 | [
"PUB00007937",
"PUB00018994",
"PUB00021273",
"PUB00021334",
"PUB00021525",
"PUB00024655",
"PUB00024668",
"PUB00024956",
"PUB00028188",
"PUB00031608",
"PUB00031833",
"PUB00031971",
"PUB00032898"
] | [
"9514739",
"12082105",
"10048922",
"11934896",
"10986116",
"7628431",
"10860729",
"11045630",
"9253413",
"15247241",
"14559915",
"15213171",
"8759320"
] | [
"Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors.",
"The Three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus... | [
1998,
2002,
1999,
2002,
2000,
1995,
2000,
2000,
1997,
2004,
2004,
2004,
1996
] | 13 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Plasmid pIB485"
] | [
1293,
7,
10,
1
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Superantigen toxin, C-terminal | Superantigen toxin, C-terminal | SuperAg_toxin_C | 4 |
IPR016092 | 16,092 | FeS A-type assembly protein ATAP | ATAP | Family | 39,858 | false | false | Proteins in this entry include HesB, IscA, SufA and ErpA and related FeS cluster proteins from all kingdoms. 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 ATAP family consists ... | [
"GO:0051536",
"GO:0016226"
] | [
"iron-sulfur cluster binding",
"iron-sulfur cluster assembly"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR00049"
] | [
""
] | [
39858
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00887",
"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"
] | [
"PROSITEDOC:PDOC00887",
"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:... | 12 | [
"1nwb",
"1r94",
"1r95",
"1s98",
"1x0g",
"2apn",
"2d2a"
] | 7 | [
"PUB00003442",
"PUB00003602",
"PUB00010345",
"PUB00017349",
"PUB00028014",
"PUB00030961",
"PUB00035635",
"PUB00035636",
"PUB00035637",
"PUB00035638",
"PUB00035639",
"PUB00035640",
"PUB00058194",
"PUB00058195",
"PUB00058196",
"PUB00160404",
"PUB00160405",
"PUB00160406"
] | [
"8875867",
"10217509",
"10322040",
"9582371",
"11498000",
"15050828",
"16221578",
"16211402",
"16843540",
"15937904",
"17350000",
"15278785",
"17698959",
"22363723",
"16824008",
"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,
1998,
2001,
2004,
2005,
2005,
2006,
2005,
2007,
2004,
2007,
2012,
2006,
2013,
2020,
2021
] | 18 | [] | [
"IPR011298",
"IPR011302",
"IPR023063",
"IPR031108"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
518,
29681,
8994,
27,
638
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
15,
3,
3,
2,
3,
3,
4,
1,
13,
6,
1,
2,
22
] | 13 | true | Family | FeS A-type assembly protein ATAP | FeS A-type assembly protein ATAP | ATAP | 8 |
IPR016093 | 16,093 | MIR motif | MIR_motif | Domain | 28,646 | false | false | The MIR domain is named after three of the proteins in which it occurs: protein Mannosyltransferase ( ), Inositol 1,4,5-trisphosphate receptor (IP3R) and Ryanodine receptor (RyR). MIR domains have also been found in eukaryotic stromal cell-derived factor 2 (SDF-2) [ ] and in Chlamydia trachomatis protein CT153. The MIR... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF02815",
"PS50919",
"SM00472"
] | [
"MIR",
"MIR",
"MIR"
] | [
26751,
28010,
27509
] | 3 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1455",
"PDOC50919",
"R-CEL-114508",
"R-CEL-139853",
"R-CEL-381676",
"R-CEL-5578775",
"R-CEL-9717207",
"R-CEL-983695",
"R-DME-114508",
"R-DME-139853",
"R-DME-381676",
"R-DME-5578775",
"R-DME-8932504",
"R-DME-8932505",
"R-DME-8932506",
"R-DME-9717207",
"R-DME-9768727",
"R-DME... | [
"GP:GenProp1455",
"PROSITEDOC:PDOC50919",
"REACTOME:R-CEL-114508",
"REACTOME:R-CEL-139853",
"REACTOME:R-CEL-381676",
"REACTOME:R-CEL-5578775",
"REACTOME:R-CEL-9717207",
"REACTOME:R-CEL-983695",
"REACTOME:R-DME-114508",
"REACTOME:R-DME-139853",
"REACTOME:R-DME-381676",
"REACTOME:R-DME-5578775",... | 69 | [
"1n4k",
"1t9f",
"1xzz",
"2mc2",
"2xoa",
"3hsm",
"3ila",
"3im5",
"3im6",
"3im7",
"3j8h",
"3jav",
"3jrr",
"3mal",
"3qr5",
"3t8s",
"3uj0",
"3uj4",
"4i0y",
"4i1e",
"4i2s",
"4i37",
"4i3n",
"4i6i",
"4i7i",
"4i8m",
"4i96",
"4jkq",
"4kei",
"4kej",
"4kek",
"4l4h"... | 257 | [
"PUB00001957",
"PUB00002638",
"PUB00095658"
] | [
"7829078",
"1645727",
"28597544"
] | [
"Mutation screening of the RYR1 gene in malignant hyperthermia: detection of a novel Tyr to Ser mutation in a pedigree with associated central cores.",
"Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity.",
"Endoplasmic reticulum proteins SDF2 and SDF2L1 act as comp... | [
1994,
1991,
2017
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"organismal metagenomes"
] | [
58,
28586,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
6,
19,
115,
13,
60,
26,
4,
4,
50,
7,
3,
6
] | 12 | true | Domain | MIR motif | MIR motif | MIR_motif | 5 |
IPR016097 | 16,097 | Domain of unknown function DUF695 | DUF695 | Domain | 2,169 | false | false | This domain is found at the N terminus of a number of bacterial proteins of unknown function. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF05117"
] | [
"DUF695"
] | [
2169
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
2154,
2,
13
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function DUF695 | Domain of unknown function DUF695 | DUF695 | 6 |
IPR016098 | 16,098 | Cyclase-associated protein CAP/septum formation inhibitor MinC, C-terminal | CAP/MinC_C | Homologous_superfamily | 27,266 | false | false | Cyclase-associated proteins (CAPs) are highly conserved monomeric actin-binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways [ , , , ]. Only yeas... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.160.20.70"
] | [
""
] | [
27266
] | 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 | [
"1hf2",
"1k4z",
"1k8f",
"1kq5",
"2b0r",
"2bx6",
"2yuh",
"3bh6",
"3bh7",
"4v02",
"5aj8",
"5cya",
"5xdm",
"6fm2",
"6riq",
"9m1m",
"9m1n"
] | 17 | [
"PUB00007159",
"PUB00008426",
"PUB00042568",
"PUB00042569",
"PUB00042570",
"PUB00042573"
] | [
"12351838",
"10869074",
"11919151",
"17635992",
"10658207",
"17085577"
] | [
"Crystallization of cyclase-associated protein from Dictyostelium discoideum.",
"Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ.",
"Cyclase-associated proteins: CAPacity for linking signal transduction and actin polymerization.",
"Arabidopsis CAP1 - a key regulator... | [
2002,
2000,
2002,
2007,
2000,
2007
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
11319,
15843,
16,
88
] | 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",... | [
23,
8,
9,
4,
1,
18,
13,
3,
14,
23,
2,
2,
47
] | 13 | true | Homologous_superfamily | Cyclase-associated protein CAP/septum formation inhibitor MinC, C-terminal | Cyclase-associated protein CAP/septum formation inhibitor MinC, C-terminal | CAP/MinC_C | 2 |
IPR016100 | 16,100 | Prismane, alpha-bundle | Prismane_a-bundle | Homologous_superfamily | 6,906 | false | false | Prismane (hybrid-cluster) proteins are present in a wide range of bacteria and archaea, and are characterised by their two Fe/S centres: a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O] cluster [ ]. Prismane proteins (hybrid cluster proteins) contain four domains: two spectrin repeat-like 3-helical bundle domains, a... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:1.20.1270.20"
] | [
""
] | [
6906
] | 1 | [
"EC"
] | [
"1.7.99.1"
] | [
"EC:1.7.99.1"
] | 1 | [
"1e1d",
"1e2u",
"1e9v",
"1gn9",
"1gnl",
"1gnt",
"1oa0",
"1oa1",
"1upx",
"1w9m",
"7e0l",
"7wsx",
"8cnr",
"8cns"
] | 14 | [
"PUB00007375"
] | [
"10651802"
] | [
"The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
276,
6313,
238,
79
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | Prismane, alpha-bundle | Prismane, alpha-bundle | Prismane_a-bundle | 7 |
IPR016101 | 16,101 | CO dehydrogenase, alpha-bundle | CO_DH_a-bundle | Homologous_superfamily | 2,175 | false | false | This superfamily represents an α-bundle domain with an up-and-down topology found in Ni-containing carbon monoxide dehydrogenases (CODH) ( ). These enzymes reversibly oxidise CO to CO(2), and play key roles in the energy-yielding pathways of various autotrophic anaerobes, allowing these organisms to grow with CO as the... | [
"GO:0016151",
"GO:0043885",
"GO:0051539",
"GO:0006091"
] | [
"nickel cation binding",
"anaerobic carbon-monoxide dehydrogenase activity",
"4 iron, 4 sulfur cluster binding",
"generation of precursor metabolites and energy"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"CATHGENE3D"
] | [
"G3DSA:1.20.1270.30"
] | [
""
] | [
2175
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.2.7.4",
"PWY-5372",
"PWY-6780"
] | [
"EC:1.2.7.4",
"METACYC:PWY-5372",
"METACYC:PWY-6780"
] | 3 | [
"1jqk",
"1mjg",
"1oao",
"1su6",
"1su7",
"1su8",
"1suf",
"2yiv",
"2z8y",
"3b51",
"3b52",
"3b53",
"3i01",
"3i04",
"3i39",
"4udx",
"4udy",
"5fle",
"6b6v",
"6b6w",
"6b6x",
"6b6y",
"6dc2",
"6elq",
"6onc",
"6ond",
"6ons",
"6t7j",
"6vwy",
"6vwz",
"6vx0",
"6vx1"... | 112 | [
"PUB00015141",
"PUB00015142",
"PUB00015143"
] | [
"12627225",
"15221479",
"15248760"
] | [
"Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase.",
"Crystallographic evidence for a CO/CO(2) tunnel gating mechanism in the bifunctional carbon monoxide dehydrogenase/acetyl coenzyme A synthase from Moorella thermoacetica.",
"CO-induce... | [
2003,
2004,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Cyprideis torosa",
"unclassified sequences"
] | [
258,
1705,
1,
211
] | 4 | [] | [] | 0 | true | Homologous_superfamily | CO dehydrogenase, alpha-bundle | CO dehydrogenase, alpha-bundle | CO_DH_a-bundle | 4 |
IPR016102 | 16,102 | Succinyl-CoA synthetase-like | Succinyl-CoA_synth-like | Homologous_superfamily | 92,592 | false | false | This superfamily represents a structural domain consisting of 3-layers, α/β/α. This domain is found in both the alpha and beta chains of succinate--CoA ligase (also known as succinyl-CoA synthase; (GDP-forming) and (ADP-forming)) [ , ]. This domain can also be found in ATP citrate synthase ( ), malate-CoA ligase ( ) an... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.40.50.261",
"SSF52210"
] | [
"",
""
] | [
92443,
89540
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"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",
"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-6798695",
"R-... | [
"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",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-75105",
"REACTOM... | 40 | [
"1cqi",
"1cqj",
"1euc",
"1eud",
"1jkj",
"1jll",
"1oi7",
"1scu",
"2csu",
"2fp4",
"2fpg",
"2fpi",
"2fpp",
"2nu6",
"2nu7",
"2nu8",
"2nu9",
"2nua",
"2scu",
"2yv1",
"2yv2",
"3dmy",
"3mwd",
"3mwe",
"3pff",
"3ufx",
"4xx0",
"4xyl",
"4xym",
"4xz3",
"4y8v",
"4yaj"... | 90 | [
"PUB00015984",
"PUB00036671"
] | [
"9917402",
"10873456"
] | [
"A detailed structural description of Escherichia coli succinyl-CoA synthetase.",
"Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase."
