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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR019734 | 19,734 | Tetratricopeptide repeat | TPR_rpt | Repeat | 805,075 | false | false | The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins [ , , ]. It mediates protein-protein interactions and the assembly of multiprotein complexes [ ]. The TPR motif consists of 3-16 tandem-repeats of 34 amino acids residues, although individual TPR motifs can be dispersed... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00515",
"PF13174",
"PF13176",
"PF13181",
"PS50005",
"SM00028"
] | [
"TPR_1",
"TPR_6",
"TPR_7",
"TPR_8",
"TPR",
"TPR"
] | [
91515,
40150,
24123,
218569,
635744,
693095
] | 6 | [
"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-141430",
"R-BTA-1650814",
"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-2467813",
"R-BTA-2559582",
"R-BTA-2672351",
"R-BTA-3371497",
"R-BTA-429947",
"R-BT... | [
"REACTOME:R-BTA-141430",
"REACTOME:R-BTA-1650814",
"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",
"REACTOME:R-BTA-176409",
"REACTOME:R-BTA-176412",
"REACTOME:R-BTA-17... | 495 | [
"1a17",
"1e96",
"1elr",
"1elw",
"1fch",
"1hh8",
"1ihg",
"1iip",
"1kt0",
"1kt1",
"1na0",
"1na3",
"1ouv",
"1p5q",
"1qz2",
"1tjc",
"1w3b",
"1wao",
"1wm5",
"1xnf",
"2avp",
"2bug",
"2c0l",
"2c0m",
"2c2l",
"2dba",
"2e2e",
"2fbn",
"2fi7",
"2fo7",
"2gw1",
"2ho1"... | 746 | [
"PUB00001313",
"PUB00005443",
"PUB00005695",
"PUB00014195"
] | [
"9482716",
"7667876",
"1882418",
"14659697"
] | [
"The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.",
"Tetratrico peptide repeat interactions: to TPR or not to TPR?",
"The TPR snap helix: a novel protein repeat motif from mitosis to transcription.",
"TPR proteins: the versati... | [
1998,
1995,
1991,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5035,
365676,
426001,
152,
8211
] | 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",... | [
582,
64,
469,
166,
11,
859,
407,
36,
412,
570,
25,
30,
828
] | 13 | true | Repeat | Tetratricopeptide repeat | Tetratricopeptide repeat | TPR_rpt | 2 |
IPR019735 | 19,735 | Synapsin, conserved site | Synapsin_CS | Conserved_site | 2,233 | false | false | The synapsins are a family of neuron-specific phosphoproteins that coat synaptic vesicles and are involved in the binding between these vesicles and the cytoskeleton (including actin filaments). The family comprises 5 homologous proteins Ia, Ib, IIa, IIb and III. Synapsins I, II, and III are encoded by 3 different gene... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00416"
] | [
"SYNAPSIN_2"
] | [
2233
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-181429",
"R-HSA-212676",
"R-HSA-9662360",
"R-MMU-181429",
"R-MMU-212676",
"R-RNO-181429",
"R-RNO-212676"
] | [
"REACTOME:R-HSA-181429",
"REACTOME:R-HSA-212676",
"REACTOME:R-HSA-9662360",
"REACTOME:R-MMU-181429",
"REACTOME:R-MMU-212676",
"REACTOME:R-RNO-181429",
"REACTOME:R-RNO-212676"
] | 7 | [
"1auv",
"1aux",
"1i7l",
"1i7n",
"1pk8",
"1px2",
"2p0a"
] | 7 | [
"PUB00018754",
"PUB00018755",
"PUB00053858",
"PUB00053859"
] | [
"10940454",
"7777057",
"2859595",
"10804215"
] | [
"Upregulation of synapsin IIa and IIb mRNAs in the paraventricular and supraoptic nuclei in chronic salt loaded and lactating rats.",
"Essential functions of synapsins I and II in synaptic vesicle regulation.",
"Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neuro... | [
2000,
1995,
1985,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
2233
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
10,
7,
14
] | 4 | true | Conserved_site | Synapsin, conserved site | Synapsin, conserved site | Synapsin_CS | 7 |
IPR019736 | 19,736 | Synapsin, phosphorylation site | Synapsin_P_site | PTM | 2,789 | false | false | This entry represents a conserved octapeptide in the immediate N-terminal domain, which contains the phosphorylated serine residue. The synapsins are a family of neuron-specific phosphoproteins that coat synaptic vesicles and are involved in the binding between these vesicles and the cytoskeleton (including actin filam... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE"
] | [
"PF10581",
"PS00415"
] | [
"Synapsin_N",
"SYNAPSIN_1"
] | [
2785,
2574
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-181429",
"R-DME-212676",
"R-HSA-181429",
"R-HSA-212676",
"R-HSA-9662360",
"R-MMU-181429",
"R-MMU-212676",
"R-RNO-181429",
"R-RNO-212676"
] | [
"REACTOME:R-DME-181429",
"REACTOME:R-DME-212676",
"REACTOME:R-HSA-181429",
"REACTOME:R-HSA-212676",
"REACTOME:R-HSA-9662360",
"REACTOME:R-MMU-181429",
"REACTOME:R-MMU-212676",
"REACTOME:R-RNO-181429",
"REACTOME:R-RNO-212676"
] | 9 | [
"1pk8",
"1px2"
] | 2 | [
"PUB00018754",
"PUB00018755",
"PUB00053858",
"PUB00053859"
] | [
"10940454",
"7777057",
"2859595",
"10804215"
] | [
"Upregulation of synapsin IIa and IIb mRNAs in the paraventricular and supraoptic nuclei in chronic salt loaded and lactating rats.",
"Essential functions of synapsins I and II in synaptic vesicle regulation.",
"Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neuro... | [
2000,
1995,
1985,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Eukaryota"
] | [
2,
2787
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
3,
11,
6,
14
] | 5 | true | PTM | Synapsin, phosphorylation site | Synapsin, phosphorylation site | Synapsin_P_site | 3 |
IPR019737 | 19,737 | Homeobox engrailed-type, conserved site | Homeobox-engrailed_CS | Conserved_site | 2,177 | false | false | This entry identifies a conserved region of some 20 amino-acid residues, specific to engrailed proteins, located at the C-terminal of the 'homeobox' domain; the specific function of these residues is unclear. Homeodomain proteins are transcription factors that share a related DNA-binding homeodomain [ ]. The homeodomai... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00033"
] | [
"ENGRAILED"
] | [
2177
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000591",
"PUB00003347",
"PUB00004373",
"PUB00005101",
"PUB00005390",
"PUB00010002",
"PUB00013192",
"PUB00013193",
"PUB00013194"
] | [
"2568852",
"7707374",
"1970866",
"2884726",
"1357790",
"12445403",
"10377888",
"12215502",
"9739097"
] | [
"The structure and function of the homeodomain.",
"The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance.",
"Specific DNA binding of the two chicken Deformed family homeodomain proteins, Chox-1.4 and Chox-a.",
"Homeo boxes in the study of development.",
"T... | [
1989,
1995,
1990,
1987,
1992,
2002,
1999,
2002,
1998
] | 9 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
2177
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
5,
2,
3,
4
] | 5 | true | Conserved_site | Homeobox engrailed-type, conserved site | Homeobox engrailed-type, conserved site | Homeobox-engrailed_CS | 3 |
IPR019738 | 19,738 | Myelin P0 protein, conserved site | Myelin_P0_CS | Conserved_site | 197 | false | false | The P0 protein is a major structural glycoprotein of the peripheral nervous system (PNS) myelin, which probably plays an important role for the formation and the maintenance of myelin structure; it is well conserved across species [ , ]. P0 is a protein of about 28 Kd that consists of three domains: a N-terminal extrac... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00568"
] | [
"MYELIN_P0"
] | [
197
] | 1 | [
"REACTOME"
] | [
"R-HSA-9619665"
] | [
"REACTOME:R-HSA-9619665"
] | 1 | [] | 0 | [
"PUB00000719",
"PUB00003466"
] | [
"1285424",
"1710279"
] | [
"Myelin P0-protein, more than just a structural protein?",
"Folding and function of the myelin proteins from primary sequence data."
] | [
1992,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
197
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
3,
6
] | 3 | true | Conserved_site | Myelin P0 protein, conserved site | Myelin P0 protein, conserved site | Myelin_P0_CS | 5 |
IPR019739 | 19,739 | CTF transcription factor/nuclear factor 1, conserved site | CTF/NFI_DNA-bd_CS | Conserved_site | 8,290 | false | false | Nuclear factor I (NF-I) or CCAAT box-binding transcription factor (CTF) [ , , ] (also known as TGGCA-binding proteins) are a family of vertebrate nuclear proteins which recognise and bind, as dimers, the palindromic DNA sequence 5'-TGGCANNNTGCCA-3'. This family was first described for its role in stimulating the initia... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00349"
] | [
"CTF_NFI_1"
] | [
8290
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-73980",
"R-HSA-749476"
] | [
"REACTOME:R-HSA-73980",
"REACTOME:R-HSA-749476"
] | 2 | [
"7qqd",
"7qqe",
"9qky"
] | 3 | [
"PUB00000833",
"PUB00001922",
"PUB00004374",
"PUB00004597",
"PUB00017915",
"PUB00097185",
"PUB00097186"
] | [
"2504497",
"8543151",
"2339052",
"6216480",
"1618796",
"19584245",
"28962832"
] | [
"The proline-rich transcriptional activator of CTF/NF-I is distinct from the replication and DNA binding domain.",
"A proline-rich TGF-beta-responsive transcriptional activator interacts with histone H3.",
"Chicken NFI/TGGCA proteins are encoded by at least three independent genes: NFI-A, NFI-B and NFI-C with h... | [
1989,
1995,
1990,
1982,
1992,
2009,
2017
] | 7 | [] | [] | 0 | 0 | null | [
"Chordata"
] | [
8290
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
138,
46,
28,
40
] | 4 | true | Conserved_site | CTF transcription factor/nuclear factor 1, conserved site | CTF transcription factor/nuclear factor 1, conserved site | CTF/NFI_DNA-bd_CS | 2 |
IPR019740 | 19,740 | Pyridoxamine 5'-phosphate oxidase, conserved site | Pyridox_Oxase_CS | Conserved_site | 18,584 | false | false | Pyridoxamine 5'-phosphate oxidase ( ) is a FMN flavoprotein involved in the de novo synthesis of pyridoxine (vitamin B6) and pyridoxal phosphate. It oxidizes pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P. The sequences of the enzyme from bacterial (genes pdxH or fprA) [ ] and fungal (gene PDX3) [ ] s... | [
"GO:0016638"
] | [
"oxidoreductase activity, acting on the CH-NH2 group of donors"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01064"
] | [
"PYRIDOX_OXIDASE"
] | [
18584
] | 1 | [
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.4.3.5",
"PWY-7204",
"PWY-7282",
"R-BTA-964975",
"R-CEL-964975",
"R-DDI-964975",
"R-HSA-964975",
"R-MMU-964975",
"R-RNO-964975",
"R-SCE-964975",
"R-SPO-964975"
] | [
"EC:1.4.3.5",
"METACYC:PWY-7204",
"METACYC:PWY-7282",
"REACTOME:R-BTA-964975",
"REACTOME:R-CEL-964975",
"REACTOME:R-DDI-964975",
"REACTOME:R-HSA-964975",
"REACTOME:R-MMU-964975",
"REACTOME:R-RNO-964975",
"REACTOME:R-SCE-964975",
"REACTOME:R-SPO-964975"
] | 11 | [
"1ci0",
"1dnl",
"1g76",
"1g77",
"1g78",
"1g79",
"1jnw",
"1nrg",
"1t9m",
"1ty9",
"1wv4",
"2a2j",
"4hms",
"4hmt",
"4hmu",
"4hmv",
"6h00",
"8qyt",
"8ros"
] | 19 | [
"PUB00001735",
"PUB00002199",
"PUB00002264"
] | [
"8586283",
"1356963",
"7896706"
] | [
"Molecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium. Pseudomonas aureofaciens 30-84.",
"Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations.",
"Sterol uptake induced by an impairment ... | [
1995,
1992,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
14583,
3729,
4,
268
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
3,
1,
1,
2,
1,
6,
1,
1,
5,
2,
1,
1,
3
] | 13 | true | Conserved_site | Pyridoxamine 5'-phosphate oxidase, conserved site | Pyridoxamine 5'-phosphate oxidase, conserved site | Pyridox_Oxase_CS | 8 |
IPR019741 | 19,741 | Galactokinase, conserved site | Galactokinase_CS | Conserved_site | 17,578 | false | false | This entry represents a conserved signature pattern located in the N-terminal domain of galactokinases. Galactokinase catalyses the first reaction in the galactose metabolism pathway, the ATP-dependent phosphorylation of galactose, yielding galactose-1-phosphate [ , ]. Deficiency in this enzyme results in the disease g... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00106"
] | [
"GALACTOKINASE"
] | [
17578
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.6",
"PWY-3821",
"PWY-6317",
"PWY-6527",
"R-BTA-70370",
"R-CFA-70370",
"R-HSA-5609976",
"R-HSA-70370",
"R-MMU-70370"
] | [
"EC:2.7.1.6",
"METACYC:PWY-3821",
"METACYC:PWY-6317",
"METACYC:PWY-6527",
"REACTOME:R-BTA-70370",
"REACTOME:R-CFA-70370",
"REACTOME:R-HSA-5609976",
"REACTOME:R-HSA-70370",
"REACTOME:R-MMU-70370"
] | 9 | [
"1pie",
"1s4e",
"1wuu",
"2a2c",
"2a2d",
"2aj4",
"2cz9",
"2dei",
"2dej",
"3v2u",
"3v5r",
"6gr2",
"6q3w",
"6q3x",
"6q8z",
"6q90",
"6q91",
"6qje",
"6tep",
"6teq",
"6ter",
"6zfh",
"6zgv",
"6zgw",
"6zgx",
"6zgy",
"6zgz",
"6zh0",
"7ozx",
"7rcl",
"7rcm",
"7s49"... | 33 | [
"PUB00003653",
"PUB00004765"
] | [
"3062381",
"1438294"
] | [
"Yeast regulatory gene GAL3: carbon regulation; UASGal elements in common with GAL1, GAL2, GAL7, GAL10, GAL80, and MEL1; encoded protein strikingly similar to yeast and Escherichia coli galactokinases.",
"Cloning of a human galactokinase gene (GK2) on chromosome 15 by complementation in yeast."
] | [
1988,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctmP19",
"metagenomes"
] | [
40,
11546,
5840,
1,
151
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
4,
1,
2,
1,
1,
17,
10,
1,
2,
11,
2,
1,
6
] | 13 | true | Conserved_site | Galactokinase, conserved site | Galactokinase, conserved site | Galactokinase_CS | 8 |
IPR019742 | 19,742 | Alpha-2-macroglobulin, conserved site | MacrogloblnA2_CS | Conserved_site | 13,829 | false | false | This entry represents a conserved region, located towards the C terminus, which contains the two residues involved in the thiol ester bond. This entry contains serum complement C3 and C4 precursors and alpha-macrogrobulins. The alpha-macroglobulin (aM) family of proteins includes protease inhibitors [ ], typified by th... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00477"
] | [
"ALPHA_2_MACROGLOBULIN"
] | [
13829
] | 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-173736",
"R-BTA-174577",
"R-BTA-198933",
"R-BTA-375276",
"R-BTA-381426",
"R-BTA-418594",
"R-BTA-6798695",
"R-BTA-8957275",
"R-BTA-977606",
"R-HSA-114608",
"R-HSA-140837",
"R-HSA-1474228",
"R-HSA-163125",
"R-HSA-166663",
"R-HSA-173736",
"R-HSA-174577",
"R-HSA-198933",
"R-HSA-... | [
"REACTOME:R-BTA-173736",
"REACTOME:R-BTA-174577",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-977606",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-140837",
"REACTOME:R-HSA-1... | 54 | [
"1hzf",
"2a73",
"2i07",
"2icf",
"2pn5",
"2wii",
"2win",
"2xwb",
"2xwj",
"3g6j",
"3l5n",
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"4d94",
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"5jpm",
"5jpn",
"5jtw",
"5o32",
"5o35",
"6ehg",
"6rmt",
"6rmu",
"6ru5",
"6rur",
"6ruv",
"6tav"... | 73 | [
"PUB00002498",
"PUB00015030",
"PUB00015031",
"PUB00015032",
"PUB00015033",
"PUB00015034"
] | [
"2473064",
"2472396",
"2469470",
"2430968",
"9914899",
"10426429"
] | [
"Alpha-macroglobulins: structure, shape, and mechanism of proteinase complex formation.",
"Proteinase binding and inhibition by the monomeric alpha-macroglobulin rat alpha 1-inhibitor-3.",
"A conserved region in alpha-macroglobulins participates in binding to the mammalian alpha-macroglobulin receptor.",
"Hum... | [
1989,
1989,
1989,
1986,
1998,
1999
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"Methanosarcinales",
"ecological metagenomes"
] | [
83,
13723,
1,
18,
4
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
99,
81,
26,
19,
44
] | 6 | true | Conserved_site | Alpha-2-macroglobulin, conserved site | Alpha-2-macroglobulin, conserved site | MacrogloblnA2_CS | 8 |
IPR019743 | 19,743 | Involucrin, conserved site | Involucrin_CS | Conserved_site | 103 | false | false | Involucrin [ , ] is a highly reactive, soluble, transglutaminase substrate protein present in keratinocytes of epidermis and other stratified squamous epithelia. Involucrin first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase thus helping in the formation of an... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00795"
] | [
"INVOLUCRIN"
] | [
103
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-6809371",
"R-HSA-9725554"
] | [
"REACTOME:R-HSA-6809371",
"REACTOME:R-HSA-9725554"
] | 2 | [] | 0 | [
"PUB00003188",
"PUB00003634",
"PUB00003636"
] | [
"8098344",
"1359382",
"8277848"
] | [
"Involucrin--structure and role in envelope assembly.",
"Consecutive actions of different gene-altering mechanisms in the evolution of involucrin.",
"The involucrin genes of the mouse and the rat: study of their shared repeats."
] | [
1993,
1992,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Eutheria"
] | [
103
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
5
] | 3 | true | Conserved_site | Involucrin, conserved site | Involucrin, conserved site | Involucrin_CS | 4 |
IPR019744 | 19,744 | Amyloidogenic glycoprotein, copper-binding domain conserved site | APP_CUBD_CS | Conserved_site | 6,385 | false | false | Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [ , , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with D... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00319"
] | [
"APP_CUBD"
] | [
6385
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-114608",
"R-CEL-3000178",
"R-CEL-381426",
"R-CEL-416476",
"R-CEL-8957275",
"R-CEL-9609523",
"R-DME-114608",
"R-DME-3000178",
"R-DME-381426",
"R-DME-416476",
"R-DME-8957275",
"R-DME-9609523",
"R-DME-9837999",
"R-HSA-114608",
"R-HSA-3000178",
"R-HSA-381426",
"R-HSA-416476",
"R... | [
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-3000178",
"REACTOME:R-CEL-381426",
"REACTOME:R-CEL-416476",
"REACTOME:R-CEL-8957275",
"REACTOME:R-CEL-9609523",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-3000178",
"REACTOME:R-DME-381426",
"REACTOME:R-DME-416476",
"REACTOME:R-DME-8957275",
"REACTOME:R-DM... | 67 | [
"1owt",
"2fjz",
"2fk1",
"2fk2",
"2fk3",
"2fkl",
"2fma",
"2m05",
"3ktm",
"4pwq",
"7mqy",
"7mrk",
"7mrm",
"7mrn",
"7mrs",
"8kew",
"8kf1",
"8kf3",
"8kf4",
"8kf5",
"8kf6",
"8otf"
] | 22 | [
"PUB00029624",
"PUB00033916",
"PUB00033917",
"PUB00033918",
"PUB00099232",
"PUB00099233"
] | [
"12611883",
"16301322",
"16406235",
"16364896",
"28713158",
"33302541"
] | [
"Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis.",
"Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging.",
"The amyloid precursor protein and postnatal neurogenesis/... | [
2003,
2006,
2006,
2005,
2017,
2020
] | 6 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
6385
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
16,
6,
20,
21,
16
] | 6 | true | Conserved_site | Amyloidogenic glycoprotein, copper-binding domain conserved site | Amyloidogenic glycoprotein, copper-binding domain conserved site | APP_CUBD_CS | 8 |
IPR019745 | 19,745 | Amyloidogenic glycoprotein, intracellular domain, conserved site | Amyloid_glyco_intracell_CS | Conserved_site | 6,173 | false | false | Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [ , , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with D... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00320"
] | [
"APP_INTRA"
] | [
6173
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
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"R-CEL-8957275",
"R-CEL-9609523",
"R-DME-114608",
"R-DME-3000178",
"R-DME-381426",
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"R-DME-9837999",
"R-HSA-114608",
"R-HSA-3000178",
"R-HSA-381426",
"R-HSA-416476",
"R... | [
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"REACTOME:R-CEL-3000178",
"REACTOME:R-CEL-381426",
"REACTOME:R-CEL-416476",
"REACTOME:R-CEL-8957275",
"REACTOME:R-CEL-9609523",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-3000178",
"REACTOME:R-DME-381426",
"REACTOME:R-DME-416476",
"REACTOME:R-DME-8957275",
"REACTOME:R-DM... | 67 | [
"1aqc",
"1m7e",
"1oqn",
"1x11",
"2lp1",
"2roz",
"2ysz",
"2yt0",
"2yt1",
"3dxc",
"3dxd",
"3dxe",
"3sv1",
"6itu",
"6iyc",
"8kew",
"8kf1",
"8kf3",
"8kf4",
"8kf5",
"8kf6",
"8otf",
"8s4y",
"8x52",
"8x54"
] | 25 | [
"PUB00029624",
"PUB00033916",
"PUB00033917",
"PUB00033918",
"PUB00099232",
"PUB00099233"
] | [
"12611883",
"16301322",
"16406235",
"16364896",
"28713158",
"33302541"
] | [
"Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis.",
"Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging.",
"The amyloid precursor protein and postnatal neurogenesis/... | [
2003,
2006,
2006,
2005,
2017,
2020
] | 6 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
6173
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
16,
6,
22,
19,
17
] | 6 | true | Conserved_site | Amyloidogenic glycoprotein, intracellular domain, conserved site | Amyloidogenic glycoprotein, intracellular domain, conserved site | Amyloid_glyco_intracell_CS | 2 |
IPR019747 | 19,747 | FERM conserved site | FERM_CS | Conserved_site | 50,020 | false | false | This entry represents the conserved sites of the FERM domain. The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane [ ]. FERM domains are found in a number of cytoskeletal-associated proteins that associate ... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00660",
"PS00661"
] | [
"FERM_1",
"FERM_2"
] | [
39483,
39541
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-373752",
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"R-CEL-5675221",
"R-CEL-9013149",
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"R-DME-6794361",
"R-HSA-114608",
"R-HSA-166016",
"R-HSA-182971",
"R-HSA-2029482",
"R-HSA-354192",
"R-HSA-354194",
"R-H... | [
"REACTOME:R-BTA-373752",
"REACTOME:R-BTA-6794361",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-182971",
"REACTOME:R-CEL-446353",
"REACTOME:R-CEL-5675221",
"REACTOME:R-CEL-9013149",
"REACTOME:R-CEL-9013423",
"REACTOME:R-DDI-114608",
"REACTOME:R-DME-373752",
"REACTOME:R-DME-6794361",
"REACTOME:R-HS... | 75 | [
"1e5w",
"1ef1",
"1gc6",
"1gc7",
"1gg3",
"1h4r",
"1isn",
"1j19",
"1mix",
"1miz",
"1mk7",
"1mk9",
"1ni2",
"1sgh",
"1y19",
"2d10",
"2d11",
"2d2q",
"2ems",
"2emt",
"2he7",
"2i1j",
"2i1k",
"2kc2",
"2kma",
"2yvc",
"2zpy",
"3bin",
"3g9w",
"3ivf",
"3qij",
"3u8z"... | 132 | [
"PUB00005484",
"PUB00013213",
"PUB00017978"
] | [
"9757824",
"10847681",
"10970839"
] | [
"The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.",
"Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.",
"Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domai... | [
1998,
2000,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"marine sediment metagenome"
] | [
50019,
1
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
15,
374,
24,
127,
136,
150
] | 7 | true | Conserved_site | FERM conserved site | FERM conserved site | FERM_CS | 5 |
IPR019748 | 19,748 | FERM central domain | FERM_central | Domain | 98,708 | false | false | This entry represents the FERM central domain of a group of proteins mainly from animals and some plant species. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites [ , ... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF00373",
"cd14473"
] | [
"FERM_M",
"FERM_B-lobe"
] | [
87277,
95554
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
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"R-CEL-2453902",
"R-CEL-446353",
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"R-CEL-9013149",
"R-CEL-9013423",
"R-DDI-114608",
"R-DDI-9013418",
"R-DDI-9013419",
"R-DDI-9013420",
"R-DDI-9013422",
"R-DDI-9013425",
"R-DME-114608",
... | [
"REACTOME:R-BTA-114608",
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"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-182971",
"REACTOME:R-CEL-2453902",
"REACTOME:R-CEL-446353",
"REACTOME:R-CEL-5675221",
"REACTOME:R-CEL-9013149",
"REACTOME:R-CEL-9013423",
"REACTOME:R-DDI-114608",
"REACTOME:R-DD... | 311 | [
"1e5w",
"1ef1",
"1gc6",
"1gc7",
"1gg3",
"1h4r",
"1isn",
"1j19",
"1mix",
"1miz",
"1mk7",
"1mk9",
"1ni2",
"1sgh",
"1y19",
"2aeh",
"2al6",
"2d10",
"2d11",
"2d2q",
"2ems",
"2emt",
"2he7",
"2hrj",
"2i1j",
"2i1k",
"2j0j",
"2j0k",
"2j0m",
"2rq1",
"2yvc",
"2zpy"... | 185 | [
"PUB00005484",
"PUB00013213",
"PUB00017978",
"PUB00114215"
] | [
"9757824",
"10847681",
"10970839",
"20966971"
] | [
"The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.",
"Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.",
"Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domai... | [
1998,
2000,
2000,
2010
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Teubervirus",
"marine metagenome"
] | [
25,
98674,
8,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
55,
570,
66,
262,
203,
1,
250,
42
] | 9 | true | Domain | FERM central domain | FERM central domain | FERM_central | 2 |
IPR019749 | 19,749 | Band 4.1 domain | Band_41_domain | Domain | 96,271 | false | false | The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane [ ]. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma memb... | [] | [] | [] | 0 | [
"PRINTS",
"SMART"
] | [
"PR00935",
"SM00295"
] | [
"BAND41",
"B41"
] | [
49893,
95548
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-373752",
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"R-CEL-114608",
"R-CEL-182971",
"R-CEL-2029482",
"R-CEL-2453902",
"R-CEL-354192",
"R-CEL-354194",
"R-CEL-375165",
"R-CEL-3928662",
"R-CEL-418885",
"R-CEL-4420097",
"R-CEL-446353",
"R-CEL-5663213",
"R-CEL-5673001",
"R-CEL-5675221",
"R... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-373752",
"REACTOME:R-BTA-6794361",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-182971",
"REACTOME:R-CEL-2029482",
"REACTOME:R-CEL-2453902",
"REACTOME:R-CEL-354192",
"REACTOME:R-CEL-354194",
"REACTOME:R-CEL-375165",
"REACTOME:R-CEL-3928662",
"REACTOME:R-CEL... | 348 | [
"1e5w",
"1ef1",
"1gc6",
"1gc7",
"1gg3",
"1h4r",
"1isn",
"1j19",
"1mix",
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"2i1k",
"2j0j",
"2j0k",
"2j0m",
"2rq1",
"2yvc",
"2zpy",
"3au4",
"3au5",
"3bin"... | 182 | [
"PUB00005484",
"PUB00013213",
"PUB00017978"
] | [
"9757824",
"10847681",
"10970839"
] | [
"The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.",
"Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.",
"Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domai... | [
1998,
2000,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
96271
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
59,
568,
70,
249,
203,
1,
249,
36
] | 9 | true | Domain | Band 4.1 domain | Band 4.1 domain | Band_41_domain | 7 |
IPR019752 | 19,752 | Pyruvate/ketoisovalerate oxidoreductase, catalytic domain | Pyrv/ketoisovalerate_OxRed_cat | Domain | 36,665 | false | false | This domain is found in prokaryotes. It includes a region of the large protein pyruvate-flavodoxin oxidoreductase and the whole pyruvate ferredoxin oxidoreductase gamma subunit protein. It is not known whether the gamma subunit has a catalytic or regulatory role. Pyruvate oxidoreductase (POR) catalyses the final step i... | [
"GO:0016903"
] | [
"oxidoreductase activity, acting on the aldehyde or oxo group of donors"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01558"
] | [
"POR"
] | [
36665
] | 1 | [
"EC",
"GP"
] | [
"1.2.7",
"GenProp0839"
] | [
"EC:1.2.7",
"GP:GenProp0839"
] | 2 | [
"1b0p",
"1kek",
"2c3m",
"2c3o",
"2c3p",
"2c3u",
"2c3y",
"2c42",
"2pda",
"2raa",
"2uza",
"3g2e",
"3on3",
"5b46",
"5b47",
"5b48",
"5c4i",
"5exd",
"5exe",
"6cin",
"6cio",
"6cip",
"6ciq",
"6n2n",
"6n2o",
"7plm",
"8ys5",
"8ys6",
"9bt4"
] | 29 | [
"PUB00002295",
"PUB00004826"
] | [
"8550425",
"8415612"
] | [
"Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima.",
"Growth of the cyanobacterium Anabaena on molecular nitrogen: NifJ is required when iron is limited."
