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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR002846 | 2,846 | NrpR regulatory domain | NRD | Domain | 504 | false | false | NrpR is an transcriptional repressor of nitrogen assimilation genes found primarily in Euryarchaeota [ ]. In the thermophilic archaeon Methanocaldococcus jannaschii it consists of a putative N-terminal winged helix-turn-helix (wHTH) domain used for DNA binding followed by two NrpR regulatory domains (NRD1 and NRD2) tha... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01995"
] | [
"NRD1_2"
] | [
504
] | 1 | [] | [] | [] | 0 | [
"3nek"
] | 1 | [
"PUB00086619",
"PUB00086620",
"PUB00086621"
] | [
"17720835",
"15590692",
"21070950"
] | [
"Genetic screen for regulatory mutations in Methanococcus maripaludis and its use in identification of induction-deficient mutants of the euryarchaeal repressor NrpR.",
"Regulation of nif expression in Methanococcus maripaludis: roles of the euryarchaeal repressor NrpR, 2-oxoglutarate, and two operators.",
"Str... | [
2007,
2005,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"ecological metagenomes"
] | [
65,
413,
26
] | 3 | [] | [] | 0 | true | Domain | NrpR regulatory domain | NrpR regulatory domain | NRD | 6 |
IPR002847 | 2,847 | Coenzyme F420:L-glutamate ligase-like domain | F420-0_gamma-glut_ligase-dom | Domain | 7,127 | false | false | This entry represents a domain found in the coenzyme F420:L-glutamate ligase (also known as F420-0:gamma-glutamyl ligase) and related proteins. Coenzyme F420:L-glutamate ligase catalyses the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydrox... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01996"
] | [
"F420_ligase"
] | [
7127
] | 1 | [
"EC",
"EC",
"METACYC"
] | [
"6.3.2.31",
"6.3.2.34",
"PWY-5199"
] | [
"EC:6.3.2.31",
"EC:6.3.2.34",
"METACYC:PWY-5199"
] | 3 | [
"2g9i",
"2phn",
"7uld",
"7ule",
"7ulf",
"8g8p"
] | 6 | [
"PUB00002622",
"PUB00003870",
"PUB00044776",
"PUB00044777"
] | [
"2110564",
"8577249",
"12867481",
"15215601"
] | [
"DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans.",
"Molecular characterization of the lincomycin-production gene cluster of Streptomyces lincolnensis 78-11.",
"Methanococcus jannaschii coenzyme F420 analogs contain a terminal alpha-linked glutamate.",
"Identification and cloning of th... | [
1990,
1995,
2003,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1086,
5792,
35,
214
] | 4 | [] | [] | 0 | true | Domain | Coenzyme F420:L-glutamate ligase-like domain | Coenzyme F420:L-glutamate ligase-like domain | F420-0_gamma-glut_ligase-dom | 6 |
IPR002848 | 2,848 | Translin family | Translin_fam | Family | 8,415 | false | false | Translins are DNA-binding proteins that specifically recognise consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. They seem to recognise single-stranded DNA ends generated by staggered breaks occuring at recombination hot sp... | [
"GO:0043565"
] | [
"sequence-specific DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF01997",
"PTHR10741"
] | [
"Translin",
""
] | [
8292,
8253
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-426486",
"R-HSA-426486",
"R-MMU-426486",
"R-RNO-426486",
"R-SPO-426486"
] | [
"REACTOME:R-BTA-426486",
"REACTOME:R-HSA-426486",
"REACTOME:R-MMU-426486",
"REACTOME:R-RNO-426486",
"REACTOME:R-SPO-426486"
] | 5 | [
"1j1j",
"1key",
"2qrx",
"2qva",
"3axj",
"3pja",
"3qb5",
"3riu",
"3zc0",
"3zc1",
"4dg7",
"4wyv",
"5jr9",
"5jrc",
"5jre",
"8z7a"
] | 16 | [
"PUB00005776",
"PUB00028825",
"PUB00037000",
"PUB00076798"
] | [
"9013868",
"12079346",
"15039555",
"12036294"
] | [
"Isolation and characterization of a cDNA encoding a Translin-like protein, TRAX.",
"Crystal structure of TB-RBP, a novel RNA-binding and regulating protein.",
"Structure of human translin at 2.2 A resolution.",
"Identification and characterization of cDNAs encoding four novel proteins that interact with tran... | [
1997,
2002,
2004,
2002
] | 4 | [] | [
"IPR033956"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
355,
152,
7880,
28
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Ze... | [
14,
2,
5,
12,
5,
2,
8,
8,
2,
21
] | 10 | true | Family | Translin family | Translin family | Translin_fam | 4 |
IPR002849 | 2,849 | Protein of unknown function DUF131 | DUF131 | Family | 447 | false | false | This entry represents Uncharacterized protein MJ1617 from Methanocaldococcus jannaschii and related uncharacterised proteins. The proteins are predicted to contain two transmembrane helices. | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF01998",
"TIGR00304"
] | [
"DUF131",
""
] | [
442,
445
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"candidate division CPR3 bacterium",
"groundwater metagenome"
] | [
445,
1,
1
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF131 | Protein of unknown function DUF131 | DUF131 | 1 |
IPR002850 | 2,850 | MJ1680-like | MJ1680-like | Family | 6,152 | false | false | This entry represents Uncharacterized protein MJ1680 and other proteins which are part of the PIN domain superfamily . It is restricted to bacteria and archaea. A comprehensive in silico study of toxin-antitoxin systems [ ] finds evidence that this family represents the toxin-like component of one class of type 2 toxin... | [] | [] | [] | 0 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR34610",
"TIGR00305"
] | [
"",
""
] | [
5937,
5435
] | 2 | [
"GP"
] | [
"GenProp0321"
] | [
"GP:GenProp0321"
] | 1 | [] | 0 | [
"PUB00056164"
] | [
"19493340"
] | [
"Comprehensive comparative-genomic analysis of type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
162,
5854,
4,
132
] | 4 | [] | [] | 0 | true | Family | MJ1680-like | MJ1680-like | MJ1680-like | 8 |
IPR002852 | 2,852 | Uncharacterised protein family UPF0251 | UPF0251 | Family | 3,009 | false | false | The bacterial and archaeal proteins in this family have no known function. A study suggests that some archaeal members may be G-quadruplex binding proteins [ ]. | [] | [] | [] | 0 | [
"HAMAP",
"PFAM",
"PANTHER"
] | [
"MF_00674",
"PF02001",
"PTHR37478"
] | [
"UPF0251",
"DUF134",
""
] | [
2084,
3008,
2930
] | 3 | [] | [] | [] | 0 | [] | 0 | [
"PUB00098045"
] | [
"32967357"
] | [
"G-Quadruplexes in the Archaea Domain."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
392,
2523,
2,
92
] | 4 | [] | [] | 0 | true | Family | Uncharacterised protein family UPF0251 | Uncharacterised protein family UPF0251 | UPF0251 | 5 |
IPR002853 | 2,853 | Transcription initiation factor IIE subunit alpha, N-terminal | TFIIE_asu | Domain | 6,032 | false | false | This entry represents the conserved N-terminal region of eukaryotic TFIIE-alpha and proteins from archaebacteria (TFE) that are also presumed to be TFIIE-alpha subunits [ ]. Initiation of eukaryotic mRNA transcription requires melting of promoter DNA with the help of the general transcription factors TFIIE and TFIIH. I... | [
"GO:0006367"
] | [
"transcription initiation at RNA polymerase II promoter"
] | [
"biological_process"
] | 1 | [
"SMART"
] | [
"SM00531"
] | [
"TFIIE"
] | [
6032
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-674695",
"R-BTA-6807505",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-75953",
"R-BTA-76042",
"R-DDI-674695",
"R-DDI-6807505",
"R-DDI-73776",
"R-DDI-73779",
"R-DDI-75953",
"R-DDI-76042",
"R-HSA-167161",
"R-HSA-167162",
"R-HSA-167172",
"R-HSA-674695",
"R-HSA-6807505",
"R-HSA-73776",
... | [
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-73776",
"REACTOME:R-BTA-73779",
"REACTOME:R-BTA-75953",
"REACTOME:R-BTA-76042",
"REACTOME:R-DDI-674695",
"REACTOME:R-DDI-6807505",
"REACTOME:R-DDI-73776",
"REACTOME:R-DDI-73779",
"REACTOME:R-DDI-75953",
"REACTOME:R-DDI-76042",
... | 39 | [
"5fmf",
"5fyw",
"5fz5",
"5gpy",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5iya",
"5iyb",
"5iyc",
"5iyd",
"5oqj",
"5oqm",
"5sva",
"6gyl",
"6gym",
"6kf4",
"6kf9",
"6o9l",
"6pln",
"6xjf",
"7eg9",
"7ega",
"7egb",
"7egc",
"7ena",
"7enc",
"7lbm",
"7ml0",
"7ml1",
"7ml2"... | 76 | [
"PUB00005802",
"PUB00006521"
] | [
"9389475",
"10716934"
] | [
"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.",
"Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface."
] | [
1997,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Candidatus Vampirococcus lugosii",
"Eukaryota",
"ecological metagenomes"
] | [
861,
1,
5141,
29
] | 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... | [
21,
1,
3,
1,
3,
4,
1,
8,
2,
1,
1,
24
] | 12 | true | Domain | Transcription initiation factor IIE subunit alpha, N-terminal | Transcription initiation factor IIE subunit alpha, N-terminal | TFIIE_asu | 9 |
IPR002855 | 2,855 | Phosphopantoate/pantothenate synthetase | PPS/PS | Family | 912 | false | false | Proteins in this family include pantothenate synthetase ( ) from Methanosarcina mazei and 4-phosphopantoate--beta-alanine ligase, also known as phosphopantothenate synthetase, ( ) from Pyrococcus kodakaraensis. Pantothenate synthetase catalyses the condensation of pantoate with beta-alanine in an ATP-dependent and ADP-... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM",
"NCBIFAM",
"PFAM",
"PIRSF",
"PANTHER"
] | [
"MF_02224",
"NF010324",
"NF041123",
"PF02006",
"PIRSF004853",
"PTHR40695"
] | [
"PPS",
"PRK13761.1",
"phpantohe_syn_Arch",
"PPS_PS",
"UCP004853",
""
] | [
834,
877,
739,
905,
823,
910
] | 6 | [
"EC",
"METACYC"
] | [
"6.3.2.36",
"PWY-6654"
] | [
"EC:6.3.2.36",
"METACYC:PWY-6654"
] | 2 | [
"3wdk",
"3wdl",
"3wdm",
"4mb0",
"4mb2"
] | 5 | [
"PUB00060435",
"PUB00066834",
"PUB00104918",
"PUB00105931"
] | [
"19666462",
"18422645",
"22940806",
"23200110"
] | [
"Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the Archaea.",
"A novel isoform of pantothenate synthetase in the Archaea.",
"A detailed biochemical characterization of phosphopantothenate synthetase, a novel enzyme involved in coenzyme A biosynthesis in ... | [
2009,
2008,
2012,
2013
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Geodia barretti",
"unclassified sequences"
] | [
851,
25,
1,
35
] | 4 | [] | [] | 0 | true | Family | Phosphopantoate/pantothenate synthetase | Phosphopantoate/pantothenate synthetase | PPS/PS | 6 |
IPR002857 | 2,857 | Zinc finger, CXXC-type | Znf_CXXC | Domain | 17,676 | false | false | Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b... | [
"GO:0003677",
"GO:0008270"
] | [
"DNA binding",
"zinc ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF02008",
"PS51058"
] | [
"zf-CXXC",
"ZF_CXXC"
] | [
16508,
17596
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51058",
"R-BTA-9772755",
"R-DME-9772755",
"R-HSA-212300",
"R-HSA-3214841",
"R-HSA-3214842",
"R-HSA-381038",
"R-HSA-3899300",
"R-HSA-427413",
"R-HSA-4655427",
"R-HSA-5221030",
"R-HSA-5334118",
"R-HSA-5368598",
"R-HSA-8936459",
"R-HSA-8939236",
"R-HSA-8951664",
"R-HSA-9018519",
... | [
"PROSITEDOC:PDOC51058",
"REACTOME:R-BTA-9772755",
"REACTOME:R-DME-9772755",
"REACTOME:R-HSA-212300",
"REACTOME:R-HSA-3214841",
"REACTOME:R-HSA-3214842",
"REACTOME:R-HSA-381038",
"REACTOME:R-HSA-3899300",
"REACTOME:R-HSA-427413",
"REACTOME:R-HSA-4655427",
"REACTOME:R-HSA-5221030",
"REACTOME:R-H... | 39 | [
"2j2s",
"2jyi",
"2kkf",
"3av4",
"3av5",
"3av6",
"3pt6",
"3pta",
"3qmb",
"3qmc",
"3qmd",
"3qmg",
"3qmh",
"3qmi",
"3swr",
"4bbq",
"4d4w",
"4hp1",
"4hp3",
"4nw3",
"4o64",
"4pzi",
"4wxx",
"4yoc",
"4z3c",
"5exh",
"5vc9",
"5w9q",
"5w9s",
"5wy1",
"6asb",
"6asd"... | 38 | [
"PUB00005790",
"PUB00014077",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"9207790",
"12665246",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins.",
"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: get... | [
1997,
2002,
2007,
2005,
2005,
1999,
2001
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Sodalis glossinidius (strain morsitans)"
] | [
17675,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
73,
6,
68,
39,
56
] | 6 | true | Domain | Zinc finger, CXXC-type | Zinc finger, CXXC-type | Znf_CXXC | 6 |
IPR002859 | 2,859 | PKD/REJ-like domain | PKD/REJ-like | Domain | 7,294 | false | false | The REJ (Receptor for Egg Jelly) domain is found in PKD1 and the sperm receptor for egg jelly [ ]. The exact function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridge... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02010"
] | [
"REJ"
] | [
7294
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-5620916",
"R-MMU-5620916"
] | [
"REACTOME:R-HSA-5620916",
"REACTOME:R-MMU-5620916"
] | 2 | [] | 0 | [
"PUB00005842",
"PUB00101153"
] | [
"9949214",
"23762046"
] | [
"Identification of a human homologue of the sea urchin receptor for egg jelly: a polycystic kidney disease-like protein.",
"Analysis of the REJ Module of Polycystin-1 Using Molecular Modeling and Force-Spectroscopy Techniques."
] | [
1999,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Candidatus Nitrosocosmicus arcticus",
"Eukaryota",
"Pseudomonadati",
"ecological metagenomes"
] | [
1,
7266,
25,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
11,
6,
16,
8,
9
] | 6 | true | Domain | PKD/REJ-like domain | PKD/REJ-like domain | PKD/REJ-like | 8 |
IPR002860 | 2,860 | BNR repeat | BNR_rpt | Repeat | 3,440 | false | false | Members of this entry contain multiple BNR (bacterial neuraminidase repeat) repeats or Asp-boxes. The repeats are short, however the repeats are never found closer than 40 residues together suggesting that the repeat is structurally longer. These repeats are found in a variety of non-homologous proteins, including bact... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF02012",
"PF15899"
] | [
"BNR",
"BNR_6"
] | [
3024,
472
] | 2 | [] | [] | [] | 0 | [
"1sqj",
"2cn2",
"2cn3",
"2ebs",
"2jkb",
"2vw0",
"2vw1",
"2vw2",
"3a0f",
"4foq",
"4fov",
"4fow",
"4foy",
"4fp2",
"4fp3",
"4fpc",
"4fpe",
"4fpf",
"4fpg",
"4fph",
"4fpj",
"4fpk",
"4fpl",
"4fpo",
"4fpy",
"4fq4",
"4xe9",
"4xhb",
"4xhx",
"4xik",
"4xil",
"4xio"... | 55 | [
"PUB00014861"
] | [
"11266614"
] | [
"Sialidase-like Asp-boxes: sequence-similar structures within different protein folds."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
108,
3097,
152,
83
] | 4 | [
"Homo sapiens"
] | [
2
] | 1 | true | Repeat | BNR repeat | BNR repeat | BNR_rpt | 2 |
IPR002861 | 2,861 | Reeler domain | Reeler_dom | Domain | 10,896 | false | false | The reeler or reelin domain is a ~170 amino acid module, which has been identified in the amino terminus of the extracellular matrix proteins reelin and F-spondin (renamed Spon1) [ , ]. The reelin domain is found in association with other modules, such as the thrombospondin type I repeat (TSP1), the spondin domain, the... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"CDD"
] | [
"PF02014",
"PS51019",
"cd08544"
] | [
"Reeler",
"REELIN",
"Reeler"
] | [
10402,
9378,
9706
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC51019",
"R-BTA-5173214",
"R-HSA-5083635",
"R-HSA-5173214",
"R-HSA-8866376",
"R-MMU-5173214",
"R-MMU-8866376",
"R-RNO-5173214",
"R-RNO-8866376"
] | [
"PROSITEDOC:PDOC51019",
"REACTOME:R-BTA-5173214",
"REACTOME:R-HSA-5083635",
"REACTOME:R-HSA-5173214",
"REACTOME:R-HSA-8866376",
"REACTOME:R-MMU-5173214",
"REACTOME:R-MMU-8866376",
"REACTOME:R-RNO-5173214",
"REACTOME:R-RNO-8866376"
] | 9 | [
"2zot",
"2zou",
"3coo"
] | 3 | [
"PUB00006213",
"PUB00006387",
"PUB00018463",
"PUB00051075",
"PUB00058327"
] | [
"10409509",
"9338784",
"9441663",
"18602404",
"19020352"
] | [
"F-spondin and mindin: two structurally and functionally related genes expressed in the hippocampus that promote outgrowth of embryonic hippocampal neurons.",
"Scrambler and yotari disrupt the disabled gene and produce a reeler-like phenotype in mice.",
"Mindin/F-spondin family: novel ECM proteins expressed in ... | [
1999,
1997,
1997,
2008,
2008
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5,
111,
10775,
5
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
53,
10,
6,
10,
17
] | 6 | true | Domain | Reeler domain | Reeler domain | Reeler_dom | 5 |
IPR002862 | 2,862 | Domain of unknown function DUF16 | DUF16 | Domain | 94 | false | false | Proteins that contain this domain are of unknown function. It appears to be confined to proteins from Mycoplasma pneumoniae [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01519"
] | [
"DUF16"
] | [
94
] | 1 | [] | [] | [] | 0 | [
"2ba2"
] | 1 | [
"PUB00004470"
] | [
"8948633"
] | [
"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Mycoplasmoides pneumoniae"
] | [
94
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF16 | Domain of unknown function DUF16 | DUF16 | 2 |
IPR002864 | 2,864 | Acyl-ACP thioesterase, N-terminal hotdog domain | Acyl-ACP_thioesterase_NHD | Domain | 9,681 | false | false | This entry represents the N-terminal hotdog domain of various acyl-acyl carrier protein (ACP) thioesterases (TE) which terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid [ ]. These proteins usually contain of a pair of tandem HotDog domains. This entry represents the N-terminal one of th... | [
"GO:0016790",
"GO:0006633"
] | [
"thiolester hydrolase activity",
"fatty acid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01643"
] | [
"Acyl-ACP_TE"
] | [
9681
] | 1 | [
"EC"
] | [
"3.1.2"
] | [
"EC:3.1.2"
] | 1 | [
"2ess",
"2own",
"4gak",
"5x04",
"7hqq",
"7hqr",
"7hqs",
"7hqt",
"7hqu",
"7hqv",
"7hqw",
"7hqx",
"7hqy",
"7hqz",
"7hr0",
"7hr1",
"7hr2",
"7hr3",
"7hr4",
"7hr5",
"7hr6",
"7hr7",
"7hr8",
"7hr9",
"7hra",
"7hrb",
"7hrc",
"7hrd",
"7hre",
"7hrf",
"7hrg",
"7hrh"... | 144 | [
"PUB00004856"
] | [
"7479856"
] | [
"Modification of the substrate specificity of an acyl-acyl carrier protein thioesterase by protein engineering."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4,
5969,
3617,
91
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
10,
16,
65
] | 3 | true | Domain | Acyl-ACP thioesterase, N-terminal hotdog domain | Acyl-ACP thioesterase, N-terminal hotdog domain | Acyl-ACP_thioesterase_NHD | 9 |
IPR002866 | 2,866 | Maturase MatK | Maturase_MatK | Family | 144,413 | false | false | Group II introns are widespread in plant cell organelles [ ]. In vivo, most plant group II introns do not self-splice, but require the assistance of proteinaceous splicing factors, known as maturases. In higher plants, maturases are encoded for in the nuclear genes [ ], but are otherwise encoded by organellar introns. ... | [
"GO:0006397",
"GO:0009507"
] | [
"mRNA processing",
"chloroplast"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"PANTHER"
] | [
"MF_01390",
"PTHR34811"
] | [
"MatK",
""
] | [
50356,
144411
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00043292",
"PUB00043293"
] | [
"16763758",
"12527773"
] | [
"Evolutionary origin of a plant mitochondrial group II intron from a reverse transcriptase/maturase-encoding ancestor.",
"Putative proteins related to group II intron reverse transcriptase/maturases are encoded by nuclear genes in higher plants."