] | [
1999,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"Sym plasmid",
"unclassified sequences"
] | [
3048,
63908,
23530,
5,
1,
2100
] | 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",... | [
29,
6,
17,
14,
5,
31,
14,
5,
10,
26,
2,
4,
52
] | 13 | true | Homologous_superfamily | Succinyl-CoA synthetase-like | Succinyl-CoA synthetase-like | Succinyl-CoA_synth-like | 2 |
IPR016103 | 16,103 | ProQ/FinO domain | ProQ/FinO | Domain | 6,730 | false | false | This entry represents a structural domain consisting of six helices in an irregular non-globular array; it also contains two small β-hairpins. This domain is found at the C terminus of the RNA-binding fertility inhibitor FinO that represses the conjugative transfer of F-like plasmids in Escherichia coli. FinO blocks th... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF04352",
"SM00945"
] | [
"ProQ",
"ProQ"
] | [
6045,
6404
] | 2 | [] | [] | [] | 0 | [
"1dvo",
"3mw6",
"5nb9",
"6s10",
"7rgs",
"7rgt",
"7rgu"
] | 7 | [
"PUB00010460",
"PUB00020191"
] | [
"10876242",
"10049386"
] | [
"Crystal structure of the bacterial conjugation repressor finO.",
"Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12."
] | [
2000,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5995,
696,
26,
13
] | 4 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens"
] | [
2,
2,
1
] | 3 | true | Domain | ProQ/FinO domain | ProQ/FinO domain | ProQ/FinO | 1 |
IPR016104 | 16,104 | Pyruvoyl-dependent histidine/arginine decarboxylase | Pyr-dep_his/arg-deCO2ase | Homologous_superfamily | 1,887 | false | false | This entry represents a structural domain found in pyruvoyl-dependent histidine decarboxylase ( ) and arginine decarboxylase ( ). This domain consists of a duplication of a β-α-β(2) motif that forms a 4-layer α/β/β/α topology, which contains a silk-like β-sandwich. This domain contains two chains resulting from self-pr... | [
"GO:0016831",
"GO:0006520"
] | [
"carboxy-lyase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF56271"
] | [
""
] | [
1887
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.1.19",
"PWY-40",
"PWY-43",
"PWY-6834"
] | [
"EC:4.1.1.19",
"METACYC:PWY-40",
"METACYC:PWY-43",
"METACYC:PWY-6834"
] | 4 | [
"1hq6",
"1ibt",
"1ibu",
"1ibv",
"1ibw",
"1mt1",
"1n13",
"1n2m",
"1pya",
"2qqc",
"2qqd"
] | 11 | [
"PUB00025755",
"PUB00027451"
] | [
"11243783",
"12623016"
] | [
"pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a.",
"Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms."
] | [
2001,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
752,
1023,
27,
85
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Pyruvoyl-dependent histidine/arginine decarboxylase | Pyruvoyl-dependent histidine/arginine decarboxylase | Pyr-dep_his/arg-deCO2ase | 5 |
IPR016105 | 16,105 | Pyruvoyl-dependent histidine/arginine decarboxylase, 3-layer sandwich domain | Pyr-dep_his/arg-deCO2ase_sand | Homologous_superfamily | 1,869 | false | false | This entry represents a structural subdomain found in pyruvoyl-dependent histidine decarboxylase ( ) and arginine decarboxylase ( ). This subdomain consists of a 3-layer β-β-α sandwich. These proteins form heterohexamers [ , ]. Histidine decarboxylase catalyses the formation of histamine from histidine. It requires a p... | [
"GO:0016831",
"GO:0006520"
] | [
"carboxy-lyase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.50.20.10"
] | [
""
] | [
1869
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.1.19",
"PWY-40",
"PWY-43",
"PWY-6834"
] | [
"EC:4.1.1.19",
"METACYC:PWY-40",
"METACYC:PWY-43",
"METACYC:PWY-6834"
] | 4 | [
"1hq6",
"1ibt",
"1ibu",
"1ibv",
"1ibw",
"1mt1",
"1n13",
"1n2m",
"1pya",
"2qqc",
"2qqd"
] | 11 | [
"PUB00025755",
"PUB00027451"
] | [
"11243783",
"12623016"
] | [
"pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a.",
"Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms."
] | [
2001,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
750,
1008,
27,
84
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Pyruvoyl-dependent histidine/arginine decarboxylase, 3-layer sandwich domain | Pyruvoyl-dependent histidine/arginine decarboxylase, 3-layer sandwich domain | Pyr-dep_his/arg-deCO2ase_sand | 7 |
IPR016106 | 16,106 | Histidine decarboxylase proenzyme, N-terminal | Pyr-dep_his-deCO2ase_N | Homologous_superfamily | 174 | false | false | This entry represents a structural subdomain found at the N terminus in Histidine decarboxylase proenzyme. This subdomain has an irregular structure containing both β-strand and α-helical regions. These proteins form heterohexamers [ ]. Histidine decarboxylase catalyses the formation of histamine from histidine. It req... | [
"GO:0004398"
] | [
"histidine decarboxylase activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:4.10.510.10"
] | [
""
] | [
174
] | 1 | [
"EC",
"METACYC"
] | [
"4.1.1.22",
"PWY-6173"
] | [
"EC:4.1.1.22",
"METACYC:PWY-6173"
] | 2 | [
"1hq6",
"1ibt",
"1ibu",
"1ibv",
"1ibw",
"1pya"
] | 6 | [
"PUB00025755"
] | [
"11243783"
] | [
"pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcina barkeri",
"marine sediment metagenome"
] | [
168,
3,
2,
1
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Histidine decarboxylase proenzyme, N-terminal | Histidine decarboxylase proenzyme, N-terminal | Pyr-dep_his-deCO2ase_N | 7 |
IPR016107 | 16,107 | Adenovirus Pll, hexon, N-terminal | Adenovirus_Pll_hexon_N | Domain | 7,536 | false | false | Hexon is a major coat protein found in various species-specific Adenoviruses, which are type II dsDNA viruses. Hexon coat proteins are synthesised during late infection and form homo-trimers. The 240 copies of the hexon trimer that are produced are organised so that 12 lie on each of the 20 facets. The central 9 hexons... | [
"GO:0019028"
] | [
"viral capsid"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF01065"
] | [
"Adeno_hexon"
] | [
7536
] | 1 | [] | [] | [] | 0 | [
"1p2z",
"1p30",
"2iny",
"2obe",
"3tg7",
"3zif",
"4v4u",
"5ldn",
"5ogi",
"6b1t",
"6cgv",
"6eqc",
"6qi5",
"6yba",
"6z7n",
"7rd1",
"7s78",
"7tau",
"8q7c",
"8roq",
"9cli",
"9cln",
"9cls",
"9cm2",
"9cm9",
"9cmo",
"9ivx",
"9iw0",
"9lr9"
] | 29 | [
"PUB00003331",
"PUB00022393"
] | [
"7932702",
"12915569"
] | [
"The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 A resolution.",
"Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution x-ray crystallographic, molecular modeling, and sequence-based methods."