] | [
1996,
1993
] | 2 | [] | [
"IPR011894"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2902,
31161,
1459,
1143
] | 4 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1,
1
] | 2 | true | Domain | Pyruvate/ketoisovalerate oxidoreductase, catalytic domain | Pyruvate/ketoisovalerate oxidoreductase, catalytic domain | Pyrv/ketoisovalerate_OxRed_cat | 3 |
IPR019755 | 19,755 | Restriction endonuclease, type II, EcoRV, Proteobacteria | Restrct_endonuc_II_EcoRV_Pbac | Family | 3 | false | false | There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000995"
] | [
"RE_EcoRV"
] | [
3
] | 1 | [] | [] | [] | 0 | [
"1eo3",
"1eo4",
"1eon",
"1eoo",
"1eop",
"1rve",
"2b0d",
"2b0e"
] | 8 | [
"PUB00031198",
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035705",
"PUB00035707"
] | [
"15170321",
"15770420",
"14576294",
"11827971",
"11557805",
"15121719",
"12665693"
] | [
"DNA cleavage by EcoRV endonuclease: two metal ions in three metal ion binding sites.",
"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship between different subgroups of restriction... | [
2004,
2005,
2003,
2002,
2001,
2004,
2003
] | 7 | [
"IPR015314"
] | [] | 1 | 0 | 1 | [
"Pseudomonadati"
] | [
3
] | 1 | [] | [] | 0 | true | Family | Restriction endonuclease, type II, EcoRV, Proteobacteria | Restriction endonuclease, type II, EcoRV, Proteobacteria | Restrct_endonuc_II_EcoRV_Pbac | 9 |
IPR019756 | 19,756 | Peptidase S26A, signal peptidase I, serine active site | Pept_S26A_signal_pept_1_Ser-AS | Active_site | 26,383 | false | false | Signal peptidases (SPases) [ ] (also known as leader peptidases) remove the signal peptides from secretory proteins. In prokaryotes three types of SPases are known: type I (gene lepB) which is responsible for the processing of the majority of exported pre-proteins; type II (gene lsp) which only process lipoproteins, an... | [
"GO:0004252",
"GO:0016020"
] | [
"serine-type endopeptidase activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00501"
] | [
"SPASE_I_1"
] | [
26383
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.21.89",
"R-BTA-422085",
"R-BTA-9768727",
"R-CFA-422085",
"R-CFA-9768727",
"R-HSA-1799339",
"R-HSA-381771",
"R-HSA-400511",
"R-HSA-422085",
"R-HSA-9760173",
"R-HSA-9768727",
"R-HSA-9828806",
"R-MMU-422085",
"R-MMU-9768727",
"R-RNO-422085",
"R-RNO-9768727"
] | [
"EC:3.4.21.89",
"REACTOME:R-BTA-422085",
"REACTOME:R-BTA-9768727",
"REACTOME:R-CFA-422085",
"REACTOME:R-CFA-9768727",
"REACTOME:R-HSA-1799339",
"REACTOME:R-HSA-381771",
"REACTOME:R-HSA-400511",
"REACTOME:R-HSA-422085",
"REACTOME:R-HSA-9760173",
"REACTOME:R-HSA-9768727",
"REACTOME:R-HSA-9828806... | 16 | [
"1b12",
"1kn9",
"1t7d",
"3iiq",
"3s04",
"4me8",
"4nv4",
"4wvh",
"4wvi",
"4wvj",
"6b88",
"7p2p",
"7p2q"
] | 13 | [
"PUB00002224",
"PUB00002718",
"PUB00003576",
"PUB00005177",
"PUB00005393"
] | [
"8394311",
"1618816",
"7845208",
"8266095",
"1455520"
] | [
"Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad.",
"Identification of potential active-site residues in the Escherichia coli leader peptidase.",
"Families of serine peptidases.",
"A mitochondrial protease with two catalytic subu... | [
1993,
1992,
1994,
1993,
1992
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
194,
19204,
19,
6722,
244
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
21,
2,
1,
2,
1,
10,
9,
1,
9,
14,
3,
19
] | 12 | true | Active_site | Peptidase S26A, signal peptidase I, serine active site | Peptidase S26A, signal peptidase I, serine active site | Pept_S26A_signal_pept_1_Ser-AS | 1 |
IPR019758 | 19,758 | Peptidase S26A, signal peptidase I, conserved site | Pept_S26A_signal_pept_1_CS | Conserved_site | 40,805 | false | false | Signal peptidases (SPases) [ ] (also known as leader peptidases) remove the signal peptides from secretory proteins. In prokaryotes three types of SPases are known: type I (gene lepB) which is responsible for the processing of the majority of exported pre-proteins; type II (gene lsp) which only process lipoproteins, an... | [
"GO:0004252",
"GO:0016020"
] | [
"serine-type endopeptidase activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00761"
] | [
"SPASE_I_3"
] | [
40805
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.21.89",
"R-BTA-422085",
"R-BTA-9768727",
"R-CFA-422085",
"R-CFA-9768727",
"R-HSA-1799339",
"R-HSA-381771",
"R-HSA-400511",
"R-HSA-422085",
"R-HSA-9760173",
"R-HSA-9768727",
"R-HSA-9828806",
"R-MMU-422085",
"R-MMU-9768727",
"R-RNO-422085",
"R-RNO-9768727"
] | [
"EC:3.4.21.89",
"REACTOME:R-BTA-422085",
"REACTOME:R-BTA-9768727",
"REACTOME:R-CFA-422085",
"REACTOME:R-CFA-9768727",
"REACTOME:R-HSA-1799339",
"REACTOME:R-HSA-381771",
"REACTOME:R-HSA-400511",
"REACTOME:R-HSA-422085",
"REACTOME:R-HSA-9760173",
"REACTOME:R-HSA-9768727",
"REACTOME:R-HSA-9828806... | 16 | [
"1b12",
"1kn9",
"1t7d",
"3iiq",
"3s04",
"4me8",
"4nv4",
"4wvg",
"4wvh",
"4wvi",
"4wvj",
"6b88",
"7p2p",
"7p2q"
] | 14 | [
"PUB00002224",
"PUB00002718",
"PUB00003576",
"PUB00005177",
"PUB00005393"
] | [
"8394311",
"1618816",
"7845208",
"8266095",
"1455520"
] | [
"Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad.",
"Identification of potential active-site residues in the Escherichia coli leader peptidase.",
"Families of serine peptidases.",
"A mitochondrial protease with two catalytic subu... | [
1993,
1992,
1994,
1993,
1992
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
6,
33287,
6920,
3,
589
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
17,
1,
2,
6,
1,
13,
9,
8,
16,
2,
21
] | 11 | true | Conserved_site | Peptidase S26A, signal peptidase I, conserved site | Peptidase S26A, signal peptidase I, conserved site | Pept_S26A_signal_pept_1_CS | 8 |
IPR019762 | 19,762 | Dynamin, GTPase region, conserved site | Dynamin_GTPase_CS | Conserved_site | 25,642 | false | false | The P-loop guanosine triphosphatases (GTPases) control a multitude of biological processes, ranging from cell division, cell cycling, and signal transduction, to ribosome assembly and protein synthesis. GTPases exert their control by interchanging between an inactive GDP-bound state and an active GTP-bound state, there... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00410"
] | [
"G_DYNAMIN_1"
] | [
25642
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1169408",
"R-BTA-166016",
"R-BTA-190873",
"R-BTA-196025",
"R-BTA-2132295",
"R-BTA-437239",
"R-BTA-75153",
"R-BTA-8856828",
"R-CEL-190873",
"R-CEL-196025",
"R-CEL-3928665",
"R-CEL-432720",
"R-CEL-432722",
"R-CEL-437239",
"R-CEL-75153",
"R-CEL-8856828",
"R-CFA-1169408",
"R-DDI... | [
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-190873",
"REACTOME:R-BTA-196025",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-437239",
"REACTOME:R-BTA-75153",
"REACTOME:R-BTA-8856828",
"REACTOME:R-CEL-190873",
"REACTOME:R-CEL-196025",
"REACTOME:R-CEL-3928665",
"REACTOME:R-CEL-... | 73 | [
"1jwy",
"1jx2",
"2aka",
"2x2e",
"2x2f",
"3l43",
"3snh",
"3szr",
"3t34",
"3t35",
"3w6n",
"3w6o",
"3w6p",
"3zvr",
"3zyc",
"3zys",
"4bej",
"4h1u",
"4h1v",
"4p4s",
"4p4t",
"4p4u",
"4uud",
"4uuk",
"4whj",
"5a3f",
"5d3q",
"5gtm",
"5uot",
"5wp9",
"6dlu",
"6dlv"... | 52 | [
"PUB00013952",
"PUB00014977",
"PUB00057048",
"PUB00072480",
"PUB00072481",
"PUB00072482"
] | [
"11916378",
"15040446",
"21927001",
"10201074",
"23977156",
"21962493"
] | [
"Classification and evolution of P-loop GTPases and related ATPases.",
"The dynamin superfamily: universal membrane tubulation and fission molecules?",
"The crystal structure of dynamin.",
"Functional diversity in the dynamin family.",
"Functional mapping of human dynamin-1-like GTPase domain based on x-ray... | [
2002,
2004,
2011,
1999,
2013,
2011
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Klosneuvirinae",
"metagenomes"
] | [
4,
25630,
3,
5
] | 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... | [
43,
3,
76,
10,
44,
27,
3,
26,
41,
3,
3,
65
] | 12 | true | Conserved_site | Dynamin, GTPase region, conserved site | Dynamin, GTPase region, conserved site | Dynamin_GTPase_CS | 3 |
IPR019763 | 19,763 | Dynein light chain, type 1/2, conserved site | Dynein_light_1/2_CS | Conserved_site | 5,594 | false | false | Dynein is a multisubunit microtubule-dependent motor enzyme that acts as the force generating protein of eukaryotic cilia and flagella. The cytoplasmic isoform of dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein is composed of a number of ATP-binding... | [
"GO:0007017",
"GO:0005875"
] | [
"microtubule-based process",
"microtubule associated complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS01239"
] | [
"DYNEIN_LIGHT_1"
] | [
5594
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-111446",
"R-BTA-139910",
"R-BTA-141444",
"R-BTA-1632852",
"R-BTA-2132295",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-2565942",
"R-BTA-3371497",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-5620912",
"R-BTA-5620924",
"R-BTA-5663220",
"R-BTA-6798695",
... | [
"REACTOME:R-BTA-111446",
"REACTOME:R-BTA-139910",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-1632852",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-380259",
"REACTOME:R-BTA-380270",
"REACTOME:R-B... | 111 | [
"1cmi",
"1f3c",
"1f95",
"1f96",
"1pwj",
"1re6",
"1rhw",
"2p2t",
"2pg1",
"2xqq",
"3bri",
"3brl",
"3dvh",
"3dvp",
"3dvt",
"3e2b",
"3fm7",
"3glw",
"3p8m",
"3rjs",
"3zke",
"3zkf",
"4d07",
"4ds1",
"4ht6",
"4qh7",
"4qh8",
"5e0l",
"5e0m",
"5wof",
"6gzj",
"6gzl"... | 61 | [
"PUB00002901",
"PUB00003701",
"PUB00023989",
"PUB00037504",
"PUB00097852",
"PUB00097853"
] | [
"7744782",
"8628263",
"10426949",
"14561217",
"25646085",
"17546040"
] | [
"The M(r) = 8,000 and 11,000 outer arm dynein light chains from Chlamydomonas flagella have cytoplasmic homologues.",
"Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster.",
"Structure of the PIN/LC8 dimer with a bound peptide.",
"Localization o... | [
1995,
1996,
1999,
2004,
2015,
2007
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5594
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
2,
3,
5,
3,
3,
1,
3,
4,
1,
1,
3
] | 12 | true | Conserved_site | Dynein light chain, type 1/2, conserved site | Dynein light chain, type 1/2, conserved site | Dynein_light_1/2_CS | 1 |
IPR019765 | 19,765 | Ephrin, conserved site | Ephrin_CS | Conserved_site | 6,448 | false | false | Ephrins are a family of proteins [ ] that are ligands of class V (EPH-related) receptor protein-tyrosine kinases. These receptors and their ligands have been implicated in regulating neuronal axon guidance and in patterning of the developing nervous system and may also serve a patterning and compartmentalisation role o... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PROSITE"
] | [
"PS01299"
] | [
"EPHRIN_RBD_1"
] | [
6448
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DRE-2682334",
"R-DRE-3928663",
"R-DRE-3928665",
"R-HSA-2682334",
"R-HSA-3928662",
"R-HSA-3928663",
"R-HSA-3928664",
"R-HSA-3928665",
"R-MMU-2682334",
"R-MMU-3928662",
"R-MMU-3928663",
"R-MMU-3928664",
"R-MMU-3928665",
"R-RNO-2682334",
"R-RNO-3928662",
"R-RNO-3928663",
"R-RNO-39286... | [
"REACTOME:R-DRE-2682334",
"REACTOME:R-DRE-3928663",
"REACTOME:R-DRE-3928665",
"REACTOME:R-HSA-2682334",
"REACTOME:R-HSA-3928662",
"REACTOME:R-HSA-3928663",
"REACTOME:R-HSA-3928664",
"REACTOME:R-HSA-3928665",
"REACTOME:R-MMU-2682334",
"REACTOME:R-MMU-3928662",
"REACTOME:R-MMU-3928663",
"REACTOM... | 18 | [
"1iko",
"1kgy",
"1shw",
"1shx",
"2hle",
"2i85",
"2vsk",
"2vsm",
"2wo2",
"2wo3",
"2x11",
"3czu",
"3d12",
"3gxu",
"3hei",
"3mbw",
"3mx0",
"4bk5",
"4bka",
"4bkf",
"4l0p",
"4m4r",
"4uf7",
"6p7s",
"6p7y",
"6pdl",
"6thg",
"9dvd"
] | 28 | [
"PUB00004495"
] | [
"7838529"
] | [
"Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
6448
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
19,
14,
19,
37
] | 4 | true | Conserved_site | Ephrin, conserved site | Ephrin, conserved site | Ephrin_CS | 3 |
IPR019766 | 19,766 | Signal peptidase I, all-beta subdomain | Sign_pep_all-beta_subdom | Homologous_superfamily | 2,015 | false | false | The S26 family includes Escherichia coli signal peptidase, SPase, which is a membrane-bound endopeptidase with two N-terminal transmembrane segments and a C-terminal catalytic region [ ]. SPase functions to release proteins that have been translocated into the inner membrane from the cell interior, by cleaving off thei... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.170.230.10"
] | [
""
] | [
2015
] | 1 | [
"EC",
"REACTOME"
] | [
"3.4.21.89",
"R-HSA-9760173"
] | [
"EC:3.4.21.89",
"REACTOME:R-HSA-9760173"
] | 2 | [
"1b12",
"1kn9",
"1t7d",
"3iiq",
"3s04",
"6b88"
] | 6 | [
"PUB00014247",
"PUB00031367"
] | [
"9823901",
"15136583"
] | [
"Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor.",
"Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor."
] | [
1998,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5",
"marine sediment metagenome"
] | [
2013,
1,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | Signal peptidase I, all-beta subdomain | Signal peptidase I, all-beta subdomain | Sign_pep_all-beta_subdom | 1 |
IPR019767 | 19,767 | Erythropoietin/thrombopoeitin, conserved site | EPO/TPO_CS | Conserved_site | 860 | false | false | Erythropoietin, a plasma glycoprotein, is the primary physiological mediator of erythropoiesis [ ]. It is involved in the regulation of the level of peripheral erythrocytes by stimulating the differentiation of erythroid progenitor cells, found in the spleen and bone marrow, into mature erythrocytes [ ]. It is primaril... | [
"GO:0005179",
"GO:0005576"
] | [
"hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00817"
] | [
"EPO_TPO"
] | [
860
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-9027276",
"R-BTA-9027284",
"R-HSA-1234158",
"R-HSA-76009",
"R-HSA-9006335",
"R-HSA-9027276",
"R-HSA-9027277",
"R-HSA-9027283",
"R-HSA-9027284",
"R-MMU-9027276",
"R-MMU-9027284",
"R-RNO-9027276",
"R-RNO-9027284",
"R-SSC-9027276",
"R-SSC-9027284"
] | [
"REACTOME:R-BTA-9027276",
"REACTOME:R-BTA-9027284",
"REACTOME:R-HSA-1234158",
"REACTOME:R-HSA-76009",
"REACTOME:R-HSA-9006335",
"REACTOME:R-HSA-9027276",
"REACTOME:R-HSA-9027277",
"REACTOME:R-HSA-9027283",
"REACTOME:R-HSA-9027284",
"REACTOME:R-MMU-9027276",
"REACTOME:R-MMU-9027284",
"REACTOME:... | 15 | [
"1buy",
"1cn4",
"1eer",
"1v7m",
"1v7n",
"8g04",
"8u18",
"8vu5"
] | 8 | [
"PUB00000639",
"PUB00001756",
"PUB00002479",
"PUB00003648"
] | [
"1420369",
"2877922",
"3346214",
"3773894"
] | [
"Nucleotide sequence of rat erythropoietin.",
"Monkey erythropoietin gene: cloning, expression and comparison with the human erythropoietin gene.",
"Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary ce... | [
1992,
1986,
1988,
1986
] | 4 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
860
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
7,
7
] | 3 | true | Conserved_site | Erythropoietin/thrombopoeitin, conserved site | Erythropoietin/thrombopoeitin, conserved site | EPO/TPO_CS | 5 |
IPR019769 | 19,769 | Translation initiation factor 5A, hypusine site | Trans_elong_IF5A_hypusine_site | PTM | 7,811 | false | false | This entry represents a site centred around the hypusine residue of IF5A proteins. Translation initiation factor 5A (IF-5A) was previously reported to be involved in the first step of peptide bond formation in translation; however more recent work implicates it as a universally conserved translation elongation factor [... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00302"
] | [
"IF5A_HYPUSINE"
] | [
7811
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-204626",
"R-CEL-204626",
"R-DDI-204626",
"R-DME-204626",
"R-DRE-204626",
"R-GGA-204626",
"R-HSA-204626",
"R-MMU-204626",
"R-RNO-204626",
"R-SCE-204626",
"R-SPO-204626"
] | [
"REACTOME:R-BTA-204626",
"REACTOME:R-CEL-204626",
"REACTOME:R-DDI-204626",
"REACTOME:R-DME-204626",
"REACTOME:R-DRE-204626",
"REACTOME:R-GGA-204626",
"REACTOME:R-HSA-204626",
"REACTOME:R-MMU-204626",
"REACTOME:R-RNO-204626",
"REACTOME:R-SCE-204626",
"REACTOME:R-SPO-204626"
] | 11 | [
"1bkb",
"1eif",
"1iz6",
"1x6o",
"1xtd",
"2eif",
"3cpf",
"3er0",
"3hks",
"5dat",
"5dc3",
"5dge",
"5dgf",
"5dlq",
"5gak",
"5hy6",
"5mc6",
"6q84",
"6tnu",
"7n4d",
"7nrc",
"7oya",
"7oyc",
"7oyd",
"7rr5",
"8a0e",
"8aaf",
"8agt",
"8agu",
"8agv",
"8agx",
"8agz"... | 44 | [
"PUB00000742",
"PUB00003672",
"PUB00010716",
"PUB00046010"
] | [
"8347280",
"1903841",
"9753699",
"19424157"
] | [
"Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation.",
"Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.",
"Structure of translation initiation factor 5A... | [
1993,
1991,
1998,
2009
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Imitervirales",
"Pseudomonadota",
"metagenomes"
] | [
875,
6894,
3,
2,
37
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
3,
6,
1,
8,
5,
1,
13,
7,
2,
2,
17
] | 12 | true | PTM | Translation initiation factor 5A, hypusine site | Translation initiation factor 5A, hypusine site | Trans_elong_IF5A_hypusine_site | 8 |
IPR019770 | 19,770 | Eukaryotic translation initiation factor 4E (eIF-4E), conserved site | TIF_eIF_4E_CS | Conserved_site | 10,638 | false | false | Eukaryotic translation initiation factor 4E (eIF-4E) [ ] is a protein that binds to the cap structure of eukaryotic cellular mRNAs. eIF-4E recognises and binds the 7-methylguanosine-containing (m7Gppp) cap during an early step in the initiation of protein synthesis and facilitates ribosome binding to a mRNA by inducing... | [
"GO:0003723",
"GO:0003743",
"GO:0006413",
"GO:0005737"
] | [
"RNA binding",
"translation initiation factor activity",
"translational initiation",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PROSITE"
] | [
"PS00813"
] | [
"IF4E"
] | [
10638
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-1169408",
"R-CEL-156827",
"R-CEL-72649",
"R-CEL-72662",
"R-CEL-72702",
"R-DME-110523",
"R-DME-1169408",
"R-DME-156827",
"R-DME-159227",
"R-DME-159230",
"R-DME-159231",
"R-DME-166208",
"R-DME-72649",
"R-DME-72662",
"R-DME-72702",
"R-DRE-1169408",
"R-DRE-156827",
"R-DRE-166208... | [
"REACTOME:R-CEL-1169408",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-72649",
"REACTOME:R-CEL-72662",
"REACTOME:R-CEL-72702",
"REACTOME:R-DME-110523",
"REACTOME:R-DME-1169408",
"REACTOME:R-DME-156827",
"REACTOME:R-DME-159227",
"REACTOME:R-DME-159230",
"REACTOME:R-DME-159231",
"REACTOME:R-DME-1662... | 66 | [
"1ap8",
"1ej1",
"1ej4",
"1ejh",
"1ipb",
"1ipc",
"1l8b",
"1rf8",
"1wkw",
"2gpq",
"2idr",
"2idv",
"2jgb",
"2jgc",
"2v8w",
"2v8x",
"2v8y",
"2w97",
"2wmc",
"3am7",
"3hxg",
"3hxi",
"3m93",
"3m94",
"3tf2",
"3u7x",
"4axg",
"4aza",
"4bea",
"4dt6",
"4dum",
"4tpw"... | 105 | [
"PUB00000866",
"PUB00001603"
] | [
"1733496",
"1672854"
] | [
"Cap recap: the involvement of eIF-4F in regulating gene expression.",
"Combination of Trp and Glu residues for recognition of mRNA cap structure. Analysis of m7G base recognition site of human cap binding protein (IF-4E) by site-directed mutagenesis."