] | [
2006,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unidentified"
] | [
10,
144398,
5
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
14,
7,
3
] | 3 | true | Family | Maturase MatK | Maturase MatK | Maturase_MatK | 6 |
IPR002867 | 2,867 | IBR domain | IBR_dom | Domain | 49,510 | false | false | The IBR (In Between Ring fingers) domain is often found to occur between pairs of ring fingers. This domain has also been called the C6HC domain and DRIL (for double RING finger linked) domain [ ]. Proteins that contain two Ring fingers and an IBR domain (these proteins are also termed RBR family proteins) are thought ... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF01485",
"SM00647"
] | [
"IBR",
"IBR"
] | [
44315,
43916
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.3.2.31",
"R-BTA-1169408",
"R-BTA-9833482",
"R-BTA-9909505",
"R-CEL-1169408",
"R-CEL-983168",
"R-CEL-9833482",
"R-CEL-9909505",
"R-DDI-5675482",
"R-DDI-5689877",
"R-DDI-9646399",
"R-DDI-983168",
"R-DME-1169408",
"R-DME-5205685",
"R-DME-5689877",
"R-DME-9646399",
"R-DME-983168",
"... | [
"EC:2.3.2.31",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-9833482",
"REACTOME:R-BTA-9909505",
"REACTOME:R-CEL-1169408",
"REACTOME:R-CEL-983168",
"REACTOME:R-CEL-9833482",
"REACTOME:R-CEL-9909505",
"REACTOME:R-DDI-5675482",
"REACTOME:R-DDI-5689877",
"REACTOME:R-DDI-9646399",
"REACTOME:R-DDI-9831... | 67 | [
"2ct7",
"2jmo",
"2m48",
"2m9y",
"4bm9",
"4i1f",
"4i1h",
"4k7d",
"4k95",
"4kbl",
"4kc9",
"4zyn",
"5c1z",
"5c23",
"5c9v",
"5caw",
"5edv",
"5n2w",
"5n38",
"5tte",
"5udh",
"6djw",
"6djx",
"6glc",
"6hue",
"6n13",
"6sc5",
"6sc6",
"6sc7",
"6sc8",
"6sc9",
"7b5l"... | 55 | [
"PUB00005861",
"PUB00033665"
] | [
"10422847",
"15152079"
] | [
"TRIADs: a new class of proteins with a novel cysteine-rich signature.",
"Parkin and relatives: the RBR family of ubiquitin ligases."
] | [
1999,
2004
] | 2 | [] | [
"IPR047540",
"IPR047542",
"IPR047548",
"IPR047551",
"IPR047552",
"IPR047555",
"IPR047556",
"IPR047561",
"IPR047564"
] | 0 | 9 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
6,
49481,
16,
7
] | 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... | [
185,
24,
49,
8,
45,
35,
10,
75,
72,
2,
2,
121
] | 12 | true | Domain | IBR domain | IBR domain | IBR_dom | 3 |
IPR002868 | 2,868 | Hepatitis C virus, Non-structural 5a protein | HCV_NS5a | Domain | 18,102 | false | false | Although Hepatitis A virus, Hepatitis B virus, and Hepatitis C virus have similar names, because they all cause liver inflammation, these are distinctly different viruses both genetically and clinically. The Hepatitis C virus (HCV) is a small (50-80 nm in diameter), enveloped, single-stranded, positive sense RNA virus.... | [
"GO:0003968",
"GO:0004197",
"GO:0004252",
"GO:0017111"
] | [
"RNA-directed RNA polymerase activity",
"cysteine-type endopeptidase activity",
"serine-type endopeptidase activity",
"ribonucleoside triphosphate phosphatase activity"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function"
] | 4 | [
"PFAM"
] | [
"PF01506"
] | [
"HCV_NS5a"
] | [
18102
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME"
] | [
"2.7.7.48",
"3.4.21.98",
"3.4.22.-",
"3.6.1.15",
"3.6.4.13",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210",
"R-HSA-5621480",
"R-HSA-8854214"
] | [
"EC:2.7.7.48",
"EC:3.4.21.98",
"EC:3.4.22.-",
"EC:3.6.1.15",
"EC:3.6.4.13",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210",
"REACTOME:R-HSA-5621480",
"REACTOME:R-HSA-8854214"
] | 12 | [
"1r7c",
"1r7d",
"1r7e",
"1r7f",
"1r7g"
] | 5 | [
"PUB00017179",
"PUB00017180",
"PUB00099826",
"PUB00099828",
"PUB00099830",
"PUB00099831",
"PUB00099832"
] | [
"9143277",
"9710605",
"25443344",
"15339921",
"23463199",
"20926572",
"28743875"
] | [
"Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein.",
"Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation.",
"Virology and cell biology of the hepat... | [
1997,
1998,
2014,
2004,
2013,
2010,
2017
] | 7 | [] | [] | 0 | 0 | null | [
"Flaviviridae"
] | [
18102
] | 1 | [] | [] | 0 | true | Domain | Hepatitis C virus, Non-structural 5a protein | Hepatitis C virus, Non-structural 5a protein | HCV_NS5a | 3 |
IPR002869 | 2,869 | Pyruvate-flavodoxin oxidoreductase, central domain | Pyrv_flavodox_OxRed_cen | Homologous_superfamily | 37,393 | false | false | This superfamily represents a domain 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) cata... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.40.920.10",
"SSF53323"
] | [
"",
""
] | [
37321,
36815
] | 2 | [
"EC"
] | [
"1.2.7"
] | [
"EC:1.2.7"
] | 1 | [
"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 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2915,
31119,
2147,
1212
] | 4 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1,
1
] | 4 | true | Homologous_superfamily | Pyruvate-flavodoxin oxidoreductase, central domain | Pyruvate-flavodoxin oxidoreductase, central domain | Pyrv_flavodox_OxRed_cen | 5 |
IPR002870 | 2,870 | Peptidase M12B, propeptide | Peptidase_M12B_N | Domain | 35,128 | false | false | This signature covers the region of the propeptide for members of the MEROPS peptidase family M12B (clan MA(M), adamalysin family). The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins, which mediate cell-cell or cell-matrix interactions. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01562"
] | [
"Pep_M12B_propep"
] | [
35128
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"3.4.24.-",
"PWY-8119",
"R-BTA-1650814",
"R-BTA-5173214",
"R-HSA-1442490",
"R-HSA-1474228",
"R-HSA-1650814",
"R-HSA-177929",
"R-HSA-2534343",
"R-HSA-5083635",
"R-HSA-5173214",
"R-HSA-5682910",
"R-HSA-6798695",
"R-HSA-8941237",
"R-HSA-9762292",
"R-MMU-1474228",
"R-MMU-1650814",
"R-M... | [
"EC:3.4.24.-",
"METACYC:PWY-8119",
"REACTOME:R-BTA-1650814",
"REACTOME:R-BTA-5173214",
"REACTOME:R-HSA-1442490",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-1650814",
"REACTOME:R-HSA-177929",
"REACTOME:R-HSA-2534343",
"REACTOME:R-HSA-5083635",
"REACTOME:R-HSA-5173214",
"REACTOME:R-HSA-5682910",
... | 26 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Escherichia coli",
"Eukaryota"
] | [
1,
35127
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
94,
16,
125,
130,
134
] | 6 | true | Domain | Peptidase M12B, propeptide | Peptidase M12B, propeptide | Peptidase_M12B_N | 4 |
IPR002871 | 2,871 | NIF system FeS cluster assembly, NifU, N-terminal | NIF_FeS_clus_asmbl_NifU_N | Domain | 29,889 | false | false | This entry represents the N-terminal of NifU and homologous proteins. NifU contains two domains: an N-terminal and a C-terminal domain ( ) [ ]. These domains exist either together or on different polypeptides. They can be found in organisms that do not perform nitrogen fixation. Iron-sulphur (FeS) clusters are importan... | [
"GO:0005506",
"GO:0051536",
"GO:0016226"
] | [
"iron ion binding",
"iron-sulfur cluster binding",
"iron-sulfur cluster assembly"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PANTHER",
"CDD"
] | [
"PF01592",
"PTHR10093",
"cd06664"
] | [
"NifU_N",
"",
"IscU_like"
] | [
29122,
25748,
28762
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-1362409",
"R-DME-9865881",
"R-HSA-1362409",
"R-HSA-9694301",
"R-HSA-9854311",
"R-HSA-9865881",
"R-MMU-1362409",
"R-MMU-9854311",
"R-MMU-9865881",
"R-PFA-1362409",
"R-SCE-1362409",
"R-SCE-9865881",
"R-SPO-1362409",
"R-SPO-9865881"
] | [
"REACTOME:R-DME-1362409",
"REACTOME:R-DME-9865881",
"REACTOME:R-HSA-1362409",
"REACTOME:R-HSA-9694301",
"REACTOME:R-HSA-9854311",
"REACTOME:R-HSA-9865881",
"REACTOME:R-MMU-1362409",
"REACTOME:R-MMU-9854311",
"REACTOME:R-MMU-9865881",
"REACTOME:R-PFA-1362409",
"REACTOME:R-SCE-1362409",
"REACTOM... | 14 | [
"1q48",
"1r9p",
"1su0",
"1wfz",
"1xjs",
"2azh",
"2kqk",
"2l4x",
"2qq4",
"2z7e",
"3lvl",
"4eb5",
"4eb7",
"5kz5",
"5t0v",
"5tre",
"5uft",
"5wkp",
"5wlw",
"5xt5",
"5xt6",
"6a6f",
"6a6g",
"6jzv",
"6jzw",
"6nzu",
"6uxe",
"6w1d",
"6wi2",
"6wih",
"7c8m",
"7c8n"... | 48 | [
"PUB00003442",
"PUB00005420",
"PUB00028014",
"PUB00035635",
"PUB00035636",
"PUB00035637",
"PUB00035638",
"PUB00035639",
"PUB00035640"
] | [
"8875867",
"8048161",
"11498000",
"16221578",
"16211402",
"16843540",
"15937904",
"17350000",
"15278785"
] | [
"A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.",
"The modular structure of NifU proteins.",
"Incorporation of iron-sulphur clusters in membrane-bound proteins.",
"How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins.",
"Mechanisms of iron-s... | [
1996,
1994,
2001,
2005,
2005,
2006,
2005,
2007,
2004
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
871,
22696,
5574,
11,
737
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
10,
1,
4,
1,
1,
6,
3,
1,
6,
4,
2,
1,
23
] | 13 | true | Domain | NIF system FeS cluster assembly, NifU, N-terminal | NIF system FeS cluster assembly, NifU, N-terminal | NIF_FeS_clus_asmbl_NifU_N | 6 |
IPR002872 | 2,872 | Proline dehydrogenase domain | Proline_DH_dom | Domain | 30,160 | false | false | The proline oxidase/dehydrogenase is responsible for the first step in the conversion of proline to glutamate for use as a carbon and nitrogen source. The enzyme requires FAD as a cofactor, and is induced by proline. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01619"
] | [
"Pro_dh"
] | [
30160
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.5.5.2",
"GenProp1401",
"PWY-5737",
"PWY-6922",
"R-CEL-389661",
"R-CEL-70688",
"R-DDI-389661",
"R-DDI-70688",
"R-DME-389661",
"R-DME-70688",
"R-HSA-389661",
"R-HSA-70688",
"R-MMU-389661",
"R-MMU-70688",
"R-RNO-389661",
"R-RNO-70688",
"R-SCE-389661",
"R-SCE-70688",
"R-SPO-389661... | [
"EC:1.5.5.2",
"GP:GenProp1401",
"METACYC:PWY-5737",
"METACYC:PWY-6922",
"REACTOME:R-CEL-389661",
"REACTOME:R-CEL-70688",
"REACTOME:R-DDI-389661",
"REACTOME:R-DDI-70688",
"REACTOME:R-DME-389661",
"REACTOME:R-DME-70688",
"REACTOME:R-HSA-389661",
"REACTOME:R-HSA-70688",
"REACTOME:R-MMU-389661",... | 20 | [
"1tiw",
"1tj0",
"1tj1",
"1tj2",
"2ekg",
"2fzm",
"2fzn",
"2g37",
"3e2q",
"3e2r",
"3e2s",
"3haz",
"3itg",
"4h6q",
"4h6r",
"4jny",
"4jnz",
"4nm9",
"4nma",
"4nmb",
"4nmc",
"4nmd",
"4nme",
"4nmf",
"4o8a",
"4q71",
"4q72",
"4q73",
"5kf6",
"5kf7",
"5m42",
"5ur2"... | 79 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
499,
21040,
8331,
5,
285
] | 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,
8,
4,
1,
11,
8,
1,
4,
11,
1,
1,
6
] | 13 | true | Domain | Proline dehydrogenase domain | Proline dehydrogenase domain | Proline_DH_dom | 6 |
IPR002873 | 2,873 | Rotavirus non-structural protein NSP3 | Rotavirus_NSP3 | Family | 2,885 | false | false | This family consists of rotaviral non-structural RNA binding protein 34 (NS34 or NSP3). The NSP3 protein has been shown to bind viral RNA. The NSP3 protein consists of 3 conserved functional domains; a basic region which binds ssRNA, a region containing heptapeptide repeats mediating oligomerisation and a leucine zippe... | [
"GO:0003723"
] | [
"RNA binding"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"HAMAP",
"PFAM"
] | [
"MF_04090",
"MF_04094",
"PF01665"
] | [
"ROTA_NSP3",
"ROTA_A_NSP3",
"Rota_NSP3"
] | [
2710,
2586,
2864
] | 3 | [] | [] | [] | 0 | [
"1knz",
"1lj2"
] | 2 | [
"PUB00005589",
"PUB00005606"
] | [
"1326821",
"7871749"
] | [
"Characterization of an oligomerization domain and RNA-binding properties on rotavirus nonstructural protein NS34.",
"Comparative nucleotide and amino acid sequence analysis of the sequence-specific RNA-binding rotavirus nonstructural protein NSP3."
] | [
1992,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Rotavirus"
] | [
2885
] | 1 | [] | [] | 0 | true | Family | Rotavirus non-structural protein NSP3 | Rotavirus non-structural protein NSP3 | Rotavirus_NSP3 | 7 |
IPR002874 | 2,874 | Alphaherpesvirus glycoprotein I | Herpes_gI | Family | 403 | false | false | This family consists of glycoprotein I from various members of the alphaherpesvirinae. These include Human herpesvirus 1 (HHV-1), Human herpesvirus 3 (HHV-3) and Suid herpesvirus 1 (Pseudorabies virus). Glycoprotein I (gI) is important during natural infection, mutants lacking gI produce smaller lesions at the site of ... | [
"GO:0043657"
] | [
"host cell"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF01688"
] | [
"Herpes_gI"
] | [
403
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00003155",
"PUB00003523"
] | [
"8207390",
"8764058"
] | [
"Identification of the feline herpesvirus type 1 (FHV-1) genes encoding glycoproteins G, D, I and E: expression of FHV-1 glycoprotein D in vaccinia and raccoon poxviruses.",
"Biosynthesis of glycoproteins E and I of feline herpesvirus: gE-gI interaction is required for intracellular transport."
] | [
1994,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Alphaherpesvirinae"
] | [
403
] | 1 | [] | [] | 0 | true | Family | Alphaherpesvirus glycoprotein I | Alphaherpesvirus glycoprotein I | Herpes_gI | 4 |
IPR002876 | 2,876 | Transcriptional regulator TACO1-like | Transcrip_reg_TACO1-like | Family | 33,469 | false | false | This is a family of transcriptional regulators. In mammals, TACO1 ( ) activates the transcription of mitochondrially-encoded cytochrome c oxidase (COX1). Defects in TACO1 are a cause of Leigh syndrome (LS). LS is a severe neurological disorder characterised by bilaterally symmetrical necrotic lesions in subcortical bra... | [] | [] | [] | 0 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_00693",
"PTHR12532",
"TIGR01033"
] | [
"Transcrip_reg_TACO1",
"",
""
] | [
28837,
33447,
24924
] | 3 | [
"REACTOME"
] | [
"R-HSA-9864848"
] | [
"REACTOME:R-HSA-9864848"
] | 1 | [
"1kon",
"1lfp",
"1mw7",
"4f3q",
"5ekz"
] | 5 | [
"PUB00057436",
"PUB00057437"
] | [
"19503089",
"18641136"
] | [
"Mutation in TACO1, encoding a translational activator of COX I, results in cytochrome c oxidase deficiency and late-onset Leigh syndrome.",
"The YebC family protein PA0964 negatively regulates the Pseudomonas aeruginosa quinolone signal system and pyocyanin production."