] | [
1994,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Adenoviridae"
] | [
7536
] | 1 | [] | [] | 0 | true | Domain | Adenovirus Pll, hexon, N-terminal | Adenovirus Pll, hexon, N-terminal | Adenovirus_Pll_hexon_N | 1 |
IPR016108 | 16,108 | Adenovirus Pll, hexon, C-terminal | Adenovirus_Pll_hexon_C | Domain | 3,145 | false | false | Hexon is a major coat protein found in various species-specific Adenoviruses, which are type II dsDNA viruses. Hexon coat proteins are synthesised during late infection and form homo-trimers. The 240 copies of the hexon trimer that are produced are organised so that 12 lie on each of the 20 facets. The central 9 hexons... | [
"GO:0019028"
] | [
"viral capsid"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF03678"
] | [
"Adeno_hexon_C"
] | [
3145
] | 1 | [] | [] | [] | 0 | [
"1p2z",
"1p30",
"2iny",
"2obe",
"3tg7",
"3zif",
"4v4u",
"5ldn",
"5ogi",
"6b1t",
"6cgv",
"6eqc",
"6qi5",
"6yba",
"6z7n",
"7rd1",
"7s78",
"7tau",
"8q7c",
"8roq",
"9cli",
"9cln",
"9cls",
"9cm2",
"9cm9",
"9cmo",
"9ivx",
"9iw0",
"9lr9"
] | 29 | [
"PUB00003331",
"PUB00022393"
] | [
"7932702",
"12915569"
] | [
"The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 A resolution.",
"Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution x-ray crystallographic, molecular modeling, and sequence-based methods."
] | [
1994,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Adenoviridae"
] | [
3145
] | 1 | [] | [] | 0 | true | Domain | Adenovirus Pll, hexon, C-terminal | Adenovirus Pll, hexon, C-terminal | Adenovirus_Pll_hexon_C | 7 |
IPR016110 | 16,110 | Adenovirus Pll, hexon, subdomain 3 | Adenovirus_Pll_hexon_sub3 | Homologous_superfamily | 5,634 | false | false | Hexon is a major coat protein found in various species-specific Adenoviruses, which are type II dsDNA viruses. Hexon coat proteins are synthesised during late infection and form homo-trimers. The 240 copies of the hexon trimer that are produced are organised so that 12 lie on each of the 20 facets. The central 9 hexons... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.249.10"
] | [
""
] | [
5634
] | 1 | [] | [] | [] | 0 | [
"2iny",
"3zif",
"6qi5",
"6yba",
"6z7n",
"7rd1",
"7tau",
"8roq",
"9ivx",
"9iw0",
"9lr9"
] | 11 | [
"PUB00003331",
"PUB00022393"
] | [
"7932702",
"12915569"
] | [
"The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 A resolution.",
"Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution x-ray crystallographic, molecular modeling, and sequence-based methods."
] | [
1994,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Adenoviridae"
] | [
5634
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Adenovirus Pll, hexon, subdomain 3 | Adenovirus Pll, hexon, subdomain 3 | Adenovirus_Pll_hexon_sub3 | 4 |
IPR016112 | 16,112 | Group II dsDNA virus coat/capsid protein | VP_dsDNA_II | Homologous_superfamily | 14,719 | false | false | Hexon is a major coat protein found in various species-specific Adenoviruses, which are type II dsDNA viruses. Hexon coat proteins are synthesised during late infection and form homo-trimers. The 240 copies of the hexon trimer that are produced are organised so that 12 lie on each of the 20 facets. The central 9 hexons... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF49749"
] | [
""
] | [
14719
] | 1 | [] | [] | [] | 0 | [
"1cjd",
"1gw7",
"1gw8",
"1hb5",
"1hb7",
"1hb9",
"1hqn",
"1hx6",
"1m4x",
"1p2z",
"1p30",
"1w8x",
"2iny",
"2obe",
"3kk5",
"3tg7",
"3zif",
"4v4u",
"5j7o",
"5j7u",
"5j7v",
"5ldn",
"5ogi",
"5tip",
"5tiq",
"6b1t",
"6cgv",
"6eqc",
"6ku9",
"6l2t",
"6ncl",
"6ojn"... | 61 | [
"PUB00003331",
"PUB00010097",
"PUB00022136",
"PUB00022393",
"PUB00028629"
] | [
"7932702",
"10082389",
"12411581",
"12915569",
"11752778"
] | [
"The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 A resolution.",
"Comparison of the major capsid protein genes, terminal redundancies, and DNA-DNA homologies of two New Zealand iridoviruses.",
"The structure and evolution of the major capsid protein of a large, lipid-... | [
1994,
1999,
2002,
2003,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Nocardioides zeae",
"Viruses",
"metagenomes"
] | [
124,
1,
13823,
771
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Group II dsDNA virus coat/capsid protein | Group II dsDNA virus coat/capsid protein | VP_dsDNA_II | 5 |
IPR016115 | 16,115 | Bacteriophage PRD1, P3, N-terminal | Phage_PRD1_P3_N | Homologous_superfamily | 25 | false | false | The major capsid protein P3 from Bacteriophage PRD1 adopts a double-barrel structure comprising two eight-stranded viral β-barrels or jelly rolls, each of which contains a 12-residue α-helix. This protein then trimerises through a 'trimerisation loop' sequence, and is incorporated within the viral capsid [ ]. | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.70.9.30"
] | [
""
] | [
25
] | 1 | [] | [] | [] | 0 | [
"1cjd",
"1gw7",
"1gw8",
"1hb5",
"1hb7",
"1hb9",
"1hqn",
"1hx6",
"1w8x",
"6q5u",
"7ook"
] | 11 | [
"PUB00028629"
] | [
"11752778"
] | [
"The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 A resolution."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Tectiviridae",
"Wuchereria bancrofti",
"marine sediment metagenome"
] | [
12,
11,
1,
1
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Bacteriophage PRD1, P3, N-terminal | Bacteriophage PRD1, P3, N-terminal | Phage_PRD1_P3_N | 8 |
IPR016117 | 16,117 | ArgJ-like domain superfamily | ArgJ-like_dom_sf | Homologous_superfamily | 34,063 | false | false | This superfamily represents a structural domain found in ArgJ, a bifunctional protein that catalyses the first ( ) and fifth ( ) steps in arginine biosynthesis [ ]. The domain also occurs in a number of proteins annotated as DmpA serine peptidases. | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF56266"
] | [
""
] | [
34063
] | 1 | [
"EC",
"EC",
"METACYC"
] | [
"2.3.1.1",
"2.3.1.35",
"PWY-5154"
] | [
"EC:2.3.1.1",
"EC:2.3.1.35",
"METACYC:PWY-5154"
] | 3 | [
"1b65",
"1vra",
"1vz6",
"1vz7",
"1vz8",
"2drh",
"2v4i",
"2vzk",
"2yep",
"3axg",
"3it4",
"3it6",
"3n2w",
"3n33",
"3n5i",
"3ndv",
"3nfb",
"3s3u",
"3tm1",
"3tm2",
"4ihd",
"4ihe",
"5tzb",
"5xyg",
"5xyo",
"5xyp",
"5xyq",
"5xys",
"5xyt",
"5y0l",
"5y0m",
"7yu0"... | 36 | [
"PUB00005708"
] | [
"8473852"
] | [
"Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megamimivirinae",
"unclassified sequences"
] | [
367,
28907,
4061,
16,
712
] | 5 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
4,
1,
2,
1,
1,
9
] | 6 | true | Homologous_superfamily | ArgJ-like domain superfamily | ArgJ-like domain superfamily | ArgJ-like_dom_sf | 8 |
IPR016119 | 16,119 | Bromoperoxidase/chloroperoxidase C-terminal | Br/Cl_peroxidase_C | Homologous_superfamily | 1,983 | false | false | This superfamily represents an α helical domain is found in bromoperoxidases and at the C-terminal of chloroperoxidases, both being haloperoxidases [ ]. The structure of chloroperoxidase from the fungus Curvularia inaequalis consists of a duplication containing two core α-helical bundles arranged as in other family dim... | [
"GO:0004601"
] | [
"peroxidase activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.606.10"
] | [
""
] | [
1983
] | 1 | [
"EC"
] | [
"1.11.1.18"
] | [
"EC:1.11.1.18"
] | 1 | [
"1idq",
"1idu",
"1qhb",
"1qi9",
"1up8",
"1vnc",
"1vne",
"1vnf",
"1vng",
"1vnh",
"1vni",
"1vns",
"3bb0",
"3w35",
"3w36",
"5aa6",
"5lpc",
"7qvw",
"7qw3",
"7qwi",
"7qyy",
"8cxl",
"8q20",
"8q21",
"8q22",
"8vgx",
"8vh0",
"8vix",
"8vjq"
] | 29 | [
"PUB00022515",
"PUB00022835"
] | [
"10843856",
"10499093"
] | [
"Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis.",
"X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis."