] | [
1992,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Alphaentomopoxvirus acuprea",
"Eukaryota"
] | [
1,
10637
] | 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... | [
17,
6,
14,
13,
19,
20,
2,
3,
18,
1,
2,
17
] | 12 | true | Conserved_site | Eukaryotic translation initiation factor 4E (eIF-4E), conserved site | Eukaryotic translation initiation factor 4E (eIF-4E), conserved site | TIF_eIF_4E_CS | 6 |
IPR019771 | 19,771 | F-actin capping protein, beta subunit, conserved site | F-actin_capping_bsu_CS | Conserved_site | 4,480 | false | false | The actin filament system, a prominent part of the cytoskeleton in eukaryotic cells, is both a static structure and a dynamic network that can undergo rearrangements: it is thought to be involved in processes such as cell movement and phagocytosis [ ], as well as muscle contraction. The F-actin capping protein binds in... | [
"GO:0003779",
"GO:0030036",
"GO:0005737",
"GO:0008290"
] | [
"actin binding",
"actin cytoskeleton organization",
"cytoplasm",
"F-actin capping protein complex"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PROSITE"
] | [
"PS00231"
] | [
"F_ACTIN_CAPPING_BETA"
] | [
4480
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-6807878",
"R-CEL-6811436",
"R-CEL-9013405",
"R-CEL-9035034",
"R-CEL-983231",
"R-DDI-6807878",
"R-DDI-983231",
"R-DME-3371497",
"R-DME-6807878",
"R-DME-6811436",
"R-DME-9013405",
"R-DME-9035034",
"R-DME-983231",
"R-GGA-3371497",
"R-GGA-6807878",
"R-GGA-6811436",
"R-GGA-9013405"... | [
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811436",
"REACTOME:R-CEL-9013405",
"REACTOME:R-CEL-9035034",
"REACTOME:R-CEL-983231",
"REACTOME:R-DDI-6807878",
"REACTOME:R-DDI-983231",
"REACTOME:R-DME-3371497",
"REACTOME:R-DME-6807878",
"REACTOME:R-DME-6811436",
"REACTOME:R-DME-9013405",
"REACTOME:... | 51 | [
"1izn",
"2kxp",
"2kz7",
"3aa0",
"3aa1",
"3aa6",
"3aa7",
"3aaa",
"3aae",
"3lk2",
"3lk3",
"3lk4",
"4akr",
"5adx",
"5afu",
"5nw4",
"6f1t",
"6f1u",
"6f38",
"6f3a",
"6znl",
"7ccc",
"7ds2",
"7ds3",
"7ds4",
"7ds6",
"7ds8",
"7dsa",
"7dsb",
"7pdz",
"7t5q",
"7z8f"... | 44 | [
"PUB00002626",
"PUB00004059"
] | [
"2341404",
"2179733"
] | [
"Beta-actinin is equivalent to Cap Z protein.",
"Disruption of the actin cytoskeleton in yeast capping protein mutants."
] | [
1990,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
8,
4472
] | 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... | [
3,
1,
2,
2,
8,
9,
1,
2,
14,
1,
1,
4
] | 12 | true | Conserved_site | F-actin capping protein, beta subunit, conserved site | F-actin capping protein, beta subunit, conserved site | F-actin_capping_bsu_CS | 2 |
IPR019772 | 19,772 | Ferrochelatase, active site | Ferrochelatase_AS | Active_site | 17,823 | false | false | null | [
"GO:0004325",
"GO:0006783"
] | [
"ferrochelatase activity",
"heme biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00534"
] | [
"FERROCHELATASE"
] | [
17823
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.98.1.1",
"R-BTA-189451",
"R-BTA-9837999",
"R-DDI-189451",
"R-DDI-9837999",
"R-DME-189451",
"R-DME-9837999",
"R-GGA-421984",
"R-HSA-189451",
"R-HSA-9837999",
"R-MMU-189451",
"R-MMU-9837999",
"R-SCE-189451",
"R-SCE-9837999",
"R-SPO-189451",
"R-SPO-9837999"
] | [
"EC:4.98.1.1",
"REACTOME:R-BTA-189451",
"REACTOME:R-BTA-9837999",
"REACTOME:R-DDI-189451",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-189451",
"REACTOME:R-DME-9837999",
"REACTOME:R-GGA-421984",
"REACTOME:R-HSA-189451",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-189451",
"REACTOME:R-MMU-9837999",... | 16 | [
"1ak1",
"1c1h",
"1c9e",
"1doz",
"1hrk",
"1l8x",
"1lbq",
"1ld3",
"1n0i",
"2ac2",
"2c8j",
"2h1v",
"2hk6",
"2hrc",
"2hre",
"2pnj",
"2po7",
"2q2n",
"2qd1",
"2qd2",
"2qd3",
"2qd4",
"2qd5",
"3aqi",
"3goq",
"3hcn",
"3hco",
"3hcp",
"3hcr",
"3m4z",
"3w1w",
"4f4d"... | 47 | [
"PUB00002620",
"PUB00004754",
"PUB00006691",
"PUB00006693",
"PUB00012956",
"PUB00021315",
"PUB00022076",
"PUB00026989",
"PUB00079463",
"PUB00079464",
"PUB00079465",
"PUB00079466",
"PUB00079467"
] | [
"2185242",
"1704134",
"9384565",
"11175906",
"12196143",
"10704318",
"12427010",
"12761666",
"11215517",
"10582332",
"7592569",
"8122254",
"6390167"
] | [
"The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption, and expression of its structural gene HEM15.",
"Cloning of murine ferrochelatase.",
"Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis.",
"The 2.0 A structure of human ferrochelatase, the terminal enzyme of he... | [
1990,
1991,
1997,
2001,
2002,
2000,
2002,
2003,
2000,
1999,
1995,
1993,
1984
] | 13 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermococcus",
"unclassified sequences"
] | [
12882,
4779,
3,
159
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae... | [
7,
3,
1,
1,
7,
7,
1,
6,
6,
1,
2,
17
] | 12 | true | Active_site | Ferrochelatase, active site | Ferrochelatase, active site | Ferrochelatase_AS | 7 |
IPR019773 | 19,773 | Tyrosine 3-monooxygenase-like | Tyrosine_3-monooxygenase-like | Family | 6,860 | false | false | Phenylalanine, tyrosine and tryptophan hydroxylases constitute a family of tetrahydrobiopterin-dependent aromatic amino acid hydroxylases, all of which are rate-limiting catalysts for important metabolic pathways [ ]. The proteins are structurally and functionally related, each containing iron, and catalysing ring hydr... | [
"GO:0016714"
] | [
"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000336"
] | [
"TH"
] | [
6860
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.16",
"R-BTA-8964208",
"R-CEL-209905",
"R-CEL-8964208",
"R-DDI-209905",
"R-DDI-209931",
"R-DDI-8964208",
"R-DME-209905",
"R-DME-8964208",
"R-HSA-209905",
"R-HSA-209931",
"R-HSA-2160456",
"R-HSA-8964208",
"R-HSA-9031628",
"R-MMU-209905",
"R-MMU-209931",
"R-MMU-8964208",
"R-RNO-... | [
"EC:1.14.16",
"REACTOME:R-BTA-8964208",
"REACTOME:R-CEL-209905",
"REACTOME:R-CEL-8964208",
"REACTOME:R-DDI-209905",
"REACTOME:R-DDI-209931",
"REACTOME:R-DDI-8964208",
"REACTOME:R-DME-209905",
"REACTOME:R-DME-8964208",
"REACTOME:R-HSA-209905",
"REACTOME:R-HSA-209931",
"REACTOME:R-HSA-2160456",
... | 20 | [
"1phz",
"2phm",
"5den",
"5egq",
"5fgj",
"5jk5",
"5jk6",
"5jk8",
"5l01",
"6hpo",
"6hyc",
"6n1k",
"6zvp",
"7a2g",
"7wiy",
"9hb7",
"9hb8"
] | 17 | [
"PUB00003956",
"PUB00004640"
] | [
"9406548",
"3475690"
] | [
"Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria.",
"Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases."
] | [
1997,
1987
] | 2 | [
"IPR001273"
] | [
"IPR005961",
"IPR005962",
"IPR005963"
] | 1 | 3 | 0 | [
"Eukaryota"
] | [
6860
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
9,
8,
9,
7,
21
] | 6 | true | Family | Tyrosine 3-monooxygenase-like | Tyrosine 3-monooxygenase-like | Tyrosine_3-monooxygenase-like | 2 |
IPR019774 | 19,774 | Aromatic amino acid hydroxylase, C-terminal | Aromatic-AA_hydroxylase_C | Domain | 18,811 | false | false | This entry represents a domain containing the catalytic domain and the coiled-coil C-terminal oligomerization motif. Hydroxylation of the aromatic amino acids phenylalanine, tyrosine and tryptophan is carried out by a family of non-heme iron and tetrahydrobiopterin (BH4) dependent enzymes: the aromatic amino acid hydro... | [
"GO:0016714"
] | [
"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF00351",
"PR00372",
"PS51410"
] | [
"Biopterin_H",
"FYWHYDRXLASE",
"BH4_AAA_HYDROXYL_2"
] | [
18550,
15375,
18717
] | 3 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.16",
"R-BTA-8964208",
"R-CEL-209905",
"R-CEL-8964208",
"R-DDI-209905",
"R-DDI-209931",
"R-DDI-8964208",
"R-DME-209905",
"R-DME-8964208",
"R-HSA-209905",
"R-HSA-209931",
"R-HSA-2160456",
"R-HSA-8964208",
"R-HSA-9031628",
"R-MMU-209905",
"R-MMU-209931",
"R-MMU-8964208",
"R-RNO-... | [
"EC:1.14.16",
"REACTOME:R-BTA-8964208",
"REACTOME:R-CEL-209905",
"REACTOME:R-CEL-8964208",
"REACTOME:R-DDI-209905",
"REACTOME:R-DDI-209931",
"REACTOME:R-DDI-8964208",
"REACTOME:R-DME-209905",
"REACTOME:R-DME-8964208",
"REACTOME:R-HSA-209905",
"REACTOME:R-HSA-209931",
"REACTOME:R-HSA-2160456",
... | 20 | [
"1dmw",
"1j8t",
"1j8u",
"1kw0",
"1lrm",
"1ltu",
"1ltv",
"1ltz",
"1mlw",
"1mmk",
"1mmt",
"1pah",
"1phz",
"1tdw",
"1tg2",
"1toh",
"2pah",
"2phm",
"2toh",
"2v27",
"2v28",
"2xsn",
"3e2t",
"3hf6",
"3hf8",
"3hfb",
"3pah",
"3tcy",
"3tk2",
"3tk4",
"4anp",
"4bpt"... | 78 | [
"PUB00002657",
"PUB00004466",
"PUB00004640",
"PUB00004833",
"PUB00037005",
"PUB00086611",
"PUB00086612"
] | [
"1655752",
"8594560",
"3475690",
"8108417",
"11718561",
"14640675",
"15537351"
] | [
"Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases.",
"PAH Mutation Analysis Consortium Database: a database for disease-producing and other allelic variation at the human PAH locu... | [
1991,
1996,
1987,
1994,
2001,
2003,
2004
] | 7 | [] | [
"IPR041903",
"IPR041904",
"IPR041912"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
22,
6469,
12227,
13,
80
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
10,
9,
47,
15,
22
] | 6 | true | Domain | Aromatic amino acid hydroxylase, C-terminal | Aromatic amino acid hydroxylase, C-terminal | Aromatic-AA_hydroxylase_C | 5 |
IPR019775 | 19,775 | WD40 repeat, conserved site | WD40_repeat_CS | Conserved_site | 459,790 | false | false | This entry represents a conserved site found in the WD40 repeat. WD-40 repeats (also known as WD or beta-transducin repeats) are short ~40 amino acid motifs, often terminating in a Trp-Asp (W-D) dipeptide. WD40 repeats usually assume a 7-8 bladed β-propeller fold, but proteins have been found with 4 to 16 repeated unit... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00678"
] | [
"WD_REPEATS_1"
] | [
459790
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1296041",
"R-BTA-1538133",
"R-BTA-156827",
"R-BTA-159227",
"R-BTA-159230",
"R-BTA-159231",
"R-BTA-159236",
"R-BTA-1632852",
"R-BTA-165159",
"R-BTA-166208",
"R-BTA-168638",
"R-BTA-170822",
"R-BTA-177929",
"R-BTA-191859",
"R-BTA-202040",
"R-BTA-212300",
"R-BTA-2485179",
"R-BTA... | [
"REACTOME:R-BTA-1296041",
"REACTOME:R-BTA-1538133",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-159227",
"REACTOME:R-BTA-159230",
"REACTOME:R-BTA-159231",
"REACTOME:R-BTA-159236",
"REACTOME:R-BTA-1632852",
"REACTOME:R-BTA-165159",
"REACTOME:R-BTA-166208",
"REACTOME:R-BTA-168638",
"REACTOME:R-BTA-... | 1,092 | [
"1a0r",
"1b9x",
"1b9y",
"1erj",
"1gg2",
"1got",
"1gp2",
"1gxr",
"1nex",
"1nr0",
"1omw",
"1p22",
"1pev",
"1s4u",
"1sq9",
"1tbg",
"1trj",
"1vyh",
"1xhm",
"2aq5",
"2b4e",
"2bcj",
"2ce8",
"2ce9",
"2cnx",
"2co0",
"2g99",
"2g9a",
"2gnq",
"2h13",
"2h14",
"2h68"... | 2,904 | [
"PUB00005491",
"PUB00015237",
"PUB00094364"
] | [
"10322433",
"11814058",
"30069656"
] | [
"The WD repeat: a common architecture for diverse functions.",
"WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases.",
"WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions."
] | [
1999,
2001,
2018
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
52,
19112,
440356,
62,
208
] | 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... | [
618,
61,
527,
170,
607,
411,
53,
309,
573,
42,
53,
991
] | 12 | true | Conserved_site | WD40 repeat, conserved site | WD40 repeat, conserved site | WD40_repeat_CS | 7 |
IPR019776 | 19,776 | Flagellar basal body rod protein, conserved site | Flagellar_basal_body_rod_CS | Conserved_site | 43,564 | false | false | Many bacterial species swim actively by means of flagella. The flagella organelle is made of three parts: the basal body, the hook and the filament. The basal body consists of four rings (L,P,S, and M) mounted on a central rod [ ]. In Salmonella typhimurium and related organisms the rod has been shown to consist of fou... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00588"
] | [
"FLAGELLA_BB_ROD"
] | [
43564
] | 1 | [] | [] | [] | 0 | [
"3a69",
"5npy",
"5wrh",
"6jzr",
"6jzt",
"6k3i",
"6k9q",
"6kfk",
"7bin",
"7cbm",
"7cg0",
"7cgb",
"7cgo",
"7e80",
"7e82",
"7nvg",
"8wk3",
"8wk4",
"8wki",
"8wkk",
"8wkq",
"8wl2",
"8wlh",
"8wln",
"8wlp",
"8wlq",
"8wlt",
"8wo5",
"8woe",
"8z5s",
"8z5u",
"8z5w"... | 37 | [
"PUB00003254"
] | [
"2129540"
] | [
"FlgB, FlgC, FlgF and FlgG. A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanimicrococcus stummii",
"unclassified sequences"
] | [
43004,
94,
1,
465
] | 4 | [
"Escherichia coli (strain K12)"
] | [
5
] | 1 | true | Conserved_site | Flagellar basal body rod protein, conserved site | Flagellar basal body rod protein, conserved site | Flagellar_basal_body_rod_CS | 6 |
IPR019777 | 19,777 | Formate C-acetyltransferase glycine radical, conserved site | Form_AcTrfase_GR_CS | Conserved_site | 20,261 | false | false | This entry represents a conserved site found in Formate acetyltransferase. Protein radicals are components of several biologically important reactions. Glycyl radical enzymes are involved in a great variety of functions, for example, nucleotide, pyruvate and toluene metabolism [ ]. These enzymes are post-translationall... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00850"
] | [
"GLY_RADICAL_1"
] | [
20261
] | 1 | [] | [] | [] | 0 | [
"1cm5",
"1h16",
"1h17",
"1h18",
"1mzo",
"1r8w",
"1r9d",
"2pfl",
"3pfl",
"4mtj",
"4pkc",
"4pkf",
"5a0u",
"5a0z",
"5bwd",
"5bwe",
"5fau",
"5fav",
"5faw",
"5fay",
"5i2a",
"5i2g",
"5kdp",
"5ymr",
"6lon",
"6nd3",
"6owr",
"6vue",
"6xs4",
"7e7l",
"7kq3",
"7kq4"... | 44 | [
"PUB00004806",
"PUB00004820",
"PUB00014425",
"PUB00033790",
"PUB00033791"
] | [
"1310545",
"8421692",
"11444864",
"10574800",
"8051113"
] | [
"The free radical in pyruvate formate-lyase is located on glycine-734.",
"A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene.",
"YfiD of Escherichia coli and Y06I of bacteriophage T4 as autonomous glycyl radical cofactors reconstit... | [
1992,
1993,
2001,
1999,
1994
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2,
19034,
180,
957,
88
] | 5 | [
"Escherichia coli (strain K12)"
] | [
6
] | 1 | true | Conserved_site | Formate C-acetyltransferase glycine radical, conserved site | Formate C-acetyltransferase glycine radical, conserved site | Form_AcTrfase_GR_CS | 8 |
IPR019778 | 19,778 | Class I Hydrophobin, conserved site | Class_I_Hydrophobin_CS | Conserved_site | 1,597 | false | false | This entry represents a cysteine-rich conserved site found at the C-terminal end of class I hydrophobin sequences. Hydrophobins are small, moderately hydrophobic extracellular proteins characterised by eight cysteine residues arranged in a strictly conserved motif. They are typically found on the outer surface of conid... | [
"GO:0005199",
"GO:0009277"
] | [
"structural constituent of cell wall",
"fungal-type cell wall"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00956"
] | [
"HYDROPHOBIN"
] | [
1597
] | 1 | [] | [] | [] | 0 | [
"2fmc",
"2k6a",
"2lfn",
"2lsh",
"2n4o",
"2nbh",
"5w0y",
"6gcj",
"7s7s",
"7s86"
] | 10 | [
"PUB00001789",
"PUB00001900",
"PUB00001904",
"PUB00012827",
"PUB00059146",
"PUB00059147",
"PUB00089655",
"PUB00160789"
] | [
"2401401",
"2065971",
"1459459",
"11343402",
"10584000",
"9344630",
"10336622",
"3080312"
] | [
"Two genes specifically expressed in fruiting dikaryons of Schizophyllum commune: homologies with a gene not regulated by mating-type genes.",
"Rodletless, a new Aspergillus developmental mutant induced by directed gene inactivation.",
"Developmental and light regulation of eas, the structural gene for the rodl... | [
1990,
1991,
1992,
2001,
1999,
1997,
1999,
1986
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
3,
1594
] | 2 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Conserved_site | Class I Hydrophobin, conserved site | Class I Hydrophobin, conserved site | Class_I_Hydrophobin_CS | 7 |
IPR019779 | 19,779 | Galactose-1-phosphate uridyl transferase, class I His-active site | GalP_UDPtransf1_His-AS | Active_site | 10,802 | false | false | Galactose-1-phosphate uridyl transferase (galT) catalyses the transfer of an uridyldiphosphate group on galactose (or glucose) 1-phosphate. During the reaction, the uridyl moiety links to a histidine residue. In the Escherichia coli enzyme, it has been shown [ ] that two histidine residues separated by a single proline... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00117"
] | [
"GAL_P_UDP_TRANSF_I"
] | [
10802
] | 1 | [
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.12",
"PWY-6317",
"PWY-6527",
"R-CEL-70370",
"R-DME-70370",
"R-HSA-5609978",
"R-HSA-70370",
"R-MMU-70370",
"R-RNO-70370"
] | [
"EC:2.7.7.12",
"METACYC:PWY-6317",
"METACYC:PWY-6527",
"REACTOME:R-CEL-70370",
"REACTOME:R-DME-70370",
"REACTOME:R-HSA-5609978",
"REACTOME:R-HSA-70370",
"REACTOME:R-MMU-70370",
"REACTOME:R-RNO-70370"
] | 9 | [
"1hxp",
"1hxq",
"5in3",
"6gqd"
] | 4 | [
"PUB00002146",
"PUB00004352"
] | [
"2066342",
"2845364"
] | [
"Galactose utilization in Lactobacillus helveticus: isolation and characterization of the galactokinase (galK) and galactose-1-phosphate uridyl transferase (galT) genes.",
"Conservation of short patches of amino acid sequence amongst proteins with a common function but evolutionarily distinct origins: implication... | [
1991,
1988
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
7245,
3381,
7,
169
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
... | [
1,
4,
2,
1,
7,
6,
1,
4,
1,
1
] | 10 | true | Active_site | Galactose-1-phosphate uridyl transferase, class I His-active site | Galactose-1-phosphate uridyl transferase, class I His-active site | GalP_UDPtransf1_His-AS | 4 |
IPR019780 | 19,780 | Germin, manganese binding site | Germin_Mn-BS | Binding_site | 14,947 | false | false | Germins and germin-like proteins [ ] are a family of hexameric ubiquitous plant glycoproteins. They are not restricted to germinating grains as initially thought and therefore called 'germins', but they exist in all organs and developmental stages. They are all partly associated with the extracellular matrix. A wide ra... | [
"GO:0030145"
] | [
"manganese ion binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00725"
] | [
"GERMIN"
] | [
14947
] | 1 | [] | [] | [] | 0 | [
"1fi2",
"2et1",
"2et7",
"2ete"
] | 4 | [
"PUB00001527",
"PUB00003443"
] | [
"8143935",
"9541544"
] | [
"Oxalate, germin, and the extracellular matrix of higher plants.",
"Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase."