] | [
2009,
2008
] | 2 | [] | [
"IPR026562"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctREU2",
"unclassified sequences",
"uncultured marine group II/III euryarchaeote KM3_86_F07"
] | [
29068,
3740,
1,
659,
1
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
4,
1,
3,
5,
2,
3,
2,
1,
2,
2,
1,
1,
12
] | 13 | true | Family | Transcriptional regulator TACO1-like | Transcriptional regulator TACO1-like | Transcrip_reg_TACO1-like | 8 |
IPR002877 | 2,877 | Ribosomal RNA methyltransferase, FtsJ domain | RNA_MeTrfase_FtsJ_dom | Domain | 63,303 | false | false | This entry represents FtsJ domain, which is found in proteins that methylate RNA, including Ribosomal RNA large subunit methyltransferase E (formerly known as RrmJ or FtsJ). RrmJ is a well conserved heat shock protein with close homologs in prokaryotes, archaea, and eukaryotes. RrmJ is responsible for methylating 23 S ... | [
"GO:0008168",
"GO:0032259"
] | [
"methyltransferase activity",
"methylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01728"
] | [
"FtsJ"
] | [
63303
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1",
"R-HSA-6782315",
"R-HSA-6791226",
"R-HSA-6793080",
"R-MMU-6791226",
"R-RNO-6791226"
] | [
"EC:2.1.1",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-6791226",
"REACTOME:R-HSA-6793080",
"REACTOME:R-MMU-6791226",
"REACTOME:R-RNO-6791226"
] | 6 | [
"1eiz",
"1ej0",
"1l9k",
"1r6a",
"2nyu",
"2oxt",
"2oy0",
"2p1d",
"2p3l",
"2p3o",
"2p3q",
"2p40",
"2p41",
"2plw",
"2px2",
"2px4",
"2px5",
"2px8",
"2pxa",
"2pxc",
"2wa1",
"2wa2",
"2xbm",
"3dou",
"3eld",
"3elu",
"3elw",
"3ely",
"3emb",
"3emd",
"3eva",
"3evb"... | 193 | [
"PUB00007205",
"PUB00011786",
"PUB00058135",
"PUB00100386",
"PUB00100387",
"PUB00100388"
] | [
"10983982",
"11976298",
"20713356",
"24595062",
"15375145",
"32134554"
] | [
"RNA methylation under heat shock control.",
"Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase.",
"Characterization of hMTr1, a human Cap1 2'-O-ribose methyltransferase.",
"FTSJ2, a heat shock-inducible mitochondrial protein, suppresses cell invasion and... | [
2000,
2002,
2010,
2014,
2004,
2020
] | 6 | [] | [
"IPR025807",
"IPR025816",
"IPR026490"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
837,
29650,
20172,
11853,
791
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
25,
8,
11,
10,
2,
20,
9,
4,
14,
21,
3,
4,
32
] | 13 | true | Domain | Ribosomal RNA methyltransferase, FtsJ domain | Ribosomal RNA methyltransferase, FtsJ domain | RNA_MeTrfase_FtsJ_dom | 3 |
IPR002878 | 2,878 | ChsH2, C-terminal OB-fold domain | ChsH2_C | Domain | 19,022 | false | false | This domain is found at the C-terminal end of the probable enoyl-CoA hydratase alpha subunit from Thermomonospora curvata (ChsH2) and similar archaeal and bacterial proteins. ChsH2 is likely to be involved in bile acid degradation. The C-terminal region of this protein is organised into two domains: an N-terminal zinc ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01796"
] | [
"OB_ChsH2_C"
] | [
19022
] | 1 | [] | [] | [] | 0 | [
"3irb",
"5m3k",
"5mg5",
"6esq",
"6et9",
"6ok1",
"7pxp",
"7pyt",
"7yxm",
"9myr"
] | 10 | [
"PUB00070339",
"PUB00097287",
"PUB00154875",
"PUB00154876",
"PUB00154877",
"PUB00154878",
"PUB00155451",
"PUB00155452"
] | [
"23793631",
"20944206",
"22045806",
"25203216",
"31568719",
"29531083",
"31209106",
"35313080"
] | [
"Haloarchaeal-type β-ketothiolases involved in Poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthesis in Haloferax mediterranei.",
"The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role.",
"Pa... | [
2013,
2010,
2011,
2014,
2019,
2018,
2019,
2022
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1756,
16684,
22,
560
] | 4 | [] | [] | 0 | true | Domain | ChsH2, C-terminal OB-fold domain | ChsH2, C-terminal OB-fold domain | ChsH2_C | 6 |
IPR002880 | 2,880 | Pyruvate flavodoxin/ferredoxin oxidoreductase, pyrimidine binding domain | Pyrv_Fd/Flavodoxin_OxRdtase_N | Domain | 37,150 | false | false | This entry represents the N-terminal region of the pyruvate ferredoxin oxidoreductase, corresponding to the first two structural domains. This region is involved in inter subunit contacts [ ]. Pyruvate oxidoreductase (POR) catalyses the final step in the fermentation of carbohydrates in anaerobic microorganisms [ ]. Th... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"CDD"
] | [
"PF01855",
"cd07034"
] | [
"POR_N",
"TPP_PYR_PFOR_IOR-alpha_like"
] | [
29792,
36299
] | 2 | [
"EC",
"GP"
] | [
"1.2.7",
"GenProp0839"
] | [
"EC:1.2.7",
"GP:GenProp0839"
] | 2 | [
"1b0p",
"1kek",
"1yd7",
"2c3m",
"2c3o",
"2c3p",
"2c3u",
"2c3y",
"2c42",
"2pda",
"2uza",
"4wbx",
"5b46",
"5b47",
"5b48",
"5c4i",
"5exd",
"5exe",
"6cin",
"6cio",
"6cip",
"6ciq",
"6n2n",
"6n2o",
"7plm",
"8ys5",
"8ys6",
"9bt4"
] | 28 | [
"PUB00002295",
"PUB00004826",
"PUB00005843",
"PUB00097744"
] | [
"8550425",
"8415612",
"10048931",
"11023353"
] | [
"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.",
"Crystal st... | [
1996,
1993,
1999,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3141,
31007,
1827,
1175
] | 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 flavodoxin/ferredoxin oxidoreductase, pyrimidine binding domain | Pyruvate flavodoxin/ferredoxin oxidoreductase, pyrimidine binding domain | Pyrv_Fd/Flavodoxin_OxRdtase_N | 5 |
IPR002881 | 2,881 | Domain of unknown function DUF58 | DUF58 | Domain | 38,643 | false | false | This domain is found in a family of prokaryotic proteins that have no known function. Proteins belonging to this family include hypothetical proteins from eubacteria and archaebacteria. Some of these proteins also contain the Von Willebrand factor, type A domain (see ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01882"
] | [
"DUF58"
] | [
38643
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1702,
36324,
44,
2,
571
] | 5 | [] | [] | 0 | true | Domain | Domain of unknown function DUF58 | Domain of unknown function DUF58 | DUF58 | 2 |
IPR002882 | 2,882 | 2-phospho-L-lactate transferase CofD | CofD | Family | 19,611 | false | false | This entry contains 2-phospho-L-lactate transferase (CofD), phosphoenolpyruvate transferase and related sequences. CofD catalyses the fourth step in the biosynthesis of coenzyme F420, which is the transfer of the 2-phospholactate moiety from lactyl (2) diphospho-(5') guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deaza... | [
"GO:0043743"
] | [
"LPPG:FO 2-phospho-L-lactate transferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01933"
] | [
"CofD"
] | [
19611
] | 1 | [] | [] | [] | 0 | [
"2hzb",
"2o2z",
"2p0y",
"2ppv",
"2q7x",
"3c3d",
"3c3e",
"3cgw",
"6uvx",
"6uw1",
"6uw3",
"6uw5",
"6uw7"
] | 13 | [
"PUB00013496",
"PUB00050875"
] | [
"11888293",
"18252724"
] | [
"Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F(420) biosynthesis in Methanococcus jannaschii.",
"Molecular insights into the biosynthesis of the F420 coenzyme."
] | [
2002,
2008
] | 2 | [] | [
"IPR010115",
"IPR010119",
"IPR027591"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Streptococcus phage MM1",
"unclassified sequences"
] | [
733,
16039,
2445,
1,
393
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
8,
1,
1,
6,
1,
13
] | 6 | true | Family | 2-phospho-L-lactate transferase CofD | 2-phospho-L-lactate transferase CofD | CofD | 5 |
IPR002883 | 2,883 | CBM10/dockerin domain | CBM10/Dockerin_dom | Domain | 1,325 | false | false | Plant cell wall hydrolases generally have a modular structure consisting of a catalytic domain linked to one or more noncatalytic carbohydrate-binding modules (CBMs). The majority of these CBMs interact with cellulose and are thus referred to as cellulose-binding domains or CBDs. CBM10s are small molecules, comprising ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF02013",
"PS51763"
] | [
"CBM_10",
"CBM10"
] | [
1273,
1323
] | 2 | [
"EC"
] | [
"3.2.1"
] | [
"EC:3.2.1"
] | 1 | [
"1e8p",
"1e8q",
"1e8r",
"1qld",
"2j4m",
"2j4n"
] | 6 | [
"PUB00005749",
"PUB00006338",
"PUB00010608",
"PUB00011754",
"PUB00077758"
] | [
"7492333",
"7493964",
"11524680",
"10653641",
"10653642"
] | [
"Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus.",
"The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a pr... | [
1995,
1995,
2001,
2000,
2000
] | 5 | [] | [
"IPR009031"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota"
] | [
286,
1039
] | 2 | [] | [] | 0 | true | Domain | CBM10/dockerin domain | CBM10/dockerin domain | CBM10/Dockerin_dom | 8 |
IPR002884 | 2,884 | P domain | P_dom | Domain | 24,699 | false | false | In eukaryotes, many essential secreted proteins and peptide hormones are excised from larger precursors by members of a class of calcium-dependent endoproteinases, the prohormone-proprotein convertases (PCs).The P (known as such because it is essential for proteolytic activity), or Homo B, domain of ~150 residues is a ... | [
"GO:0004252",
"GO:0006508"
] | [
"serine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF01483",
"PS51829"
] | [
"P_proprotein",
"P_HOMO_B"
] | [
24144,
24557
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.21",
"R-CEL-1592389",
"R-CEL-186797",
"R-CEL-2173789",
"R-CEL-2173796",
"R-DME-1592389",
"R-DME-186797",
"R-DME-2173789",
"R-DME-2173796",
"R-DME-8963889",
"R-DME-9768727",
"R-HSA-1181150",
"R-HSA-1442490",
"R-HSA-1566948",
"R-HSA-1592389",
"R-HSA-159782",
"R-HSA-167060",
"R-H... | [
"EC:3.4.21",
"REACTOME:R-CEL-1592389",
"REACTOME:R-CEL-186797",
"REACTOME:R-CEL-2173789",
"REACTOME:R-CEL-2173796",
"REACTOME:R-DME-1592389",
"REACTOME:R-DME-186797",
"REACTOME:R-DME-2173789",
"REACTOME:R-DME-2173796",
"REACTOME:R-DME-8963889",
"REACTOME:R-DME-9768727",
"REACTOME:R-HSA-1181150... | 65 | [
"1ot5",
"1p8j",
"1r64",
"2id4",
"3hjr",
"3wqb",
"4omc",
"4omd",
"4ryd",
"4z2a",
"5jmo",
"5jxg",
"5jxh",
"5jxi",
"5jxj",
"5mim",
"6eqv",
"6eqw",
"6eqx",
"6hlb",
"6hld",
"6hle",
"6hza",
"6hzb",
"6hzc",
"6hzd",
"6yd2",
"6yd3",
"6yd4",
"6yd7",
"7lcu",
"7o1u"... | 47 | [
"PUB00003014",
"PUB00006382",
"PUB00006441",
"PUB00014208",
"PUB00029766",
"PUB00053054",
"PUB00087110"
] | [
"9556596",
"9307023",
"10212221",
"10842308",
"12794637",
"19654332",
"9636145"
] | [
"Regulatory roles of the P domain of the subtilisin-like prohormone convertases.",
"The integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking.",
"The RGD motif and the C-terminal segment of proprotein convertase 1 ... | [
1998,
1997,
1999,
2000,
2003,
2009,
1998
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Heunggongvirae",
"unclassified sequences"
] | [
26,
8779,
15821,
7,
66
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
4,
21,
8,
27,
18,
1,
29,
1,
1
] | 9 | true | Domain | P domain | P domain | P_dom | 9 |
IPR002885 | 2,885 | Pentatricopeptide repeat | PPR_rpt | Repeat | 325,261 | false | false | This entry represents the PPR repeat. Pentatricopeptide repeat (PPR) proteins are characterised by tandem repeats of a degenerate 35 amino acid motif [ ]. PPR proteins are sequence-specific RNA-binding proteins that are involved in multiple aspects of RNA metabolism [ , ]. They can bind a diversity of sequences that co... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROFILE",
"NCBIFAM"
] | [
"PF01535",
"PF12854",
"PF13041",
"PF13812",
"PS51375",
"TIGR00756"
] | [
"PPR",
"PPR_1",
"PPR_2",
"PPR_3",
"PPR",
"PPR"
] | [
257623,
69170,
257455,
60181,
310008,
299962
] | 6 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-DME-5389840",
"R-DME-5419276",
"R-DME-9937383",
"R-DRE-5389840",
"R-DRE-5419276",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-8876198",
"R-HSA-9836573",
"R-HSA-9937008",
"R-HSA-9937383",
"R-MMU-163282",
"R-MMU-538984... | [
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-DME-5389840",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-9937383",
"REACTOME:R-DRE-5389840",
"REACTOME:R-DRE-5419276",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOM... | 21 | [
"3j9m",
"3jd5",
"4g23",
"4g24",
"4g25",
"4g26",
"4leu",
"4m57",
"4m59",
"4oe1",
"4ozs",
"4pjq",
"4pjr",
"4pjs",
"4wn4",
"4wsl",
"5i9d",
"5i9f",
"5i9g",
"5i9h",
"5iwb",
"5iww",
"5izw",
"5orm",
"5orq",
"6bv5",
"6bv6",
"6bv8",
"6bv9",
"6een",
"6gaw",
"6gaz"... | 132 | [
"PUB00015445",
"PUB00015446",
"PUB00017589",
"PUB00043700",
"PUB00043701",
"PUB00043702",
"PUB00043703",
"PUB00090551",
"PUB00090552",
"PUB00094369"
] | [
"15270678",
"15269332",
"10664580",
"12782738",
"12832482",
"18031283",
"17560114",
"24162847",
"22576772",
"30125002"
] | [
"Chloroplast RNA-binding and pentatricopeptide repeat proteins.",
"Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesis.",
"The PPR motif - a TPR-related motif prevalent in plant organellar proteins.",
"HCF152, an Arabidopsis RNA binding pe... | [
2004,
2004,
2000,
2003,
2003,
2007,
2007,
2013,
2012,
2018
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes",
"unclassified dsDNA viruses"
] | [
9,
629,
324596,
22,
5
] | 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... | [
2145,
10,
25,
10,
55,
19,
6,
1503,
29,
4,
6,
1752
] | 12 | true | Repeat | Pentatricopeptide repeat | Pentatricopeptide repeat | PPR_rpt | 6 |
IPR002888 | 2,888 | [2Fe-2S]-binding | 2Fe-2S-bd | Domain | 62,857 | false | false | The [2Fe-2S] binding domain is found in a range of enzymes including dehydrogenases, oxidases and oxidoreductases. The aldehyde oxido-reductase (Mop) from the sulphate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas is a homodimer of 907 amino acid residues subunits and is a member of the xanthine oxidas... | [
"GO:0016491",
"GO:0046872"
] | [
"oxidoreductase activity",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF01799"
] | [
"Fer2_2"
] | [
62857
] | 1 | [
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1236",
"GenProp1255",
"GenProp1469",
"GenProp1753",
"R-CEL-964975",
"R-DDI-74259",
"R-DDI-964975",
"R-DDI-9748787",
"R-DME-74259",
"R-DME-964975",
"R-DME-9748787",
"R-GGA-421178",
"R-HSA-74259",
"R-HSA-8851680",
"R-HSA-964975",
"R-HSA-9748787",
"R-MMU-74259",
"R-MMU-8851680... | [
"GP:GenProp1236",
"GP:GenProp1255",
"GP:GenProp1469",
"GP:GenProp1753",
"REACTOME:R-CEL-964975",
"REACTOME:R-DDI-74259",
"REACTOME:R-DDI-964975",
"REACTOME:R-DDI-9748787",
"REACTOME:R-DME-74259",
"REACTOME:R-DME-964975",
"REACTOME:R-DME-9748787",
"REACTOME:R-GGA-421178",
"REACTOME:R-HSA-7425... | 24 | [
"1dgj",
"1ffu",
"1ffv",
"1fiq",
"1fo4",
"1jro",
"1jrp",
"1n5w",
"1n5x",
"1n60",
"1n61",
"1n62",
"1n63",
"1rm6",
"1sb3",
"1sij",
"1t3q",
"1v97",
"1vdv",
"1vlb",
"1wyg",
"1zxi",
"2ckj",
"2e1q",
"2e3t",
"2w3r",
"2w3s",
"2w54",
"2w55",
"3am9",
"3amz",
"3an1"... | 86 | [
"PUB00005209"
] | [
"7502041"
] | [
"Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
582,
49314,
12047,
914
] | 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",... | [
38,
3,
4,
7,
3,
6,
18,
1,
18,
23,
67
] | 11 | true | Domain | [2Fe-2S]-binding | [2Fe-2S]-binding | 2Fe-2S-bd | 6 |
IPR002889 | 2,889 | Carbohydrate-binding WSC | WSC_carb-bd | Domain | 23,072 | false | false | The WSC domain is a putative carbohydrate binding domain. The domain contains up to eight conserved cysteine residues that may be involved in disulphide bridges [ ]. The Trichoderma harzianum beta-1,3 exoglucanase contains two copies of the WSC domain, while the yeast SLG1 protein contains only one. This domain folds a... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01822",
"PS51212",
"SM00321"
] | [
"WSC",
"WSC",
"WSC"
] | [
21001,
22515,
19791
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC51212",
"R-CEL-1971475",
"R-DME-114604",
"R-DME-1971475",
"R-DME-354192",
"R-DME-5621480",
"R-DME-9013407",
"R-DME-912631",
"R-DME-9674555",
"R-DME-9705462",
"R-HSA-201681",
"R-HSA-3772470",
"R-HSA-5339717",
"R-HSA-5620916",
"R-MMU-3772470",
"R-MMU-5620916",
"R-RNO-3772470"
] | [
"PROSITEDOC:PDOC51212",
"REACTOME:R-CEL-1971475",
"REACTOME:R-DME-114604",
"REACTOME:R-DME-1971475",
"REACTOME:R-DME-354192",
"REACTOME:R-DME-5621480",
"REACTOME:R-DME-9013407",
"REACTOME:R-DME-912631",
"REACTOME:R-DME-9674555",
"REACTOME:R-DME-9705462",
"REACTOME:R-HSA-201681",
"REACTOME:R-HS... | 17 | [
"5fws",
"5fwt",
"5fwu",
"5fwv",
"5fww",
"6snw",
"7bzt",
"7bzu",
"7pz2"
] | 9 | [
"PUB00008017",
"PUB00102533"
] | [
"10469603",
"27524201"
] | [
"A latrophilin/CL-1-like GPS domain in polycystin-1.",
"Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf."