] | [
2000,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
19,
1518,
418,
13,
15
] | 5 | [] | [] | 0 | true | Homologous_superfamily | Bromoperoxidase/chloroperoxidase C-terminal | Bromoperoxidase/chloroperoxidase C-terminal | Br/Cl_peroxidase_C | 3 |
IPR016120 | 16,120 | Signal transduction histidine kinase, sporulation regulator SpoOB | Sig_transdc_His_kin_SpoOB | Homologous_superfamily | 14,484 | false | false | Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [ ]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [ ]. These pathways have been adapt... | [
"GO:0000155",
"GO:0016772",
"GO:0000160"
] | [
"phosphorelay sensor kinase activity",
"transferase activity, transferring phosphorus-containing groups",
"phosphorelay signal transduction system"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"SSF"
] | [
"SSF55890"
] | [
""
] | [
14484
] | 1 | [
"EC"
] | [
"2.7.13.3"
] | [
"EC:2.7.13.3"
] | 1 | [
"1f51",
"1ixm",
"2ftk"
] | 3 | [
"PUB00000966",
"PUB00007866",
"PUB00010651",
"PUB00011096",
"PUB00013246",
"PUB00013247",
"PUB00013562",
"PUB00013563",
"PUB00020801",
"PUB00028707",
"PUB00042582",
"PUB00042583",
"PUB00042804",
"PUB00042805",
"PUB00042806",
"PUB00042807"
] | [
"9989504",
"11406410",
"12372152",
"10966457",
"8868347",
"10426948",
"8029829",
"1482126",
"11145881",
"9809070",
"1664534",
"12949160",
"16176121",
"18076326",
"11934609",
"11489844"
] | [
"Structure of CheA, a signal-transducing histidine kinase.",
"Histidine kinases and response regulator proteins in two-component signaling systems.",
"Histidine protein kinases: key signal transducers outside the animal kingdom.",
"Two-component signal transduction.",
"Protein aspartate phosphatases control... | [
1999,
2001,
2002,
2000,
1996,
1999,
1994,
1992,
2000,
1998,
1991,
2003,
2005,
2007,
2002,
2001
] | 16 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
14421,
8,
18,
37
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Homologous_superfamily | Signal transduction histidine kinase, sporulation regulator SpoOB | Signal transduction histidine kinase, sporulation regulator SpoOB | Sig_transdc_His_kin_SpoOB | 8 |
IPR016122 | 16,122 | Sporulation initiation phosphotransferase B, C-terminal | SpoOB_C | Domain | 786 | false | false | Response regulatory proteins such as sensor kinases control a variety of environmentally induced responses in bacteria. SpoOB is a response regulator that responds to nutritional stress by inducing sporulation. SpoOB is a phosphotransferase that acts upon SpoOA using SpoOF as the phosphor-donor. Phosphorylated SpoOA ca... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF14682",
"SM01317"
] | [
"SPOB_ab",
"SPOB_ab"
] | [
783,
676
] | 2 | [] | [] | [] | 0 | [
"1f51",
"1ixm",
"2ftk"
] | 3 | [
"PUB00028707",
"PUB00042582"
] | [
"9809070",
"1664534"
] | [
"Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase.",
"Control of the initiation of sporulation in Bacillus subtilis by a phosphorelay."
] | [
1998,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillales",
"Rhizophagus irregularis"
] | [
785,
1
] | 2 | [] | [] | 0 | true | Domain | Sporulation initiation phosphotransferase B, C-terminal | Sporulation initiation phosphotransferase B, C-terminal | SpoOB_C | 2 |
IPR016125 | 16,125 | Peptidase C15, pyroglutamyl peptidase I-like | Peptidase_C15-like | Family | 13,025 | false | false | This group of cysteine peptidases belong to MEROPS peptidase family C15 (pyroglutamyl peptidase I, clan CF). The type example being pyroglutamyl peptidase I of Bacillus amyloliquefaciens. There are similarities in structure between members of clan CF and members of three clans of metallopeptidases (MC, MF and MH) and a... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF01470",
"PTHR23402"
] | [
"Peptidase_C15",
""
] | [
11802,
12558
] | 2 | [
"EC",
"METACYC"
] | [
"3.4.19.3",
"PWY-7942"
] | [
"EC:3.4.19.3",
"METACYC:PWY-7942"
] | 2 | [
"1a2z",
"1aug",
"1iof",
"1ioi",
"1iu8",
"1x10",
"1x12",
"1z8t",
"1z8w",
"1z8x",
"2df5",
"2ebj",
"2eo8",
"3giu",
"3lac",
"3rnz",
"3ro0",
"4gxh",
"4hps",
"5z40",
"5z47",
"5z48",
"6ltq"
] | 23 | [
"PUB00001639",
"PUB00002244",
"PUB00004992",
"PUB00076955"
] | [
"1353026",
"7909543",
"7824521",
"1999"
] | [
"Characterization of the pcp gene encoding the pyrrolidone carboxyl peptidase of Bacillus subtilis.",
"Characterization of the pcp gene of Pseudomonas fluorescens and of its product, pyrrolidone carboxyl peptidase (Pcp).",
"Pyrrolidone carboxyl peptidase (Pcp): an enzyme that removes pyroglutamic acid (pGlu) fr... | [
1992,
1994,
1994,
1975
] | 4 | [] | [
"IPR000816",
"IPR010381"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
183,
6621,
6177,
44
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
11,
11,
9,
1,
7,
7,
1,
7,
3,
11
] | 10 | true | Family | Peptidase C15, pyroglutamyl peptidase I-like | Peptidase C15, pyroglutamyl peptidase I-like | Peptidase_C15-like | 9 |
IPR016128 | 16,128 | Pyosin/cloacin translocation domain | Pyosin/cloacin_T_dom | Domain | 2,374 | false | false | This entry represents a structural domain with a complex fold made of several coiled β-sheets. This domain is found at the N-terminal of both colicin E3 and colicin B, and acts as a translocation domain. It also occurs in S-type pyocin. Both pyocin and cloacin are bacteriocins, protein antibiotics that kill bacteria cl... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF03515",
"PF06958"
] | [
"Cloacin",
"Pyocin_S"
] | [
377,
2117
] | 2 | [] | [] | [] | 0 | [
"1jch",
"1rh1",
"2axc",
"2b5u",
"3mfb",
"5ew5",
"5znm",
"7nst",
"7nsu"
] | 9 | [
"PUB00014774"
] | [
"12409205"
] | [
"Colicin crystal structures: pathways and mechanisms for colicin insertion into membranes."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
2374
] | 1 | [] | [] | 0 | true | Domain | Pyosin/cloacin translocation domain | Pyosin/cloacin translocation domain | Pyosin/cloacin_T_dom | 3 |
IPR016129 | 16,129 | Peptidase family C14A, His active site | Caspase_his_AS | Active_site | 11,695 | false | false | Interleukin-1 beta converting enzyme ( ) (ICE) [ , ] is responsible for the cleavage of the IL-1 beta precursor at an Asp-Ala bond to generate the mature biologically active cytokine. ICE a thiol protease composed of two subunits of 10 (p10) and 20 Kd (p20), both derived by the autocleavage of a 45 Kd precursor (p45). ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01121"
] | [
"CASPASE_HIS"
] | [
11695
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.22",
"PDOC00864",
"R-BTA-5620971",
"R-CEL-111465",
"R-CEL-140342",
"R-CEL-198323",
"R-CEL-2028269",
"R-CEL-264870",
"R-CEL-351906",
"R-CEL-418889",
"R-CEL-5357905",
"R-DME-111458",
"R-DME-111459",
"R-DME-111465",
"R-DME-111469",
"R-DME-140342",
"R-DME-198323",
"R-DME-2028269",... | [
"EC:3.4.22",
"PROSITEDOC:PDOC00864",
"REACTOME:R-BTA-5620971",
"REACTOME:R-CEL-111465",
"REACTOME:R-CEL-140342",
"REACTOME:R-CEL-198323",
"REACTOME:R-CEL-2028269",
"REACTOME:R-CEL-264870",
"REACTOME:R-CEL-351906",
"REACTOME:R-CEL-418889",
"REACTOME:R-CEL-5357905",
"REACTOME:R-DME-111458",
"R... | 139 | [
"1bmq",
"1cp3",
"1f1j",
"1f9e",
"1gfw",
"1gqf",
"1i3o",
"1i4e",
"1i4o",
"1i51",
"1ibc",
"1ice",
"1jxq",
"1k86",
"1k88",
"1kmc",
"1m72",
"1nme",
"1nmq",
"1nms",
"1nw9",
"1pau",
"1pyo",
"1qdu",
"1qtn",
"1qx3",
"1re1",
"1rhj",
"1rhk",
"1rhm",
"1rhq",
"1rhr"... | 316 | [
"PUB00000943",
"PUB00005031",
"PUB00005441",
"PUB00005470"
] | [
"8861900",
"7773174",
"7610484",
"9270303"
] | [
"Human ICE/CED-3 protease nomenclature.",
"Interleukin-1 beta converting enzyme: a novel cysteine protease required for IL-1 beta production and implicated in programmed cell death.",
"ICE-like proteases in apoptosis.",
"Caspases: killer proteases."