] | [
1994,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"marine metagenome"
] | [
6,
290,
14650,
1
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
104,
51,
99
] | 3 | true | Binding_site | Germin, manganese binding site | Germin, manganese binding site | Germin_Mn-BS | 9 |
IPR019783 | 19,783 | Ribosome maturation protein SDO1/SBDS, N-terminal | SDO1/SBDS_N | Domain | 7,563 | false | false | This entry represents the N-terminal domain of proteins that are highly conserved in species ranging from archaea to vertebrates and plants [ ], including several Shwachman-Bodian-Diamond syndrome (SBDS, OMIM 260400) proteins from both mouse and humans. Shwachman-Diamond syndrome is an autosomal recessive disorder with... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01172"
] | [
"SBDS_N"
] | [
7563
] | 1 | [] | [] | [] | 0 | [
"1nyn",
"1p9q",
"1t95",
"2kdo",
"2l9n",
"2wbm",
"5an9",
"5anb",
"5anc",
"6fsw",
"6qkl",
"6skg"
] | 12 | [
"PUB00020303",
"PUB00020304",
"PUB00020305",
"PUB00045126",
"PUB00076340"
] | [
"12496757",
"15701634",
"15701631",
"17353896",
"21536732"
] | [
"Mutations in SBDS are associated with Shwachman-Diamond syndrome.",
"The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism.",
"Structural and mutational analysis of the SBDS protein family. Insight into the leukemia-associated Shwachman-Diamond Syndrome.",
"The Shwachman-Bodian-D... | [
2003,
2005,
2005,
2007,
2011
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
905,
3,
6613,
42
] | 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... | [
5,
1,
2,
3,
10,
3,
2,
2,
4,
2,
2,
3
] | 12 | true | Domain | Ribosome maturation protein SDO1/SBDS, N-terminal | Ribosome maturation protein SDO1/SBDS, N-terminal | SDO1/SBDS_N | 9 |
IPR019786 | 19,786 | Zinc finger, PHD-type, conserved site | Zinc_finger_PHD-type_CS | Conserved_site | 170,343 | false | false | Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01359"
] | [
"ZF_PHD_1"
] | [
170343
] | 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-6807505",
"R-BTA-9772755",
"R-CEL-114608",
"R-CEL-2299718",
"R-CEL-3214841",
"R-CEL-3214842",
"R-CEL-3214847",
"R-CEL-4551638",
"R-CEL-6804758",
"R-CEL-8936459",
"R-CEL-9031628",
"R-CEL-9772755",
"R-DME-114608",
"R-DME-201722",
"R-DME-209407",
"R-DME-209421",
"R-DME-3214815",
... | [
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-9772755",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-2299718",
"REACTOME:R-CEL-3214841",
"REACTOME:R-CEL-3214842",
"REACTOME:R-CEL-3214847",
"REACTOME:R-CEL-4551638",
"REACTOME:R-CEL-6804758",
"REACTOME:R-CEL-8936459",
"REACTOME:R-CEL-9031628",
"REACTOME... | 141 | [
"1f62",
"1fp0",
"1mm2",
"1mm3",
"1we9",
"1wee",
"1wem",
"1wen",
"1wep",
"1wes",
"1weu",
"1wev",
"1wew",
"1wil",
"1x4i",
"1xwh",
"2dx8",
"2e6r",
"2e6s",
"2f6j",
"2f6n",
"2fsa",
"2fui",
"2fuu",
"2g6q",
"2k16",
"2k17",
"2k1j",
"2ke1",
"2kft",
"2ku3",
"2kwj"... | 419 | [
"PUB00005446",
"PUB00014077",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"7701562",
"12665246",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"The PHD finger: implications for chromatin-mediated transcriptional regulation.",
"Zinc fingers--folds for many occasions.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
"Zinc finger proteins: getting a grip on RNA.",
"Zinc f... | [
1995,
2002,
2007,
2005,
2005,
1999,
2001
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes",
"unclassified Marseilleviridae"
] | [
16,
18,
170297,
10,
2
] | 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... | [
375,
42,
423,
81,
314,
205,
14,
133,
264,
11,
19,
774
] | 12 | true | Conserved_site | Zinc finger, PHD-type, conserved site | Zinc finger, PHD-type, conserved site | Zinc_finger_PHD-type_CS | 4 |
IPR019787 | 19,787 | Zinc finger, PHD-finger | Znf_PHD-finger | Domain | 209,810 | false | false | This entry represents the PHD (homeodomain) zinc finger domain [ ], which is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in chromatin-mediated transcriptional regulation. The PHD finger motif is reminiscent of, but distinct from the C3HC4 type RING finger. The function of this domain... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF00628",
"PF13831",
"PF16866",
"PF27108",
"PS50016"
] | [
"PHD",
"PHD_2",
"PHD_4",
"PHD_Pygo",
"ZF_PHD_2"
] | [
142298,
27809,
6207,
4082,
191610
] | 5 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-6807505",
"R-BTA-9772755",
"R-CEL-114608",
"R-CEL-3214842",
"R-CEL-3214847",
"R-CEL-4551638",
"R-CEL-6804758",
"R-CEL-9031628",
"R-DME-114608",
"R-DME-201722",
"R-DME-209407",
"R-DME-209421",
"R-DME-3214815",
"R-DME-6804758",
"R-DME-6807505",
"R-DME-8866911",
"R-DME-8936459",
... | [
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-9772755",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-3214842",
"REACTOME:R-CEL-3214847",
"REACTOME:R-CEL-4551638",
"REACTOME:R-CEL-6804758",
"REACTOME:R-CEL-9031628",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-201722",
"REACTOME:R-DME-209407",
"REACTOME:R-... | 159 | [
"1f62",
"1fp0",
"1mm2",
"1mm3",
"1we9",
"1wee",
"1wem",
"1wen",
"1wep",
"1wes",
"1weu",
"1wev",
"1x4i",
"1xwh",
"2dx8",
"2e6r",
"2e6s",
"2f6j",
"2f6n",
"2fsa",
"2fui",
"2fuu",
"2g6q",
"2k16",
"2k17",
"2k1j",
"2ke1",
"2kft",
"2kgg",
"2kgi",
"2ku3",
"2ku7"... | 438 | [
"PUB00005446",
"PUB00014077",
"PUB00018073",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00045076"
] | [
"7701562",
"12665246",
"11124022",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"17142463"
] | [
"The PHD finger: implications for chromatin-mediated transcriptional regulation.",
"Zinc fingers--folds for many occasions.",
"Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA re... | [
1995,
2002,
2000,
2007,
2005,
2005,
1999,
2001,
2007
] | 9 | [
"IPR001965"
] | [
"IPR028940",
"IPR031202",
"IPR037373",
"IPR037877",
"IPR039054",
"IPR039546",
"IPR039548",
"IPR039550",
"IPR041947",
"IPR042008",
"IPR042009",
"IPR042010",
"IPR042011",
"IPR042014",
"IPR042019",
"IPR042020",
"IPR042023",
"IPR042025",
"IPR044075",
"IPR044104",
"IPR044133",
"... | 1 | 38 | 0 | [
"Archaea",
"Bacillati",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
4,
2,
209787,
3,
14
] | 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... | [
387,
41,
619,
101,
428,
275,
16,
163,
354,
12,
17,
782
] | 12 | true | Domain | Zinc finger, PHD-finger | Zinc finger, PHD-finger | Znf_PHD-finger | 5 |
IPR019789 | 19,789 | Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, thiamine diphosphate binding site | Xul5P/Fru6P_PKetolase_ThDP_BS | Binding_site | 8,988 | false | false | Phosphoketolases (PK) are key enzymes of the pentose phosphate pathway of heterofermentative and facultative homofermentative lactic acid bacteria and of the D-fructose 6-phosphate shunt of bifidobacteria. PK activity has been sporadically reported in other microorganisms including eukaryotic yeasts. Xylulose-5-phospha... | [
"GO:0016832",
"GO:0005975"
] | [
"aldehyde-lyase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS60003"
] | [
"PHOSPHOKETOLASE_2"
] | [
8988
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"4.1.2.-",
"PWY-7085",
"PWY-7089"
] | [
"EC:4.1.2.-",
"METACYC:PWY-7085",
"METACYC:PWY-7089"
] | 3 | [
"3ahc",
"3ahd",
"3ahe",
"3ahf",
"3ahg",
"3ahh",
"3ahi",
"3ahj",
"3ai7",
"6gua",
"6lxv",
"7c8h",
"7c8i",
"8io6",
"8io7",
"8io8",
"8io9",
"8ioa",
"8ioe",
"9cd3",
"9cd4"
] | 21 | [
"PUB00008466",
"PUB00045300"
] | [
"11292814",
"15899413"
] | [
"Characterization of the D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase gene (xfp) from Bifidobacterium lactis.",
"The gene encoding xylulose-5-phosphate/fructose-6-phosphate phosphoketolase (xfp) is conserved among Bifidobacterium species within a more variable region of the genome and both are us... | [
2001,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
7092,
1856,
40
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
1
] | 2 | true | Binding_site | Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, thiamine diphosphate binding site | Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, thiamine diphosphate binding site | Xul5P/Fru6P_PKetolase_ThDP_BS | 6 |
IPR019790 | 19,790 | Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, conserved site | Xul5P/Fru6P_PKetolase_CS | Conserved_site | 9,507 | false | false | Phosphoketolases (PK) are key enzymes of the pentose phosphate pathway of heterofermentative and facultative homofermentative lactic acid bacteria and of the D-fructose 6-phosphate shunt of bifidobacteria. PK activity has been sporadically reported in other microorganisms including eukaryotic yeasts. Xylulose-5-phospha... | [
"GO:0016832",
"GO:0005975"
] | [
"aldehyde-lyase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS60002"
] | [
"PHOSPHOKETOLASE_1"
] | [
9507
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"4.1.2.-",
"PWY-7085",
"PWY-7089"
] | [
"EC:4.1.2.-",
"METACYC:PWY-7085",
"METACYC:PWY-7089"
] | 3 | [
"3ahc",
"3ahd",
"3ahe",
"3ahf",
"3ahg",
"3ahh",
"3ahi",
"3ahj",
"3ai7",
"6gua",
"6lxv",
"7c8h",
"7c8i",
"8io6",
"8io7",
"8io8",
"8io9",
"8ioa",
"8ioe",
"9cd3",
"9cd4"
] | 21 | [
"PUB00008466",
"PUB00045300"
] | [
"11292814",
"15899413"
] | [
"Characterization of the D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase gene (xfp) from Bifidobacterium lactis.",
"The gene encoding xylulose-5-phosphate/fructose-6-phosphate phosphoketolase (xfp) is conserved among Bifidobacterium species within a more variable region of the genome and both are us... | [
2001,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
7594,
1870,
43
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
1
] | 2 | true | Conserved_site | Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, conserved site | Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, conserved site | Xul5P/Fru6P_PKetolase_CS | 5 |
IPR019791 | 19,791 | Haem peroxidase, animal-type | Haem_peroxidase_animal | Family | 32,555 | false | false | Peroxidases are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Peroxidases are found in bacteria, fungi, plants and animals. On the basis of sequence similarity, a number of animal haem peroxidases can be categorised as members of a superfamily: ... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF03098",
"PR00457",
"PS50292"
] | [
"An_peroxidase",
"ANPEROXIDASE",
"PEROXIDASE_3"
] | [
32239,
23867,
32102
] | 3 | [
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp0213",
"GenProp1603",
"GenProp1728",
"R-BTA-8941413",
"R-CEL-209968",
"R-CEL-6798695",
"R-CEL-8941413",
"R-CFA-140180",
"R-CFA-209968",
"R-CFA-2162123",
"R-DDI-209968",
"R-DDI-6798695",
"R-DDI-8941413",
"R-DME-209968",
"R-DME-6798695",
"R-DME-8941413",
"R-GGA-2142770",
"R-G... | [
"GP:GenProp0213",
"GP:GenProp1603",
"GP:GenProp1728",
"REACTOME:R-BTA-8941413",
"REACTOME:R-CEL-209968",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-8941413",
"REACTOME:R-CFA-140180",
"REACTOME:R-CFA-209968",
"REACTOME:R-CFA-2162123",
"REACTOME:R-DDI-209968",
"REACTOME:R-DDI-6798695",
"REACTOM... | 57 | [
"1cqe",
"1cvu",
"1cx2",
"1cxp",
"1d2v",
"1d5l",
"1d7w",
"1ddx",
"1diy",
"1dnu",
"1dnw",
"1ebv",
"1eqg",
"1eqh",
"1fe2",
"1ht5",
"1ht8",
"1igx",
"1igz",
"1mhl",
"1myp",
"1pge",
"1pgf",
"1pgg",
"1prh",
"1pth",
"1pxx",
"1q4g",
"1u67",
"2ayl",
"2e9e",
"2efb"... | 233 | [
"PUB00000306",
"PUB00000580",
"PUB00001259",
"PUB00001479",
"PUB00003292",
"PUB00004165",
"PUB00004979",
"PUB00005246"
] | [
"2548579",
"6295491",
"8062820",
"7774640",
"1320128",
"8121489",
"2840655",
"7922023"
] | [
"Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene.",
"The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase.",
"Peroxidasin: a novel enzyme-matrix protein of Drosophila development.",
"Human eosinophil peroxidase enhances ... | [
1989,
1982,
1994,
1995,
1992,
1994,
1988,
1994
] | 8 | [] | [
"IPR029589",
"IPR034815"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
34,
3353,
29100,
14,
54
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
10,
14,
38,
23,
45,
29,
3,
5,
35,
8
] | 10 | true | Family | Haem peroxidase, animal-type | Haem peroxidase, animal-type | Haem_peroxidase_animal | 9 |
IPR019792 | 19,792 | Gonadoliberin | Gonadoliberin | Family | 1,429 | false | false | The gonadotropin-releasing hormones (GnRH) (gonadoliberin) are a family of peptides that play a pivotal role in reproduction. The main function of GnRH is to act on the pituitary to stimulate the synthesis and secretion of luteinizing and follicle-stimulating hormones, but GnRH also acts on the brain, retina, sympathet... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR10522"
] | [
""
] | [
1429
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-GGA-375281",
"R-GGA-416476",
"R-HSA-375281",
"R-HSA-416476",
"R-MMU-375281",
"R-MMU-416476",
"R-RNO-375281",
"R-RNO-416476",
"R-SSC-375281",
"R-SSC-416476"
] | [
"REACTOME:R-GGA-375281",
"REACTOME:R-GGA-416476",
"REACTOME:R-HSA-375281",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-375281",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-375281",
"REACTOME:R-RNO-416476",
"REACTOME:R-SSC-375281",
"REACTOME:R-SSC-416476"
] | 10 | [] | 0 | [
"PUB00092644"
] | [
"18284378"
] | [
"Structural and functional evolution of gonadotropin-releasing hormone in vertebrates."
] | [
2008
] | 1 | [] | [
"IPR004079"
] | 0 | 1 | 0 | [
"Chordata"
] | [
1429
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
3,
3
] | 4 | true | Family | Gonadoliberin | Gonadoliberin | Gonadoliberin | 8 |
IPR019793 | 19,793 | Peroxidases heam-ligand binding site | Peroxidases_heam-ligand_BS | Binding_site | 59,890 | false | false | null | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00435"
] | [
"PEROXIDASE_1"
] | [
59890
] | 1 | [
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME"
] | [
"1.11.1",
"1.11.1.21",
"PWY-5506",
"R-HSA-1222387",
"R-HSA-2408557"
] | [
"EC:1.11.1",
"EC:1.11.1.21",
"METACYC:PWY-5506",
"REACTOME:R-HSA-1222387",
"REACTOME:R-HSA-2408557"
] | 5 | [
"1a2g",
"1aa4",
"1ac4",
"1ac8",
"1aeb",
"1aed",
"1aee",
"1aef",
"1aeg",
"1aeh",
"1aej",
"1aek",
"1aem",
"1aen",
"1aeo",
"1aeq",
"1aes",
"1aet",
"1aeu",
"1aev",
"1apx",
"1arp",
"1aru",
"1arv",
"1arw",
"1arx",
"1ary",
"1atj",
"1b80",
"1b82",
"1bej",
"1bek"... | 484 | [
"PUB00000617",
"PUB00001259",
"PUB00001743",
"PUB00005246"
] | [
"1954228",
"8062820",
"8167033",
"7922023"
] | [
"Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily.",
"Peroxidasin: a novel enzyme-matrix protein of Drosophila development.",
"Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium.",
"Structural variation in heme enzymes: a com... | [
1991,
1994,
1994,
1994
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
401,
11290,
48096,
103
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Homo sapiens",
"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"
] | [
287,
1,
3,
2,
408,
1,
476
] | 7 | true | Binding_site | Peroxidases heam-ligand binding site | Peroxidases heam-ligand binding site | Peroxidases_heam-ligand_BS | 9 |
IPR019794 | 19,794 | Peroxidase, active site | Peroxidases_AS | Active_site | 56,596 | false | false | null | [
"GO:0004601"
] | [
"peroxidase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00436"
] | [
"PEROXIDASE_2"
] | [
56596
] | 1 | [
"EC",
"EC",
"METACYC",
"REACTOME"
] | [
"1.11.1",
"1.11.1.21",
"PWY-5506",
"R-HSA-1222387"
] | [
"EC:1.11.1",
"EC:1.11.1.21",
"METACYC:PWY-5506",
"REACTOME:R-HSA-1222387"
] | 4 | [
"1a2f",
"1a2g",
"1aa4",
"1ac4",
"1ac8",
"1aeb",
"1aed",
"1aee",
"1aef",
"1aeg",
"1aeh",
"1aej",
"1aek",
"1aem",
"1aen",
"1aeo",
"1aeq",
"1aes",
"1aet",
"1aeu",
"1aev",
"1apx",
"1arp",
"1aru",
"1arv",
"1arw",
"1arx",
"1ary",
"1atj",
"1b80",
"1b82",
"1b85"... | 430 | [
"PUB00000617",
"PUB00001259",
"PUB00001743",
"PUB00005246"
] | [
"1954228",
"8062820",
"8167033",
"7922023"
] | [
"Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily.",
"Peroxidasin: a novel enzyme-matrix protein of Drosophila development.",
"Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium.",
"Structural variation in heme enzymes: a com... | [
1991,
1994,
1994,
1994
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
418,
13448,
42579,
151
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
241,
1,
2,
348,
1,
369
] | 6 | true | Active_site | Peroxidase, active site | Peroxidase, active site | Peroxidases_AS | 2 |
IPR019795 | 19,795 | Globin, bacterial-like, conserved site | Globin_bac-like_CS | Conserved_site | 4,430 | false | false | Globins are haem-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family that is widely distributed in many organisms [ ]. Globins have evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric gl... | [
"GO:0019825",
"GO:0015671"
] | [
"oxygen binding",
"oxygen transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS01213"
] | [
"GLOBIN_FAM_2"
] | [
4430
] | 1 | [
"REACTOME"
] | [
"R-HSA-1222538"
] | [
"REACTOME:R-HSA-1222538"
] | 1 | [
"1dlw",
"1dly",
"1idr",
"1mwb",
"1ngk",
"1rte",
"1rtx",
"1s56",
"1s61",
"1s69",
"1s6a",
"1uvx",
"1uvy",
"1ux8",
"2bmm",
"2gkm",
"2gkn",
"2gl3",
"2gln",
"2hz1",
"2hz2",
"2hz3",
"2qrw",
"3aq5",
"3aq6",
"3aq7",
"3aq8",
"3aq9",
"4uzv",
"5ab8",
"5d1v",
"5v3t"... | 42 | [
"PUB00016016",
"PUB00029465",
"PUB00035865",
"PUB00035866",
"PUB00035867",
"PUB00035868",
"PUB00035869",
"PUB00035870",
"PUB00035871",
"PUB00035872",
"PUB00035873",
"PUB00035877",
"PUB00035878",
"PUB00035879",
"PUB00035880",
"PUB00035881",
"PUB00055462",
"PUB00055463",
"PUB001536... | [
"15096613",
"12962627",
"16600051",
"17540514",
"11092893",
"11481493",
"15598488",
"16888280",
"15598493",
"15339940",
"15804833",
"17084861",
"16814781",
"11796724",
"10684619",
"11526234",
"17540516",
"17701548",
"21495624"
] | [
"Ancestral hemoglobins in Archaea.",
"Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity.",
"A phylogenomic profile of globins.",
"A model of globin evolution.",
"Flavohemoglobin, a globin with a peroxidase-like catalytic site.",
"Globin-coupled sensors: a class of he... | [
2004,
2003,
2006,
2007,
2001,
2001,
2005,
2006,
2005,
2004,
2004,
2007,
2006,
2002,
2000,
2001,
2007,
2007,
2011
] | 19 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
39,
4123,
142,
126
] | 4 | [] | [] | 0 | true | Conserved_site | Globin, bacterial-like, conserved site | Globin, bacterial-like, conserved site | Globin_bac-like_CS | 3 |
IPR019796 | 19,796 | Glucose-6-phosphate dehydrogenase, active site | G6P_DH_AS | Active_site | 30,728 | false | false | Glucose-6-phosphate dehydrogenase (G6PD) [ ] catalyses the first step in the pentose pathway, the reduction of glucose-6-phosphate to gluconolactone 6-phosphate. A lysine residue has been identified as a reactive nucleophile associated with the activity of the enzyme [ ]. The sequence around this lysine is totally cons... | [
"GO:0004345",
"GO:0006006"
] | [
"glucose-6-phosphate dehydrogenase activity",
"glucose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00069"
] | [
"G6P_DEHYDROGENASE"
] | [
30728
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"1.1.1.49",
"PWY-7268",
"PWY-8004",
"R-CEL-5628897",
"R-CEL-71336",
"R-DDI-5628897",
"R-DDI-71336",
"R-DME-5628897",
"R-DME-71336",
"R-HSA-5628897",
"R-HSA-71336",
"R-HSA-9818028",
"R-MMU-5628897",
"R-MMU-71336",
"R-RNO-5628897",
"R-RNO-71336",
"R-SCE-5628897",
"R-SCE-71... | [
"EC:1.1.1",
"EC:1.1.1.49",
"METACYC:PWY-7268",
"METACYC:PWY-8004",
"REACTOME:R-CEL-5628897",
"REACTOME:R-CEL-71336",
"REACTOME:R-DDI-5628897",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-5628897",
"REACTOME:R-DME-71336",
"REACTOME:R-HSA-5628897",
"REACTOME:R-HSA-71336",
"REACTOME:R-HSA-9818028",... | 21 | [
"1dpg",
"1e77",
"1h93",
"1h94",
"1h9a",
"1h9b",
"1qki",
"2bh9",
"2bhl",
"2dpg",
"4lgv",
"5aq1",
"5ukw",
"6d23",
"6d24",
"6e07",
"6e08",
"6jyu",
"6va0",
"6va7",
"6va8",
"6va9",
"6vaq",
"7e6h",
"7e6i",
"7seh",
"7sei",
"7snf",
"7sng",
"7snh",
"7toe",
"7tof"... | 53 | [
"PUB00001438",
"PUB00045349"
] | [
"8444164",
"3126064"
] | [
"Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure.",
"Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a reactive lysyl residue labelled with pyridoxal 5'-phosphate."
] | [
1993,
1988
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"unclassified sequences"
] | [
21647,
2,
8876,
203
] | 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,
1,
10,
1,
1,
24,
6,
1,
16,
5,
1,
1,
20
] | 13 | true | Active_site | Glucose-6-phosphate dehydrogenase, active site | Glucose-6-phosphate dehydrogenase, active site | G6P_DH_AS | 7 |
IPR019797 | 19,797 | Glutamate 5-kinase, conserved site | Glutamate_5-kinase_CS | Conserved_site | 25,325 | false | false | Glutamate 5-kinase ( ) (gamma-glutamyl kinase) (GK) is the enzyme that catalyzes the first step in the biosynthesis of proline from glutamate, the ATP-dependent phosphorylation of L-glutamate into L-glutamate 5-phosphate. In eubacteria (gene proB) and yeast [ ] (gene PRO1), GK is a monofunctional protein, while in plan... | [
"GO:0004349",
"GO:0055129"
] | [
"glutamate 5-kinase activity",
"L-proline biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00902"
] | [
"GLUTAMATE_5_KINASE"
] | [
25325
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.2.11",
"PWY-6922",
"R-CEL-8964539",
"R-CEL-9837999",
"R-HSA-8964539",
"R-HSA-9837999",
"R-MMU-8964539",
"R-MMU-9837999"
] | [
"EC:2.7.2.11",
"METACYC:PWY-6922",
"REACTOME:R-CEL-8964539",
"REACTOME:R-CEL-9837999",
"REACTOME:R-HSA-8964539",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-8964539",
"REACTOME:R-MMU-9837999"
] | 8 | [
"2ako",
"2j5t",
"2j5v",
"2w21",
"4q1t",
"7f5t",
"7f5u",
"7f5v",
"7f5x",
"7wx3",
"7wx4",
"7wxf",
"7wxg",
"7wxh",
"7wxi",
"8j0e",
"8j0f",
"8j0g",
"8j27",
"8j28",
"8y2h",
"8zpj",
"8zpr",
"8zri"
] | 24 | [
"PUB00002185",
"PUB00004804"
] | [
"1350780",
"1384052"
] | [
"Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase.",
"A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants."