] | [
1999,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Clandestinovirus",
"Eukaryota",
"Pseudomonadati",
"metagenomes"
] | [
1,
23045,
19,
7
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
1,
13,
3,
10,
7,
14,
15,
4,
1
] | 9 | true | Domain | Carbohydrate-binding WSC | Carbohydrate-binding WSC | WSC_carb-bd | 5 |
IPR002890 | 2,890 | Macroglobulin domain | MG2 | Domain | 27,922 | false | false | The proteinase-binding alpha-macroglobulins (A2M) [ ] are large glycoproteins found in the plasma of vertebrates, in the hemolymph of some invertebrates and in reptilian and avian egg white. A2M-like proteins are able to inhibit all four classes of proteinases by a 'trapping' mechanism. They have a peptide stretch, cal... | [
"GO:0004866"
] | [
"endopeptidase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01835"
] | [
"MG2"
] | [
27922
] | 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-166665",
"R-HSA-173736",
"R-HSA-174577",
"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... | 57 | [
"2a73",
"2a74",
"2i07",
"2ice",
"2icf",
"2p9r",
"2pn5",
"2qki",
"2wii",
"2win",
"2xwb",
"2xwj",
"3cu7",
"3frp",
"3g6j",
"3hrz",
"3hs0",
"3kls",
"3km9",
"3l3o",
"3l5n",
"3nms",
"3ohx",
"3prx",
"3pvm",
"3t4a",
"4a5w",
"4d94",
"4e0s",
"4lnv",
"4rtd",
"4u48"... | 109 | [
"PUB00002498",
"PUB00039169",
"PUB00059352",
"PUB00091001",
"PUB00100415"
] | [
"2473064",
"16177781",
"22290936",
"25221932",
"34970276"
] | [
"Alpha-macroglobulins: structure, shape, and mechanism of proteinase complex formation.",
"Structures of complement component C3 provide insights into the function and evolution of immunity.",
"The Crystal Structure of Human α(2) -Macroglobulin Reveals a Unique Molecular Cage.",
"Structure of a bacterial α2-m... | [
1989,
2005,
2012,
2014,
2021
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Myoviridae sp. ctTrm2",
"metagenomes"
] | [
38,
12463,
15308,
1,
112
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
57,
69,
2,
32,
32,
51
] | 7 | true | Domain | Macroglobulin domain | Macroglobulin domain | MG2 | 7 |
IPR002891 | 2,891 | APS kinase | APS | Family | 25,200 | false | false | Adenylylsulphate kinase ( ) catalyses the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulphate. It is often found as a fusion protein with sulphate adenylyltransferase. Both enzymes are required for PAPS (phosphoadenosine-phosphosulphate) synthesis from inorganic sulphate [ ]. | [
"GO:0004020",
"GO:0005524",
"GO:0000103"
] | [
"adenylylsulfate kinase activity",
"ATP binding",
"sulfate assimilation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00065",
"TIGR00455"
] | [
"Adenylyl_sulf_kinase",
"apsK"
] | [
21953,
25067
] | 2 | [
"EC",
"GP",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.25",
"GenProp1283",
"GenProp1573",
"PWY-5340",
"R-CEL-174362",
"R-HSA-174362",
"R-HSA-2408550",
"R-HSA-3560796",
"R-HSA-6802952",
"R-MMU-174362",
"R-MTU-936635",
"R-SCE-174362",
"R-SPO-174362"
] | [
"EC:2.7.1.25",
"GP:GenProp1283",
"GP:GenProp1573",
"METACYC:PWY-5340",
"REACTOME:R-CEL-174362",
"REACTOME:R-HSA-174362",
"REACTOME:R-HSA-2408550",
"REACTOME:R-HSA-3560796",
"REACTOME:R-HSA-6802952",
"REACTOME:R-MMU-174362",
"REACTOME:R-MTU-936635",
"REACTOME:R-SCE-174362",
"REACTOME:R-SPO-17... | 13 | [
"1d6j",
"1i2d",
"1m7g",
"1m7h",
"1m8p",
"1x6v",
"1xjq",
"1xnj",
"2ax4",
"2gks",
"2ofw",
"2ofx",
"2pey",
"2pez",
"2yvu",
"3cr7",
"3cr8",
"3uie",
"4bzp",
"4bzq",
"4bzx",
"4fxp",
"4rfv",
"5cb6",
"5cb8",
"6b8v",
"6c6b",
"7yq0",
"7yq1",
"8a8h",
"8i1m",
"8i1n"... | 33 | [
"PUB00001859"
] | [
"8522184"
] | [
"A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
142,
15782,
8975,
11,
290
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
15,
1,
4,
5,
1,
5,
7,
2,
7,
5,
1,
1,
31
] | 13 | true | Family | APS kinase | APS kinase | APS | 4 |
IPR002895 | 2,895 | Paramecium surface antigen | Paramecium_SA | Repeat | 671 | false | false | The G surface protein of Paramecium primaurelia has important internal homologies and a periodic structure, which could be dictated in part by the rigid scaffolding of cysteine residues. The predicted secondary structure shows a quasi absence of α-helix and an abundance of β-pleated sheets and random coils. The monoton... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF01508",
"SM00639"
] | [
"Paramecium_SA",
"PSA"
] | [
628,
612
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00003212",
"PUB00006245"
] | [
"3783679",
"2308165"
] | [
"Nucleotide sequence of the Paramecium primaurelia G surface protein. A huge protein with a highly periodic structure.",
"Conserved sequences flank variable tandem repeats in two alleles of the G surface protein of Paramecium primaurelia."
] | [
1986,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Legionella shakespearei DSM 23087"
] | [
670,
1
] | 2 | [] | [] | 0 | true | Repeat | Paramecium surface antigen | Paramecium surface antigen | Paramecium_SA | 4 |
IPR002900 | 2,900 | Domain of unknown function DUF38/FTH, Caenorhabditis species | DUF38/FTH_CAE_spp | Domain | 2,950 | false | false | This domain with no known function is presumed to be a protein-protein interaction module specific to proteins from several Caenorhabditis species. It is named FTH after FOG-2 homology domain [ ]. The domain is found associated with, and C-terminal to, the cyclin-like F-box . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01827"
] | [
"FTH"
] | [
2950
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00101027"
] | [
"15630478"
] | [
"fog-2 and the evolution of self-fertile hermaphroditism in Caenorhabditis."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Caenorhabditis"
] | [
2950
] | 1 | [
"Caenorhabditis elegans"
] | [
235
] | 1 | true | Domain | Domain of unknown function DUF38/FTH, Caenorhabditis species | Domain of unknown function DUF38/FTH, Caenorhabditis species | DUF38/FTH_CAE_spp | 2 |
IPR002901 | 2,901 | Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain | MGlyc_endo_b_GlcNAc-like_dom | Domain | 24,285 | false | false | This domain is found in many different proteins including mannosyl-glycoprotein endo-beta-N-acetylglucosamidase ( ). It is also found in flagellar protein J ( ), which has been shown to hydrolyse peptidoglycan [ ]. | [
"GO:0004040"
] | [
"amidase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF01832",
"SM00047"
] | [
"Glucosaminidase",
"LYZ2"
] | [
24136,
19966
] | 2 | [
"EC"
] | [
"3.2.1"
] | [
"EC:3.2.1"
] | 1 | [
"2zyc",
"3fi7",
"3k3t",
"3vwo",
"4kt3",
"4pi7",
"4pi8",
"4pi9",
"4pia",
"4q2w",
"4qdn",
"5dn4",
"5dn5",
"5t1q",
"5wqw",
"6fxo",
"6fxp",
"6u0o",
"7pj3",
"7pj4",
"7pj5",
"7pj6",
"7pl3",
"7pod",
"7qfu",
"8yxk",
"8yxn"
] | 27 | [
"PUB00005848"
] | [
"10049388"
] | [
"Peptidoglycan-hydrolyzing activity of the FlgJ protein, essential for flagellar rod formation in Salmonella typhimurium."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"unclassified sequences"
] | [
23620,
27,
14,
407,
217
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
2
] | 2 | true | Domain | Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain | Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain | MGlyc_endo_b_GlcNAc-like_dom | 1 |
IPR002902 | 2,902 | Gnk2-homologous domain | GNK2 | Domain | 32,297 | false | false | Ginkbilobin-2 (Gnk2) is an antifungal protein found in the endosperm of Ginkgo seeds, which inhibits the growth of phytopathogenic fungi such as Fusarium oxysporum. Gnk2 has considerable homology (~85%) to embryo-abundant proteins (EAP) from the gymnosperms Picea abies and P. glauca. Plant EAP are expressed in the late... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF01657",
"PS51473"
] | [
"Stress-antifung",
"GNK2"
] | [
31683,
32130
] | 2 | [] | [] | [] | 0 | [
"3a2e",
"4xre",
"6gre",
"6grf"
] | 4 | [
"PUB00052808",
"PUB00057421"
] | [
"19603485",
"11402176"
] | [
"Crystal structure of ginkbilobin-2 with homology to the extracellular domain of plant cysteine-rich receptor-like kinases.",
"A superfamily of proteins with novel cysteine-rich repeats."
] | [
2009,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Actinoallomurus vinaceus",
"Eukaryota",
"Halococcus"
] | [
1,
32294,
2
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
449,
259,
184
] | 3 | true | Domain | Gnk2-homologous domain | Gnk2-homologous domain | GNK2 | 4 |
IPR002903 | 2,903 | Ribosomal RNA small subunit methyltransferase H | RsmH | Family | 30,489 | false | false | RsmH (previously known as MraW) is a methyltransferase responsible for one of the two methylations (N4-methylation) of C1402 in Escherichia coli 16S rRNA. The N4, 2'-O-dimethylcytidine (m4Cm) at position 1402 of the 16S rRNA directly interacts with the P-site codon of the mRNA. These conserved methyl-modifications may ... | [
"GO:0008168"
] | [
"methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM",
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"MF_01007",
"PF01795",
"PIRSF004486",
"PTHR11265",
"TIGR00006"
] | [
"16SrRNA_methyltr_H",
"Methyltransf_5",
"MraW",
"",
""
] | [
28752,
30482,
26843,
30315,
29330
] | 5 | [
"EC",
"GP",
"GP"
] | [
"2.1.1.199",
"GenProp0802",
"GenProp1082"
] | [
"EC:2.1.1.199",
"GP:GenProp0802",
"GP:GenProp1082"
] | 3 | [
"1m6y",
"1n2x",
"1wg8",
"3tka",
"6sg9",
"6sga",
"6sgb",
"7pnv",
"7pnx",
"7pny",
"7pnz",
"8ipi",
"8ipk",
"8ipl",
"8ipm",
"8qrl",
"9g5c",
"9g5d",
"9hny"
] | 19 | [
"PUB00054204"
] | [
"19965768"
] | [
"Fine-tuning of the ribosomal decoding center by conserved methyl-modifications in the Escherichia coli 16S rRNA."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences",
"uncultured marine group II/III euryarchaeote KM3_94_C01"
] | [
26690,
3088,
1,
709,
1
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
5,
13,
1,
1,
3,
2,
3,
3,
5
] | 9 | true | Family | Ribosomal RNA small subunit methyltransferase H | Ribosomal RNA small subunit methyltransferase H | RsmH | 4 |
IPR002904 | 2,904 | Lysine-tRNA ligase | Lys-tRNA-ligase | Family | 5,850 | false | false | Lysine-tRNA ligase (also known as Lysyl-tRNA synthetase) ( ) is an alpha 2 homodimer that belong to both class I and class II. In eubacteria and eukaryota lysine-tRNA ligases belong to class II in the same family as aspartyl tRNA ligase. The class Ic lysine-tRNA ligase family is present in archaea and in a number of ba... | [
"GO:0000166",
"GO:0004824",
"GO:0005524",
"GO:0006430",
"GO:0005737"
] | [
"nucleotide binding",
"lysine-tRNA ligase activity",
"ATP binding",
"lysyl-tRNA aminoacylation",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00177",
"PF01921",
"PTHR37940",
"TIGR00467"
] | [
"Lys_tRNA_synth_class1",
"tRNA-synt_1f",
"",
"lysS_arch"
] | [
5423,
5801,
5788,
5103
] | 4 | [
"EC",
"GP"
] | [
"6.1.1.6",
"GenProp0258"
] | [
"EC:6.1.1.6",
"GP:GenProp0258"
] | 2 | [
"1irx"
] | 1 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00005800",
"PUB00006477",
"PUB00006540",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"9353192",
"10673435",
"10913247",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
1997,
2000,
2000,
1990,
1999,
2000,
2002
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Halogranum tailed virus 1",
"unclassified sequences"
] | [
838,
4842,
26,
1,
143
] | 5 | [] | [] | 0 | true | Family | Lysine-tRNA ligase | Lysine-tRNA ligase | Lys-tRNA-ligase | 4 |
IPR002905 | 2,905 | tRNA methyltransferase, Trm1 | Trm1 | Family | 8,854 | false | false | Trm1 ( ) dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups [ , ]. In Saccharomyces cerevisiae, Trm1 is required for the modification of both mitochondrial and cytoplasmic tRNAs [ ]. This family also includes the related TRMT1-like prote... | [
"GO:0003723",
"GO:0016423",
"GO:0008033"
] | [
"RNA binding",
"tRNA (guanine) methyltransferase activity",
"tRNA processing"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PROFILE",
"PANTHER",
"NCBIFAM"
] | [
"PF02005",
"PS51626",
"PTHR10631",
"TIGR00308"
] | [
"TRM",
"SAM_MT_TRM1",
"",
"TRM1"
] | [
8752,
8791,
8694,
4443
] | 4 | [
"EC",
"GP",
"METACYC",
"REACTOME"
] | [
"2.1.1.216",
"GenProp1521",
"PWY-6829",
"R-HSA-6782315"
] | [
"EC:2.1.1.216",
"GP:GenProp1521",
"METACYC:PWY-6829",
"REACTOME:R-HSA-6782315"
] | 4 | [
"2dul",
"2ejt",
"2eju",
"2ytz",
"3axs",
"3axt"
] | 6 | [
"PUB00005827",
"PUB00058111",
"PUB00058112",
"PUB00154466"
] | [
"9685492",
"10438627",
"2426253",
"17198746"
] | [
"The tRNA(guanine-26,N2-N2) methyltransferase (Trm1) from the hyperthermophilic archaeon Pyrococcus furiosus: cloning, sequencing of the gene and its expression in Escherichia coli.",
"Characterisation and enzymatic properties of tRNA(guanine 26, N (2), N (2))-dimethyltransferase (Trm1p) from Pyrococcus furiosus.... | [
1998,
1999,
1986,
2007
] | 4 | [] | [
"IPR022923"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
924,
130,
7740,
60
] | 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... | [
12,
1,
3,
1,
13,
15,
1,
12,
14,
1,
1,
42
] | 12 | true | Family | tRNA methyltransferase, Trm1 | tRNA methyltransferase, Trm1 | Trm1 | 8 |
IPR002906 | 2,906 | Small ribosomal subunit protein eS31 | Ribosomal_eS31 | Domain | 5,930 | false | false | This entry represents the eS31 (also known as S27a) ribosomal domain from both archaea and eukaryotes. In eukaryotes, the 40S ribosomal protein eS31 is synthesized as a C-terminal extension of ubiquitin ( ), and this fusion protein is known as UBS27 [ ]. The eS31 domain comprises the C-terminal half of the protein. The... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF01599",
"SM01402"
] | [
"Ribosomal_S27",
"Ribosomal_S27"
] | [
5906,
5837
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-110312",
"R-BTA-110314",
"R-BTA-110320",
"R-BTA-1169091",
"R-BTA-1234176",
"R-BTA-1253288",
"R-BTA-1295596",
"R-BTA-1358803",
"R-BTA-156827",
"R-BTA-168638",
"R-BTA-174048",
"R-BTA-174084",
"R-BTA-174113",
"R-BTA-174154",
"R-BTA-174178",
"R-BTA-174184",
"R-BTA-179409",
"R-BT... | [
"REACTOME:R-BTA-110312",
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-110320",
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-1253288",
"REACTOME:R-BTA-1295596",
"REACTOME:R-BTA-1358803",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-168638",
"REACTOME:R-BTA-174048",
"REACTOME:R-BT... | 1,078 | [
"2k4x",
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7p",
"3j7r",
"3j80",
"3j81",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jam",
"3jan",
"3jap",
"4bts",
"4d5l",
"4d61",
"4kzx",
"4kzy",
"4kzz",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q",
"4u4r",
"4u4u",
"4u4y",
"4u4z"... | 497 | [
"PUB00004044",
"PUB00004045",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00083514"
] | [
"2538753",
"2538756",
"11297922",
"11290319",
"11114498",
"16185873"
] | [
"The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis.",
"Identification of the long ubiquitin extension as ribosomal protein S27a.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structu... | [
1989,
1989,
2001,
2001,
2000,
2005
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Pestivirus bovis",
"ecological metagenomes"
] | [
746,
9,
5137,
14,
24
] | 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... | [
6,
1,
1,
2,
5,
3,
1,
4,
8,
1,
2,
14
] | 12 | true | Domain | Small ribosomal subunit protein eS31 | Small ribosomal subunit protein eS31 | Ribosomal_eS31 | 7 |
IPR002908 | 2,908 | Frataxin/CyaY | Frataxin/CyaY | Family | 9,241 | false | false | The eukaryotic proteins in this entry include Frataxin, the protein that is mutated in Friedreich's ataxia [ ], and related sequences. Friedreich's ataxia is a progressive neurodegenerative disorder caused by loss of function mutations in the gene encoding Frataxin (FRDA). Frataxin mRNA is predominantly expressed in ti... | [
"GO:0008199",
"GO:0016226"
] | [
"ferric iron binding",
"iron-sulfur cluster assembly"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROFILE",
"PANTHER",
"SMART",
"NCBIFAM"
] | [
"PF01491",
"PR00904",
"PS50810",
"PTHR16821",
"SM01219",
"TIGR03421"
] | [
"Frataxin_Cyay",
"FRATAXIN",
"FRATAXIN_2",
"",
"Frataxin_Cyay",
"FeS_CyaY"
] | [
9164,
2526,
9141,
8482,
9055,
8602
] | 6 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp0138",
"PDOC01043",
"R-BTA-1268020",
"R-BTA-1362409",
"R-BTA-9854311",
"R-BTA-9865881",
"R-CEL-1362409",
"R-CEL-9854311",
"R-DDI-1362409",
"R-DDI-9854311",
"R-DDI-9865881",
"R-DME-1362409",
"R-DME-9854311",
"R-DME-9865881",
"R-HSA-1268020",
"R-HSA-1362409",
"R-HSA-9854311",
... | [
"GP:GenProp0138",
"PROSITEDOC:PDOC01043",
"REACTOME:R-BTA-1268020",
"REACTOME:R-BTA-1362409",
"REACTOME:R-BTA-9854311",
"REACTOME:R-BTA-9865881",
"REACTOME:R-CEL-1362409",
"REACTOME:R-CEL-9854311",
"REACTOME:R-DDI-1362409",
"REACTOME:R-DDI-9854311",
"REACTOME:R-DDI-9865881",
"REACTOME:R-DME-13... | 34 | [
"1ekg",
"1ew4",
"1ly7",
"1soy",
"2eff",
"2fql",
"2ga5",
"2p1x",
"3oeq",
"3oer",
"3s4m",
"3s5d",
"3s5e",
"3s5f",
"3t3j",
"3t3k",
"3t3l",
"3t3t",
"3t3x",
"4ec2",
"4hs5",
"4jpd",
"4lk8",
"4lp1",
"5kz5",
"5t0v",
"5tre",
"6fco",
"6nzu",
"6z1p",
"7n9i",
"8hz1"... | 38 | [
"PUB00003904",
"PUB00004328",
"PUB00005217",
"PUB00005550",
"PUB00034422",
"PUB00042953",
"PUB00042954"
] | [
"9241270",
"8815938",
"8596916",
"8931268",
"16930487",
"16603772",
"16428423"
] | [
"Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin.",
"Clinical and genetic abnormalities in patients with Friedreich's ataxia.",
"Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion.",
"Friedreich's ataxia protein: phyl... | [
1997,
1996,
1996,
1996,
2006,
2006,
2006
] | 7 | [] | [
"IPR017789",
"IPR047584"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4774,
4424,
43
] | 3 | [
"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,
2,
1,
1,
10,
6,
1,
3,
4,
1,
1,
9
] | 13 | true | Family | Frataxin/CyaY | Frataxin/CyaY | Frataxin/CyaY | 3 |
IPR002909 | 2,909 | IPT domain | IPT_dom | Domain | 65,788 | false | false | The IPT (Ig-like, plexins, transcription factors) domain has an immunoglobulin like fold [ ]. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. The Ron tyrosine kinase receptor shares with the members of its subfa... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF01833",
"SM00429"
] | [
"TIG",
"IPT"
] | [
50893,
46975
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-264876",
"R-CEL-416482",
"R-CEL-416550",
"R-CEL-416572",
"R-CEL-5620916",
"R-CEL-9013405",
"R-CFA-1169091",
"R-CFA-1810476",
"R-CFA-193692",
"R-CFA-202424",
"R-CFA-209560",
"R-CFA-2871837",
"R-CFA-3134963",
"R-CFA-3214841",
"R-CFA-445989",
"R-CFA-448706",
"R-CFA-5607764",
"R... | [
"REACTOME:R-CEL-264876",
"REACTOME:R-CEL-416482",
"REACTOME:R-CEL-416550",
"REACTOME:R-CEL-416572",
"REACTOME:R-CEL-5620916",
"REACTOME:R-CEL-9013405",
"REACTOME:R-CFA-1169091",
"REACTOME:R-CFA-1810476",
"REACTOME:R-CFA-193692",
"REACTOME:R-CFA-202424",
"REACTOME:R-CFA-209560",
"REACTOME:R-CFA... | 237 | [
"1a02",
"1a3q",
"1a47",
"1bfs",
"1bft",
"1cdg",
"1cgt",
"1cgu",
"1cgv",
"1cgw",
"1cgx",
"1cgy",
"1ciu",
"1cxe",
"1cxf",
"1cxh",
"1cxi",
"1cxk",
"1cxl",
"1cyg",
"1d3c",
"1d7f",
"1ded",
"1dtu",
"1eo5",
"1eo7",
"1gji",
"1hk6",
"1i75",
"1ikn",
"1imh",
"1k3z"... | 170 | [
"PUB00005856",
"PUB00006356"
] | [
"10390613",
"8816464"
] | [
"Domains in plexins: links to integrins and transcription factors.",
"A splicing variant of the RON transcript induces constitutive tyrosine kinase activity and an invasive phenotype."