] | [
1996,
1995,
1995,
1997
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
34,
11659,
2
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
40,
4,
44,
29,
43
] | 6 | true | Active_site | Peptidase family C14A, His active site | Peptidase family C14A, His active site | Caspase_his_AS | 7 |
IPR016130 | 16,130 | Protein-tyrosine phosphatase, active site | Tyr_Pase_AS | Active_site | 194,529 | false | false | This entry includes proteins of two subfamilies: Ser/Thr ( ) and Tyr dual specificity protein phosphatase and tyrosine specific protein phosphatase ( ). Both of these subfamilies may also have inactive phosphatase domains, and dependent on the domain composition this loss of catalytic activity has different effects on ... | [
"GO:0016311"
] | [
"dephosphorylation"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS00383"
] | [
"TYR_PHOSPHATASE_1"
] | [
194529
] | 1 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"3.1.3",
"3.1.3.48",
"PDOC00323",
"R-BTA-112409",
"R-BTA-1483248",
"R-BTA-1660499",
"R-BTA-1660516",
"R-BTA-1660517",
"R-BTA-388844",
"R-BTA-5675221",
"R-BTA-77387",
"R-BTA-8849932",
"R-CEL-112409",
"R-CEL-1483248",
"R-CEL-1660499",
"R-CEL-1660516",
"R-CEL-1660517",
"R-CEL-182971",... | [
"EC:3.1.3",
"EC:3.1.3.48",
"PROSITEDOC:PDOC00323",
"REACTOME:R-BTA-112409",
"REACTOME:R-BTA-1483248",
"REACTOME:R-BTA-1660499",
"REACTOME:R-BTA-1660516",
"REACTOME:R-BTA-1660517",
"REACTOME:R-BTA-388844",
"REACTOME:R-BTA-5675221",
"REACTOME:R-BTA-77387",
"REACTOME:R-BTA-8849932",
"REACTOME:R... | 427 | [
"1a5y",
"1bzc",
"1bzh",
"1bzj",
"1c83",
"1c84",
"1c85",
"1c86",
"1c87",
"1c88",
"1d5r",
"1ecv",
"1g4u",
"1g4w",
"1g7f",
"1g7g",
"1gfy",
"1gwz",
"1i9s",
"1i9t",
"1jf7",
"1jln",
"1kak",
"1kav",
"1l8g",
"1l8k",
"1lar",
"1lqf",
"1nl9",
"1nny",
"1no6",
"1nwe"... | 765 | [
"PUB00014502"
] | [
"14739250"
] | [
"Evolution of the multifunctional protein tyrosine phosphatase family."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
405,
17184,
176130,
464,
346
] | 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",... | [
79,
84,
696,
83,
1,
328,
242,
13,
52,
371,
10,
7,
126
] | 13 | true | Active_site | Protein-tyrosine phosphatase, active site | Protein-tyrosine phosphatase, active site | Tyr_Pase_AS | 9 |
IPR016131 | 16,131 | Haemerythrin, iron-binding site | Haemerythrin_Fe_BS | Binding_site | 5,042 | false | false | The hemerythrin family is composed of hemerythrin proteins found in invertebrates, and a broader collection of bacterial and archaeal homologues. Hemerythrin is an oxygen-binding protein found in the vascular system and coelomic fluid, or in muscles (myohemerythrin) in invertebrates [ ]. Many of the homologous proteins... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00550"
] | [
"HEMERYTHRINS"
] | [
5042
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00476"
] | [
"PROSITEDOC:PDOC00476"
] | 1 | [
"1a7d",
"1a7e",
"1hmd",
"1hmo",
"1hrb",
"1i4y",
"1i4z",
"2avk",
"2awc",
"2awy",
"2hmq",
"2hmz",
"2mhr",
"3agt",
"3agu",
"3waq",
"3whn",
"4xpw",
"4xpx",
"4xpy",
"4xq1"
] | 21 | [
"PUB00001429",
"PUB00001615",
"PUB00003224",
"PUB00004613",
"PUB00005066"
] | [
"1425663",
"2065779",
"3681996",
"3856224",
"2362933"
] | [
"Ovohemerythrin, a major 14-kDa yolk protein distinct from vitellogenin in leech.",
"Primary structure of myohemerythrin from the annelid Nereis diversicolor.",
"Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution.",
"Active site structures of deoxyhemerythrin and oxyhemerythrin.",
"Th... | [
1992,
1991,
1987,
1985,
1990
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
41,
4538,
346,
117
] | 4 | [] | [] | 0 | true | Binding_site | Haemerythrin, iron-binding site | Haemerythrin, iron-binding site | Haemerythrin_Fe_BS | 5 |
IPR016132 | 16,132 | Phytochrome chromophore attachment domain | Phyto_chromo_attachment | Domain | 24,211 | false | false | Phytochrome [ , , ] is a plant protein that acts as a regulatory photoreceptor and which mediates red-light effects on a wide variety of physiological and molecular responses. Phytochrome can undergo a reversible photochemical conversion between a biologically inactive red light-absorbing form and the active far-red li... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50046"
] | [
"PHYTOCHROME_2"
] | [
24211
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00218"
] | [
"PROSITEDOC:PDOC00218"
] | 1 | [
"1ztu",
"2k2n",
"2kli",
"2koi",
"2lb5",
"2lb9",
"2m7u",
"2m7v",
"2o9b",
"2o9c",
"2ool",
"2vea",
"3c2w",
"3g6o",
"3ibr",
"3nhq",
"3nop",
"3not",
"3nou",
"3s7n",
"3s7o",
"3s7p",
"3s7q",
"3vv4",
"3w2z",
"3zq5",
"4bwi",
"4cqh",
"4e04",
"4fof",
"4glq",
"4gw9"... | 208 | [
"PUB00000104",
"PUB00000736",
"PUB00097030"
] | [
"1812812",
"9230690",
"27789797"
] | [
"Phytochrome: a light-activated molecular switch that regulates plant gene expression.",
"The phytochromes: a biochemical mechanism of signaling in sight?",
"Phytochromes function as thermosensors in Arabidopsis."
] | [
1991,
1997,
2016
] | 3 | [
"IPR003018"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Phaeovirus",
"unclassified sequences"
] | [
10746,
13442,
4,
3,
16
] | 5 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
78,
2,
36,
42
] | 4 | true | Domain | Phytochrome chromophore attachment domain | Phytochrome chromophore attachment domain | Phyto_chromo_attachment | 2 |
IPR016133 | 16,133 | Insect cysteine-rich antifreeze protein | Insect_cyst_antifreeze_prot | Homologous_superfamily | 471 | false | false | Antifreeze proteins (AFPs) are a class of proteins that are able to bind to and inhibit the growth of macromolecular ice, thereby permitting an organism to survive subzero temperatures by decreasing the probability of ice nucleation in their bodies [ ]. These proteins have been characterised from a variety of organisms... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51156"
] | [
""
] | [
471
] | 1 | [] | [] | [] | 0 | [
"1ezg",
"1l1i"
] | 2 | [
"PUB00015093",
"PUB00015094"
] | [
"10917536",
"15291806"
] | [
"Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein.",
"Cold survival in freeze-intolerant insects: the structure and function of beta-helical antifreeze proteins."
] | [
2000,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
33,
422,
16
] | 3 | [
"Arabidopsis thaliana",
"Mus musculus"
] | [
1,
1
] | 2 | true | Homologous_superfamily | Insect cysteine-rich antifreeze protein | Insect cysteine-rich antifreeze protein | Insect_cyst_antifreeze_prot | 3 |
IPR016134 | 16,134 | Dockerin domain | Dockerin_dom | Domain | 7,112 | false | false | Plant cell wall polysaccharides comprise the most abundant reservoir of organic carbon in the biosphere. The cellulosome is a large multienzyme complex used by many anaerobic bacteria for the efficient degradation of plant-cell wall polysaccharides. The principal component of the cellulosome is a scaffolding subunit, a... | [
"GO:0000272"
] | [
"polysaccharide catabolic process"
] | [
"biological_process"
] | 1 | [
"PROFILE"
] | [
"PS51766"
] | [
"DOCKERIN"
] | [
7112
] | 1 | [
"EC"
] | [
"3.2.1"
] | [
"EC:3.2.1"
] | 1 | [
"1clc",
"1daq",
"1dav",
"1ohz",
"2b59",
"2ccl",
"2jnk",
"2mte",
"2ozn",
"2vn5",
"2vn6",
"2y3n",
"2yik",
"3kcp",
"3ul4",
"4cj0",
"4cj1",
"4dh2",
"4fl4",
"4u3s",
"4uyp",
"4uyq",
"4wi0",
"5g5d",
"5k39",
"5lxv",
"5m0y",
"5m2o",
"5m2s",
"5nrk",
"5nrm",
"6kg9"... | 42 | [
"PUB00039522",
"PUB00077745",
"PUB00077746",
"PUB00077747"
] | [
"16384918",
"9408948",
"15487947",
"25270376"
] | [
"Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex.",
"Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain.",
... | [
2006,
1997,
2004,
2014
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
435,
6307,
4,
50,
316
] | 5 | [] | [] | 0 | true | Domain | Dockerin domain | Dockerin domain | Dockerin_dom | 4 |
IPR016135 | 16,135 | Ubiquitin-conjugating enzyme/RWD-like | UBQ-conjugating_enzyme/RWD | Homologous_superfamily | 186,859 | false | false | This superfamily represents a structural domain with an α-β(4)-α(3) core fold. Domains of this structure are found in: Ubiquitin conjugating enzyme E2, as well as related proteins such as ubiquitin carrier protein 4 and ubiquitin-protein ligase W [ ]. The UEV domain in tumour susceptibility gene 101 [ ] and vacuolar pr... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.10.110.10",
"SSF54495"
] | [
"",
""
] | [
184297,
182929
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.3.2",
"R-BTA-110314",
"R-BTA-1169408",
"R-BTA-1234176",
"R-BTA-141430",
"R-BTA-174048",
"R-BTA-174084",
"R-BTA-174154",
"R-BTA-174178",
"R-BTA-174184",
"R-BTA-176407",
"R-BTA-176408",
"R-BTA-176409",
"R-BTA-176412",
"R-BTA-179409",
"R-BTA-201451",
"R-BTA-202424",
"R-BTA-2173789"... | [
"EC:2.3.2",
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-141430",
"REACTOME:R-BTA-174048",
"REACTOME:R-BTA-174084",