] | [
1992,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Hyperionvirus sp.",
"unclassified sequences"
] | [
81,
18785,
6101,
1,
357
] | 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,
1,
4,
1,
1,
1,
4,
1,
4,
2,
2,
1,
32
] | 13 | true | Conserved_site | Glutamate 5-kinase, conserved site | Glutamate 5-kinase, conserved site | Glutamate_5-kinase_CS | 1 |
IPR019798 | 19,798 | Serine hydroxymethyltransferase, pyridoxal phosphate binding site | Ser_HO-MeTrfase_PLP_BS | Binding_site | 41,200 | false | false | null | [
"GO:0030170"
] | [
"pyridoxal phosphate binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00096"
] | [
"SHMT"
] | [
41200
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"2.1.2.1",
"PWY-1622",
"PWY-181",
"PWY-2161",
"PWY-2201",
"PWY-3661",
"PWY-3841",
"PWY-5497",
"PWY-8325",
"PWY-8362",
"PWY-8363",
"R-BTA-196757",
"R-BTA-9013408",
"R-BTA-9837999",
"R-CEL-196757",
"R-CEL-71262",
"R-DDI-196757",
"R-DDI-71262",
"R-DDI-9013408",
"R-DDI-9837999",
... | [
"EC:2.1.2.1",
"METACYC:PWY-1622",
"METACYC:PWY-181",
"METACYC:PWY-2161",
"METACYC:PWY-2201",
"METACYC:PWY-3661",
"METACYC:PWY-3841",
"METACYC:PWY-5497",
"METACYC:PWY-8325",
"METACYC:PWY-8362",
"METACYC:PWY-8363",
"REACTOME:R-BTA-196757",
"REACTOME:R-BTA-9013408",
"REACTOME:R-BTA-9837999",
... | 28 | [
"1bj4",
"1cj0",
"1dfo",
"1eji",
"1eqb",
"1kkj",
"1kkp",
"1kl1",
"1kl2",
"1ls3",
"1rv3",
"1rv4",
"1rvu",
"1rvy",
"2dkj",
"2vgs",
"2vgt",
"2vgu",
"2vgv",
"2vgw",
"2vi8",
"2vi9",
"2via",
"2vib",
"2vmn",
"2vmo",
"2vmp",
"2vmq",
"2vmr",
"2vms",
"2vmt",
"2vmu"... | 144 | [
"PUB00000663",
"PUB00006301",
"PUB00006322",
"PUB00014432",
"PUB00014439"
] | [
"8305478",
"8112347",
"7748903",
"10828359",
"11877399"
] | [
"The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases.",
"Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families.",
"Pyridoxal phos... | [
1994,
1994,
1995,
2000,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
795,
29123,
10932,
8,
342
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
29,
1,
1,
6,
1,
16,
5,
2,
20,
8,
2,
2,
18
] | 13 | true | Binding_site | Serine hydroxymethyltransferase, pyridoxal phosphate binding site | Serine hydroxymethyltransferase, pyridoxal phosphate binding site | Ser_HO-MeTrfase_PLP_BS | 6 |
IPR019799 | 19,799 | Glycoside hydrolase family 22 domain | Glyco_hydro_22_CS | Domain | 4,416 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00128"
] | [
"GLYCOSYL_HYDROL_F22_1"
] | [
4416
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.2.1.17",
"R-BTA-6798695",
"R-BTA-6803157",
"R-CFA-6798695",
"R-CFA-6803157",
"R-DME-5653890",
"R-GGA-5653890",
"R-GGA-6798695",
"R-GGA-6803157",
"R-HSA-5653890",
"R-HSA-6798695",
"R-HSA-6803157",
"R-HSA-977225",
"R-MMU-5653890",
"R-MMU-6798695",
"R-MMU-6803157",
"R-RNO-6798695",
... | [
"EC:3.2.1.17",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6803157",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-6803157",
"REACTOME:R-DME-5653890",
"REACTOME:R-GGA-5653890",
"REACTOME:R-GGA-6798695",
"REACTOME:R-GGA-6803157",
"REACTOME:R-HSA-5653890",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-680... | 21 | [
"132l",
"133l",
"134l",
"135l",
"193l",
"194l",
"1a2y",
"1a4v",
"1aki",
"1alc",
"1at5",
"1at6",
"1azf",
"1b0d",
"1b2k",
"1b5u",
"1b5v",
"1b5w",
"1b5x",
"1b5y",
"1b5z",
"1b7l",
"1b7m",
"1b7n",
"1b7o",
"1b7p",
"1b7q",
"1b7r",
"1b7s",
"1b9o",
"1bb3",
"1bb4"... | 1,590 | [
"PUB00001331",
"PUB00001375",
"PUB00001550",
"PUB00002334",
"PUB00002403",
"PUB00002496",
"PUB00003998",
"PUB00004870",
"PUB00005266"
] | [
"3104032",
"2731545",
"3666156",
"3148618",
"6715332",
"2738070",
"3785375",
"7624375",
"8535779"
] | [
"Alpha-lactalbumin and related proteins: a versatile gene family with an interesting parentage.",
"The evolution of lysozyme and alpha-lactalbumin.",
"The calcium-binding property of equine lysozyme.",
"Amino acid sequence of a lysozyme (B-enzyme) from Bacillus subtilis YT-25.",
"Evolution of alpha-lactalbu... | [
1986,
1989,
1987,
1988,
1984,
1989,
1986,
1995,
1995
] | 9 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Hymenobacter edaphi",
"Pseudomonas phage LKA1"
] | [
4414,
1,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
14,
21,
19,
19,
23
] | 6 | true | Domain | Glycoside hydrolase family 22 domain | Glycoside hydrolase family 22 domain | Glyco_hydro_22_CS | 1 |
IPR019800 | 19,800 | Glycoside hydrolase, family 3, active site | Glyco_hydro_3_AS | Active_site | 38,522 | false | false | null | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00775"
] | [
"GLYCOSYL_HYDROL_F3"
] | [
38522
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.2.1.52",
"PWY-6902",
"PWY-7822",
"PWY-7883"
] | [
"EC:3.2.1.52",
"METACYC:PWY-6902",
"METACYC:PWY-7822",
"METACYC:PWY-7883"
] | 4 | [
"1tr9",
"1y65",
"2oxn",
"2x40",
"2x41",
"3abz",
"3ac0",
"3bmx",
"3gs6",
"3gsm",
"3nvd",
"3tev",
"4gvf",
"4gvg",
"4gvh",
"4hzm",
"4iib",
"4iic",
"4iid",
"4iie",
"4iif",
"4iig",
"4iih",
"4zoa",
"4zob",
"4zod",
"4zoe",
"5bu9",
"5fji",
"5fjj",
"5g1m",
"5g2m"... | 66 | [
"PUB00000578",
"PUB00004870",
"PUB00005266",
"PUB00005846"
] | [
"6783081",
"7624375",
"8535779",
"10368285"
] | [
"Isolation and structure of a tryptic glycopeptide from the active site of beta-glucosidase A3 from Aspergillus wentii.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Three-dimensional st... | [
1980,
1995,
1995,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Pandoravirus",
"unclassified sequences"
] | [
171,
29142,
8979,
2,
228
] | 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",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
24,
2,
5,
4,
1,
6
] | 6 | true | Active_site | Glycoside hydrolase, family 3, active site | Glycoside hydrolase, family 3, active site | Glyco_hydro_3_AS | 4 |
IPR019801 | 19,801 | Glycoside hydrolase, family 35, conserved site | Glyco_hydro_35_CS | Conserved_site | 19,309 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS01182"
] | [
"GLYCOSYL_HYDROL_F35"
] | [
19309
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"3.2.1.23",
"PWY-6807",
"R-CFA-2022857",
"R-CFA-2024101",
"R-CFA-4085001",
"R-CFA-6798695",
"R-CFA-9840310",
"R-DDI-2022857",
"R-DDI-2024101",
"R-DDI-6798695",
"R-DDI-9840310",
"R-HSA-2022857",
"R-HSA-2024101",
"R-HSA-2206308",
"R-HSA-4085001",
"R-HSA-4341670",
"R-HSA-6798695",
"R-... | [
"EC:3.2.1.23",
"METACYC:PWY-6807",
"REACTOME:R-CFA-2022857",
"REACTOME:R-CFA-2024101",
"REACTOME:R-CFA-4085001",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-9840310",
"REACTOME:R-DDI-2022857",
"REACTOME:R-DDI-2024101",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-9840310",
"REACTOME:R-HSA-2022857",... | 27 | [
"1tg7",
"1xc6",
"3og2",
"3ogr",
"3ogs",
"3ogv",
"3thc",
"3thd",
"3w5f",
"3w5g",
"3wez",
"3wf0",
"3wf1",
"3wf2",
"3wf3",
"3wf4",
"4iug",
"4mad",
"5ifp",
"5ift",
"5ihr",
"5juv",
"5mgc",
"5mgd",
"6ik5",
"7kdv",
"8fa5"
] | 27 | [
"PUB00004870",
"PUB00005266"
] | [
"7624375",
"8535779"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1995,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Ignisphaera aggregans",
"metagenomes"
] | [
3479,
15819,
2,
9
] | 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"
] | [
87,
1,
5,
1,
6,
17,
1,
34,
24,
121
] | 10 | true | Conserved_site | Glycoside hydrolase, family 35, conserved site | Glycoside hydrolase, family 35, conserved site | Glyco_hydro_35_CS | 1 |
IPR019802 | 19,802 | Glycoside hydrolase, family 4, conserved site | GlycHydrolase_4_CS | Conserved_site | 9,731 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS01324"
] | [
"GLYCOSYL_HYDROL_F4"
] | [
9731
] | 1 | [
"EC"
] | [
"3.2.1"
] | [
"EC:3.2.1"
] | 1 | [
"1obb",
"1s6y",
"1u8x",
"1up4",
"1up6",
"1up7",
"3fef",
"5c3m",
"6dux",
"6dvv",
"6vc6"
] | 11 | [
"PUB00003025",
"PUB00004870",
"PUB00005266"
] | [
"9765262",
"7624375",
"8535779"
] | [
"The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-alpha-glucosidase. Assignment to family 4 of the glycosylhydrolase superfamily.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechan... | [
1998,
1995,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
30,
9655,
14,
32
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
3
] | 2 | true | Conserved_site | Glycoside hydrolase, family 4, conserved site | Glycoside hydrolase, family 4, conserved site | GlycHydrolase_4_CS | 9 |
IPR019803 | 19,803 | Glypican, conserved site | Glypican_CS | Conserved_site | 4,833 | false | false | Glypicans [ , ] are a family of heparan sulphate proteoglycans which are anchored to cell membranes by a glycosylphosphatidylinositol (GPI) linkage. Six members (GPC1-6) are known in vertebrates [ ]. Structurally, these proteins consist of three separate domains: A signal sequence; An extracellular domain of about 500 ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01207"
] | [
"GLYPICAN"
] | [
4833
] | 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-DRE-1971475",
"R-DRE-2022928",
"R-DRE-2024096",
"R-HSA-1971475",
"R-HSA-2022928",
"R-HSA-2024096",
"R-HSA-202733",
"R-HSA-3560783",
"R-HSA-3560801",
"R-HSA-3656237",
"R-HSA-3656253",
"R-HSA-376176",
"R-HSA-381426",
"R-HSA-4420332",
"R-HSA-5362798",
"R-HSA-8957275",
"R-HSA-9694614"... | [
"REACTOME:R-DRE-1971475",
"REACTOME:R-DRE-2022928",
"REACTOME:R-DRE-2024096",
"REACTOME:R-HSA-1971475",
"REACTOME:R-HSA-2022928",
"REACTOME:R-HSA-2024096",
"REACTOME:R-HSA-202733",
"REACTOME:R-HSA-3560783",
"REACTOME:R-HSA-3560801",
"REACTOME:R-HSA-3656237",
"REACTOME:R-HSA-3656253",
"REACTOME... | 36 | [
"4acr",
"4ad7",
"4bwe",
"4ywt",
"6wjl",
"7t62",
"7za1",
"7za2",
"7za3",
"7zav",
"7zaw",
"9ntq"
] | 12 | [
"PUB00003081",
"PUB00003899",
"PUB00034826"
] | [
"7657705",
"8589707",
"11474185"
] | [
"K-glypican: a novel GPI-anchored heparan sulfate proteoglycan that is highly expressed in developing brain and kidney.",
"Glypicans: a growing trend.",
"Mapping of the rat glypican genes."
] | [
1995,
1996,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
4833
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
17,
23,
25
] | 4 | true | Conserved_site | Glypican, conserved site | Glypican, conserved site | Glypican_CS | 6 |
IPR019804 | 19,804 | Ras guanine-nucleotide exchange factor, conserved site | Ras_G-nucl-exch_fac_CS | Conserved_site | 26,671 | false | false | Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyse GTP to GDP [ ]. The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of boun... | [
"GO:0005085",
"GO:0007264"
] | [
"guanyl-nucleotide exchange factor activity",
"small GTPase-mediated signal transduction"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00720"
] | [
"RASGEF"
] | [
26671
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-354192",
"R-CEL-381676",
"R-CEL-392517",
"R-CEL-5673001",
"R-DDI-193648",
"R-DDI-354192",
"R-DDI-381676",
"R-DDI-392517",
"R-DDI-9013148",
"R-DDI-9013149",
"R-DME-112412",
"R-DME-1250347",
"R-DME-1433557",
"R-DME-1433559",
"R-DME-167044",
"R-DME-179812",
"R-DME-180336",
"R-D... | [
"REACTOME:R-CEL-354192",
"REACTOME:R-CEL-381676",
"REACTOME:R-CEL-392517",
"REACTOME:R-CEL-5673001",
"REACTOME:R-DDI-193648",
"REACTOME:R-DDI-354192",
"REACTOME:R-DDI-381676",
"REACTOME:R-DDI-392517",
"REACTOME:R-DDI-9013148",
"REACTOME:R-DDI-9013149",
"REACTOME:R-DME-112412",
"REACTOME:R-DME-... | 189 | [
"1bkd",
"1nvu",
"1nvv",
"1nvw",
"1nvx",
"1xd2",
"1xd4",
"1xdv",
"2byv",
"2ii0",
"2ije",
"3cf6",
"3ksy",
"4f7z",
"4jgw",
"4mgi",
"4mgk",
"4mgy",
"4mgz",
"4mh0",
"4nyi",
"4nyj",
"4nym",
"4uru",
"4urv",
"4urw",
"4urx",
"4ury",
"4urz",
"4us0",
"4us1",
"4us2"... | 110 | [
"PUB00001017",
"PUB00004087",
"PUB00004162",
"PUB00006190"
] | [
"15335949",
"1898771",
"8259209",
"9690470"
] | [
"Ras regulation: putting back the GTP.",
"The GTPase superfamily: conserved structure and molecular mechanism.",
"Proteins regulating Ras and its relatives.",
"The structural basis of the activation of Ras by Sos."
] | [
1992,
1991,
1993,
1998
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
26670,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
9,
82,
31,
74,
52,
1,
75,
4,
1
] | 9 | true | Conserved_site | Ras guanine-nucleotide exchange factor, conserved site | Ras guanine-nucleotide exchange factor, conserved site | Ras_G-nucl-exch_fac_CS | 7 |
IPR019805 | 19,805 | Heat shock protein Hsp90, conserved site | Heat_shock_protein_90_CS | Conserved_site | 27,050 | false | false | Prokaryotes and eukaryotes respond to heat shock and other forms of environmental stress by inducing synthesis of heat-shock proteins (hsp) [ ]. The 90kDa heat shock protein, Hsp90, is one of the most abundant proteins in eukaryotic cells, comprising 1-2% of cellular proteins under non-stress conditions [ ]. Its contri... | [
"GO:0005524",
"GO:0051082",
"GO:0006457"
] | [
"ATP binding",
"unfolded protein binding",
"protein folding"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00298"
] | [
"HSP90"
] | [
27050
] | 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-1227986",
"R-BTA-1474151",
"R-BTA-1679131",
"R-BTA-168928",
"R-BTA-2029482",
"R-BTA-203615",
"R-BTA-2565942",
"R-BTA-3371497",
"R-BTA-3371511",
"R-BTA-3371568",
"R-BTA-3371571",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-381426",
"R-BTA-399954",
"... | [
"REACTOME:R-BTA-1227986",
"REACTOME:R-BTA-1474151",
"REACTOME:R-BTA-1679131",
"REACTOME:R-BTA-168928",
"REACTOME:R-BTA-2029482",
"REACTOME:R-BTA-203615",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-3371511",
"REACTOME:R-BTA-3371568",
"REACTOME:R-BTA-3371571",
"REACTOME:... | 257 | [
"1a4h",
"1ah6",
"1ah8",
"1am1",
"1amw",
"1bgq",
"1byq",
"1osf",
"1qy8",
"1qye",
"1tbw",
"1tc0",
"1tc6",
"1u0z",
"1u2o",
"1us7",
"1uy6",
"1uy7",
"1uy8",
"1uy9",
"1uyc",
"1uyd",
"1uye",
"1uyf",
"1uyg",
"1uyh",
"1uyi",
"1uyk",
"1uyl",
"1uym",
"1y4s",
"1y4u"... | 604 | [
"PUB00000102",
"PUB00002788",
"PUB00005421",
"PUB00014968"
] | [
"2853609",
"8419347",
"7914036",
"15069952"
] | [
"The heat-shock proteins.",
"Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases.",
"Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones.",
"Hsp90 isoforms: functions, expression and clinical importance."
] | [
1988,
1993,
1994,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Imitervirales",
"Methanomethylophilus alvi",
"metagenomes"
] | [
12574,
14313,
4,
2,
157
] | 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,
1,
4,
4,
1,
30,
22,
1,
29,
11,
2,
1,
67
] | 13 | true | Conserved_site | Heat shock protein Hsp90, conserved site | Heat shock protein Hsp90, conserved site | Heat_shock_protein_90_CS | 7 |
IPR019806 | 19,806 | Heat-stable enterotoxin, conserved site | Heat-stable_enterotox_CS | Conserved_site | 52 | false | false | This entry represents a group of heat-stable enterotoxins, such as STa from Escherichia coli, which are an important cause of acute diarrhoea in infants and travellers in developing countries. The mature STa protein is a 19-residue peptide containing three disulphide bridges that are functionally important. STa contain... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PROSITE"
] | [
"PS00273"
] | [
"ENTEROTOXIN_H_STABLE"
] | [
52
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-8942233",
"R-HSA-9760173"
] | [
"REACTOME:R-HSA-8942233",
"REACTOME:R-HSA-9760173"
] | 2 | [
"7css",
"7d37"
] | 2 | [
"PUB00016492",
"PUB00035778",
"PUB00035779",
"PUB00035780"
] | [
"15049831",
"10799798",
"17094787",
"12813912"
] | [
"Structural features of Escherichia coli heat-stable enterotoxin that activates membrane-associated guanylyl cyclase.",
"Characterization of the interaction of Escherichia coli heat-stable enterotoxin (STa) with its putative receptor on the intestinal tract of newborn calves.",
"Interaction of Escherichia coli ... | [
2004,
2000,
2007,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
52
] | 1 | [] | [] | 0 | true | Conserved_site | Heat-stable enterotoxin, conserved site | Heat-stable enterotoxin, conserved site | Heat-stable_enterotox_CS | 8 |
IPR019808 | 19,808 | Histidine triad, conserved site | Histidine_triad_CS | Conserved_site | 30,683 | false | false | The Histidine Triad (HIT) motif, His-x-His-x-His-x-x (x, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms [ ]. Crystal structure of rabbit Hint, purified as an adenosine and AMP-binding protein, showed that proteins in the HIT superfamily are conserved as nucleotide-binding p... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00892"
] | [
"HIT_1"
] | [
30683
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-9013405",
"R-CEL-9824594",
"R-CEL-9825892",
"R-CEL-9856649",
"R-HSA-429958",
"R-HSA-9013405",
"R-HSA-9824594",
"R-HSA-9825892",
"R-HSA-9856649",
"R-MMU-429958",
"R-MMU-9013405",
"R-MMU-9824594",
"R-MMU-9825892",
"R-MMU-9856649",
"R-RNO-429958",
"R-RNO-9824594",
"R-RNO-9825892"... | [
"REACTOME:R-BTA-9013405",
"REACTOME:R-CEL-9824594",
"REACTOME:R-CEL-9825892",
"REACTOME:R-CEL-9856649",
"REACTOME:R-HSA-429958",
"REACTOME:R-HSA-9013405",
"REACTOME:R-HSA-9824594",
"REACTOME:R-HSA-9825892",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-429958",
"REACTOME:R-MMU-9013405",
"REACTOME:... | 20 | [
"1av5",
"1ems",
"1fhi",
"1fit",
"1kpa",
"1kpb",
"1kpc",
"1kpe",
"1kpf",
"1rzy",
"1vlr",
"1xml",
"1xmm",
"1y23",
"2eo4",
"2fit",
"3bl7",
"3bl9",
"3bla",
"3fit",
"3imi",
"3ksv",
"3n1s",
"3o0m",
"3o1c",
"3o1x",
"3o1z",
"3oj7",
"3omf",
"3oxk",
"3qgz",
"3rhn"... | 104 | [
"PUB00000430",
"PUB00001122",
"PUB00001599",
"PUB00002608",
"PUB00003940",
"PUB00008002",
"PUB00008003",
"PUB00008004",
"PUB00008005"
] | [
"8794732",
"1472710",
"1899836",
"2307677",
"9164465",
"11805111",
"10758156",
"9576908",
"12119013"
] | [
"Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5\"'-P1,P3-triphosphate hydrolase.",
"The HIT protein family: a new family of proteins present in prokaryotes, yeast and mammals.",
"Characterization of a novel zinc binding site of protein kinase C inhibitor-1.",
"Amino acid sequence and char... | [
1996,
1992,
1991,
1990,
1997,
2002,
2000,
1998,
2002
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Nevevirus",
"unclassified sequences"
] | [
541,
16323,
13490,
4,
325
] | 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,
2,
11,
4,
1,
16,
9,
4,
24,
19,
4,
2,
16
] | 13 | true | Conserved_site | Histidine triad, conserved site | Histidine triad, conserved site | Histidine_triad_CS | 4 |
IPR019809 | 19,809 | Histone H4, conserved site | Histone_H4_CS | Conserved_site | 9,391 | false | false | Histone H4 is one of the four histones, along with H2A, H2B and H3, which form the eukaryotic nucleosome core. The sequence of histone H4 has remained almost invariant in more then 2 billion years of evolution [ ]. The signature pattern for this entry is a pentapeptide found in positions 14 to 18 of all H4 sequences. I... | [
"GO:0003677",
"GO:0000786"
] | [
"DNA binding",
"nucleosome"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00047"
] | [
"HISTONE_H4"
] | [
9391
] | 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-110330",
"R-BTA-110331",
"R-BTA-171306",
"R-BTA-201722",
"R-BTA-212300",
"R-BTA-2299718",
"R-BTA-2559580",
"R-BTA-2559582",
"R-BTA-2559586",
"R-BTA-3214815",
"R-BTA-3214841",
"R-BTA-3214842",
"R-BTA-3214847",
"R-BTA-3214858",
"R-BTA-427359",
"R-BTA-427413",
"R-BTA-4551638",
... | [
"REACTOME:R-BTA-110330",
"REACTOME:R-BTA-110331",
"REACTOME:R-BTA-171306",
"REACTOME:R-BTA-201722",
"REACTOME:R-BTA-212300",
"REACTOME:R-BTA-2299718",
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-2559582",
"REACTOME:R-BTA-2559586",
"REACTOME:R-BTA-3214815",
"REACTOME:R-BTA-3214841",
"REACTOME:R-B... | 278 | [
"1eqz",
"1f66",
"1hq3",
"1id3",
"1kx3",
"1kx4",
"1kx5",
"1m18",
"1m19",
"1m1a",
"1p34",
"1p3a",
"1p3b",
"1p3f",
"1p3g",
"1p3i",
"1p3k",
"1p3l",
"1p3m",
"1p3o",
"1p3p",
"1q2c",
"1s32",
"1tzy",
"1u35",
"1zbb",
"1zla",
"2aro",
"2cv5",
"2f8n",
"2fj7",
"2hio"... | 873 | [
"PUB00003642",
"PUB00004015",
"PUB00004448"
] | [
"6808351",
"3340182",
"8121801"
] | [
"Acetylation of histones in nucleosomes.",
"A highly basic histone H4 domain bound to the sharply bent region of nucleosomal DNA.",
"Phylogenetic analysis of the core histones H2A, H2B, H3, and H4."