] | [
1999,
1996
] | 2 | [] | [
"IPR032397",
"IPR038006"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
87,
8938,
56500,
23,
240
] | 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... | [
22,
11,
279,
39,
106,
111,
2,
14,
131,
2,
1,
115
] | 12 | true | Domain | IPT domain | IPT domain | IPT_dom | 4 |
IPR002910 | 2,910 | Floricaula/leafy protein | FLO_LFY | Family | 4,613 | false | false | This family consists of various plant development proteins which are homologues of Floricaula (FLO) and leafy (LFY) proteins which are floral meristem identity proteins. FLO and LFY proteins are floral meristem identity proteins [ , ]. Mutations in the sequences of these proteins affect flower and leaf development. LFY... | [
"GO:0003677",
"GO:0006355"
] | [
"DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER"
] | [
"PTHR36079"
] | [
""
] | [
4613
] | 1 | [] | [] | [] | 0 | [
"2vy1",
"2vy2",
"4bhk",
"4ude",
"8s8q",
"9fwy",
"9g19"
] | 7 | [
"PUB00000873",
"PUB00001038",
"PUB00085053"
] | [
"1350515",
"9259553",
"27097556"
] | [
"LEAFY controls floral meristem identity in Arabidopsis.",
"UNIFOLIATA regulates leaf and flower morphogenesis in pea.",
"A SAM oligomerization domain shapes the genomic binding landscape of the LEAFY transcription factor."
] | [
1992,
1997,
2016
] | 3 | [] | [] | 0 | 0 | null | [
"Streptophyta"
] | [
4613
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
6,
18
] | 3 | true | Family | Floricaula/leafy protein | Floricaula/leafy protein | FLO_LFY | 6 |
IPR002912 | 2,912 | ACT domain | ACT_dom | Domain | 257,491 | false | false | The ACT domain is found in a variety of contexts and is proposed to be a conserved regulatory binding fold. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. The archetypical ACT domain is the C-terminal regulatory domain of 3-phosphoglycerate dehydrogenase (3PG... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF01842",
"PF13291",
"PS51671"
] | [
"ACT",
"ACT_4",
"ACT"
] | [
84685,
33224,
252672
] | 3 | [
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1358",
"GenProp1419",
"GenProp1475",
"GenProp1553",
"R-BTA-8964208",
"R-CEL-8964208",
"R-DDI-209905",
"R-DDI-209931",
"R-DDI-8964208",
"R-DME-8964208",
"R-HSA-209931",
"R-HSA-2160456",
"R-HSA-8964208",
"R-HSA-9031628",
"R-MMU-209931",
"R-MMU-8964208",
"R-RNO-209931",
"R-RNO... | [
"GP:GenProp1358",
"GP:GenProp1419",
"GP:GenProp1475",
"GP:GenProp1553",
"REACTOME:R-BTA-8964208",
"REACTOME:R-CEL-8964208",
"REACTOME:R-DDI-209905",
"REACTOME:R-DDI-209931",
"REACTOME:R-DDI-8964208",
"REACTOME:R-DME-8964208",
"REACTOME:R-HSA-209931",
"REACTOME:R-HSA-2160456",
"REACTOME:R-HSA... | 18 | [
"1phz",
"1psd",
"1sc6",
"1vr9",
"1y7p",
"1yba",
"1ygy",
"1zpv",
"2cdq",
"2dt9",
"2dtj",
"2f06",
"2f1f",
"2fgc",
"2hmf",
"2j0w",
"2j0x",
"2jhe",
"2ko1",
"2lvw",
"2nyi",
"2p9c",
"2p9e",
"2p9g",
"2pa3",
"2pc6",
"2phm",
"2qmw",
"2qmx",
"2re1",
"2zho",
"3aaw"... | 111 | [
"PUB00007206",
"PUB00068713"
] | [
"11751050",
"12481063"
] | [
"The ACT domain family.",
"Molecular characterization of a novel gene family encoding ACT domain repeat proteins in Arabidopsis."
] | [
2001,
2002
] | 2 | [] | [
"IPR039557",
"IPR044074",
"IPR044561",
"IPR047896",
"IPR054352"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5166,
209348,
38574,
8,
4395
] | 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",... | [
151,
3,
6,
6,
13,
17,
10,
5,
134,
13,
5,
5,
271
] | 13 | true | Domain | ACT domain | ACT domain | ACT_dom | 4 |
IPR002913 | 2,913 | START domain | START_lipid-bd_dom | Domain | 52,011 | false | false | START (StAR-related lipid-transfer) is a lipid-binding domain in StAR, HD-ZIP and signalling proteins [ ]. StAR (Steroidogenic Acute Regulatory protein) is a mitochondrial protein that is synthesised in response to luteinising hormone stimulation [ ]. Expression of the protein in the absence of hormone stimulation is s... | [
"GO:0008289"
] | [
"lipid binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01852",
"PS50848",
"SM00234"
] | [
"START",
"START",
"START"
] | [
49790,
50328,
35906
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50848",
"R-BTA-1483191",
"R-BTA-159418",
"R-BTA-1660661",
"R-BTA-196108",
"R-BTA-77289",
"R-BTA-9837999",
"R-DRE-1660661",
"R-DRE-196108",
"R-DRE-9837999",
"R-GGA-196108",
"R-GGA-9837999",
"R-HSA-1483191",
"R-HSA-159418",
"R-HSA-1660661",
"R-HSA-196108",
"R-HSA-2142789",
"R-HS... | [
"PROSITEDOC:PDOC50848",
"REACTOME:R-BTA-1483191",
"REACTOME:R-BTA-159418",
"REACTOME:R-BTA-1660661",
"REACTOME:R-BTA-196108",
"REACTOME:R-BTA-77289",
"REACTOME:R-BTA-9837999",
"REACTOME:R-DRE-1660661",
"REACTOME:R-DRE-196108",
"REACTOME:R-DRE-9837999",
"REACTOME:R-GGA-196108",
"REACTOME:R-GGA-... | 46 | [
"1em2",
"1jss",
"1ln1",
"1ln2",
"1ln3",
"2e3m",
"2e3n",
"2e3o",
"2e3p",
"2e3q",
"2e3r",
"2e3s",
"2mou",
"2pso",
"2r55",
"2z9y",
"2z9z",
"3fo5",
"3h3q",
"3h3r",
"3h3s",
"3h3t",
"3p0l",
"3qsz",
"5brl",
"5i9j",
"5jjd",
"5zyg",
"5zyh",
"5zyi",
"5zyj",
"5zyk"... | 49 | [
"PUB00002877",
"PUB00005851",
"PUB00007207",
"PUB00007208"
] | [
"7961770",
"10322415",
"11276083",
"10802740"
] | [
"The purification, cloning, and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 mouse Leydig tumor cells. Characterization of the steroidogenic acute regulatory protein (StAR).",
"START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins.",
"Adaptations of the helix-... | [
1994,
1999,
2001,
2000
] | 4 | [] | [
"IPR029867",
"IPR041949",
"IPR041950",
"IPR041951",
"IPR041952"
] | 0 | 5 | 0 | [
"Bacteria",
"Eukaryota",
"Halorubrum tibetense",
"Viruses",
"metagenomes"
] | [
2191,
49774,
1,
12,
33
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
217,
12,
68,
9,
71,
58,
71,
63,
277
] | 9 | true | Domain | START domain | START domain | START_lipid-bd_dom | 9 |
IPR002914 | 2,914 | Pollen allergen Poa p IX/Phl p VI | Poa_pIX/Phl_pVI | Domain | 178 | false | false | Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS All... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01620"
] | [
"Pollen_allerg_2"
] | [
178
] | 1 | [] | [] | [] | 0 | [
"1l3p",
"1nlx",
"2m64",
"6trk"
] | 4 | [
"PUB00001686",
"PUB00002641",
"PUB00026911"
] | [
"7729555",
"1702432",
"12077438"
] | [
"Major allergen Phl p Vb in timothy grass is a novel pollen RNase.",
"Nucleotide sequence analysis of three cDNAs coding for Poa p IX isoallergens of Kentucky bluegrass pollen.",
"Structure of the functional domain of the major grass-pollen allergen Phlp 5b."
] | [
1995,
1991,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Pooideae"
] | [
178
] | 1 | [] | [] | 0 | true | Domain | Pollen allergen Poa p IX/Phl p VI | Pollen allergen Poa p IX/Phl p VI | Poa_pIX/Phl_pVI | 2 |
IPR002915 | 2,915 | DeoC/FbaB/LacD aldolase | DeoC/FbaB/LacD_aldolase | Family | 39,502 | false | false | This entry represents diverse aldolases, such as deoxyribose-phosphate aldolase, tagatose 1,6-diphosphate aldolase, fructose-bisphosphate aldolase class 1, 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase, 2-amino-4,5-dihydroxy-6-one-heptanoic acid-7-phosphate synthase, phospho-2-dehydro-3-deoxyheptonate aldolase,... | [
"GO:0016829"
] | [
"lyase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF01791",
"SM01133"
] | [
"DeoC",
"DeoC"
] | [
38816,
38403
] | 2 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.2",
"4.1.2.4",
"GenProp1306",
"GenProp1344",
"GenProp1407",
"GenProp1476",
"GenProp1559",
"PWY-7180",
"PWY-8060",
"R-BTA-6798695",
"R-BTA-71336",
"R-CEL-6798695",
"R-CEL-71336",
"R-HSA-6798695",
"R-HSA-71336",
"R-MMU-6798695",
"R-MMU-71336"
] | [
"EC:4.1.2",
"EC:4.1.2.4",
"GP:GenProp1306",
"GP:GenProp1344",
"GP:GenProp1407",
"GP:GenProp1476",
"GP:GenProp1559",
"METACYC:PWY-7180",
"METACYC:PWY-8060",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-71336",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-71336",
"REACTOME:R-HSA-6798695",
"REACT... | 17 | [
"1j2w",
"1jcj",
"1jcl",
"1ktn",
"1mzh",
"1n7k",
"1ojx",
"1ok4",
"1ok6",
"1p1x",
"1to3",
"1ub3",
"1vcv",
"1w8s",
"2a4a",
"2qjg",
"2qjh",
"2qji",
"2yce",
"3gkf",
"3glc",
"3gnd",
"3iv3",
"3jrk",
"3kao",
"3mhf",
"3mhg",
"3myo",
"3myp",
"3ndo",
"3ng3",
"3ngj"... | 84 | [
"PUB00038045",
"PUB00040690",
"PUB00060480",
"PUB00060481",
"PUB00060482",
"PUB00060483",
"PUB00060484",
"PUB00060485",
"PUB00153746",
"PUB00153747"
] | [
"15766250",
"16843441",
"13950007",
"5972827",
"5793710",
"5816380",
"20427286",
"11387336",
"20433874",
"25284756"
] | [
"Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates.",
"Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus.",
"The mechanism of action of aldolases. III. Schiff base formation with lysine.",
"Organic phosphate grou... | [
2005,
2006,
1962,
1966,
1969,
1969,
2010,
2001,
2010,
2015
] | 10 | [] | [
"IPR005927",
"IPR011343",
"IPR017291",
"IPR041720"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured marine phage"
] | [
2115,
32926,
3748,
712,
1
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus"
] | [
1,
1,
2,
4,
7,
5,
1,
6
] | 8 | true | Family | DeoC/FbaB/LacD aldolase | DeoC/FbaB/LacD aldolase | DeoC/FbaB/LacD_aldolase | 9 |
IPR002919 | 2,919 | Trypsin Inhibitor-like, cysteine rich domain | TIL_dom | Domain | 22,615 | false | false | This domain is found in proteinase inhibitors, as well as in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9 [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01826"
] | [
"TIL"
] | [
22615
] | 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-CFA-114608",
"R-CFA-216083",
"R-CFA-354192",
"R-CFA-354194",
"R-CFA-372708",
"R-CFA-430116",
"R-CFA-5674135",
"R-CFA-75892",
"R-HSA-114608",
"R-HSA-140837",
"R-HSA-163125",
"R-HSA-216083",
"R-HSA-354192",
"R-HSA-354194",
"R-HSA-372708",
"R-HSA-430116",
"R-HSA-5083625",
"R-HSA-50... | [
"REACTOME:R-CFA-114608",
"REACTOME:R-CFA-216083",
"REACTOME:R-CFA-354192",
"REACTOME:R-CFA-354194",
"REACTOME:R-CFA-372708",
"REACTOME:R-CFA-430116",
"REACTOME:R-CFA-5674135",
"REACTOME:R-CFA-75892",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-140837",
"REACTOME:R-HSA-163125",
"REACTOME:R-HSA-216... | 58 | [
"1ata",
"1atb",
"1atd",
"1ate",
"1ccv",
"1cou",
"1eai",
"1hx2",
"2h9e",
"2mhp",
"2mhq",
"2p3f",
"3ssb",
"6n29",
"6tm2",
"7a5o",
"7kwo",
"7pmv",
"7pnf",
"7pov",
"7pp6",
"7prl",
"7skl",
"7skm",
"7wn3",
"7wn4",
"7wn6",
"7wpp",
"7wpq",
"7wpr",
"7wps",
"7wqt"... | 45 | [
"PUB00160773"
] | [
"29147019"
] | [
"Identification and characterization of serine protease inhibitors in a parasitic wasp, Pteromalus puparum."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"viral metagenome"
] | [
5,
22595,
12,
3
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
39,
36,
14,
38,
50,
40
] | 6 | true | Domain | Trypsin Inhibitor-like, cysteine rich domain | Trypsin Inhibitor-like, cysteine rich domain | TIL_dom | 9 |
IPR002921 | 2,921 | Fungal lipase-type domain | Fungal_lipase-type | Domain | 56,157 | false | false | This entry represents a domain with an α/β hydrolase fold found in a group of proteins from eukaryotes and bacteria, including Feruloyl esterase A from Aspergillus niger [ ], Triacylglycerol lipase OBL1 from Arabidopsis thaliana [ ], human Diacylglycerol lipase-alpha [ ], Toxin TseL from Vibrio cholerae [ ]. It is simi... | [
"GO:0006629"
] | [
"lipid metabolic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01764"
] | [
"Lipase_3"
] | [
56157
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.1",
"R-HSA-426048",
"R-MMU-426048",
"R-RNO-426048"
] | [
"EC:3.1.1",
"REACTOME:R-HSA-426048",
"REACTOME:R-MMU-426048",
"REACTOME:R-RNO-426048"
] | 4 | [
"1dt3",
"1dt5",
"1dte",
"1du4",
"1ein",
"1gt6",
"1lgy",
"1tgl",
"1tia",
"1tib",
"1tic",
"1usw",
"1uwc",
"1uza",
"2bjh",
"2hl6",
"2ix9",
"2ory",
"2yij",
"3g7n",
"3ngm",
"3o0d",
"3tgl",
"3uue",
"3uuf",
"4dyh",
"4ea6",
"4flf",
"4gbg",
"4ghw",
"4gi1",
"4glb"... | 82 | [
"PUB00031463",
"PUB00031895",
"PUB00097154",
"PUB00101267",
"PUB00103747"
] | [
"7656005",
"15081808",
"29178188",
"24348240",
"26668358"
] | [
"An unusual buried polar cluster in a family of fungal lipases.",
"The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family.",
"Characterization of the enzymatic activity and physiological function of the lipid droplet-associated t... | [
1994,
2004,
2018,
2013,
2016
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3,
5408,
50520,
61,
165
] | 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... | [
238,
36,
8,
7,
7,
3,
6,
137,
6,
2,
1,
234
] | 12 | true | Domain | Fungal lipase-type domain | Fungal lipase-type domain | Fungal_lipase-type | 2 |
IPR002922 | 2,922 | Thiazole biosynthetic enzyme Thi4 family | Thi4_fam | Family | 3,614 | false | false | Thiamine (vitamin B1) can be synthesised de novo in prokaryotes, plants and fungi. In eukaryotes, THI4 is involved in the biosynthesis of the thiamine precursor thiazole, and is repressed by thiamine [ ]. Archaea harbour structural homologues of both the bacterial (ThiS-ThiF) and eukaryotic (THI4) proteins for thiazole... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00292"
] | [
""
] | [
3614
] | 1 | [
"EC",
"GP",
"GP"
] | [
"2.4.2",
"GenProp1513",
"GenProp1697"
] | [
"EC:2.4.2",
"GP:GenProp1513",
"GP:GenProp1697"
] | 3 | [
"1rp0",
"3fpz",
"3jsk",
"4y4l",
"4y4m",
"4y4n",
"6hk1",
"7rk0"
] | 8 | [
"PUB00005732",
"PUB00046626",
"PUB00059231",
"PUB00059232",
"PUB00072882"
] | [
"7961415",
"16912043",
"15375115",
"8541506",
"25348237"
] | [
"Cloning, nucleotide sequence, and regulation of Schizosaccharomyces pombe thi4, a thiamine biosynthetic gene.",
"Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana.",
"Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea.",
"Evidence for the thiamine bios... | [
1994,
2006,
2004,
1995,
2014
] | 5 | [] | [
"IPR022828",
"IPR027495"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
708,
376,
2488,
42
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
3,
1,
3,
1,
1,
11
] | 6 | true | Family | Thiazole biosynthetic enzyme Thi4 family | Thiazole biosynthetic enzyme Thi4 family | Thi4_fam | 1 |
IPR002924 | 2,924 | Adenovirus small t-antigen, E1B 19kDa protein | Adenovir_t-Ag_E1B_19kDa | Family | 333 | false | false | This family consists of adenovirus E1B 19kDa protein or small t-antigen. The E1B 19kDa protein inhibits E1A induced apoptosis and hence prolongs the viability of the host cell [ ]. It can also inhibit apoptosis mediated by tumour necrosis factor alpha and Fas antigen [ ]. E1B 19kDa blocks apoptosis by interacting with ... | [
"GO:0033668"
] | [
"symbiont-mediated suppression of host apoptosis"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01691"
] | [
"Adeno_E1B_19K"
] | [
333
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001927",
"PUB00003510"
] | [
"8600029",
"8083992"
] | [
"The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53-inducible and death-promoting Bax protein.",
"Functional complementation of the adenovirus E1B 19-kilodalton protein with Bcl-2 in the inhibition of apoptosis in infected cells."