"REACTOME:R-BTA-174154",
"REACTOME:R-BTA-174178",
"REACTOME:R-BTA-174184",
"REACTOME:R-BTA-176407",
"REACTOME:R-BTA-176408",
"RE... | 483 | [
"1a3s",
"1ayz",
"1c4z",
"1fbv",
"1fxt",
"1fzy",
"1i7k",
"1j74",
"1j7d",
"1jas",
"1jat",
"1jbb",
"1kpp",
"1kpq",
"1kps",
"1m4p",
"1m4q",
"1pzv",
"1q34",
"1qcq",
"1s1q",
"1tte",
"1u9a",
"1u9b",
"1ukx",
"1ur6",
"1uzx",
"1w4u",
"1wzv",
"1wzw",
"1x23",
"1y6l"... | 546 | [
"PUB00020283",
"PUB00026321",
"PUB00031958",
"PUB00040485",
"PUB00042603"
] | [
"15273307",
"11885984",
"15044434",
"16552148",
"17825256"
] | [
"Solution structure of the RWD domain of the mouse GCN2 protein.",
"The NMR structure of the class I human ubiquitin-conjugating enzyme 2b.",
"Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins.",
"Structure of human TSG101 UEV domain.",
... | [
2004,
2002,
2004,
2006,
2007
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
36,
620,
185679,
217,
307
] | 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... | [
243,
41,
142,
93,
266,
214,
25,
180,
239,
19,
19,
505
] | 12 | true | Homologous_superfamily | Ubiquitin-conjugating enzyme/RWD-like | Ubiquitin-conjugating enzyme/RWD-like | UBQ-conjugating_enzyme/RWD | 2 |
IPR016136 | 16,136 | DNA helicase DnaB, N-terminal/DNA primase DnaG, C-terminal | DNA_helicase_N/primase_C | Homologous_superfamily | 46,557 | false | false | This superfamily represents a structural domain with a multi-helical structure that forms an orthogonal bundle; a segment-swapped dimer. This domain is found at the N-terminal of the DNA helicase DnaB [ ] and replicative DNA helicase DnaC, as well as at the C-terminal of the DNA primase DnaG [ ]. The hexameric helicase... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.860.10"
] | [
""
] | [
46557
] | 1 | [] | [] | [] | 0 | [
"1b79",
"1jwe",
"1t3w",
"1z8s",
"2haj",
"2lzn",
"2q6t",
"2r5u",
"2r6a",
"2r6c",
"2r6d",
"2r6e",
"2vye",
"2vyf",
"3bgw",
"3gxv",
"4ehs",
"4esv",
"4im9",
"4m4w",
"4nmn",
"4zc0",
"6bbm",
"6cbr",
"6cbs",
"6cbt",
"6qel",
"6qem",
"6t66",
"7qxm",
"7t20",
"7t21"... | 38 | [
"PUB00017119",
"PUB00019435",
"PUB00031319"
] | [
"8308039",
"10404598",
"15649896"
] | [
"Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork.",
"Crystal structure of the N-terminal domain of the DnaB hexameric helicase.",
"Crystal and solution structures of the helicase-binding domain of Escherichia coli primase.... | [
1994,
1999,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
6,
44579,
473,
485,
1014
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Homologous_superfamily | DNA helicase DnaB, N-terminal/DNA primase DnaG, C-terminal | DNA helicase DnaB, N-terminal/DNA primase DnaG, C-terminal | DNA_helicase_N/primase_C | 3 |
IPR016137 | 16,137 | RGS domain | RGS | Domain | 69,598 | false | false | This entry represents a structural domain with a multi-helical fold consisting of a 4-helical bundle with a left-handed twist and an up-and-down topology. This domain can be divided into two all-α subdomains. This domain is found in regulation of G-protein signalling (RGS) proteins, as well as other related proteins, i... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00615",
"PR01301",
"PS50132",
"SM00315"
] | [
"RGS",
"RGSPROTEIN",
"RGS",
"RGS"
] | [
64955,
34638,
67672,
63094
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-111933",
"R-BTA-2514859",
"R-BTA-416476",
"R-BTA-418555",
"R-BTA-418594",
"R-BTA-418597",
"R-BTA-5635838",
"R-BTA-6814122",
"R-BTA-8856825",
"R-CEL-111933",
"R-CEL-195253",
"R-CEL-196299",
"R-CEL-2514859",
"R-CEL-416476",
"R-CEL-418594",
"R-CEL-418597",
"R-CEL-4641262",
"R-C... | [
"REACTOME:R-BTA-111933",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-418597",
"REACTOME:R-BTA-5635838",
"REACTOME:R-BTA-6814122",
"REACTOME:R-BTA-8856825",
"REACTOME:R-CEL-111933",
"REACTOME:R-CEL-195253",
"REACTOME:R-CEL... | 135 | [
"1agr",
"1cmz",
"1dk8",
"1emu",
"1ezt",
"1ezy",
"1fqi",
"1fqj",
"1fqk",
"1htj",
"1omw",
"1ym7",
"1zv4",
"2a72",
"2acx",
"2af0",
"2bcj",
"2bt2",
"2bv1",
"2crp",
"2d9j",
"2dlr",
"2dlv",
"2ebz",
"2es0",
"2gtp",
"2i59",
"2ihb",
"2ihd",
"2ik8",
"2jm5",
"2jnu"... | 132 | [
"PUB00000946",
"PUB00021520",
"PUB00023994",
"PUB00024994",
"PUB00025791",
"PUB00028666",
"PUB00029494"
] | [
"9108480",
"10811618",
"10452897",
"11234020",
"11470431",
"11524686",
"12764189"
] | [
"Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis.",
"Structural basis of the Axin-adenomatous polyposis coli interaction.",
"Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling.",
"Structural determi... | [
1997,
2000,
1999,
2001,
2001,
2001,
2003
] | 7 | [] | [
"IPR015212",
"IPR034483",
"IPR034949",
"IPR034951",
"IPR034953",
"IPR034956",
"IPR037879",
"IPR037880",
"IPR037881",
"IPR037892",
"IPR037896",
"IPR037956",
"IPR047077",
"IPR048073",
"IPR048074",
"IPR048075"
] | 0 | 16 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"marine metagenome"
] | [
182,
69400,
14,
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)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizo... | [
10,
40,
229,
27,
181,
150,
5,
183,
3,
3
] | 10 | true | Domain | RGS domain | RGS domain | RGS | 9 |
IPR016138 | 16,138 | Ribosome-inactivating protein, subdomain 1 | Ribosome_inactivat_prot_sub1 | Homologous_superfamily | 3,665 | false | false | A number of bacterial and plant toxins act by inhibiting protein synthesis in eukaryotic cells. The toxins of the shiga and ricin family inactivate 60S ribosomal subunits by an N-glycosidic cleavage which releases a specific adenine base from the sugar-phosphate backbone of 28S rRNA [ , , ]. Members of the family inclu... | [
"GO:0030598",
"GO:0017148"
] | [
"rRNA N-glycosylase activity",
"negative regulation of translation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.420.10"
] | [
""
] | [
3665
] | 1 | [
"EC"
] | [
"3.2.2.22"
] | [
"EC:3.2.2.22"
] | 1 | [
"1abr",
"1aha",
"1ahb",
"1ahc",
"1apa",
"1br5",
"1br6",
"1bry",
"1ce7",
"1cf5",
"1d6a",
"1d8v",
"1dm0",
"1f8q",
"1ggp",
"1gik",
"1gis",
"1giu",
"1hwm",
"1hwn",
"1hwo",
"1hwp",
"1ifs",
"1ift",
"1ifu",
"1il3",
"1il4",
"1il5",
"1il9",
"1j1m",
"1j1q",
"1j1r"... | 309 | [
"PUB00000690",
"PUB00001175",
"PUB00001357",
"PUB00003312",
"PUB00004654",
"PUB00004990"
] | [
"1742358",
"2714255",
"3276522",
"8411176",
"3357883",
"8066085"
] | [
"Conserved amino acid residues in ribosome-inactivating proteins from plants.",
"Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides.",
"Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosome... | [
1991,
1989,
1988,
1993,
1988,
1994
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
658,
2906,
101
] | 3 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
108,
37
] | 2 | true | Homologous_superfamily | Ribosome-inactivating protein, subdomain 1 | Ribosome-inactivating protein, subdomain 1 | Ribosome_inactivat_prot_sub1 | 2 |
IPR016139 | 16,139 | Ribosome-inactivating protein, subdomain 2 | Ribosome_inactivat_prot_sub2 | Homologous_superfamily | 1,812 | false | false | A number of bacterial and plant toxins act by inhibiting protein synthesis in eukaryotic cells. The toxins of the shiga and ricin family inactivate 60S ribosomal subunits by an N-glycosidic cleavage which releases a specific adenine base from the sugar-phosphate backbone of 28S rRNA [ , , ]. Members of the family inclu... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:4.10.470.10"
] | [
""
] | [
1812
] | 1 | [
"EC"
] | [
"3.2.2.22"
] | [
"EC:3.2.2.22"
] | 1 | [
"1abr",
"1aha",
"1ahb",
"1ahc",
"1apa",
"1br5",
"1br6",
"1bry",
"1ce7",
"1cf5",
"1d6a",
"1d8v",
"1dm0",
"1f8q",
"1ggp",
"1gik",
"1gis",
"1giu",
"1hwm",
"1hwn",
"1hwo",
"1hwp",
"1ifs",
"1ift",
"1ifu",
"1il3",
"1il4",
"1il5",
"1il9",
"1j1m",
"1j1q",
"1j1r"... | 305 | [
"PUB00000690",
"PUB00001175",
"PUB00001357",
"PUB00003312",
"PUB00004654",
"PUB00004990"
] | [
"1742358",
"2714255",
"3276522",
"8411176",
"3357883",
"8066085"
] | [
"Conserved amino acid residues in ribosome-inactivating proteins from plants.",
"Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides.",
"Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosome... | [
1991,
1989,
1988,
1993,
1988,
1994
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
310,
1405,
97
] | 3 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
21
] | 2 | true | Homologous_superfamily | Ribosome-inactivating protein, subdomain 2 | Ribosome-inactivating protein, subdomain 2 | Ribosome_inactivat_prot_sub2 | 9 |
IPR016142 | 16,142 | Citrate synthase-like, large alpha subdomain | Citrate_synth-like_lrg_a-sub | Homologous_superfamily | 59,777 | false | false | This entry represents the large α-helical domain from type I and II citrate synthase enzymes, as well as a homologous domain found in the related enzyme 2-methylcitrate synthase. 2-Methylcitrate ( ) synthase catalyses the conversion of oxaloacetate and propanoyl-CoA into (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate and... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.580.10"