] | [
1982,
1988,
1994
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bracoviriform",
"Eukaryota"
] | [
6,
11,
9374
] | 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... | [
3,
1,
7,
2,
3,
2,
1,
4,
2,
1,
1,
30
] | 12 | true | Conserved_site | Histone H4, conserved site | Histone H4, conserved site | Histone_H4_CS | 8 |
IPR019810 | 19,810 | Citrate synthase active site | Citrate_synthase_AS | Active_site | 45,553 | false | false | Citrate synthase is a member of a small family of enzymes that can directly form a carbon-carbon bond without the presence of metal ion cofactors. It catalyses the first reaction in the Krebs' cycle, namely the conversion of oxaloacetate and acetyl-coenzyme A into citrate and coenzyme A. This reaction is important for ... | [
"GO:0046912"
] | [
"acyltransferase activity, acyl groups converted into alkyl on transfer"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00480"
] | [
"CITRATE_SYNTHASE"
] | [
45553
] | 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-71403",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-71403",
"R-CEL-9837999",
"R-DDI-71403",
"R-DDI-9837999",
"R-DME-71403",
"R-DME-9837999",
"R-DRE-71403",
"R-DRE-9854311",
"R-GGA-372987",
"R-HSA-1268020",
"R-HSA-71403",
"R-HSA-9837999",
"R-HSA-9854311",
... | [
"EC:2.3.3",
"EC:2.3.3.16",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-71403",
"REACTOME:R-DME-9837999",
"REACTOME:R-DRE-71403",
"REACTOME:R-DRE... | 31 | [
"1a59",
"1aj8",
"1al6",
"1amz",
"1csc",
"1csh",
"1csi",
"1csr",
"1css",
"1cts",
"1nxe",
"1nxg",
"1o7x",
"1owb",
"1owc",
"1vgm",
"1vgp",
"2c6x",
"2csc",
"2cts",
"2h12",
"2ibp",
"2ifc",
"2p2w",
"2r26",
"2r9e",
"3csc",
"3enj",
"3hwk",
"3msu",
"3o8j",
"3tqg"... | 106 | [
"PUB00000321",
"PUB00013490",
"PUB00042604",
"PUB00042605",
"PUB00042606",
"PUB00042607",
"PUB00090961",
"PUB00094532",
"PUB00094533"
] | [
"2337600",
"9579066",
"15147839",
"17087502",
"16952946",
"16007201",
"28956599",
"17973657",
"29420286"
] | [
"Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A.",
"Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships.",
"Investigating the accessibility of the closed ... | [
1990,
1998,
2004,
2006,
2006,
2005,
2017,
2008,
2018
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
327,
36359,
8372,
495
] | 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,
1,
2,
4,
2,
6,
4,
2,
13,
7,
3,
1,
32
] | 13 | true | Active_site | Citrate synthase active site | Citrate synthase active site | Citrate_synthase_AS | 6 |
IPR019811 | 19,811 | Homoserine dehydrogenase, conserved site | HDH_CS | Conserved_site | 32,335 | false | false | Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids -lysine, threonine, methionine and isoleucine -in a series of reactions known as the aspartate pathway. Additionally, several important metabolic intermediates are produced by these reactions, such as diaminopimelic acid, an essential compo... | [
"GO:0006520"
] | [
"amino acid metabolic process"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS01042"
] | [
"HOMOSER_DHGENASE"
] | [
32335
] | 1 | [
"EC"
] | [
"1.1.1.3"
] | [
"EC:1.1.1.3"
] | 1 | [
"1ebf",
"1ebu",
"1q7g",
"1tve",
"2ejw",
"3do5",
"3ing",
"3mtj",
"4pg4",
"4pg5",
"4pg6",
"4pg7",
"4pg8",
"4ydr",
"5avo",
"5x9d",
"5xdf",
"6a0r",
"6a0s",
"6a0t",
"6a0u",
"6dzs",
"7f4b",
"7f4c"
] | 24 | [
"PUB00000699",
"PUB00001656",
"PUB00021481",
"PUB00034672"
] | [
"8395899",
"8500624",
"10700284",
"11352712"
] | [
"Evolutionary comparisons of three enzymes of the threonine biosynthetic pathway among several microbial species.",
"Evolutionary relationships between yeast and bacterial homoserine dehydrogenases.",
"Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases.",
"T... | [
1993,
1993,
2000,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
709,
27840,
3332,
454
] | 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"
] | [
20,
2,
1,
15,
1,
1,
27
] | 7 | true | Conserved_site | Homoserine dehydrogenase, conserved site | Homoserine dehydrogenase, conserved site | HDH_CS | 2 |
IPR019812 | 19,812 | Hydrogenase assembly chaperone, conserved site | Hydgase_assmbl_chp_CS | Conserved_site | 6,639 | false | false | The large subunit of [NiFe]-hydrogenase, as well as other nickel metalloenzymes, is synthesised as a precursor devoid of the metalloenzyme active site. This precursor then undergoes a complex post-translational maturation process that requires a number of accessory proteins. The hydrogenase expression/formation protein... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01097"
] | [
"HUPF_HYPC"
] | [
6639
] | 1 | [] | [] | [] | 0 | [
"2ot2",
"2z1c"
] | 2 | [
"PUB00003839",
"PUB00011027",
"PUB00014218"
] | [
"8497190",
"9485446",
"10783387"
] | [
"Organization of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of two hyp regulatory mutants.",
"Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation.",
"Anal... | [
1993,
1998,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Opisthokonta",
"unclassified sequences"
] | [
137,
6405,
4,
93
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Conserved_site | Hydrogenase assembly chaperone, conserved site | Hydrogenase assembly chaperone, conserved site | Hydgase_assmbl_chp_CS | 6 |
IPR019813 | 19,813 | Translation initiation factor 3, conserved site | Translation_initiation_fac3_CS | Conserved_site | 16,711 | false | false | Initiation factor 3 (IF-3) (gene infC) is one of the three factors required for the initiation of protein biosynthesis in bacteria. IF-3 is thought to function as a fidelity factor during the assembly of the ternary initiation complex which consist of the 30S ribosomal subunit, the initiator tRNA and the messenger RNA.... | [
"GO:0003743",
"GO:0006413"
] | [
"translation initiation factor activity",
"translational initiation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00938"
] | [
"IF3"
] | [
16711
] | 1 | [] | [] | [] | 0 | [
"1tif",
"5me0",
"5me1",
"6o6d",
"8jsg",
"8jsh",
"9fco",
"9fda",
"9fib",
"9g06",
"9h9h",
"9h9j"
] | 12 | [
"PUB00001732",
"PUB00002896"
] | [
"8405963",
"8144528"
] | [
"Molecular cloning and sequencing of infC, the gene encoding translation initiation factor IF3, from four enterobacterial species.",
"Isolation and characterization of cDNA clones for chloroplast translational initiation factor-3 from Euglena gracilis."
] | [
1993,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nitrosopumilus salarius BD31",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
15754,
1,
3,
616,
337
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
9,
1
] | 2 | true | Conserved_site | Translation initiation factor 3, conserved site | Translation initiation factor 3, conserved site | Translation_initiation_fac3_CS | 8 |
IPR019814 | 19,814 | Translation initiation factor 3, N-terminal | Translation_initiation_fac_3_N | Domain | 28,056 | false | false | Initiation factor 3 (IF-3) (gene infC) is one of the three factors required for the initiation of protein biosynthesis in bacteria. IF-3 is thought to function as a fidelity factor during the assembly of the ternary initiation complex which consist of the 30S ribosomal subunit, the initiator tRNA and the messenger RNA.... | [
"GO:0003743",
"GO:0006413"
] | [
"translation initiation factor activity",
"translational initiation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF05198"
] | [
"IF3_N"
] | [
28056
] | 1 | [
"REACTOME"
] | [
"R-HSA-5368286"
] | [
"REACTOME:R-HSA-5368286"
] | 1 | [
"1tif",
"5lmn",
"5lmo",
"5lmp",
"5lmq",
"5lmr",
"5lms",
"5lmt",
"5lmu",
"5lmv",
"5me0",
"5me1",
"6neq",
"6nf8",
"6o6d",
"6rw4",
"6rw5",
"7p2e",
"7po0",
"7po1",
"8jsg",
"8jsh",
"8qrm",
"9fco",
"9fda",
"9fib",
"9g06",
"9h9h",
"9h9j",
"9hfm",
"9hfn"
] | 31 | [
"PUB00001732",
"PUB00002896"
] | [
"8405963",
"8144528"
] | [
"Molecular cloning and sequencing of infC, the gene encoding translation initiation factor IF3, from four enterobacterial species.",
"Isolation and characterization of cDNA clones for chloroplast translational initiation factor-3 from Euglena gracilis."
] | [
1993,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Nitrososphaerota",
"Viruses",
"unclassified sequences"
] | [
24280,
3263,
2,
24,
487
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
17,
9,
1,
1,
3,
5,
3,
7
] | 8 | true | Domain | Translation initiation factor 3, N-terminal | Translation initiation factor 3, N-terminal | Translation_initiation_fac_3_N | 8 |
IPR019817 | 19,817 | Interferon regulatory factor, conserved site | Interferon_reg_fac_CS | Conserved_site | 8,348 | false | false | The expression of type I interferon genes (interferons alpha and beta) is induced by many agents, including viral attack [ ]. Induction is mediated by the binding of interferon regulatory factor 1 (IRF-1) to a region known as the interferon consensus sequence (ICS), located upstream of the interferon genes [ ]. Other f... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00601"
] | [
"IRF_1"
] | [
8348
] | 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-GGA-1227882",
"R-GGA-433819",
"R-GGA-434136",
"R-HSA-1169408",
"R-HSA-1606341",
"R-HSA-168928",
"R-HSA-3134963",
"R-HSA-3134973",
"R-HSA-3134975",
"R-HSA-3270619",
"R-HSA-5620971",
"R-HSA-6785807",
"R-HSA-877300",
"R-HSA-9013973",
"R-HSA-909733",
"R-HSA-918233",
"R-HSA-933541",
... | [
"REACTOME:R-GGA-1227882",
"REACTOME:R-GGA-433819",
"REACTOME:R-GGA-434136",
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-1606341",
"REACTOME:R-HSA-168928",
"REACTOME:R-HSA-3134963",
"REACTOME:R-HSA-3134973",
"REACTOME:R-HSA-3134975",
"REACTOME:R-HSA-3270619",
"REACTOME:R-HSA-5620971",
"REACTOME:R... | 42 | [
"1if1",
"1irf",
"1irg",
"1t2k",
"2dll",
"2irf",
"2o61",
"2o6g",
"2pi0",
"3qu3",
"3qu6",
"6td4",
"7jm4",
"7o56",
"7ogs",
"7oot",
"7rh2",
"8hcl",
"8hcm",
"8hcs",
"8jkl",
"8jkn",
"8jko",
"8jkq",
"8jks"
] | 25 | [
"PUB00000818",
"PUB00000832",
"PUB00002752"
] | [
"3409321",
"2475256",
"1460054"
] | [
"Regulated expression of a gene encoding a nuclear factor, IRF-1, that specifically binds to IFN-beta gene regulatory elements.",
"Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes.",
"Human interferon consensus sequence ... | [
1988,
1989,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
8348
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
23,
89,
49,
32
] | 4 | true | Conserved_site | Interferon regulatory factor, conserved site | Interferon regulatory factor, conserved site | Interferon_reg_fac_CS | 3 |
IPR019818 | 19,818 | Isocitrate/isopropylmalate dehydrogenase, conserved site | IsoCit/isopropylmalate_DH_CS | Conserved_site | 76,709 | false | false | Isocitrate dehydrogenase (IDH) [ , ] is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. IDH is either dependent on NAD + ( ) or on NADP + ( ). In eukaryotes there are at least three isozymes of IDH: two are located in the mitochondrial... | [
"GO:0000287",
"GO:0016616",
"GO:0051287"
] | [
"magnesium ion binding",
"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor",
"NAD binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PROSITE"
] | [
"PS00470"
] | [
"IDH_IMDH"
] | [
76709
] | 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... | [
"1.1.1",
"1.1.1.85",
"PWY-7396",
"R-BTA-2151201",
"R-BTA-71403",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-71403",
"R-CEL-9837999",
"R-DDI-389542",
"R-DDI-6798695",
"R-DDI-71403",
"R-DDI-9033241",
"R-DME-71403",
"R-DME-9837999",
"R-HSA-1268020",
"R-HSA-2151201",
"R-HSA-2978092",
"... | [
"EC:1.1.1",
"EC:1.1.1.85",
"METACYC:PWY-7396",
"REACTOME:R-BTA-2151201",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-389542",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-90... | 47 | [
"1a05",
"1ai2",
"1ai3",
"1bl5",
"1cm7",
"1cnz",
"1cw1",
"1cw4",
"1cw7",
"1dpz",
"1dr0",
"1dr8",
"1g2u",
"1gc8",
"1gc9",
"1gro",
"1grp",
"1hex",
"1hj6",
"1hqs",
"1idc",
"1idd",
"1ide",
"1idf",
"1idm",
"1ika",
"1ipd",
"1iso",
"1lwd",
"1osi",
"1osj",
"1p8f"... | 224 | [
"PUB00000160",
"PUB00002669",
"PUB00003276",
"PUB00004691",
"PUB00005036"
] | [
"8053675",
"1939242",
"1748999",
"2682654",
"7773180"
] | [
"Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases.",
"NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae.",
"Three-dimensional structure of a highly thermostable ... | [
1994,
1991,
1991,
1989,
1995
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1210,
49278,
25217,
1004
] | 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",... | [
33,
7,
8,
9,
3,
33,
14,
5,
18,
31,
7,
5,
30
] | 13 | true | Conserved_site | Isocitrate/isopropylmalate dehydrogenase, conserved site | Isocitrate/isopropylmalate dehydrogenase, conserved site | IsoCit/isopropylmalate_DH_CS | 1 |
IPR019819 | 19,819 | Carboxylesterase type B, conserved site | Carboxylesterase_B_CS | Conserved_site | 46,406 | false | false | Higher eukaryotes have many distinct esterases. Among the different types are those which act on carboxylic esters ( ). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00941"
] | [
"CARBOXYLESTERASE_B_2"
] | [
46406
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.1",
"R-BTA-422085",
"R-BTA-9749641",
"R-CEL-112311",
"R-CEL-1483191",
"R-CEL-2022377",
"R-CEL-211945",
"R-CEL-5578768",
"R-CEL-6794361",
"R-CEL-9749641",
"R-DDI-112311",
"R-DDI-1483191",
"R-DDI-2022377",
"R-DDI-211945",
"R-DDI-5578768",
"R-DDI-9749641",
"R-DME-112311",
"R-DME-... | [
"EC:3.1.1",
"REACTOME:R-BTA-422085",
"REACTOME:R-BTA-9749641",
"REACTOME:R-CEL-112311",
"REACTOME:R-CEL-1483191",
"REACTOME:R-CEL-2022377",
"REACTOME:R-CEL-211945",
"REACTOME:R-CEL-5578768",
"REACTOME:R-CEL-6794361",
"REACTOME:R-CEL-9749641",
"REACTOME:R-DDI-112311",
"REACTOME:R-DDI-1483191",
... | 47 | [
"1acj",
"1acl",
"1akn",
"1amn",
"1aql",
"1ax9",
"1b41",
"1c2b",
"1c2o",
"1c7i",
"1c7j",
"1cfj",
"1cle",
"1crl",
"1dx6",
"1e3q",
"1e66",
"1ea5",
"1eea",
"1eve",
"1f6w",
"1f8u",
"1fss",
"1gpk",
"1gpn",
"1gqr",
"1gqs",
"1gz7",
"1h22",
"1h23",
"1hbj",
"1j06"... | 494 | [
"PUB00003630",
"PUB00004750",
"PUB00005009"
] | [
"3163407",
"1862088",
"8453375"
] | [
"On the origins of esterases.",
"Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.",
"Relationship between sequence conservation and three-dimensional structure in a large family of esterases, ... | [
1988,
1991,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomicrobia",
"Viruses",
"unclassified sequences"
] | [
6264,
40043,
6,
21,
72
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
16,
70,
38,
81,
61,
6,
91,
1
] | 8 | true | Conserved_site | Carboxylesterase type B, conserved site | Carboxylesterase type B, conserved site | Carboxylesterase_B_CS | 2 |
IPR019820 | 19,820 | Sec-independent periplasmic protein translocase, conserved site | Sec-indep_translocase_CS | Conserved_site | 10,865 | false | false | Proteins encoded by the mttABC operon (formerly yigTUW), mediate a novel Sec-independent membrane targeting and translocation system in Escherichia coli that interacts with cofactor-containing redox proteins having a S/TRRXFLK "twin arginine" leader motif. This family contains the E. coli mttB gene (TATC) [ ]. A functi... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01218"
] | [
"TATC"
] | [
10865
] | 1 | [] | [] | [] | 0 | [
"4b4a",
"4hts",
"4htt",
"9dzz",
"9e01",
"9e02",
"9e04",
"9e06",
"9e07"
] | 9 | [
"PUB00000960",
"PUB00007662",
"PUB00011123"
] | [
"9546395",
"9649434",
"12163163"
] | [
"A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins.",
"Overlapping functions of components of a bacterial Sec-independent protein export pathway.",
"Topology determination and functional analysis of the Escherichia coli TatC protein."
] | [
1998,
1998,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanofastidiosum methylothiophilum",
"Eukaryota",
"unclassified sequences"
] | [
9637,
1,
1035,
192
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
1,
1,
7
] | 4 | true | Conserved_site | Sec-independent periplasmic protein translocase, conserved site | Sec-independent periplasmic protein translocase, conserved site | Sec-indep_translocase_CS | 8 |
IPR019821 | 19,821 | Kinesin motor domain, conserved site | Kinesin_motor_CS | Conserved_site | 120,613 | false | false | Kinesin [ , , ] is a microtubule-associated force-producing protein that may play a role in organelle transport. The kinesin motor activity is directed toward the microtubule's plus end. Kinesin is an oligomeric complex composed of two heavy chains and two light chains. The maintenance of the quaternary structure does ... | [
"GO:0003777",
"GO:0005524",
"GO:0007018"
] | [
"microtubule motor activity",
"ATP binding",
"microtubule-based movement"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00411"
] | [
"KINESIN_MOTOR_1"
] | [
120613
] | 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-2132295",
"R-BTA-6811434",
"R-BTA-68884",
"R-BTA-983189",
"R-CEL-5620924",
"R-CEL-6811434",
"R-CEL-983189",
"R-DDI-5610787",
"R-DDI-983189",
"R-DME-5632684",
"R-DME-6811434",
"R-DME-68884",
"R-DME-983189",
"R-DRE-5632684",
"R-DRE-983189",
"R-GGA-6811434",
"R-GGA-983189",
"R-... | [
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-6811434",
"REACTOME:R-BTA-68884",
"REACTOME:R-BTA-983189",
"REACTOME:R-CEL-5620924",
"REACTOME:R-CEL-6811434",
"REACTOME:R-CEL-983189",
"REACTOME:R-DDI-5610787",
"REACTOME:R-DDI-983189",
"REACTOME:R-DME-5632684",
"REACTOME:R-DME-6811434",
"REACTOME:R-D... | 77 | [
"1bg2",
"1cz7",
"1f9t",
"1f9u",
"1f9v",
"1goj",
"1i5s",
"1i6i",
"1ia0",
"1ii6",
"1mkj",
"1n6m",
"1q0b",
"1ry6",
"1sdm",
"1t5c",
"1v8j",
"1v8k",
"1vfv",
"1vfw",
"1vfx",
"1vfz",
"1x88",
"1yrs",
"2fky",
"2fl2",
"2fl6",
"2fme",
"2g1q",
"2gm1",
"2gry",
"2heh"... | 268 | [
"PUB00000075",
"PUB00004968",
"PUB00005370",
"PUB00005510",
"PUB00031339",
"PUB00072953"
] | [
"2142876",
"8542443",
"1832505",
"14732151",
"15236970",
"20587735"
] | [
"Motor proteins of cytoplasmic microtubules.",
"Motor proteins 1: kinesins.",
"The emerging kinesin family of microtubule motor proteins.",
"A kinesin medley: biochemical and functional heterogeneity.",
"Crystal structure of the motor domain of the human kinetochore protein CENP-E.",
"A novel kinesin 13 p... | [
1990,
1995,
1991,
1995,
2004,
2010
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5,
120601,
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... | [
276,
28,
311,
105,
198,
138,
10,
42,
182,
6,
7,
410
] | 12 | true | Conserved_site | Kinesin motor domain, conserved site | Kinesin motor domain, conserved site | Kinesin_motor_CS | 5 |
IPR019823 | 19,823 | Large-conductance mechanosensitive channel, conserved site | Mechanosensitive_channel_CS | Conserved_site | 15,018 | false | false | Mechanosensitive ion channels (MscL) play a critical role in transducing physical stresses at the cell membrane into an electrochemical response. MscL is a protein which forms a channel organised as a homopentamer, with each subunit containing two transmembrane regions [ ]. Prokaryotes harbor a large-conductance mechan... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01327"
] | [
"MSCL"
] | [
15018
] | 1 | [] | [] | [] | 0 | [
"2oar",
"3hzq",
"6ctd"
] | 3 | [
"PUB00003881",
"PUB00005232"
] | [
"9632260",
"9856938"
] | [
"Functional and structural conservation in the mechanosensitive channel MscL implicates elements crucial for mechanosensation.",
"Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel."
] | [
1998,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanotrichaceae",
"Phage sp. ctWVj20",
"metagenomes"
] | [
14773,
137,
2,
1,
105
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Conserved_site | Large-conductance mechanosensitive channel, conserved site | Large-conductance mechanosensitive channel, conserved site | Mechanosensitive_channel_CS | 2 |
IPR019824 | 19,824 | Leghaemoglobin, iron-binding site | Leghaemoglobin_Fe_BS | Binding_site | 1,168 | false | false | This entry represents a conserved site found in leghaemoglobins from leguminous and non-leguminous plants, and also non-symbiotic haemoglobins from other plants. It is centred on a histidine that acts as the haem iron distal ligand. Leghaemoglobins were first identified in the root nodules of leguminous plants, where t... | [
"GO:0019825",
"GO:0020037"
] | [
"oxygen binding",
"heme binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00208"
] | [
"PLANT_GLOBIN"
] | [
1168
] | 1 | [] | [] | [] | 0 | [
"1bin",
"1d8u",
"1fsl",
"1gdi",
"1gdj",
"1gdk",
"1gdl",
"1lh1",
"1lh2",
"1lh3",
"1lh5",
"1lh6",
"1lh7",
"2gdm",
"2gnv",
"2gnw",
"2lh1",
"2lh2",
"2lh3",
"2lh5",
"2lh6",
"2lh7",
"2oif",
"2r50",
"3qqq",
"3qqr",
"3zhw"
] | 27 | [
"PUB00016016",
"PUB00029465",
"PUB00035865",
"PUB00035866",
"PUB00035867",
"PUB00035868",
"PUB00035869",
"PUB00035870",
"PUB00035871",
"PUB00035872",
"PUB00035873",
"PUB00035877",
"PUB00035889",
"PUB00035890",
"PUB00035891",
"PUB00035892",
"PUB00035893",
"PUB00055462",
"PUB000554... | [
"15096613",
"12962627",
"16600051",
"17540514",
"11092893",
"11481493",
"15598488",
"16888280",
"15598493",
"15339940",
"15804833",
"17084861",
"15797009",
"12927972",
"11835502",
"6854938",
"16377734",
"17540516",
"17701548",
"21495624"
] | [
"Ancestral hemoglobins in Archaea.",
"Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity.",
"A phylogenomic profile of globins.",
"A model of globin evolution.",
"Flavohemoglobin, a globin with a peroxidase-like catalytic site.",
"Globin-coupled sensors: a class of he... | [
2004,
2003,
2006,
2007,
2001,
2001,
2005,
2006,
2005,
2004,
2004,
2007,
2005,
2003,
2002,
1983,
2006,
2007,
2007,
2011
] | 20 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Lamium leaf distortion virus",
"ecological metagenomes"
] | [
16,
1149,
1,
2
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
8,
5,
5
] | 3 | true | Binding_site | Leghaemoglobin, iron-binding site | Leghaemoglobin, iron-binding site | Leghaemoglobin_Fe_BS | 5 |
IPR019825 | 19,825 | Legume lectin, beta chain, Mn/Ca-binding site | Lectin_legB_Mn/Ca_BS | Binding_site | 9,315 | false | false | Lectins are carbohydrate-binding proteins. Leguminous lectins form one of the largest lectin families and resemble each other in their physicochemical properties, though they differ in their carbohydrate specificities. They bind either glucose/mannose or galactose [ ]. Carbohydrate-binding activity depends on the simul... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00307"
] | [
"LECTIN_LEGUME_BETA"
] | [
9315
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196791",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-975634",
"R-HSA-9758890"
] | [
"REACTOME:R-HSA-196791",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-HSA-975634",
"REACTOME:R-HSA-9758890"
] | 5 | [
"1apn",
"1avb",
"1ax0",
"1ax1",
"1ax2",
"1axy",
"1axz",
"1azd",
"1bjq",
"1bqp",
"1bxh",
"1bzw",
"1c57",
"1ces",
"1ciw",
"1cjp",
"1cn1",
"1con",
"1cq9",
"1cr7",
"1cvn",
"1dbn",
"1dhk",
"1dq0",
"1dq1",
"1dq2",
"1dq4",
"1dq5",
"1dq6",
"1dzq",
"1enq",
"1enr"... | 343 | [
"PUB00001507",
"PUB00046607",
"PUB00057387",
"PUB00057388",
"PUB00057389",
"PUB00057390"
] | [
"2227211",
"9546043",
"16441240",
"36624",
"3965973",
"8373823"
] | [
"Legume lectins--a large family of homologous proteins.",
"Legume lectin structure.",
"Dual-function protein in plant defence: seed lectin from Dolichos biflorus (horse gram) exhibits lipoxygenase activity.",
"The Rhizobium--legume symbiosis.",
"Polypeptide ligation occurs during post-translational modifica... | [
1990,
1998,
2006,
1979,
1985,
1993
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"ecological metagenomes"
] | [
354,
8939,
10,
5,
7
] | 5 | [
"Arabidopsis thaliana",
"Homo sapiens",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
51,
4,
106,
46
] | 4 | true | Binding_site | Legume lectin, beta chain, Mn/Ca-binding site | Legume lectin, beta chain, Mn/Ca-binding site | Lectin_legB_Mn/Ca_BS | 5 |
IPR019826 | 19,826 | Carboxylesterase type B, active site | Carboxylesterase_B_AS | Active_site | 69,958 | false | false | Higher eukaryotes have many distinct esterases. Among the different types are those which act on carboxylic esters ( ). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00122"
] | [
"CARBOXYLESTERASE_B_1"
] | [
69958
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.1",
"R-BTA-422085",
"R-BTA-9749641",
"R-CEL-112311",
"R-CEL-1483191",
"R-CEL-2022377",
"R-CEL-211945",
"R-CEL-5578768",
"R-CEL-9749641",
"R-DDI-112311",
"R-DDI-1483191",
"R-DDI-2022377",
"R-DDI-211945",
"R-DDI-5578768",
"R-DDI-9749641",
"R-DME-112311",
"R-DME-1483191",
"R-DME-... | [
"EC:3.1.1",
"REACTOME:R-BTA-422085",
"REACTOME:R-BTA-9749641",
"REACTOME:R-CEL-112311",
"REACTOME:R-CEL-1483191",
"REACTOME:R-CEL-2022377",
"REACTOME:R-CEL-211945",
"REACTOME:R-CEL-5578768",
"REACTOME:R-CEL-9749641",
"REACTOME:R-DDI-112311",
"REACTOME:R-DDI-1483191",
"REACTOME:R-DDI-2022377",
... | 44 | [
"1acj",
"1acl",
"1akn",
"1amn",
"1aql",
"1ax9",
"1b41",
"1c2b",
"1c2o",
"1c7i",
"1c7j",
"1cfj",
"1cle",
"1crl",
"1dx6",
"1e3q",
"1e66",
"1ea5",
"1eea",
"1eve",
"1f6w",
"1f8u",
"1fss",
"1gpk",
"1gpn",
"1gqr",
"1gqs",
"1gz7",
"1h22",
"1h23",
"1hbj",
"1j06"... | 507 | [
"PUB00003630",
"PUB00004750",
"PUB00005009"
] | [
"3163407",
"1862088",
"8453375"
] | [
"On the origins of esterases.",
"Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.",
"Relationship between sequence conservation and three-dimensional structure in a large family of esterases, ... | [
1988,
1991,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"Viruses",
"unclassified sequences"
] | [
17789,
51869,
58,
23,
219
] | 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)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays... | [
7,
29,
18,
62,
40,
37,
7,
73,
1,
11
] | 10 | true | Active_site | Carboxylesterase type B, active site | Carboxylesterase type B, active site | Carboxylesterase_B_AS | 5 |
IPR019827 | 19,827 | Leukemia inhibitory factor /oncostatin, conserved site | Leukemia_IF/oncostatin_CS | Conserved_site | 317 | false | false | On the basis of functional and structural similarities, the small cytokines leukemia inhibitory factor (LIF) and oncostatin (OSM) can be classified into a single family [ , ]. It has been said [ ] that LIF and OSM can be included in the IL-6 family of cytokines, but while all these cytokines seem to be structurally rel... | [
"GO:0005125",
"GO:0006955",
"GO:0005576"
] | [
"cytokine activity",
"immune response",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS00590"
] | [
"LIF_OSM"
] | [
317
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6788467",
"R-HSA-6783783",
"R-HSA-6785807",
"R-HSA-6788467",
"R-MMU-6788467",
"R-RNO-6788467"
] | [
"REACTOME:R-BTA-6788467",
"REACTOME:R-HSA-6783783",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6788467",
"REACTOME:R-MMU-6788467",
"REACTOME:R-RNO-6788467"
] | 6 | [
"1a7m",
"1emr",
"1evs",
"1lki",
"1pvh",
"2q7n",
"7n0a",
"8d6a",
"8v29",
"8v2a",
"8v2b",
"8v2c"
] | 12 | [
"PUB00002698",
"PUB00004755",
"PUB00005395"
] | [
"2026606",
"1717982",
"1566332"
] | [
"Disulfide bond assignment and identification of regions required for functional activity of oncostatin M.",
"Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6.",
"LIF: lots of interesting functions."