] | [
1996,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Adenoviridae"
] | [
333
] | 1 | [] | [] | 0 | true | Family | Adenovirus small t-antigen, E1B 19kDa protein | Adenovirus small t-antigen, E1B 19kDa protein | Adenovir_t-Ag_E1B_19kDa | 9 |
IPR002925 | 2,925 | Dienelactone hydrolase | Dienelactn_hydro | Domain | 64,180 | false | false | Dienelactone hydrolases play a crucial role in chlorocatechol degradation via the modified ortho cleavage pathway. Enzymes induced in 4-fluorobenzoate-utilizing bacteria have been classified into three groups on the basis of their specificity towards cis- and trans-dienelactone [ ]. Some proteins contain repeated small... | [
"GO:0016787"
] | [
"hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01738"
] | [
"DLH"
] | [
64180
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-211945",
"R-MMU-211945",
"R-RNO-211945",
"R-XTR-211945"
] | [
"REACTOME:R-HSA-211945",
"REACTOME:R-MMU-211945",
"REACTOME:R-RNO-211945",
"REACTOME:R-XTR-211945"
] | 4 | [
"1din",
"1ggv",
"1zi6",
"1zi8",
"1zi9",
"1zic",
"1zix",
"1ziy",
"1zj4",
"1zj5",
"2o2g",
"2r8b",
"3f67",
"3og9",
"4p92",
"4p93",
"4u2b",
"4u2c",
"4u2d",
"4u2e",
"4u2f",
"4u2g",
"4zi5",
"4zv9",
"7jiz",
"7jka",
"7qjn",
"7v8u",
"7v8v",
"7v8w",
"7v8x",
"7xrh"... | 39 | [
"PUB00006284"
] | [
"7684040"
] | [
"Dienelactone hydrolase from Pseudomonas cepacia."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudovirales sp. ctcT39",
"Eukaryota",
"unclassified sequences"
] | [
496,
43700,
1,
19293,
690
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
31,
6,
1,
8,
2,
2,
4,
8,
44,
4,
2,
2,
47
] | 13 | true | Domain | Dienelactone hydrolase | Dienelactone hydrolase | Dienelactn_hydro | 2 |
IPR002928 | 2,928 | Myosin tail | Myosin_tail | Domain | 38,609 | false | false | Muscle contraction is caused by sliding between the thick and thin filaments of the myofibril. Myosin is a major component of thick filaments and exists as a hexamer of 2 heavy chains [ ], 2 alkali light chains, and 2 regulatory light chains. The heavy chain can be subdivided into the N-terminal globular head and the C... | [
"GO:0016459"
] | [
"myosin complex"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF01576"
] | [
"Myosin_tail_1"
] | [
38609
] | 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-5627123",
"R-CFA-2029482",
"R-CFA-2173791",
"R-DDI-5627123",
"R-DME-350480",
"R-DME-445355",
"R-DME-5627123",
"R-DRE-2173791",
"R-HSA-1445148",
"R-HSA-1839117",
"R-HSA-2029482",
"R-HSA-2173791",
"R-HSA-390522",
"R-HSA-3928663",
"R-HSA-416572",
"R-HSA-445355",
"R-HSA-5625740",
... | [
"REACTOME:R-BTA-5627123",
"REACTOME:R-CFA-2029482",
"REACTOME:R-CFA-2173791",
"REACTOME:R-DDI-5627123",
"REACTOME:R-DME-350480",
"REACTOME:R-DME-445355",
"REACTOME:R-DME-5627123",
"REACTOME:R-DRE-2173791",
"REACTOME:R-HSA-1445148",
"REACTOME:R-HSA-1839117",
"REACTOME:R-HSA-2029482",
"REACTOME:... | 37 | [
"1i84",
"2fxm",
"2fxo",
"3j04",
"3jbh",
"5chx",
"5tby",
"6fsa",
"6so3",
"6xe9",
"6ysy",
"6z47",
"7jh7",
"7kog",
"7mf3",
"8efi",
"8enc",
"8g4l",
"8q6t",
"8u95",
"9fu2",
"9gz1",
"9gz2",
"9gz3",
"9syu",
"9szr"
] | 26 | [
"PUB00001579",
"PUB00002350",
"PUB00003213",
"PUB00004629",
"PUB00005168",
"PUB00005169",
"PUB00094302",
"PUB00095592"
] | [
"2806546",
"1939027",
"3783701",
"3540939",
"8316857",
"8316858",
"11919279",
"26150528"
] | [
"Human embryonic myosin heavy chain cDNA. Interspecies sequence conservation of the myosin rod, chromosomal locus and isoform specific transcription of the gene.",
"The primary structure of skeletal muscle myosin heavy chain: I. Sequence of the amino-terminal 23 kDa fragment.",
"Complete nucleotide and encoded ... | [
1989,
1991,
1986,
1986,
1993,
1993,
2002,
2015
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
11,
38598
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
159,
33,
63,
71,
90
] | 6 | true | Domain | Myosin tail | Myosin tail | Myosin_tail | 9 |
IPR002929 | 2,929 | Potato leaf roll virus readthrough protein | PLrV_ORF5 | Family | 1,313 | false | false | This family consists mainly of the Potato leafroll virus (PLrV) read through protein also known as the minor capsid protein. This is generated via a readthrough of open reading frame 3, the coat protein, allowing transcription of open reading frame 5 to give an extended coat protein with a large C-terminal addition or ... | [
"GO:0019028"
] | [
"viral capsid"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF01690"
] | [
"PLRV_ORF5"
] | [
1313
] | 1 | [] | [] | [] | 0 | [
"7uln",
"7ulo"
] | 2 | [
"PUB00005598",
"PUB00046133",
"PUB00046134",
"PUB00096160"
] | [
"7513925",
"7882968",
"9311800",
"19297484"
] | [
"Changes in the amino acid sequence of the coat protein readthrough domain of potato leafroll luteovirus affect the formation of an epitope and aphid transmission.",
"Aphid transmission of beet western yellows luteovirus requires the minor capsid read-through protein P74.",
"The N-terminal region of the luteovi... | [
1994,
1995,
1997,
2009
] | 4 | [] | [] | 0 | 0 | null | [
"Simiduia",
"Viruses"
] | [
3,
1310
] | 2 | [] | [] | 0 | true | Family | Potato leaf roll virus readthrough protein | Potato leaf roll virus readthrough protein | PLrV_ORF5 | 3 |
IPR002930 | 2,930 | Glycine cleavage system H-protein | GCV_H | Family | 30,769 | false | false | This is a family of glycine cleavage H-proteins, part of the glycine cleavage system (GCS) found in bacteria, archaea, and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine [ ]. The H-protein sh... | [
"GO:0019464",
"GO:0005960"
] | [
"glycine decarboxylation via glycine cleavage system",
"glycine cleavage complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"PANTHER"
] | [
"MF_00272",
"PTHR11715"
] | [
"GcvH",
""
] | [
27271,
30676
] | 2 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1356",
"GenProp1747",
"R-BTA-6783984",
"R-BTA-9857492",
"R-DDI-6783984",
"R-DDI-9857492",
"R-DME-6783984",
"R-DME-9857492",
"R-GGA-6783984",
"R-GGA-9857492",
"R-HSA-6783984",
"R-HSA-9857492",
"R-MMU-6783984",
"R-MMU-9857492",
"R-RNO-6783984",
"R-RNO-9857492",
"R-SCE-6783984",... | [
"GP:GenProp1356",
"GP:GenProp1747",
"REACTOME:R-BTA-6783984",
"REACTOME:R-BTA-9857492",
"REACTOME:R-DDI-6783984",
"REACTOME:R-DDI-9857492",
"REACTOME:R-DME-6783984",
"REACTOME:R-DME-9857492",
"REACTOME:R-GGA-6783984",
"REACTOME:R-GGA-9857492",
"REACTOME:R-HSA-6783984",
"REACTOME:R-HSA-9857492"... | 20 | [
"1dxm",
"1hpc",
"1htp",
"1onl",
"1zko",
"2edg",
"2ka7",
"3a7a",
"3a7l",
"3a8i",
"3a8j",
"3a8k",
"3ab9",
"3hgb",
"3ift",
"3klr",
"3mxu",
"3tzu",
"3wdn",
"8ugo",
"8v0j",
"9c19"
] | 22 | [
"PUB00004842",
"PUB00063633"
] | [
"8197146",
"11286922"
] | [
"X-ray structure determination at 2.6-A resolution of a lipoate-containing protein: the H-protein of the glycine decarboxylase complex from pea leaves.",
"The glycine decarboxylase system: a fascinating complex."
] | [
1994,
2001
] | 2 | [
"IPR033753"
] | [
"IPR017453",
"IPR017514"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
728,
22979,
6459,
2,
601
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
9,
2,
3,
1,
1,
12,
2,
1,
9,
7,
1,
1,
25
] | 13 | true | Family | Glycine cleavage system H-protein | Glycine cleavage system H-protein | GCV_H | 8 |
IPR002931 | 2,931 | Transglutaminase-like | Transglutaminase-like | Domain | 82,999 | false | false | This domain is found in many proteins known to have transglutaminase activity, i.e. which cross-link proteins through an acyl-transfer reaction between the gamma-carboxamide group of peptide-bound glutamine and the ε-amino group of peptide-bound lysine, resulting in a epsilon-(gamma-glutamyl)lysine isopeptide bond. Tra... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF01841",
"SM00460"
] | [
"Transglut_core",
"TGc"
] | [
81868,
68785
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-532668",
"R-DME-532668",
"R-DRE-532668",
"R-HSA-114608",
"R-HSA-140875",
"R-HSA-532668",
"R-HSA-6785807",
"R-HSA-6809371",
"R-MMU-114608",
"R-MMU-140875",
"R-MMU-532668",
"R-MMU-6809371",
"R-RNO-114608",
"R-RNO-140875",
"R-RNO-532668",
"R-RNO-6809371"
] | [
"REACTOME:R-CEL-532668",
"REACTOME:R-DME-532668",
"REACTOME:R-DRE-532668",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-140875",
"REACTOME:R-HSA-532668",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6809371",
"REACTOME:R-MMU-114608",
"REACTOME:R-MMU-140875",
"REACTOME:R-MMU-532668",
"REACTOME:R-MMU-6... | 16 | [
"1evu",
"1ex0",
"1f13",
"1fie",
"1g0d",
"1ggt",
"1ggu",
"1ggy",
"1kv3",
"1l9m",
"1l9n",
"1nud",
"1nuf",
"1nug",
"1qrk",
"1x3w",
"1x3z",
"2f4m",
"2f4o",
"2q3z",
"3esw",
"3isr",
"3ly6",
"3s3j",
"3s3p",
"3s3s",
"4kty",
"4pyg",
"4xz7",
"5mhl",
"5mhm",
"5mhn"... | 65 | [
"PUB00004847",
"PUB00005832",
"PUB00005863",
"PUB00010253"
] | [
"7913750",
"9791169",
"10452618",
"12366374"
] | [
"Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.",
"Molecular analysis of Methanobacterium phage psiM2.",
"A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases.",
"Transglutaminases: nature's biological glues."
] | [
1994,
1998,
1999,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1420,
58631,
22278,
4,
666
] | 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... | [
12,
2,
53,
6,
38,
27,
4,
2,
33,
2,
2,
9
] | 12 | true | Domain | Transglutaminase-like | Transglutaminase-like | Transglutaminase-like | 8 |
IPR002932 | 2,932 | Glutamate synthase domain | Glu_synthdom | Domain | 42,350 | false | false | Ferredoxin-dependent glutamate synthase (GltS) has been implicated in a number of functions including photorespiration in Arabidopsis where it may also play a role in primary nitrogen assimilation in roots [ ]. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxogl... | [
"GO:0015930",
"GO:0016638",
"GO:0006537"
] | [
"glutamate synthase activity",
"oxidoreductase activity, acting on the CH-NH2 group of donors",
"glutamate biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"CDD"
] | [
"PF01645",
"cd02808"
] | [
"Glu_synthase",
"GltS_FMN"
] | [
42349,
40530
] | 2 | [] | [] | [] | 0 | [
"1ea0",
"1llw",
"1llz",
"1lm1",
"1ofd",
"1ofe",
"2vdc",
"6s6s",
"6s6t",
"6s6u",
"6s6x",
"7mfm",
"7mft"
] | 13 | [
"PUB00005657",
"PUB00007209",
"PUB00015747",
"PUB00043791",
"PUB00080763",
"PUB00080764"
] | [
"8923741",
"9596633",
"12455964",
"15052410",
"15581577",
"12702341"
] | [
"Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain structure of yeast glutamate synthase.",
"Arabidopsis gls mutants and distinct Fd-GOGAT genes. Implications for photorespiration and primary nitrogen assimilation.",
"Evolutionary analyses of the small subunit of glutamate synthase: gen... | [
1996,
1998,
2002,
2004,
2005,
2001
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
955,
34916,
5623,
856
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Drosophila melanogaster",
"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)",
"Schizosacchar... | [
13,
2,
4,
1,
1,
7,
1,
1,
97
] | 9 | true | Domain | Glutamate synthase domain | Glutamate synthase domain | Glu_synthdom | 7 |
IPR002933 | 2,933 | Peptidase M20 | Peptidase_M20 | Family | 231,963 | false | false | This group of proteins contains the metallopeptidases and non-peptidase homologues (amidohydrolases) that belong to the MEROPS peptidase family M20 (clan MH) [ ]. The peptidases of this clan have two catalytic zinc ions at the active site, bound by His/Asp, Asp, Glu, Asp/Glu and His. The catalysed reaction involves the... | [
"GO:0016787"
] | [
"hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01546"
] | [
"Peptidase_M20"
] | [
231963
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"3.5.1",
"GenProp1242",
"GenProp1326",
"GenProp1346",
"GenProp1393",
"GenProp1466",
"R-BTA-174403",
"R-BTA-9753281",
"R-DDI-5423646",
"R-DDI-9673163",
"R-DDI-9753281",
"R-DRE-9673163",
"R-HSA-174403",
"R-HSA-5423646",
"R-HSA-5579007",
"R-HSA-9673163",
"R-HSA-9753281",
"R-MMU-174403... | [
"EC:3.5.1",
"GP:GenProp1242",
"GP:GenProp1326",
"GP:GenProp1346",
"GP:GenProp1393",
"GP:GenProp1466",
"REACTOME:R-BTA-174403",
"REACTOME:R-BTA-9753281",
"REACTOME:R-DDI-5423646",
"REACTOME:R-DDI-9673163",
"REACTOME:R-DDI-9753281",
"REACTOME:R-DRE-9673163",
"REACTOME:R-HSA-174403",
"REACTOM... | 33 | [
"1cg2",
"1fno",
"1lfw",
"1q7l",
"1r3n",
"1r43",
"1vgy",
"1vix",
"1xmb",
"1ysj",
"1z2l",
"2f7v",
"2f8h",
"2imo",
"2pok",
"2q43",
"2qyv",
"2rb7",
"2v8d",
"2v8g",
"2v8h",
"2v8v",
"2vl1",
"2zof",
"2zog",
"3ct9",
"3dlj",
"3gb0",
"3ic1",
"3ife",
"3io1",
"3isz"... | 88 | [
"PUB00003579",
"PUB00014890",
"PUB00019732",
"PUB00030157",
"PUB00079915",
"PUB00085192"
] | [
"7674922",
"10684608",
"1732229",
"12933810",
"3276674",
"5411754"
] | [
"Evolutionary families of metallopeptidases.",
"Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase.",
"Cloning and sequencing of the genes involved in the conversion of 5-substituted hydantoins to the corresponding L-amino acids from the native plasmid of Pseudomonas sp. strain NS671.",
"E... | [
1995,
2000,
1992,
2003,
1988,
1970
] | 6 | [] | [
"IPR001160",
"IPR005941",
"IPR010158",
"IPR010159",
"IPR010161",
"IPR010162",
"IPR010169",
"IPR010174",
"IPR010175",
"IPR010182",
"IPR010964",
"IPR012166",
"IPR017149",
"IPR017150",
"IPR017153",
"IPR017439",
"IPR047177"
] | 0 | 17 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4117,
188906,
36210,
5,
2725
] | 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",... | [
72,
8,
12,
13,
8,
32,
15,
6,
36,
21,
4,
3,
61
] | 13 | true | Family | Peptidase M20 | Peptidase M20 | Peptidase_M20 | 3 |
IPR002934 | 2,934 | Polymerase, nucleotidyl transferase domain | Polymerase_NTP_transf_dom | Domain | 38,094 | false | false | A small region that overlaps with a nuclear localization signal and binds to the RNA primer contains three aspartates that are essential for catalysis. Sequence and secondary structure comparisons of regions surrounding these aspartates with sequences of other polymerases revealed a significant homology to the palm str... | [
"GO:0016779"
] | [
"nucleotidyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01909"
] | [
"NTP_transf_2"
] | [
38094
] | 1 | [
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7",
"2.7.7.59",
"3.1.4.-",
"PWY-5978",
"PWY-6129",
"PWY-6689",
"PWY-7119",
"PWY-7366",
"R-HSA-877300",
"R-HSA-8983711",
"R-HSA-909733",
"R-HSA-9833110"
] | [
"EC:2.7.7",
"EC:2.7.7.59",
"EC:3.1.4.-",
"METACYC:PWY-5978",
"METACYC:PWY-6129",
"METACYC:PWY-6689",
"METACYC:PWY-7119",
"METACYC:PWY-7366",
"REACTOME:R-HSA-877300",
"REACTOME:R-HSA-8983711",
"REACTOME:R-HSA-909733",
"REACTOME:R-HSA-9833110"
] | 12 | [
"1jaj",
"1jms",
"1jqr",
"1kdh",
"1kej",
"1no5",
"1px5",
"1r89",
"1r8a",
"1r8b",
"1r8c",
"1sz1",
"1tfw",
"1tfy",
"1uet",
"1ueu",
"1uev",
"1wot",
"1ylq",
"2dr5",
"2dr7",
"2dr8",
"2dr9",
"2dra",
"2drb",
"2dvi",
"2m2t",
"2m2u",
"2m2v",
"2m2w",
"2rff",
"2zh1"... | 130 | [
"PUB00005745",
"PUB00006346"
] | [
"7482698",
"8665867"
] | [
"DNA polymerase beta belongs to an ancient nucleotidyltransferase superfamily.",
"Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases."