] | [
""
] | [
59777
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"2.3.3",
"2.3.3.16",
"R-BTA-6798695",
"R-BTA-71403",
"R-BTA-75105",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-6798695",
"R-CEL-71403",
"R-CEL-75105",
"R-CEL-9837999",
"R-DDI-6798695",
"R-DDI-71403",
"R-DDI-75105",
"R-DDI-9837999",
"R-DME-71403",
"R-DME-9837999",
"R-DRE-71403",
"R-... | [
"EC:2.3.3",
"EC:2.3.3.16",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-75105",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-75105",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-6798695",
"REACTOME:R-D... | 41 | [
"1a59",
"1aj8",
"1al6",
"1amz",
"1csc",
"1csh",
"1csi",
"1csr",
"1css",
"1cts",
"1iom",
"1ixe",
"1nxe",
"1nxg",
"1o7x",
"1owb",
"1owc",
"1vgm",
"1vgp",
"2c6x",
"2csc",
"2cts",
"2h12",
"2ibp",
"2ifc",
"2p2w",
"2r26",
"2r9e",
"3csc",
"3enj",
"3hwk",
"3msu"... | 118 | [
"PUB00013490",
"PUB00042604",
"PUB00042605"
] | [
"9579066",
"15147839",
"17087502"
] | [
"Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships.",
"Investigating the accessibility of the closed domain conformation of citrate synthase using essential dynamics sampling.",
"Structure of a NADH-insensitive hexameric citrate synthase that resists acid inact... | [
1998,
2004,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"unclassified sequences"
] | [
861,
45367,
12753,
5,
791
] | 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",... | [
30,
8,
10,
7,
2,
24,
7,
2,
16,
10,
3,
1,
46
] | 13 | true | Homologous_superfamily | Citrate synthase-like, large alpha subdomain | Citrate synthase-like, large alpha subdomain | Citrate_synth-like_lrg_a-sub | 3 |
IPR016143 | 16,143 | Citrate synthase-like, small alpha subdomain | Citrate_synth-like_sm_a-sub | Homologous_superfamily | 60,367 | false | false | This entry represents the small α-helical domain from type I and II citrate synthase enzymes, as well as a homolgous domain found in the related enzyme ATP citrate synthase. ATP citrate synthase ( ) (also known as ATP citrate lyase) catalyses the MgATP-dependent, CoA-dependent cleavage of citrate into oxaloacetate and ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.230.10"
] | [
""
] | [
60367
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"2.3.3",
"2.3.3.16",
"R-BTA-6798695",
"R-BTA-71403",
"R-BTA-75105",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-6798695",
"R-CEL-71403",
"R-CEL-75105",
"R-CEL-9837999",
"R-DDI-6798695",
"R-DDI-71403",
"R-DDI-75105",
"R-DDI-9837999",
"R-DME-71403",
"R-DME-9837999",
"R-DRE-71403",
"R-... | [
"EC:2.3.3",
"EC:2.3.3.16",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-75105",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-75105",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-6798695",
"REACTOME:R-D... | 46 | [
"1a59",
"1aj8",
"1al6",
"1amz",
"1csc",
"1csh",
"1csi",
"1csr",
"1css",
"1cts",
"1iom",
"1ixe",
"1nxe",
"1nxg",
"1o7x",
"1owb",
"1owc",
"1vgm",
"1vgp",
"2c6x",
"2csc",
"2cts",
"2h12",
"2ibp",
"2ifc",
"2p2w",
"2r26",
"2r9e",
"3csc",
"3enj",
"3hwk",
"3msu"... | 140 | [
"PUB00042604",
"PUB00042605",
"PUB00042606",
"PUB00042607"
] | [
"15147839",
"17087502",
"16952946",
"16007201"
] | [
"Investigating the accessibility of the closed domain conformation of citrate synthase using essential dynamics sampling.",
"Structure of a NADH-insensitive hexameric citrate synthase that resists acid inactivation.",
"Both subunits of ATP-citrate lyase from Chlorobium tepidum contribute to catalytic activity."... | [
2004,
2006,
2006,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"unclassified sequences"
] | [
842,
44567,
14293,
5,
660
] | 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",... | [
30,
24,
13,
8,
2,
9,
11,
3,
15,
14,
3,
2,
40
] | 13 | true | Homologous_superfamily | Citrate synthase-like, small alpha subdomain | Citrate synthase-like, small alpha subdomain | Citrate_synth-like_sm_a-sub | 1 |
IPR016147 | 16,147 | Pili assembly chaperone, N-terminal | Pili_assmbl_chaperone_N | Domain | 25,292 | false | false | Most Gram-negative bacteria possess a supramolecular structure - the pili - on their surface, which mediates attachment to specific receptors. Many interactive subunits are required to assemble pili, but their assembly only takes place after translocation across the cytoplasmic membrane. Periplasmic chaperones assist p... | [
"GO:0071555",
"GO:0030288"
] | [
"cell wall organization",
"outer membrane-bounded periplasmic space"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00345"
] | [
"PapD_N"
] | [
25292
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00552"
] | [
"PROSITEDOC:PDOC00552"
] | 1 | [
"1bf8",
"1kiu",
"1klf",
"1l4i",
"1n0l",
"1p5u",
"1p5v",
"1pdk",
"1qpp",
"1qpx",
"1qun",
"1z9s",
"1ze3",
"2co6",
"2co7",
"2j2z",
"2j7l",
"2os7",
"2uy6",
"2uy7",
"2w07",
"2wmp",
"2xg4",
"2xg5",
"3bwu",
"3dos",
"3dpa",
"3dpb",
"3dsn",
"3f65",
"3f6i",
"3f6l"... | 70 | [
"PUB00000121",
"PUB00001218",
"PUB00001290",
"PUB00020121",
"PUB00041859",
"PUB00098587"
] | [
"1683764",
"1348692",
"8670884",
"2478891",
"17082819",
"27353649"
] | [
"Chaperone-assisted assembly and molecular architecture of adhesive pili.",
"Conserved immunoglobulin-like features in a family of periplasmic pilus chaperones in bacteria.",
"Molecular basis of two subfamilies of immunoglobulin-like chaperones.",
"Crystal structure of chaperone protein PapD reveals an immuno... | [
1991,
1992,
1996,
1989,
2006,
2016
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
25222,
39,
31
] | 3 | [
"Escherichia coli (strain K12)"
] | [
11
] | 1 | true | Domain | Pili assembly chaperone, N-terminal | Pili assembly chaperone, N-terminal | Pili_assmbl_chaperone_N | 8 |
IPR016148 | 16,148 | Pili assembly chaperone, C-terminal | Pili_assmbl_chaperone_C | Domain | 19,777 | false | false | Most Gram-negative bacteria possess a supramolecular structure - the pili - on their surface, which mediates attachment to specific receptors. Many interactive subunits are required to assemble pili, but their assembly only takes place after translocation across the cytoplasmic membrane. Periplasmic chaperones assist p... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02753"
] | [
"PapD_C"
] | [
19777
] | 1 | [] | [] | [] | 0 | [
"1bf8",
"1kiu",
"1klf",
"1l4i",
"1n0l",
"1p5u",
"1p5v",
"1pdk",
"1qpp",
"1qpx",
"1qun",
"1z9s",
"1ze3",
"2co6",
"2co7",
"2j2z",
"2j7l",
"2os7",
"2uy6",
"2uy7",
"2w07",
"2wmp",
"2xg4",
"2xg5",
"3bwu",
"3dos",
"3dpa",
"3dpb",
"3dsn",
"3jwn",
"3me0",
"3q48"... | 61 | [
"PUB00000121",
"PUB00001218",
"PUB00001290",
"PUB00041859",
"PUB00098587"
] | [
"1683764",
"1348692",
"8670884",
"17082819",
"27353649"
] | [
"Chaperone-assisted assembly and molecular architecture of adhesive pili.",
"Conserved immunoglobulin-like features in a family of periplasmic pilus chaperones in bacteria.",
"Molecular basis of two subfamilies of immunoglobulin-like chaperones.",
"Molecular mechanism of P pilus termination in uropathogenic E... | [
1991,
1992,
1996,
2006,
2016
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
19739,
28,
10
] | 3 | [
"Escherichia coli (strain K12)"
] | [
10
] | 1 | true | Domain | Pili assembly chaperone, C-terminal | Pili assembly chaperone, C-terminal | Pili_assmbl_chaperone_C | 1 |
IPR016149 | 16,149 | Casein kinase II, regulatory subunit, N-terminal | Casein_kin_II_reg-sub_N | Homologous_superfamily | 9,423 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0019887",
"GO:0005956"
] | [
"protein kinase regulator activity",
"protein kinase CK2 complex"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.1820.10"
] | [
""
] | [
9423
] | 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-1483191",
"R-BTA-201688",
"R-BTA-2514853",
"R-BTA-6798695",
"R-BTA-6804756",
"R-BTA-6814122",
"R-BTA-8934903",
"R-BTA-8939243",
"R-BTA-8948751",
"R-BTA-9768727",
"R-CEL-1483191",
"R-CEL-201688",
"R-CEL-445144",
"R-CEL-6798695",
"R-CEL-6804756",
"R-CEL-6814122",
"R-CEL-8934903"... | [
"REACTOME:R-BTA-1483191",
"REACTOME:R-BTA-201688",
"REACTOME:R-BTA-2514853",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6804756",
"REACTOME:R-BTA-6814122",
"REACTOME:R-BTA-8934903",
"REACTOME:R-BTA-8939243",
"REACTOME:R-BTA-8948751",
"REACTOME:R-BTA-9768727",
"REACTOME:R-CEL-1483191",
"REACTOME... | 93 | [
"1jwh",
"1qf8",
"1rqf",
"2r6m",
"3eed",
"4dgl",
"4md7",
"4md8",
"4md9",
"4nh1"
] | 10 | [
"PUB00001376",
"PUB00002646",
"PUB00002858",
"PUB00002899",
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899"
] | [
"2666134",
"1856204",
"8027080",
"7737972",
"3291115",
"12368087",
"12471243",
"15078142",
"15320712"
] | [
"Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta.",