] | [
1991,
1991,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Theria"
] | [
317
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
4,
8
] | 3 | true | Conserved_site | Leukemia inhibitory factor /oncostatin, conserved site | Leukemia inhibitory factor /oncostatin, conserved site | Leukemia_IF/oncostatin_CS | 4 |
IPR019828 | 19,828 | Lysyl oxidase, conserved site | Lysyl_oxidase_CS | Conserved_site | 6,283 | false | false | Lysyl oxidase ( ) (LOX) [ ] is an extracellular copper-dependent enzyme that catalyses the oxidative deamination of peptidyl lysine residues in precursors of various collagens and elastins, yielding alpha-aminoadipic-delta-semialdehyde. The deaminated lysines are then able to form semialdehyde cross-links, resulting in... | [
"GO:0005507",
"GO:0016641"
] | [
"copper ion binding",
"oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00926"
] | [
"LYSYL_OXIDASE"
] | [
6283
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.4.3.13",
"R-BTA-1566948",
"R-BTA-2243919",
"R-DRE-2243919",
"R-HSA-1566948",
"R-HSA-2243919",
"R-MMU-1566948",
"R-MMU-2243919",
"R-RNO-1566948",
"R-RNO-2243919"
] | [
"EC:1.4.3.13",
"REACTOME:R-BTA-1566948",
"REACTOME:R-BTA-2243919",
"REACTOME:R-DRE-2243919",
"REACTOME:R-HSA-1566948",
"REACTOME:R-HSA-2243919",
"REACTOME:R-MMU-1566948",
"REACTOME:R-MMU-2243919",
"REACTOME:R-RNO-1566948",
"REACTOME:R-RNO-2243919"
] | 10 | [
"5ze3"
] | 1 | [
"PUB00000655",
"PUB00003553"
] | [
"8104038",
"1357535"
] | [
"Lysyl oxidase copper-talon complex: a model.",
"The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5 (extensive sequence homology with the murine ras recision gene)."
] | [
1993,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Kangiella spongicola"
] | [
6282,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
66,
17,
15,
15
] | 4 | true | Conserved_site | Lysyl oxidase, conserved site | Lysyl oxidase, conserved site | Lysyl_oxidase_CS | 5 |
IPR019829 | 19,829 | Macrophage migration inhibitory factor, conserved site | Macrophage_inhib_fac_CS | Conserved_site | 1,573 | false | false | Macrophage migration inhibitory factor (MIF) is a key regulatory cytokine within innate and adaptive immune responses, capable of promoting and modulating the magnitude of the response [ ]. MIF is released from T-cells and macrophages, and acts within the neuroendocrine system. MIF is capable of tautomerase activity, a... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01158"
] | [
"MIF"
] | [
1573
] | 1 | [
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.3.2.1",
"5.3.3.12",
"PWY-6498",
"R-BTA-202733",
"R-BTA-6798695",
"R-GGA-202733",
"R-GGA-6798695",
"R-HSA-202733",
"R-HSA-6798695",
"R-HSA-8950505",
"R-MMU-202733",
"R-MMU-6798695",
"R-RNO-202733",
"R-RNO-6798695",
"R-SSC-202733",
"R-SSC-6798695",
"R-XTR-6798695"
] | [
"EC:5.3.2.1",
"EC:5.3.3.12",
"METACYC:PWY-6498",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-6798695",
"REACTOME:R-GGA-202733",
"REACTOME:R-GGA-6798695",
"REACTOME:R-HSA-202733",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8950505",
"REACTOME:R-MMU-202733",
"REACTOME:R-MMU-6798695",
"REACTOME:R-R... | 17 | [
"1ca7",
"1cgq",
"1dpt",
"1fim",
"1gcz",
"1gd0",
"1gif",
"1ljt",
"1mff",
"1mfi",
"1mif",
"1p1g",
"1uiz",
"2gdg",
"2ooh",
"2oow",
"2ooz",
"3b9s",
"3ce4",
"3djh",
"3dji",
"3hof",
"3ijg",
"3ijj",
"3jsf",
"3jsg",
"3jtu",
"3kan",
"3ker",
"3l5p",
"3l5r",
"3l5s"... | 146 | [
"PUB00024290",
"PUB00034437",
"PUB00034438",
"PUB00034439",
"PUB00034440"
] | [
"10079069",
"15225126",
"16331703",
"16628200",
"10644007"
] | [
"Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 A resolution.",
"Macrophage migration inhibitory factor: molecular, cellular and genetic aspects of a key neuroendocrine molecule.",
"How glucocorticoids control their own strength and the balanc... | [
1999,
2004,
2005,
2006,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Parasynechococcus marenigrum (strain WH8102)"
] | [
1572,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
1,
11,
6,
12
] | 5 | true | Conserved_site | Macrophage migration inhibitory factor, conserved site | Macrophage migration inhibitory factor, conserved site | Macrophage_inhib_fac_CS | 4 |
IPR019830 | 19,830 | Malate synthase, conserved site | Malate_synthase_CS | Conserved_site | 9,965 | false | false | Malate synthase ( ) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. Malate synthase has a TIM β/α-barrel fold [ ]. Malate synthase is a protein of 530 to 57... | [
"GO:0004474",
"GO:0006097"
] | [
"malate synthase activity",
"glyoxylate cycle"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00510"
] | [
"MALATE_SYNTHASE"
] | [
9965
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.3.9",
"PWY-7118",
"PWY-7294",
"PWY-7295",
"PWY-7854"
] | [
"EC:2.3.3.9",
"METACYC:PWY-7118",
"METACYC:PWY-7294",
"METACYC:PWY-7295",
"METACYC:PWY-7854"
] | 5 | [
"3cux",
"3cuz",
"3cv1",
"3cv2"
] | 4 | [
"PUB00005643",
"PUB00014321"
] | [
"2349836",
"10715138"
] | [
"Cloning and sequencing of the malate synthase gene from Hansenula polymorpha.",
"Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications."
] | [
1990,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
7115,
2802,
48
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
5,
1,
1,
1,
2,
2,
4
] | 7 | true | Conserved_site | Malate synthase, conserved site | Malate synthase, conserved site | Malate_synthase_CS | 7 |
IPR019832 | 19,832 | Manganese/iron superoxide dismutase, C-terminal | Mn/Fe_SOD_C | Domain | 44,018 | false | false | This entry represents the C-terminal domain of Manganese/iron superoxide dismutase. Superoxide dismutases (SODs) ( ) catalyse the conversion of superoxide radicals to molecular oxygen. Their function is to destroy the radicals that are normally produced within cells and are toxic to biological systems. Three evolutiona... | [
"GO:0004784",
"GO:0046872",
"GO:0006801"
] | [
"superoxide dismutase activity",
"metal ion binding",
"superoxide metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF02777"
] | [
"Sod_Fe_C"
] | [
44018
] | 1 | [
"EC",
"GP",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.15.1.1",
"GenProp0213",
"GenProp1598",
"PWY-6854",
"R-CEL-3299685",
"R-DDI-2151201",
"R-DDI-3299685",
"R-DME-3299685",
"R-HSA-1222387",
"R-HSA-2151201",
"R-HSA-3299685",
"R-HSA-8862803",
"R-HSA-8950505",
"R-HSA-9615017",
"R-HSA-9841251",
"R-MMU-2151201",
"R-MMU-3299685",
"R-RNO-... | [
"EC:1.15.1.1",
"GP:GenProp0213",
"GP:GenProp1598",
"METACYC:PWY-6854",
"REACTOME:R-CEL-3299685",
"REACTOME:R-DDI-2151201",
"REACTOME:R-DDI-3299685",
"REACTOME:R-DME-3299685",
"REACTOME:R-HSA-1222387",
"REACTOME:R-HSA-2151201",
"REACTOME:R-HSA-3299685",
"REACTOME:R-HSA-8862803",
"REACTOME:R-H... | 23 | [
"1ap5",
"1ap6",
"1ar4",
"1ar5",
"1avm",
"1b06",
"1bs3",
"1bsm",
"1bt8",
"1coj",
"1d5n",
"1dt0",
"1em1",
"1en4",
"1en5",
"1en6",
"1gn2",
"1gn3",
"1gn4",
"1gn6",
"1gv3",
"1i08",
"1i0h",
"1ids",
"1isa",
"1isb",
"1isc",
"1ix9",
"1ixb",
"1ja8",
"1jr9",
"1kkc"... | 222 | [
"PUB00001002",
"PUB00001553",
"PUB00003417",
"PUB00013976",
"PUB00013977"
] | [
"3315461",
"3345848",
"1556751",
"9537987",
"9931259"
] | [
"Aspects of the structure, function, and applications of superoxide dismutase.",
"Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures.",
"A comparison of evolutionary rates of the two major kinds of superoxide dismutase.",
"Crystal structure of Y34... | [
1987,
1988,
1992,
1998,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
825,
30708,
12184,
12,
289
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
25,
2,
1,
2,
2,
10,
5,
4,
5,
2,
3,
3,
42
] | 13 | true | Domain | Manganese/iron superoxide dismutase, C-terminal | Manganese/iron superoxide dismutase, C-terminal | Mn/Fe_SOD_C | 1 |
IPR019833 | 19,833 | Manganese/iron superoxide dismutase, binding site | Mn/Fe_SOD_BS | Binding_site | 37,863 | false | false | Superoxide dismutases (SODs) ( ) catalyse the conversion of superoxide radicals to molecular oxygen. Their function is to destroy the radicals that are normally produced within cells and are toxic to biological systems. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one [... | [
"GO:0004784",
"GO:0046872",
"GO:0006801"
] | [
"superoxide dismutase activity",
"metal ion binding",
"superoxide metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00088"
] | [
"SOD_MN"
] | [
37863
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.15.1.1",
"PWY-6854",
"R-CEL-3299685",
"R-DDI-2151201",
"R-DDI-3299685",
"R-DME-3299685",
"R-HSA-1222387",
"R-HSA-2151201",
"R-HSA-3299685",
"R-HSA-8862803",
"R-HSA-8950505",
"R-HSA-9615017",
"R-HSA-9841251",
"R-MMU-2151201",
"R-MMU-3299685",
"R-RNO-2151201",
"R-RNO-3299685",
"R-... | [
"EC:1.15.1.1",
"METACYC:PWY-6854",
"REACTOME:R-CEL-3299685",
"REACTOME:R-DDI-2151201",
"REACTOME:R-DDI-3299685",
"REACTOME:R-DME-3299685",
"REACTOME:R-HSA-1222387",
"REACTOME:R-HSA-2151201",
"REACTOME:R-HSA-3299685",
"REACTOME:R-HSA-8862803",
"REACTOME:R-HSA-8950505",
"REACTOME:R-HSA-9615017",... | 21 | [
"1ap5",
"1ap6",
"1ar4",
"1ar5",
"1avm",
"1b06",
"1bs3",
"1bsm",
"1bt8",
"1d5n",
"1dt0",
"1em1",
"1en4",
"1en5",
"1en6",
"1gn2",
"1gn3",
"1gn4",
"1gn6",
"1gv3",
"1i08",
"1i0h",
"1ids",
"1isa",
"1isb",
"1isc",
"1ix9",
"1ixb",
"1jr9",
"1kkc",
"1luv",
"1luw"... | 200 | [
"PUB00001002",
"PUB00001553",
"PUB00003417",
"PUB00013976",
"PUB00013977"
] | [
"3315461",
"3345848",
"1556751",
"9537987",
"9931259"
] | [
"Aspects of the structure, function, and applications of superoxide dismutase.",
"Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures.",
"A comparison of evolutionary rates of the two major kinds of superoxide dismutase.",
"Crystal structure of Y34... | [
1987,
1988,
1992,
1998,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
783,
27666,
9154,
3,
257
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
20,
2,
1,
2,
2,
7,
4,
3,
5,
2,
1,
1,
25
] | 13 | true | Binding_site | Manganese/iron superoxide dismutase, binding site | Manganese/iron superoxide dismutase, binding site | Mn/Fe_SOD_BS | 3 |
IPR019834 | 19,834 | Glycoside hydrolase, family 8, conserved site | Glyco_hydro_8_CS | Conserved_site | 2,492 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00812"
] | [
"GLYCOSYL_HYDROL_F8"
] | [
2492
] | 1 | [
"EC",
"METACYC"
] | [
"3.2.1.4",
"PWY-6788"
] | [
"EC:3.2.1.4",
"METACYC:PWY-6788"
] | 2 | [
"1cem",
"1is9",
"1kwf",
"1v5c",
"1v5d",
"1wzz",
"3qxf",
"3qxq",
"4q2b",
"5czl",
"5gy3",
"5xd0",
"7cju",
"7f81",
"7f82",
"7xgq",
"9b87"
] | 17 | [
"PUB00001778",
"PUB00004870",
"PUB00005266",
"PUB00005276"
] | [
"2806912",
"7624375",
"8535779",
"8805535"
] | [
"Cellulase families revealed by hydrophobic cluster analysis.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase fro... | [
1989,
1995,
1995,
1996
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2482,
6,
4
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Conserved_site | Glycoside hydrolase, family 8, conserved site | Glycoside hydrolase, family 8, conserved site | Glyco_hydro_8_CS | 1 |
IPR019835 | 19,835 | SWIB domain | SWIB_domain | Domain | 18,970 | false | false | The SWI/SNF family of complexes, which are conserved from yeast to humans, are ATP-dependent chromatin-remodelling proteins that facilitate transcription activation [ , , ]. The mammalian complexes are made up of 9-12 proteins called BAFs (BRG1-associated factors). The BAF60 family have at least three members: BAF60a, ... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00151"
] | [
"SWIB"
] | [
18970
] | 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-3214858",
"R-BTA-8939243",
"R-BTA-9933939",
"R-BTA-9933946",
"R-BTA-9933947",
"R-BTA-9934037",
"R-CEL-8939243",
"R-CEL-9933937",
"R-CEL-9933939",
"R-CEL-9933946",
"R-CEL-9934037",
"R-DDI-3214858",
"R-DDI-9933937",
"R-DDI-9933939",
"R-DDI-9933946",
"R-DME-3214858",
"R-DME-40020... | [
"REACTOME:R-BTA-3214858",
"REACTOME:R-BTA-8939243",
"REACTOME:R-BTA-9933939",
"REACTOME:R-BTA-9933946",
"REACTOME:R-BTA-9933947",
"REACTOME:R-BTA-9934037",
"REACTOME:R-CEL-8939243",
"REACTOME:R-CEL-9933937",
"REACTOME:R-CEL-9933939",
"REACTOME:R-CEL-9933946",
"REACTOME:R-CEL-9934037",
"REACTOM... | 62 | [
"1uhr",
"1v31",
"6lth",
"6ltj",
"7vdv",
"7y8r",
"7z0o"
] | 7 | [
"PUB00014853",
"PUB00014864",
"PUB00088122",
"PUB00097572",
"PUB00097573",
"PUB00097574"
] | [
"11147808",
"12016060",
"22952240",
"28736176",
"26791088",
"28420746"
] | [
"Characterization of SWI/SNF protein expression in human breast cancer cell lines and other malignancies.",
"The SWIB and the MDM2 domains are homologous and share a common fold.",
"SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse functions.",
"Crystal Structure of the C-terminal Domain o... | [
2001,
2002,
2012,
2017,
2016,
2017
] | 6 | [
"IPR003121"
] | [
"IPR030090",
"IPR038041",
"IPR038043"
] | 1 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1892,
16776,
31,
271
] | 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... | [
74,
3,
17,
2,
16,
9,
2,
27,
13,
2,
2,
119
] | 12 | true | Domain | SWIB domain | SWIB domain | SWIB_domain | 3 |
IPR019836 | 19,836 | Verru/Chthon cassette protein D | Verru/Chthon_D | Family | 55 | false | false | This model describes a nearly twenty member protein family in Verrucomicrobium spinosum and a somewhat smaller paralogous family in Chthoniobacter flavus. All members share a type IV pilin-like N-terminal leader sequence ( ). These proteins occur in the four-gene Verru_Chthon cassette, in which two other genes likewise... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02596"
] | [
""
] | [
55
] | 1 | [
"GP"
] | [
"GenProp0663"
] | [
"GP:GenProp0663"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Verrucomicrobiota"
] | [
55
] | 1 | [] | [] | 0 | true | Family | Verru/Chthon cassette protein D | Verru/Chthon cassette protein D | Verru/Chthon_D | 2 |
IPR019837 | 19,837 | Conserved hypothetical protein CHP02597 | CHP02597 | Family | 36 | false | false | This entry describes a paralogous family with several members in Verrucomicrobia. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02597"
] | [
""
] | [
36
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"PVC group"
] | [
36
] | 1 | [] | [] | 0 | true | Family | Conserved hypothetical protein CHP02597 | Conserved hypothetical protein CHP02597 | CHP02597 | 5 |
IPR019838 | 19,838 | Verru/Chthon cassette protein B | Verru/Chthon_B | Family | 50 | false | false | This family consists of paralogous proteins in the Verrucomicrobium spinosum and Chthoniobacter flavus. All members contain the prepilin-type N-terminal cleavage/methylation domain ( ) at the N-terminal. These proteins occur in the four-gene Verru_Chthon cassette, in which two other genes likewise encode a cleavage/met... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02598"
] | [
""
] | [
50
] | 1 | [
"GP"
] | [
"GenProp0663"
] | [
"GP:GenProp0663"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Verrucomicrobiota"
] | [
50
] | 1 | [] | [] | 0 | true | Family | Verru/Chthon cassette protein B | Verru/Chthon cassette protein B | Verru/Chthon_B | 4 |
IPR019839 | 19,839 | Verru/Chthon cassette protein C | Verru/Chthon_C | Family | 50 | false | false | This family consists of paralogous proteins in the Verrucomicrobium spinosum and Chthoniobacter flavus . All members contain the prepilin-type N-terminal cleavage/methylation domain at the N-terminal. These proteins occur in the four-gene Verru_Chthon cassette, in which two other genes likewise encode a cleavage/methyl... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02599"
] | [
""
] | [
50
] | 1 | [
"GP"
] | [
"GenProp0663"
] | [
"GP:GenProp0663"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Verrucomicrobiota"
] | [
50
] | 1 | [] | [] | 0 | true | Family | Verru/Chthon cassette protein C | Verru/Chthon cassette protein C | Verru/Chthon_C | 2 |
IPR019841 | 19,841 | Osteopontin, conserved site | Osteopontin_CS | Conserved_site | 581 | false | false | The major event of endochondrial ossification is the proteolytic degradation of calcified cartilage and the extracellular matrix, and their substitution with bone-specific extracellular matrix produced and organised by osteoblasts [ ]. One of the most abundant products of osteoblasts is osteopontin, a glycosylated phos... | [
"GO:0001503",
"GO:0007155"
] | [
"ossification",
"cell adhesion"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00884"
] | [
"OSTEOPONTIN"
] | [
581
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1474228",
"R-HSA-186797",
"R-HSA-216083",
"R-HSA-381426",
"R-HSA-8949275",
"R-HSA-8957275",
"R-HSA-9856532",
"R-MMU-1474228",
"R-MMU-186797",
"R-MMU-216083",
"R-MMU-381426",
"R-MMU-8957275",
"R-RNO-1474228",
"R-RNO-186797",
"R-RNO-216083",
"R-RNO-381426",
"R-RNO-8957275",
"R... | [
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-186797",
"REACTOME:R-HSA-216083",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8949275",
"REACTOME:R-HSA-8957275",
"REACTOME:R-HSA-9856532",
"REACTOME:R-MMU-1474228",
"REACTOME:R-MMU-186797",
"REACTOME:R-MMU-216083",
"REACTOME:R-MMU-381426",
"REACTOME:R-MM... | 22 | [] | 0 | [
"PUB00002704",
"PUB00003048"
] | [
"2033080",
"1414488"
] | [
"cDNA cloning and gene expression of chicken osteopontin. Expression of osteopontin mRNA in chondrocytes is enhanced by trypsin treatment of cells.",
"Isolation and characterization of a cDNA for osteopontin-k: a kidney cell adhesion molecule with high homology to osteopontins."