] | [
1995,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
3837,
30845,
2645,
33,
4,
730
] | 6 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
1,
1,
36,
11,
1,
26,
2
] | 7 | true | Domain | Polymerase, nucleotidyl transferase domain | Polymerase, nucleotidyl transferase domain | Polymerase_NTP_transf_dom | 9 |
IPR002935 | 2,935 | Class I-like SAM-dependent O-methyltransferase | SAM_O-MeTrfase | Family | 38,297 | false | false | Members of this family are O-methyltransferases, including catechol O-methyltransferase [ ], caffeoyl-CoA O-methyltransferase [ ] and norbelladine 4'-O-methyltransferase [ ]. The family includes also bacterial O-methyltransferases that may be involved in antibiotic production [ , ]. | [
"GO:0008171"
] | [
"O-methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF01596",
"PS51682"
] | [
"Methyltransf_3",
"SAM_OMT_I"
] | [
35026,
37327
] | 2 | [
"EC",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1",
"GenProp1668",
"GenProp1759",
"R-BTA-156581",
"R-BTA-379397",
"R-BTA-379398",
"R-DRE-156581",
"R-DRE-379397",
"R-DRE-379398",
"R-HSA-156581",
"R-HSA-379397",
"R-HSA-379398",
"R-HSA-9679191",
"R-MMU-156581",
"R-MMU-379397",
"R-MMU-379398",
"R-RNO-156581",
"R-RNO-379397",
... | [
"EC:2.1.1",
"GP:GenProp1668",
"GP:GenProp1759",
"REACTOME:R-BTA-156581",
"REACTOME:R-BTA-379397",
"REACTOME:R-BTA-379398",
"REACTOME:R-DRE-156581",
"REACTOME:R-DRE-379397",
"REACTOME:R-DRE-379398",
"REACTOME:R-HSA-156581",
"REACTOME:R-HSA-379397",
"REACTOME:R-HSA-379398",
"REACTOME:R-HSA-967... | 22 | [
"1h1d",
"1jr4",
"1sui",
"1sus",
"1vid",
"2avd",
"2cl5",
"2gpy",
"2hnk",
"2zlb",
"2zth",
"2zvj",
"3a7d",
"3a7e",
"3bwm",
"3bwy",
"3c3p",
"3c3y",
"3cbg",
"3dr5",
"3dul",
"3duw",
"3hvh",
"3hvi",
"3hvj",
"3hvk",
"3ntv",
"3nw9",
"3nwb",
"3nwe",
"3oe4",
"3oe5"... | 181 | [
"PUB00003596",
"PUB00031205",
"PUB00040056",
"PUB00085191",
"PUB00094548"
] | [
"8936303",
"15734921",
"16618795",
"25061748",
"31147608"
] | [
"Two multifunctional peptide synthetases and an O-methyltransferase are involved in the biosynthesis of the DNA-binding antibiotic and antitumour agent saframycin Mx1 from Myxococcus xanthus.",
"Crystal structures of alfalfa caffeoyl coenzyme A 3-O-methyltransferase.",
"Comparative study of ortho- and meta-nitr... | [
1996,
2005,
2006,
2014,
2019
] | 5 | [] | [
"IPR017128",
"IPR050362"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
379,
21974,
15547,
10,
387
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"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",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea... | [
24,
6,
17,
36,
5,
2,
15,
12,
2,
64
] | 10 | true | Family | Class I-like SAM-dependent O-methyltransferase | Class I-like SAM-dependent O-methyltransferase | SAM_O-MeTrfase | 7 |
IPR002938 | 2,938 | FAD-binding domain | FAD-bd | Domain | 231,043 | false | false | This domain is involved in FAD binding in a number of enzymes, including human Kynurenine 3-monooxygenase (KMO), which is related to neuroinflammatory conditions [ ], archaeal Digeranylgeranylglycerophospholipid reductase (GGR), involved in the biosynthesis of archaeal membrane lipids [ ] and bacterial 3-(3-hydroxy-phe... | [
"GO:0071949"
] | [
"FAD binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01494"
] | [
"FAD_binding_3"
] | [
231043
] | 1 | [
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"GenProp1287",
"GenProp1331",
"GenProp1458",
"GenProp1503",
"GenProp1508",
"GenProp1763",
"R-BTA-2142789",
"R-CEL-2142789",
"R-CEL-71240",
"R-DDI-2142789",
"R-DDI-71240",
"R-DME-2142789",
"R-DME-71240",
"R-DRE-2142789",
"R-DRE-71240",
"R-HSA-2142789",
"R-HSA-71240",
"R-HSA-983231",... | [
"GP:GenProp1287",
"GP:GenProp1331",
"GP:GenProp1458",
"GP:GenProp1503",
"GP:GenProp1508",
"GP:GenProp1763",
"REACTOME:R-BTA-2142789",
"REACTOME:R-CEL-2142789",
"REACTOME:R-CEL-71240",
"REACTOME:R-DDI-2142789",
"REACTOME:R-DDI-71240",
"REACTOME:R-DME-2142789",
"REACTOME:R-DME-71240",
"REACT... | 27 | [
"1bf3",
"1bgj",
"1bgn",
"1bkw",
"1cc4",
"1cc6",
"1cj2",
"1cj3",
"1cj4",
"1d7l",
"1dob",
"1doc",
"1dod",
"1doe",
"1foh",
"1ius",
"1iut",
"1iuu",
"1iuv",
"1iuw",
"1iux",
"1k0i",
"1k0j",
"1k0l",
"1pbb",
"1pbc",
"1pbd",
"1pbe",
"1pbf",
"1pdh",
"1phh",
"1pn0"... | 240 | [
"PUB00100389",
"PUB00103927"
] | [
"29429898",
"24214941"
] | [
"Structural Basis for Inhibitor-Induced Hydrogen Peroxide Production by Kynurenine 3-Monooxygenase.",
"Geranylgeranyl reductase and ferredoxin from Methanosarcina acetivorans are required for the synthesis of fully reduced archaeal membrane lipid in Escherichia coli cells."
] | [
2018,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"Plasmid pEST1226",
"unclassified sequences"
] | [
2220,
141224,
86573,
5,
1,
1020
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
68,
4,
175,
2,
7,
18,
14,
21,
53,
22,
2,
1,
95
] | 13 | true | Domain | FAD-binding domain | FAD-binding domain | FAD-bd | 2 |
IPR002941 | 2,941 | DNA methylase N-4/N-6 | DNA_methylase_N4/N6 | Domain | 44,856 | false | false | This domain is found in DNA methylases. In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. This family contains both N-4 cytosine-specific DNA methylases and N-6 Adenine-specific DNA methylases. N-4 cytosine-specific DNA methylases ( ) [ ] are enzymes th... | [
"GO:0003677",
"GO:0008170"
] | [
"DNA binding",
"N-methyltransferase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF01555"
] | [
"N6_N4_Mtase"
] | [
44856
] | 1 | [
"EC"
] | [
"2.1.1"
] | [
"EC:2.1.1"
] | 1 | [
"1boo",
"1eg2",
"1g60",
"1nw5",
"1nw6",
"1nw7",
"1nw8",
"2zie",
"2zif",
"2zig",
"4zcf",
"5hek",
"5hfj",
"6k0w",
"6pbd",
"7dsu",
"8s9m",
"8s9n",
"8s9o",
"8urk",
"9c3s",
"9c3t",
"9c3u"
] | 23 | [
"PUB00001857"
] | [
"7607512"
] | [
"Sequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferases."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1555,
38973,
495,
1412,
2421
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | DNA methylase N-4/N-6 | DNA methylase N-4/N-6 | DNA_methylase_N4/N6 | 7 |
IPR002944 | 2,944 | Sodium:neurotransmitter symporter, inebriated | Na/ntran_symport_inebriated | Family | 151 | false | false | Neurotransmitter transport systems are integral to the release, re-uptake and recycling of neurotransmitters at synapses. High affinity transport proteins found in the plasma membrane of presynaptic nerve terminals and glial cells are responsible for the removal from the extracellular space of released-transmitters, th... | [
"GO:0005034",
"GO:0005328",
"GO:0006836",
"GO:0019226",
"GO:0042065",
"GO:0016020"
] | [
"osmosensor activity",
"neurotransmitter:sodium symporter activity",
"neurotransmitter transport",
"transmission of nerve impulse",
"glial cell growth",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 6 | [
"PRINTS"
] | [
"PR01205"
] | [
"INEBRIATED"
] | [
151
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001020",
"PUB00006006",
"PUB00006007",
"PUB00006008",
"PUB00006027",
"PUB00006028",
"PUB00054917",
"PUB00054918"
] | [
"15336049",
"8811182",
"8103691",
"7823024",
"1334137",
"8917579",
"1151733",
"11880499"
] | [
"Cloners quick on the uptake.",
"Molecular biology of mammalian amino acid transporters.",
"Neurotransmitter transporters: three distinct gene families.",
"Neurotransmitter transporters: three important gene families for neuronal function.",
"Identification and characterization of inebriated, a gene affecti... | [
1992,
1996,
1993,
1994,
1992,
1996,
1975,
2002
] | 8 | [
"IPR000175"
] | [] | 1 | 0 | 1 | [
"Endopterygota"
] | [
151
] | 1 | [
"Drosophila melanogaster"
] | [
3
] | 1 | true | Family | Sodium:neurotransmitter symporter, inebriated | Sodium:neurotransmitter symporter, inebriated | Na/ntran_symport_inebriated | 5 |
IPR002945 | 2,945 | Glucose transporter, type 3 (GLUT3) | Glc_transpt_3 | Family | 632 | false | false | The ability to transport glucose across the plasma membrane is a feature common to nearly all cells, from simple bacteria through to highly specialised mammalian neurones. Facilitative sugar transport is mediated by members of the GLUT transporter family, which form an aqueous pore across the membrane through which sug... | [
"GO:0055056",
"GO:1904659",
"GO:0016020"
] | [
"D-glucose transmembrane transporter activity",
"D-glucose transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01192"
] | [
"GLUCTRSPORT3"
] | [
632
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-GGA-352832",
"R-HSA-189200",
"R-HSA-196836",
"R-HSA-6798695",
"R-HSA-9022699",
"R-MMU-189200",
"R-MMU-196836",
"R-MMU-6798695",
"R-RNO-189200",
"R-RNO-196836",
"R-RNO-6798695",
"R-SSC-189200",
"R-SSC-196836",
"R-SSC-6798695"
] | [
"REACTOME:R-GGA-352832",
"REACTOME:R-HSA-189200",
"REACTOME:R-HSA-196836",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9022699",
"REACTOME:R-MMU-189200",
"REACTOME:R-MMU-196836",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-189200",
"REACTOME:R-RNO-196836",
"REACTOME:R-RNO-6798695",
"REACTOME:R-SSC... | 14 | [
"4zw9",
"4zwb",
"4zwc",
"5c65",
"7crz",
"7sps",
"7spt"
] | 7 | [
"PUB00002464",
"PUB00003999",
"PUB00005096",
"PUB00005353",
"PUB00005398",
"PUB00006044",
"PUB00006047",
"PUB00006048"
] | [
"3170580",
"3543693",
"3839598",
"2180146",
"8438231",
"8366068",
"9841639",
"2446136"
] | [
"Evidence for a family of human glucose transporter-like proteins. Sequence and gene localization of a protein expressed in fetal skeletal muscle and other tissues.",
"Mammalian and bacterial sugar transport proteins are homologous.",
"Sequence and structure of a human glucose transporter.",
"Facilitative glu... | [
1988,
1987,
1985,
1990,
1993,
1993,
1998,
1987
] | 8 | [
"IPR045263"
] | [] | 1 | 0 | 1 | [
"Amniota"
] | [
632
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
5,
5
] | 3 | true | Family | Glucose transporter, type 3 (GLUT3) | Glucose transporter, type 3 (GLUT3) | Glc_transpt_3 | 4 |
IPR002946 | 2,946 | Intracellular chloride channel | CLIC | Family | 6,136 | false | false | The chloride intracellular channel (CLIC) family represent a subgroup of the glutathione-S-transferase (GSTs) superfamily. CLIC proteins can exist as both soluble globular proteins and integral membrane proteins with ion channel function [ ]. Membrane insertion seems to be redox-regulated [ ] and has a strong pH depend... | [] | [] | [] | 0 | [
"PRINTS",
"NCBIFAM"
] | [
"PR01263",
"TIGR00862"
] | [
"INTCLCHANNEL",
"O-ClC"
] | [
6107,
4644
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2672351",
"R-HSA-5578775",
"R-HSA-9662360",
"R-HSA-9662361",
"R-RNO-2672351",
"R-RNO-5578775"
] | [
"REACTOME:R-HSA-2672351",
"REACTOME:R-HSA-5578775",
"REACTOME:R-HSA-9662360",
"REACTOME:R-HSA-9662361",
"REACTOME:R-RNO-2672351",
"REACTOME:R-RNO-5578775"
] | 6 | [
"1k0m",
"1k0n",
"1k0o",
"1rk4",
"2ahe",
"2d2z",
"2per",
"2r4v",
"2r5g",
"3fy7",
"3kjy",
"3o3t",
"3p8w",
"3p90",
"3qr6",
"3swl",
"3tgz",
"3uvh",
"4iqa",
"4jzq",
"4k0g",
"4k0n",
"5y7i",
"6ery",
"6erz",
"6y2h",
"7f8r",
"7fbq",
"8q4i",
"8q4j"
] | 30 | [
"PUB00034628",
"PUB00072078",
"PUB00072099",
"PUB00072117"
] | [
"14613939",
"12202911",
"11978800",
"20085760"
] | [
"The intracellular chloride ion channel protein CLIC1 undergoes a redox-controlled structural transition.",
"From glutathione transferase to pore in a CLIC.",
"Recombinant CLIC1 (NCC27) assembles in lipid bilayers via a pH-dependent two-state process to form chloride ion channels with identical characteristics ... | [
2004,
2002,
2002,
2010
] | 4 | [
"IPR040079"
] | [] | 1 | 0 | 1 | [
"Eumetazoa",
"Pseudomonadota"
] | [
6134,
2
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
23,
13,
25
] | 4 | true | Family | Intracellular chloride channel | Intracellular chloride channel | CLIC | 1 |
IPR002948 | 2,948 | Thiazide-sensitive Na-K-Cl co-transporter | SLC12A3 | Family | 1,791 | false | false | Solute carrier family 12 member 3 (Slc12a3) is also known as Tsc (thiazide-sensitive Na-Cl co-transporter). Tsc is a large integral membrane protein (~1000 amino acids) that mediates the coupled transport of Na + and Cl - in an electrically silent manner. In the mammalian kidney, it is the dominant mechanism mediating ... | [
"GO:0006811",
"GO:0016020"
] | [
"monoatomic ion transport",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR01230"
] | [
"NACLTRNSPORT"
] | [
1791
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-426117",
"R-HSA-5619087",
"R-MMU-426117",
"R-RNO-426117"
] | [
"REACTOME:R-HSA-426117",
"REACTOME:R-HSA-5619087",
"REACTOME:R-MMU-426117",
"REACTOME:R-RNO-426117"
] | 4 | [
"7y6i",
"7yg0",
"7yg1",
"8fhn",
"8fho",
"8fhp",
"8fhq",
"8fhr",
"8fht",
"8vpn",
"8vpp",
"9bwt"
] | 12 | [
"PUB00006033",
"PUB00006034",
"PUB00006035"
] | [
"8464884",
"9639584",
"8528245"
] | [
"Primary structure and functional expression of a cDNA encoding the thiazide-sensitive, electroneutral sodium-chloride cotransporter.",
"The electroneutral cation-chloride cotransporters.",
"Gitelman's variant of Bartter's syndrome, inherited hypokalaemic alkalosis, is caused by mutations in the thiazide-sensit... | [
1993,
1998,
1996
] | 3 | [
"IPR004842"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
1791
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
2,
4,
3
] | 4 | true | Family | Thiazide-sensitive Na-K-Cl co-transporter | Thiazide-sensitive Na-K-Cl co-transporter | SLC12A3 | 7 |
IPR002949 | 2,949 | Cytochrome P450, E-class, CYP24A, mitochondrial | Cyt_P450_E_CYP24A_mit | Family | 113 | false | false | Cytochrome P450 enzymes are a superfamily of haem-containing mono-oxygenases that are found in all kingdoms of life, and which show extraordinary diversity in their reaction chemistry. In mammals, these proteins are found primarily in microsomes of hepatocytes and other cell types, where they oxidise steroids, fatty ac... | [
"GO:0004497",
"GO:0005506",
"GO:0016705",
"GO:0020037"
] | [
"monooxygenase activity",
"iron ion binding",
"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen",
"heme binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function"
] | 4 | [
"PRINTS"
] | [
"PR01238"
] | [
"MITP450CC24"
] | [
113
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-RNO-196791",
"R-RNO-211916"
] | [
"REACTOME:R-RNO-196791",
"REACTOME:R-RNO-211916"
] | 2 | [
"3k9v",
"3k9y"
] | 2 | [
"PUB00033965",
"PUB00033966",
"PUB00033967",
"PUB00033969",
"PUB00033971"
] | [
"16042601",
"17023115",
"15128046",
"8637843",
"16617161"
] | [
"Biodiversity of cytochrome P450 redox systems.",
"Cytochrome P450--redox partner fusion enzymes.",
"Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.",
"Structural domains of P450-containi... | [
2005,
2007,
2004,
1995,
2006
] | 5 | [
"IPR001128"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
113
] | 1 | [
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3
] | 2 | true | Family | Cytochrome P450, E-class, CYP24A, mitochondrial | Cytochrome P450, E-class, CYP24A, mitochondrial | Cyt_P450_E_CYP24A_mit | 2 |
IPR002951 | 2,951 | Atrophin-like | Atrophin-like | Family | 3,730 | false | false | Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03154"
] | [
"Atrophin-1"
] | [
3730
] | 1 | [
"REACTOME"
] | [
"R-HSA-8943724"
] | [
"REACTOME:R-HSA-8943724"
] | 1 | [] | 0 | [
"PUB00019181",
"PUB00019182"
] | [
"9647693",
"11264541"
] | [
"Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins.",
"Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity."