"Structure of the gene encoding human casein kinase II subunit beta.",
"Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta'-subunit of Saccharomyces cerevisiae casein k... | [
1989,
1991,
1994,
1995,
1988,
2002,
2002,
2004,
2004
] | 9 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9423
] | 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... | [
25,
1,
2,
23,
19,
12,
2,
10,
10,
2,
2,
27
] | 12 | true | Homologous_superfamily | Casein kinase II, regulatory subunit, N-terminal | Casein kinase II, regulatory subunit, N-terminal | Casein_kin_II_reg-sub_N | 5 |
IPR016151 | 16,151 | DNA mismatch repair protein MutS, N-terminal | DNA_mismatch_repair_MutS_N | Homologous_superfamily | 42,672 | false | false | Mismatch repair contributes to the overall fidelity of DNA replication and is essential for combating the adverse effects of damage to the genome. It involves the correction of mismatched base pairs that have been missed by the proofreading element of the DNA polymerase complex. The post-replicative Mismatch Repair Sys... | [
"GO:0005524",
"GO:0030983",
"GO:0006298"
] | [
"ATP binding",
"mismatched DNA binding",
"mismatch repair"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.40.1170.10",
"SSF55271"
] | [
"",
""
] | [
42602,
38165
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5358565",
"R-BTA-5358606",
"R-DDI-5358565",
"R-DDI-5358606",
"R-DME-5358565",
"R-HSA-5358565",
"R-HSA-5358606",
"R-HSA-5632927",
"R-HSA-5632928",
"R-HSA-5632968",
"R-HSA-6796648",
"R-MMU-5358565",
"R-MMU-5358606",
"R-RNO-5358565",
"R-SCE-5358565",
"R-SCE-5358606",
"R-SPO-53585... | [
"REACTOME:R-BTA-5358565",
"REACTOME:R-BTA-5358606",
"REACTOME:R-DDI-5358565",
"REACTOME:R-DDI-5358606",
"REACTOME:R-DME-5358565",
"REACTOME:R-HSA-5358565",
"REACTOME:R-HSA-5358606",
"REACTOME:R-HSA-5632927",
"REACTOME:R-HSA-5632928",
"REACTOME:R-HSA-5632968",
"REACTOME:R-HSA-6796648",
"REACTOM... | 18 | [
"1e3m",
"1ewq",
"1fw6",
"1ng9",
"1nne",
"1oh5",
"1oh6",
"1oh7",
"1oh8",
"1w7a",
"1wb9",
"1wbb",
"1wbd",
"2o8b",
"2o8c",
"2o8d",
"2o8e",
"2o8f",
"2wtu",
"3k0s",
"3thw",
"3thx",
"3thy",
"3thz",
"3zlj",
"5akb",
"5akc",
"5akd",
"5x9w",
"5yk4",
"6i5f",
"7ai5"... | 61 | [
"PUB00004486",
"PUB00010188",
"PUB00024413",
"PUB00042218",
"PUB00042612",
"PUB00042613",
"PUB00042614",
"PUB00042615"
] | [
"9722651",
"8036718",
"11048711",
"17426027",
"17919654",
"17599803",
"17951114",
"17965091"
] | [
"A phylogenomic study of the MutS family of proteins.",
"Colon cancer and DNA repair: have mismatches met their match?",
"The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch.",
"Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramer... | [
1998,
1994,
2000,
2007,
2007,
2007,
2008,
2007
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
810,
21126,
20139,
71,
526
] | 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",... | [
27,
2,
15,
5,
1,
35,
14,
4,
16,
8,
4,
4,
55
] | 13 | true | Homologous_superfamily | DNA mismatch repair protein MutS, N-terminal | DNA mismatch repair protein MutS, N-terminal | DNA_mismatch_repair_MutS_N | 8 |
IPR016152 | 16,152 | Phosphotransferase/anion transporter | PTrfase/Anion_transptr | Homologous_superfamily | 83,824 | false | false | This superfamily represents a structural domain found as the cytoplasmic domain in certain anion transporter proteins [ ], and as domain IIa in mannitol-specific and ntr (nitrogen regulatory) phosphotransferases [ , ]. This domain adopts a 3-layer α/β/α structure in the order, β-α(2)-β(3)-α(3). This domain can be elabo... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.40.930.10",
"SSF55804"
] | [
"",
""
] | [
83589,
83721
] | 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-425381",
"R-HSA-1237044",
"R-HSA-1247673",
"R-HSA-425381",
"R-HSA-5619050",
"R-HSA-5619054",
"R-HSA-9013405",
"R-HSA-9013406",
"R-HSA-9013407",
"R-HSA-9013409",
"R-HSA-9035034",
"R-HSA-9925563",
"R-MMU-1237044",
"R-MMU-1247673",
"R-MMU-425381",
"R-MMU-9013405",
"R-MMU-9013406"... | [
"REACTOME:R-BTA-425381",
"REACTOME:R-HSA-1237044",
"REACTOME:R-HSA-1247673",
"REACTOME:R-HSA-425381",
"REACTOME:R-HSA-5619050",
"REACTOME:R-HSA-5619054",
"REACTOME:R-HSA-9013405",
"REACTOME:R-HSA-9013406",
"REACTOME:R-HSA-9013407",
"REACTOME:R-HSA-9013409",
"REACTOME:R-HSA-9035034",
"REACTOME:... | 26 | [
"1a3a",
"1a6j",
"1hyn",
"1j6t",
"1xiz",
"2a0j",
"2few",
"2oq3",
"2oqt",
"3bjv",
"3lf6",
"3oxp",
"3t43",
"3urr",
"4gqx",
"4ky9",
"4m62",
"4m8q",
"4odx",
"4yzf",
"5jho",
"5sy8",
"5t29",
"5t5b",
"5t6l",
"5t80",
"5t85",
"5tfw",
"6caa",
"6mto",
"6mtq",
"7tvz"... | 96 | [
"PUB00014719",
"PUB00023252",
"PUB00028154"
] | [
"11049968",
"9551558",
"9636714"
] | [
"Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3.",
"The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site.",
"The three-dimensional structure of the nitrogen regulator... | [
2000,
1998,
1998
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
139,
58919,
24361,
405
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
14,
138,
21,
12,
50,
78,
72
] | 7 | true | Homologous_superfamily | Phosphotransferase/anion transporter | Phosphotransferase/anion transporter | PTrfase/Anion_transptr | 5 |
IPR016153 | 16,153 | Heat shock protein Hsp33, N-terminal | Heat_shock_Hsp33_N | Homologous_superfamily | 15,965 | false | false | This superfamily represents the N-terminal, 3-layer β/α/β domain from the heat shock protein Hsp33. Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localised protein with highly reactive cyste... | [
"GO:0051082",
"GO:0006457",
"GO:0005737"
] | [
"unfolded protein binding",
"protein folding",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.55.30.10",
"SSF64397"
] | [
"",
""
] | [
15843,
15965
] | 2 | [] | [] | [] | 0 | [
"1hw7",
"1i7f",
"1vq0",
"1vzy",
"3m7m"
] | 5 | [
"PUB00000967"
] | [
"10025400"
] | [
"Chaperone activity with a redox switch."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
15494,
346,
125
] | 3 | [
"Escherichia coli (strain K12)",
"Mus musculus"
] | [
1,
1
] | 2 | true | Homologous_superfamily | Heat shock protein Hsp33, N-terminal | Heat shock protein Hsp33, N-terminal | Heat_shock_Hsp33_N | 6 |
IPR016154 | 16,154 | Heat shock protein Hsp33, C-terminal | Heat_shock_Hsp33_C | Homologous_superfamily | 15,861 | false | false | This superfamily represents the C-terminal α/β domain from the heat shock protein Hsp33. Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localised protein with highly reactive cysteines that r... | [
"GO:0051082",
"GO:0006457",
"GO:0005737"
] | [
"unfolded protein binding",
"protein folding",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.90.1280.10",
"SSF118352"
] | [
"",
""
] | [
15790,
15860
] | 2 | [] | [] | [] | 0 | [
"1hw7",
"1i7f",
"1vq0",
"1vzy",
"1xjh"
] | 5 | [
"PUB00000967"
] | [
"10025400"
] | [
"Chaperone activity with a redox switch."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halorubrum vacuolatum",
"unclassified sequences"
] | [
15421,
323,
1,
116
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | Heat shock protein Hsp33, C-terminal | Heat shock protein Hsp33, C-terminal | Heat_shock_Hsp33_C | 8 |
IPR016155 | 16,155 | Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp | Mopterin_synth/thiamin_S_b | Homologous_superfamily | 62,223 | false | false | This entry represents a structural domain with a β-grasp fold that is found in molybdopterinsynthase subunit MoaD [ ], as well as in the thiamin biosynthesis sulphur carrier protein ThiS [ ]. ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in the thiCEFSGH operon in Escherichia coli. ThiS... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF54285"
] | [
""
] | [
62223
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6782315",
"R-HSA-947581",
"R-MTU-936654"
] | [
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-947581",
"REACTOME:R-MTU-936654"
] | 3 | [
"1f0z",
"1fm0",
"1fma",
"1jw9",
"1jwa",
"1jwb",
"1nvi",
"1rws",
"1ryj",
"1sf0",
"1tyg",
"1v8c",
"1vjk",
"1wgk",
"1xo3",
"1zud",
"2ax5",
"2cu3",
"2g1e",
"2hj1",
"2htm",
"2k22",
"2k5p",
"2k9x",
"2l32",
"2l52",
"2l83",
"2lek",
"2lji",
"2m19",
"2pko",
"2q5w"... | 58 | [
"PUB00007564",
"PUB00034477",
"PUB00036720"
] | [
"10781607",
"16388576",
"11135669"
] | [
"The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD.",
"Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis.",
"Crystal structure of molybdopterin synthase and its evolutionary relationship ... | [
2000,
2006,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
2833,
51027,
2,
7182,
1179
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
11,
2,
2,
3,
3,
3,
2,
2,
3,
4,
1,
1,
8
] | 13 | true | Homologous_superfamily | Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp | Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp | Mopterin_synth/thiamin_S_b | 2 |
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