] | [
1991,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Amniota"
] | [
581
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
11,
3
] | 3 | true | Conserved_site | Osteopontin, conserved site | Osteopontin, conserved site | Osteopontin_CS | 7 |
IPR019842 | 19,842 | Uricase, conserved site | Uricase_CS | Conserved_site | 3,545 | false | false | Uricase ( ) (urate oxidase) [ ] is the peroxisomal enzyme responsible for the degradation of urate into allantoin: Urate + O 2 + H 2 O = 5-hydroxyisourate + H 2 O 2 Some species, like primates and birds, have lost the gene for uricase and are therefore unable to degrade urate [ ]. Uricase is a protein of 300 to 400 ami... | [
"GO:0004846",
"GO:0006144"
] | [
"urate oxidase activity",
"purine nucleobase metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00366"
] | [
"URICASE"
] | [
3545
] | 1 | [
"EC",
"METACYC"
] | [
"1.7.3.3",
"PWY-5691"
] | [
"EC:1.7.3.3",
"METACYC:PWY-5691"
] | 2 | [
"1j2g",
"1r4s",
"1r4u",
"1r51",
"1r56",
"1vax",
"1vay",
"1wrr",
"1ws2",
"1ws3",
"1xt4",
"1xxj",
"1xy3",
"2fub",
"2fxl",
"2iba",
"2ic0",
"2icq",
"2pes",
"2yzb",
"2yzc",
"2yzd",
"2yze",
"2zka",
"2zkb",
"3bjp",
"3bk8",
"3cks",
"3cku",
"3f2m",
"3gko",
"3l8w"... | 111 | [
"PUB00001587",
"PUB00002471",
"PUB00004611",
"PUB00004693"
] | [
"2338140",
"3182808",
"16593585",
"2594778"
] | [
"Organization of rat uricase chromosomal gene differs greatly from that of the corresponding plant gene.",
"Cloning and sequence analysis of cDNA for rat liver uricase.",
"Primary structure of the soybean nodulin-35 gene encoding uricase II localized in the peroxisomes of uninfected cells of nodules.",
"Urate... | [
1990,
1988,
1985,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halarchaeum salinum",
"metagenomes"
] | [
1115,
2425,
1,
4
] | 4 | [
"Arabidopsis thaliana",
"Drosophila melanogaster",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
4,
2,
5,
1,
9,
1
] | 6 | true | Conserved_site | Uricase, conserved site | Uricase, conserved site | Uricase_CS | 3 |
IPR019843 | 19,843 | DNA polymerase family X, binding site | DNA_pol-X_BS | Binding_site | 6,012 | false | false | DNA carries the biological information that instructs cells how to exist in an ordered fashion: accurate replication is thus one of the most important events in the cell life cycle. This function is mediated by DNA-directed DNA-polymerases, which add nucleotide triphosphate (dNTP) residues to the 3'-end of the growing ... | [
"GO:0016779"
] | [
"nucleotidyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00522"
] | [
"DNA_POLYMERASE_X"
] | [
6012
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.7",
"R-BTA-110362",
"R-BTA-110373",
"R-BTA-110381",
"R-BTA-5649702",
"R-BTA-5651801",
"R-BTA-5689880",
"R-BTA-73930",
"R-DRE-110362",
"R-DRE-110373",
"R-DRE-5649702",
"R-DRE-73930",
"R-HSA-110362",
"R-HSA-110373",
"R-HSA-110381",
"R-HSA-5649702",
"R-HSA-5651801",
"R-HSA-5689... | [
"EC:2.7.7.7",
"REACTOME:R-BTA-110362",
"REACTOME:R-BTA-110373",
"REACTOME:R-BTA-110381",
"REACTOME:R-BTA-5649702",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-73930",
"REACTOME:R-DRE-110362",
"REACTOME:R-DRE-110373",
"REACTOME:R-DRE-5649702",
"REACTOME:R-DRE-73930",
"... | 36 | [
"1bpb",
"1bpd",
"1bpe",
"1bpx",
"1bpy",
"1bpz",
"1huo",
"1huz",
"1jaj",
"1jms",
"1jn3",
"1jqr",
"1kdh",
"1kej",
"1mq2",
"1mq3",
"1nom",
"1rpl",
"1rzt",
"1tv9",
"1tva",
"1xsl",
"1xsn",
"1xsp",
"1zjm",
"1zjn",
"1zqa",
"1zqb",
"1zqc",
"1zqd",
"1zqe",
"1zqf"... | 724 | [
"PUB00000352",
"PUB00004647",
"PUB00004955"
] | [
"2036395",
"3479792",
"2196557"
] | [
"Aspartic acid residues at positions 190 and 192 of rat DNA polymerase beta are involved in primer binding.",
"Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.",
"An attempt to unify the structure of polymerases."
] | [
1991,
1987,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Acidobacteriaceae",
"Eukaryota",
"Nucleocytoviricota",
"viral metagenome"
] | [
3,
5934,
48,
27
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"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)",
"Schizosaccharomyces pombe (st... | [
5,
12,
24,
8,
1,
2,
15,
1,
1,
8
] | 10 | true | Binding_site | DNA polymerase family X, binding site | DNA polymerase family X, binding site | DNA_pol-X_BS | 3 |
IPR019844 | 19,844 | Cold-shock domain, conserved site | CSD_CS | Conserved_site | 72,294 | false | false | The cold-shock domain (CSD) is an ancient β-barrel fold of about 70 amino acids that binds single-stranded nucleic acids (both RNA and DNA). CSD- containing proteins have been found in all three domains of life and function in a variety of processes that are related, for the most part, to post- translational gene regul... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00352"
] | [
"CSD_1"
] | [
72294
] | 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-72163",
"R-BTA-72165",
"R-BTA-72203",
"R-BTA-877300",
"R-DRE-72163",
"R-DRE-877300",
"R-HSA-2173796",
"R-HSA-72163",
"R-HSA-72165",
"R-HSA-72203",
"R-HSA-877300",
"R-HSA-9017802",
"R-MMU-72163",
"R-MMU-72165",
"R-MMU-72203",
"R-MMU-877300",
"R-MMU-9017802",
"R-RNO-72163",
... | [
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-72165",
"REACTOME:R-BTA-72203",
"REACTOME:R-BTA-877300",
"REACTOME:R-DRE-72163",
"REACTOME:R-DRE-877300",
"REACTOME:R-HSA-2173796",
"REACTOME:R-HSA-72163",
"REACTOME:R-HSA-72165",
"REACTOME:R-HSA-72203",
"REACTOME:R-HSA-877300",
"REACTOME:R-HSA-9017802",... | 22 | [
"1c9o",
"1csp",
"1csq",
"1g6p",
"1h95",
"1hz9",
"1hza",
"1hzb",
"1hzc",
"1i5f",
"1mjc",
"1nmf",
"1nmg",
"1wfq",
"1x65",
"2es2",
"2f52",
"2hax",
"2i5l",
"2i5m",
"2l15",
"2lss",
"2lxj",
"2lxk",
"2mo0",
"2mo1",
"2mqh",
"2ytx",
"2yty",
"3a0j",
"3aqq",
"3cam"... | 67 | [
"PUB00004326",
"PUB00004406",
"PUB00025582",
"PUB00054492",
"PUB00092586",
"PUB00092587"
] | [
"1622933",
"1614871",
"11851341",
"20213426",
"20091748",
"26147853"
] | [
"The product of unr, the highly conserved gene upstream of N-ras, contains multiple repeats similar to the cold-shock domain (CSD), a putative DNA-binding motif.",
"RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domain.",
"The solution structure and DNA-binding properties of the cold-sho... | [
1992,
1992,
2002,
2010,
2010,
2015
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
107,
60741,
10744,
7,
695
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
17,
3,
41,
7,
9,
40,
33,
9,
29,
13
] | 10 | true | Conserved_site | Cold-shock domain, conserved site | Cold-shock domain, conserved site | CSD_CS | 4 |
IPR019845 | 19,845 | Squalene/phytoene synthase, conserved site | Squalene/phytoene_synthase_CS | Conserved_site | 20,382 | false | false | Squalene synthase (farnesyl-diphosphate farnesyltransferase)(SQS) and phytoene synthase (PSY) share a number of functional similarities. These similarities are also reflected at the level of their primary structure [ , , ]. In particular three well conserved regions are shared by SQS and PSY; they could be involved in ... | [
"GO:0016765"
] | [
"transferase activity, transferring alkyl or aryl (other than methyl) groups"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS01044",
"PS01045"
] | [
"SQUALEN_PHYTOEN_SYN_1",
"SQUALEN_PHYTOEN_SYN_2"
] | [
12642,
18928
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.5.1",
"R-DDI-191273",
"R-HSA-191273",
"R-HSA-1989781",
"R-HSA-2426168",
"R-MMU-191273",
"R-RNO-191273",
"R-SCE-191273",
"R-SPO-191273"
] | [
"EC:2.5.1",
"REACTOME:R-DDI-191273",
"REACTOME:R-HSA-191273",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-2426168",
"REACTOME:R-MMU-191273",
"REACTOME:R-RNO-191273",
"REACTOME:R-SCE-191273",
"REACTOME:R-SPO-191273"
] | 9 | [
"1ezf",
"2zco",
"2zcq",
"2zcr",
"2zcs",
"2zy1",
"3acw",
"3acx",
"3acy",
"3ae0",
"3asx",
"3lee",
"3npr",
"3nri",
"3q2z",
"3q30",
"3tfn",
"3tfp",
"3tfv",
"3v66",
"3vj8",
"3vj9",
"3vja",
"3vjb",
"3vjc",
"3vjd",
"3vje",
"3w7f",
"3wc9",
"3wca",
"3wcb",
"3wcc"... | 65 | [
"PUB00000230",
"PUB00001836",
"PUB00003686"
] | [
"8250898",
"8294001",
"8474436"
] | [
"Expression of the genes encoding the early carotenoid biosynthetic enzymes in Capsicum annuum.",
"Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase.",
"Conservation between human and fungal squalene synthetases: similarities... | [
1993,
1993,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
370,
11854,
7909,
2,
247
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"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)",
"Schizosaccharomyces pombe (st... | [
10,
2,
10,
4,
3,
18,
3,
1,
1,
46
] | 10 | true | Conserved_site | Squalene/phytoene synthase, conserved site | Squalene/phytoene synthase, conserved site | Squalene/phytoene_synthase_CS | 8 |
IPR019846 | 19,846 | Nerve growth factor conserved site | Nerve_growth_factor_CS | Conserved_site | 10,399 | false | false | This entry covers the central region of the proteins and include two of the six cysteines involved in disulphide bonds. During the development of the vertebrate nervous system, many neurons become redundant (because they have died, failed to connect to target cells, etc.) and are eliminated. At the same time, developin... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00248"
] | [
"NGF_1"
] | [
10399
] | 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-1257604",
"R-BTA-6811558",
"R-BTA-9026527",
"R-BTA-9028731",
"R-BTA-9032759",
"R-BTA-9034013",
"R-BTA-9034793",
"R-BTA-9603381",
"R-DRE-167060",
"R-DRE-170984",
"R-DRE-205017",
"R-DRE-209543",
"R-DRE-209563",
"R-GGA-1257604",
"R-GGA-6811558",
"R-GGA-9026527",
"R-GGA-9028731",
... | [
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-6811558",
"REACTOME:R-BTA-9026527",
"REACTOME:R-BTA-9028731",
"REACTOME:R-BTA-9032759",
"REACTOME:R-BTA-9034013",
"REACTOME:R-BTA-9034793",
"REACTOME:R-BTA-9603381",
"REACTOME:R-DRE-167060",
"REACTOME:R-DRE-170984",
"REACTOME:R-DRE-205017",
"REACTOME:R... | 102 | [
"1b8k",
"1b8m",
"1b98",
"1bet",
"1bnd",
"1btg",
"1hcf",
"1nt3",
"1sg1",
"1sgf",
"1www",
"2ifg",
"3buk",
"3ij2",
"4eax",
"4ec7",
"4edw",
"4edx",
"4efv",
"4xpj",
"4zbn",
"5jz7",
"5lsd",
"6ffy",
"6xuo",
"6yw8",
"9fik"
] | 27 | [
"PUB00000638",
"PUB00001187",
"PUB00001600",
"PUB00005102",
"PUB00005408",
"PUB00043579",
"PUB00043580"
] | [
"1477101",
"2369898",
"1995338",
"3589669",
"8488558",
"2236018",
"8527932"
] | [
"Purification and amino-acid sequence of a nerve growth factor from the venom of Vipera russelli russelli.",
"Regional distribution of brain-derived neurotrophic factor mRNA in the adult mouse brain.",
"Amino acid sequences of nerve growth factors derived from cobra venoms.",
"Recruitment of enzymes as lens s... | [
1992,
1990,
1991,
1987,
1993,
1990,
1995
] | 7 | [] | [] | 0 | 0 | null | [
"Avipoxvirus",
"Bilateria"
] | [
11,
10388
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
25,
10,
11,
23
] | 4 | true | Conserved_site | Nerve growth factor conserved site | Nerve growth factor conserved site | Nerve_growth_factor_CS | 2 |
IPR019847 | 19,847 | Gliding motility associated protein GldN | Gliding_motility_assoc_GldN | Family | 2,416 | false | false | Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldN is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Cytophaga johnsonae (Flavobacterium johnsoniae) and Cytophaga hutchinsonii. Knockouts of... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF19841",
"TIGR03523"
] | [
"GldN",
"GldN"
] | [
2416,
2304
] | 2 | [
"GP"
] | [
"GenProp0781"
] | [
"GP:GenProp0781"
] | 1 | [
"7pvh",
"9myj",
"9mzu",
"9ots",
"9p6h"
] | 5 | [
"PUB00045359"
] | [
"16199564"
] | [
"Flavobacterium johnsoniae gliding motility genes identified by mariner mutagenesis."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2379,
4,
33
] | 3 | [] | [] | 0 | true | Family | Gliding motility associated protein GldN | Gliding motility associated protein GldN | Gliding_motility_assoc_GldN | 4 |
IPR019848 | 19,848 | CRISPR-associated protein, Csx14 | CRISPR-assoc_prot_Csx14 | Family | 38 | false | false | This entry is found in Cas proteins from a variety of bacterial and archaeal species, including Pelotomaculum thermopropionicum (strain DSM 13744/JCM 10971/SI), Thermoanaerobacter tengcongensis MB4, Roseiflexus sp. (strain RS-1), Thermoplasma volcanium, Picrophilus torridus, and Methanospirillum hungatei. The function ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03642"
] | [
"cas_csx14"
] | [
38
] | 1 | [
"GP"
] | [
"GenProp0021"
] | [
"GP:GenProp0021"
] | 1 | [] | 0 | [
"PUB00043286",
"PUB00043287",
"PUB00043288",
"PUB00060621",
"PUB00071890"
] | [
"17442114",
"17379808",
"16545108",
"21699496",
"24459147"
] | [
"Evolutionary conservation of sequence and secondary structures in CRISPR repeats.",
"CRISPR provides acquired resistance against viruses in prokaryotes.",
"A putative RNA-interference-based immune system in prokaryotes: computational analysis of the predicted enzymatic machinery, functional analogies with euka... | [
2007,
2007,
2006,
2011,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria"
] | [
18,
20
] | 2 | [] | [] | 0 | true | Family | CRISPR-associated protein, Csx14 | CRISPR-associated protein, Csx14 | CRISPR-assoc_prot_Csx14 | 2 |
IPR019850 | 19,850 | GldD-like | GldD-like | Family | 1,981 | false | false | This entry represents the GldD lipoprotein family, found in members of the Bacteroidetes lineage, including species such as Cytophaga johnsonae, which exhibit a poorly understood form of rapid gliding motility, as well as species that lack this capability. GldD is a post-translationally modified lipoprotein and an esse... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF25593",
"TIGR03512"
] | [
"GldD_lipo",
"GldD_lipo"
] | [
1981,
1604
] | 2 | [
"GP"
] | [
"GenProp0781"
] | [
"GP:GenProp0781"
] | 1 | [] | 0 | [
"PUB00045357"
] | [
"11418556"
] | [
"Cloning and characterization of the Flavobacterium johnsoniae gliding motility genes gldD and gldE."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteroidota",
"Eukaryota",
"ecological metagenomes"
] | [
1959,
2,
20
] | 3 | [] | [] | 0 | true | Family | GldD-like | GldD-like | GldD-like | 9 |
IPR019851 | 19,851 | CRISPR-associated protein Cas1, ECOLI subtype | CRISPR-assoc_Cas1_ECOLI | Family | 2,921 | false | false | This entry describes the Cas1 protein particular to the ECOLI subtype of CRISPR/Cas system. The CRISPR-Cas system is a prokaryotic defence mechanism against foreign genetic elements. The key elements of this defence system are the Cas proteins and the CRISPR RNA. | [
"GO:0004520",
"GO:0046872",
"GO:0043571"
] | [
"DNA endonuclease activity",
"metal ion binding",
"maintenance of CRISPR repeat elements"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03638"
] | [
"cas1_ECOLI"
] | [
2921
] | 1 | [] | [] | [] | 0 | [
"3nkd",
"3nke",
"4p6i",
"4qdl",
"5dlj",
"5dqt",
"5dqu",
"5dqz",
"5ds4",
"5ds5",
"5ds6",
"5vvj",
"5vvk",
"5vvl",
"5wfe",
"6kdv",
"6ke1",
"8fy9",
"8fya",
"8fyb",
"8fyc",
"8fyd",
"8hi1"
] | 23 | [
"PUB00043286",
"PUB00043287",
"PUB00043288",
"PUB00060621",
"PUB00071890"
] | [
"17442114",
"17379808",
"16545108",
"21699496",
"24459147"
] | [
"Evolutionary conservation of sequence and secondary structures in CRISPR repeats.",
"CRISPR provides acquired resistance against viruses in prokaryotes.",
"A putative RNA-interference-based immune system in prokaryotes: computational analysis of the predicted enzymatic machinery, functional analogies with euka... | [
2007,
2007,
2006,
2011,
2014
] | 5 | [
"IPR002729"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanomicrobia",
"Zopfia rhizophila CBS 207.26",
"unclassified sequences"
] | [
2885,
18,
1,
17
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | CRISPR-associated protein Cas1, ECOLI subtype | CRISPR-associated protein Cas1, ECOLI subtype | CRISPR-assoc_Cas1_ECOLI | 6 |
IPR019853 | 19,853 | GldB-like | GldB-like | Family | 2,590 | false | false | This entry represents the GldB protein family, which is found in various members of the Bacteroidetes lineage, including species such as Cytophaga johnsonae , known for exhibiting a poorly understood form of rapid gliding motility, as well as other species that lack this phenotype [ ]. GldB is an essential component of... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF25594",
"TIGR03514"
] | [
"GldB_lipo",
"GldB_lipo"
] | [
2590,
1180
] | 2 | [
"GP"
] | [
"GenProp0781"
] | [
"GP:GenProp0781"
] | 1 | [] | 0 | [
"PUB00045354"
] | [
"10648514"
] | [
"Cloning and characterization of the Flavobacterium johnsoniae gliding-motility genes gldB and gldC."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Russula earlei",
"metagenomes"
] | [
2561,
1,
28
] | 3 | [] | [] | 0 | true | Family | GldB-like | GldB-like | GldB-like | 5 |
IPR019854 | 19,854 | Gliding motility-associated protein, GldC | Motility-assoc_prot_GldC | Family | 1,870 | false | false | Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides) [ ]. GldC is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Cytophaga johnsonae (Flavobacterium johnsoniae) and Cytophaga hutchinsonii. Knockout... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF19937",
"TIGR03515"
] | [
"GldC-like",
"GldC"
] | [
1870,
1841
] | 2 | [
"GP"
] | [
"GenProp0781"
] | [
"GP:GenProp0781"
] | 1 | [] | 0 | [
"PUB00045354"
] | [
"10648514"
] | [
"Cloning and characterization of the Flavobacterium johnsoniae gliding-motility genes gldB and gldC."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Tanacetum cinerariifolium",
"ecological metagenomes"
] | [
1856,
1,
13
] | 3 | [] | [] | 0 | true | Family | Gliding motility-associated protein, GldC | Gliding motility-associated protein, GldC | Motility-assoc_prot_GldC | 2 |
IPR019855 | 19,855 | CRISPR-associated protein Cas1, NMENI subtype | CRISPR-assoc_Cas1_NMENI | Family | 2,530 | false | false | This entry describes the Cas1 variant of the NMENI subtype of CRISPR/Cas system. The CRISPR-Cas system is a prokaryotic defence mechanism against foreign genetic elements. The key elements of this defence system are the Cas proteins and the CRISPR RNA. | [
"GO:0004520",
"GO:0046872",
"GO:0043571"
] | [
"DNA endonuclease activity",
"metal ion binding",
"maintenance of CRISPR repeat elements"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03639"
] | [
"cas1_NMENI"
] | [
2530
] | 1 | [
"GP"
] | [
"GenProp0314"
] | [
"GP:GenProp0314"
] | 1 | [
"4zkj",
"5xvn",
"5xvo",
"5xvp",
"6qxf",
"6qxt",
"6qy3",
"8pk1",
"8q2n"
] | 9 | [
"PUB00043286",
"PUB00043287",
"PUB00043288",
"PUB00060621",
"PUB00071890"
] | [
"17442114",
"17379808",
"16545108",
"21699496",
"24459147"
] | [
"Evolutionary conservation of sequence and secondary structures in CRISPR repeats.",
"CRISPR provides acquired resistance against viruses in prokaryotes.",
"A putative RNA-interference-based immune system in prokaryotes: computational analysis of the predicted enzymatic machinery, functional analogies with euka... | [
2007,
2007,
2006,
2011,
2014
] | 5 | [
"IPR002729"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanimicrococcus",
"metagenomes"
] | [
2484,
4,
2,
40
] | 4 | [] | [] | 0 | true | Family | CRISPR-associated protein Cas1, NMENI subtype | CRISPR-associated protein Cas1, NMENI subtype | CRISPR-assoc_Cas1_NMENI | 3 |
IPR019856 | 19,856 | CRISPR-associated protein Cas1, DVULG subtype | CRISPR-assoc_Cas1_DVULG | Family | 1,924 | false | false | This entry describes the Cas1 protein particular to the DVULG subtype of CRISPR/Cas system. This is also known as Cas1 Type I-C [ ]. Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR) are a family of DNA direct repeats separated by regularly sized non-repetitive spacer sequences that are found in most b... | [
"GO:0004520",
"GO:0046872",
"GO:0043571"
] | [
"DNA endonuclease activity",
"metal ion binding",
"maintenance of CRISPR repeat elements"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM",
"CDD"
] | [
"TIGR03640",
"cd09721"
] | [
"cas1_DVULG",
"Cas1_I-C"
] | [
1924,
1411
] | 2 | [] | [] | [] | 0 | [
"8d3l",
"8d3m",
"8d3p",
"8d3q"
] | 4 | [
"PUB00020781",
"PUB00043286",
"PUB00078085"
] | [
"16292354",
"17442114",
"21552286"
] | [
"A guild of 45 CRISPR-associated (Cas) protein families and multiple CRISPR/Cas subtypes exist in prokaryotic genomes.",
"Evolutionary conservation of sequence and secondary structures in CRISPR repeats.",
"Evolution and classification of the CRISPR-Cas systems."
] | [
2005,
2007,
2011
] | 3 | [
"IPR002729"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanomicrobia",
"ecological metagenomes"
] | [
1879,
3,
20,
22
] | 4 | [] | [] | 0 | true | Family | CRISPR-associated protein Cas1, DVULG subtype | CRISPR-associated protein Cas1, DVULG subtype | CRISPR-assoc_Cas1_DVULG | 6 |
IPR019857 | 19,857 | CRISPR-associated protein Cas1, YPEST subtype | CRISPR-assoc_Cas1_YPEST-subtyp | Family | 1,022 | false | false | This entry describes the Cas1 protein particular to the YPEST subtype of CRISPR/Cas system. This is also known as Cas1 Type I-F [ ]. The CRISPR-Cas system is a prokaryotic defence mechanism against foreign genetic elements. The key elements of this defence system are the Cas proteins and the CRISPR RNA. | [
"GO:0004520",
"GO:0046872",
"GO:0043571"
] | [
"DNA endonuclease activity",
"metal ion binding",
"maintenance of CRISPR repeat elements"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM",
"CDD"
] | [
"TIGR03637",
"cd09718"
] | [
"cas1_YPEST",
"Cas1_I-F"
] | [
1022,
482
] | 2 | [
"GP"
] | [
"GenProp0310"
] | [
"GP:GenProp0310"
] | 1 | [
"3god",
"4w8k",
"5fcl",
"8flj",
"8k21",
"8k22",
"8k23",
"8k24",
"8k25",
"8k26",
"9p11",
"9p1d"
] | 12 | [
"PUB00043286",
"PUB00043287",
"PUB00043288",
"PUB00060621",
"PUB00071890",
"PUB00078085"
] | [
"17442114",
"17379808",
"16545108",
"21699496",
"24459147",
"21552286"
] | [
"Evolutionary conservation of sequence and secondary structures in CRISPR repeats.",
"CRISPR provides acquired resistance against viruses in prokaryotes.",
"A putative RNA-interference-based immune system in prokaryotes: computational analysis of the predicted enzymatic machinery, functional analogies with euka... | [
2007,
2007,
2006,
2011,
2014,
2011
] | 6 | [
"IPR002729"
] | [] | 1 | 0 | 1 | [
"Anopheles coluzzii",
"Bacteria",
"unclassified Mohonavirus",
"unclassified sequences"
] | [
1,
1006,
2,
13
] | 4 | [] | [] | 0 | true | Family | CRISPR-associated protein Cas1, YPEST subtype | CRISPR-associated protein Cas1, YPEST subtype | CRISPR-assoc_Cas1_YPEST-subtyp | 5 |
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