] | [
1998,
2001
] | 2 | [] | [
"IPR017993"
] | 0 | 1 | 0 | [
"Opisthokonta"
] | [
3730
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
24,
4,
8,
8,
10
] | 5 | true | Family | Atrophin-like | Atrophin-like | Atrophin-like | 5 |
IPR002953 | 2,953 | Filoviridae VP35 protein | Filo_VP35 | Family | 481 | false | false | The filoviridae are a group of viruses that cause haemorrhagic fevers with a high mortality rate. The family currently contains three viruses: Ebola virus sp., Lake Victoria marburgvirus and Reston ebolavirus, named after their corresponding outbreak regions. They possess negative-stranded RNA genomes, which encode at ... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF",
"PRINTS"
] | [
"PF02097",
"PIRSF018326",
"PR01240"
] | [
"Filo_VP35",
"VP35_FiloV",
"FILOVP35"
] | [
481,
287,
468
] | 3 | [] | [] | [] | 0 | [
"3fke",
"3ks4",
"3ks8",
"3l25",
"3l26",
"3l27",
"3l28",
"3l29",
"3l2a",
"4gh9",
"4gha",
"4ghl",
"4ibb",
"4ibc",
"4ibd",
"4ibe",
"4ibf",
"4ibg",
"4ibi",
"4ibj",
"4ibk",
"4ije",
"4ijf",
"4lg2",
"4ypi",
"5bpv",
"5f5o",
"5toh",
"5toi",
"5xsq",
"6dku",
"6gbo"... | 48 | [
"PUB00005976"
] | [
"8482365"
] | [
"The VP35 and VP40 proteins of filoviruses. Homology between Marburg and Ebola viruses."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Boreoeutheria",
"Filoviridae"
] | [
26,
455
] | 2 | [] | [] | 0 | true | Family | Filoviridae VP35 protein | Filoviridae VP35 protein | Filo_VP35 | 9 |
IPR002954 | 2,954 | Salmonella surface presentation of antigen M protein | Salm_SPAgM | Family | 708 | false | false | The Salmonella typhimurium Surface Presentation of Antigens M gene (SpaM) is one of 12 that form a cluster responsible for invasion properties [ ]. The gene product is required for entry by the bacterium into epithelial cells, and is thus considered to be a virulence factor [ ]. Other Spa genes in the cluster are relat... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS"
] | [
"PF02090",
"PR01227"
] | [
"SPAM",
"SSPAMPROTEIN"
] | [
707,
410
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001240",
"PUB00005977",
"PUB00005978",
"PUB00005979",
"PUB00005980"
] | [
"8404849",
"7752894",
"10066464",
"9068645",
"8751894"
] | [
"Cognate gene clusters govern invasion of host epithelial cells by Salmonella typhimurium and Shigella flexneri.",
"Functional analysis of the Salmonella typhimurium invasion genes invl and invJ and identification of a target of the protein secretion apparatus encoded in the inv locus.",
"Vaccination against en... | [
1993,
1995,
1998,
1997,
1996
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
708
] | 1 | [] | [] | 0 | true | Family | Salmonella surface presentation of antigen M protein | Salmonella surface presentation of antigen M protein | Salm_SPAgM | 3 |
IPR002955 | 2,955 | Microtubule-associated protein Tau | Tau | Family | 1,671 | false | false | Tau proteins are microtubule-associated proteins that are involved in microtubule assembly and stabilisation. They may also play a wider role in cellular shape, motility and signal transduction [ ]. Tau mRNA is expressed predominantly in neurones, and particularly in their axons. Quite a number of isoforms have been de... | [
"GO:0008017"
] | [
"microtubule binding"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR01261"
] | [
"TAUPROTEIN"
] | [
1671
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-264870",
"R-HSA-9619483",
"R-HSA-9833482",
"R-MMU-264870",
"R-MMU-9833482",
"R-RNO-264870",
"R-RNO-9833482"
] | [
"REACTOME:R-HSA-264870",
"REACTOME:R-HSA-9619483",
"REACTOME:R-HSA-9833482",
"REACTOME:R-MMU-264870",
"REACTOME:R-MMU-9833482",
"REACTOME:R-RNO-264870",
"REACTOME:R-RNO-9833482"
] | 7 | [
"6hre",
"6hrf",
"6nwp",
"6nwq",
"6tjo",
"6tjx",
"7mkf",
"7mkg",
"7mkh",
"7nrq",
"7nrs",
"7nrt",
"7nrv",
"7nrx",
"7p65",
"7p66",
"7p67",
"7p68",
"7p6a",
"7p6b",
"7p6c",
"7p6d",
"7p6e",
"7pqc",
"7pqp",
"7qjv",
"7qjw",
"7qjx",
"7qjy",
"7qjz",
"7qk1",
"7qk2"... | 149 | [
"PUB00005981",
"PUB00005982",
"PUB00005983",
"PUB00009829"
] | [
"9786340",
"8202139",
"10377376",
"12475178"
] | [
"Tau protein pathology in neurodegenerative diseases.",
"Altered microtubule organization in small-calibre axons of mice lacking tau protein.",
"The tangled biology of tau.",
"Functions and malfunctions of the tau proteins."
] | [
1998,
1994,
1999,
2002
] | 4 | [
"IPR027324"
] | [] | 1 | 0 | 1 | [
"Tetrapoda"
] | [
1671
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
7,
23
] | 3 | true | Family | Microtubule-associated protein Tau | Microtubule-associated protein Tau | Tau | 9 |
IPR002956 | 2,956 | Bride of sevenless protein | Bride_of_7less | Family | 451 | false | false | During development of the Drosophila retina, the bride of sevenless (boss) gene is required in photoreceptor neuron R8 for the development of photoreceptor neuron R7, suggesting that boss encodes or regulates an R7-specific inductive cue [ ]. The induction of R8 photoreceptor neuron neighbouring cells to assume an R7 c... | [
"GO:0005118",
"GO:0007601",
"GO:0016020"
] | [
"sevenless binding",
"visual perception",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01223"
] | [
"BRIDEOF7LESS"
] | [
451
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005984",
"PUB00005985",
"PUB00005986"
] | [
"2276620",
"1857416",
"8506350"
] | [
"Induction of cell fate in the Drosophila retina: the bride of sevenless protein is predicted to contain a large extracellular domain and seven transmembrane segments.",
"Interaction of bride of sevenless membrane-bound ligand and the sevenless tyrosine-kinase receptor.",
"The interaction of bride of sevenless ... | [
1990,
1991,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
15,
436
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus"
] | [
3,
4,
1,
1
] | 4 | true | Family | Bride of sevenless protein | Bride of sevenless protein | Bride_of_7less | 9 |
IPR002957 | 2,957 | Keratin, type I | Keratin_I | Family | 22,407 | false | false | Keratins are a well known group of intermediate filament proteins. Like actin filaments, keratins are flexible but provide a firm cell skeleton [ ]. Unlike actin, however, no known keratins are associated with motor functions. Approximately 10 keratins form the basis of hair or claw, with a further 20 found in internal... | [
"GO:0005198"
] | [
"structural molecule activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS",
"PANTHER"
] | [
"PR01248",
"PTHR23239"
] | [
"TYPE1KERATIN",
""
] | [
21368,
19304
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6805567",
"R-BTA-6809371",
"R-CFA-6805567",
"R-CFA-6809371",
"R-HSA-446107",
"R-HSA-6805567",
"R-HSA-6809371",
"R-HSA-9725554",
"R-HSA-9925563",
"R-HSA-9927432",
"R-MMU-446107",
"R-MMU-6805567",
"R-MMU-6809371",
"R-RNO-446107",
"R-RNO-6805567",
"R-RNO-6809371",
"R-XTR-6805567"... | [
"REACTOME:R-BTA-6805567",
"REACTOME:R-BTA-6809371",
"REACTOME:R-CFA-6805567",
"REACTOME:R-CFA-6809371",
"REACTOME:R-HSA-446107",
"REACTOME:R-HSA-6805567",
"REACTOME:R-HSA-6809371",
"REACTOME:R-HSA-9725554",
"REACTOME:R-HSA-9925563",
"REACTOME:R-HSA-9927432",
"REACTOME:R-MMU-446107",
"REACTOME:... | 18 | [
"3tnu",
"4zry",
"6e2j",
"6ec0",
"6jfv",
"6uui"
] | 6 | [
"PUB00101480"
] | [
"26902920"
] | [
"Autosomal Recessive Hypotrichosis with Woolly Hair Caused by a Mutation in the Keratin 25 Gene Expressed in Hair Follicles."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
9,
22397,
1
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
49,
81,
57,
95
] | 4 | true | Family | Keratin, type I | Keratin, type I | Keratin_I | 1 |
IPR002958 | 2,958 | Occludin | Occludin | Family | 916 | false | false | Occludin was the first molecular component of the tight junction to be identified. These are specialised membrane domains that form intercellular contacts between epithelial cells and create a regulated barrier to the paracellular movement of water, solutes and immune cells. They also provide a second type of barrier t... | [
"GO:0070830",
"GO:0005923",
"GO:0016020"
] | [
"bicellular tight junction assembly",
"bicellular tight junction",
"membrane"
] | [
"biological_process",
"cellular_component",
"cellular_component"
] | 3 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF005993",
"PR01258"
] | [
"Occludin",
"OCCLUDIN"
] | [
577,
814
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-351906",
"R-HSA-8935964",
"R-MMU-351906",
"R-RNO-351906"
] | [
"REACTOME:R-HSA-351906",
"REACTOME:R-HSA-8935964",
"REACTOME:R-MMU-351906",
"REACTOME:R-RNO-351906"
] | 4 | [] | 0 | [
"PUB00005987",
"PUB00005988"
] | [
"10361874",
"10370242"
] | [
"Transmembrane proteins in the tight junction barrier.",
"Occludin and claudins in tight-junction strands: leading or supporting players?"
] | [
1999,
1999
] | 2 | [
"IPR031176"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
916
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
5,
4,
2
] | 4 | true | Family | Occludin | Occludin | Occludin | 9 |
IPR002959 | 2,959 | Tumour necrosis factor alpha | TNF_alpha | Family | 424 | false | false | Cytokines can be grouped into a family on the basis of sequence, functional and structural similarities [ , , ]. Tumor necrosis factor (TNF) (also known as TNF-alpha or cachectin) is a monocyte-derived cytotoxin that has been implicated in tumour regression, septic shock and cachexia [ , ]. The protein is synthesised a... | [
"GO:0005164",
"GO:0006955",
"GO:0016020"
] | [
"tumor necrosis factor receptor binding",
"immune response",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01235"
] | [
"TNFALPHA"
] | [
424
] | 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-CFA-5357786",
"R-CFA-5357905",
"R-CFA-5357956",
"R-CFA-5626978",
"R-CFA-5668541",
"R-CFA-75893",
"R-HSA-381340",
"R-HSA-5357786",
"R-HSA-5357905",
"R-HSA-5357956",
"R-HSA-5626978",
"R-HSA-5668541",
"R-HSA-6783783",
"R-HSA-6785807",
"R-HSA-75893",
"R-MMU-5357786",
"R-MMU-5357905",
... | [
"REACTOME:R-CFA-5357786",
"REACTOME:R-CFA-5357905",
"REACTOME:R-CFA-5357956",
"REACTOME:R-CFA-5626978",
"REACTOME:R-CFA-5668541",
"REACTOME:R-CFA-75893",
"REACTOME:R-HSA-381340",
"REACTOME:R-HSA-5357786",
"REACTOME:R-HSA-5357905",
"REACTOME:R-HSA-5357956",
"REACTOME:R-HSA-5626978",
"REACTOME:R... | 33 | [
"1a8m",
"1tnf",
"2az5",
"2e7a",
"2tnf",
"2tun",
"2zjc",
"2zpx",
"3alq",
"3it8",
"3l9j",
"3wd5",
"4g3y",
"4tsv",
"4twt",
"5m2i",
"5m2j",
"5m2m",
"5mu8",
"5tsw",
"5uui",
"5wux",
"5yoy",
"6ooy",
"6ooz",
"6op0",
"6rmj",
"6x81",
"6x82",
"6x83",
"6x85",
"6x86"... | 50 | [
"PUB00002042",
"PUB00004130",
"PUB00005994",
"PUB00005995",
"PUB00006091",
"PUB00006095",
"PUB00006098",
"PUB00006101",
"PUB00015257"
] | [
"8095800",
"1377364",
"2922050",
"2009860",
"2989794",
"3349526",
"2777790",
"2268312",
"15335677"
] | [
"A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.",
"Emerging cytokine family.",
"Structure of tumour necrosis factor.",
"Localization of the active site of human tumour necrosis factor (hTNF) by mutational analysis.",
"Molecular cloning of mouse tu... | [
1993,
1992,
1989,
1991,
1985,
1988,
1989,
1990,
1993
] | 9 | [
"IPR006053"
] | [] | 1 | 0 | 1 | [
"Tetrapoda"
] | [
424
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
6,
5
] | 3 | true | Family | Tumour necrosis factor alpha | Tumour necrosis factor alpha | TNF_alpha | 4 |
IPR002960 | 2,960 | Lymphotoxin-alpha | TNF_beta | Family | 503 | false | false | Cytokines can be grouped into a family on the basis of sequence, functional and structural similarities [ , , ]. Tumor necrosis factor (TNF) (also known as TNF-alpha or cachectin) is a monocyte-derived cytotoxin that has been implicated in tumour regression, septic shock and cachexia [ , ]. The protein is synthesised a... | [
"GO:0005164",
"GO:0006955",
"GO:0016020"
] | [
"tumor necrosis factor receptor binding",
"immune response",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01236"
] | [
"TNFBETA"
] | [
503
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5668541",
"R-BTA-5669034",
"R-BTA-5676594",
"R-CFA-5668541",
"R-CFA-5669034",
"R-CFA-5676594",
"R-HSA-5668541",
"R-HSA-5669034",
"R-HSA-5676594",
"R-MMU-5668541",
"R-MMU-5669034",
"R-MMU-5676594",
"R-RNO-5668541",
"R-RNO-5669034",
"R-RNO-5676594",
"R-SSC-5668541",
"R-SSC-56690... | [
"REACTOME:R-BTA-5668541",
"REACTOME:R-BTA-5669034",
"REACTOME:R-BTA-5676594",
"REACTOME:R-CFA-5668541",
"REACTOME:R-CFA-5669034",
"REACTOME:R-CFA-5676594",
"REACTOME:R-HSA-5668541",
"REACTOME:R-HSA-5669034",
"REACTOME:R-HSA-5676594",
"REACTOME:R-MMU-5668541",
"REACTOME:R-MMU-5669034",
"REACTOM... | 18 | [
"1tnr",
"4mxv",
"4mxw",
"7dov"
] | 4 | [
"PUB00002042",
"PUB00004130",
"PUB00005996",
"PUB00006091",
"PUB00006095",
"PUB00006098",
"PUB00006101",
"PUB00015257"
] | [
"8095800",
"1377364",
"1733919",
"2989794",
"3349526",
"2777790",
"2268312",
"15335677"
] | [
"A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.",
"Emerging cytokine family.",
"The structure of human lymphotoxin (tumor necrosis factor-beta) at 1.9-A resolution.",
"Molecular cloning of mouse tumour necrosis factor cDNA and its eukaryotic express... | [
1993,
1992,
1992,
1985,
1988,
1989,
1990,
1993
] | 8 | [
"IPR006053"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
503
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
15,
2,
1
] | 4 | true | Family | Lymphotoxin-alpha | Lymphotoxin-alpha | TNF_beta | 4 |
IPR002961 | 2,961 | Lymphotoxin-beta | TNF_C | Family | 344 | false | false | Cytokines can be grouped into a family on the basis of sequence, functional and structural similarities [ , , ]. Tumor necrosis factor (TNF) (also known as TNF-alpha or cachectin) is a monocyte-derived cytotoxin that has been implicated in tumour regression, septic shock and cachexia [ , ]. The protein is synthesised a... | [
"GO:0005164",
"GO:0006955",
"GO:0016020"
] | [
"tumor necrosis factor receptor binding",
"immune response",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01237"
] | [
"TNFC"
] | [
344
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5668541",
"R-HSA-5676594",
"R-MMU-5668541",
"R-MMU-5676594"
] | [
"REACTOME:R-HSA-5668541",
"REACTOME:R-HSA-5676594",
"REACTOME:R-MMU-5668541",
"REACTOME:R-MMU-5676594"
] | 4 | [
"4mxw"
] | 1 | [
"PUB00000886",
"PUB00002042",
"PUB00004130",
"PUB00006091",
"PUB00006095",
"PUB00006098",
"PUB00006101",
"PUB00015257"
] | [
"7916655",
"8095800",
"1377364",
"2989794",
"3349526",
"2777790",
"2268312",
"15335677"
] | [
"Lymphotoxin beta, a novel member of the TNF family that forms a heteromeric complex with lymphotoxin on the cell surface.",
"A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.",
"Emerging cytokine family.",
"Molecular cloning of mouse tumour necrosis f... | [
1993,
1993,
1992,
1985,
1988,
1989,
1990,
1993
] | 8 | [
"IPR006053"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota"
] | [
25,
1,
318
] | 3 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
4,
2
] | 3 | true | Family | Lymphotoxin-beta | Lymphotoxin-beta | TNF_C | 2 |
IPR002962 | 2,962 | Peropsin | Peropsin | Family | 3,589 | false | false | Peropsin is a visual pigment-like protein found in ocular tissues. The protein has been localised to the apical face of the retinal pigment epithelium (RPE), most prominently to the microvilli that surround the photoreceptor outer segments. It is believed that peropsin may play a role in RPE physiology, either by detec... | [
"GO:0007186",
"GO:0007601",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"visual perception",
"membrane"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01244"
] | [
"PEROPSIN"
] | [
3589
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-418594",
"R-HSA-419771",
"R-MMU-418594",
"R-MMU-419771"
] | [
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-419771",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-419771"
] | 4 | [] | 0 | [
"PUB00006134"
] | [
"9275222"
] | [
"Peropsin, a novel visual pigment-like protein located in the apical microvilli of the retinal pigment epithelium."
] | [
1997
] | 1 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Eumetazoa"
] | [
3589
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
18,
5,
7,
6
] | 4 | true | Family | Peropsin | Peropsin | Peropsin | 2 |
IPR002963 | 2,963 | Expansin | Expansin | Family | 14,464 | false | false | Expansins are unusual proteins that mediate cell wall extension in plants. They are believed to act as a sort of chemical grease, allowing polymers to slide past one another by disrupting non-covalent hydrogen bonds that hold many wall polymers to one another. This process is not degradative and hence does not weaken t... | [
"GO:0009664"
] | [
"plant-type cell wall organization"
] | [
"biological_process"
] | 1 | [
"PRINTS",
"PANTHER"
] | [
"PR01226",
"PTHR31867"
] | [
"EXPANSIN",
""
] | [
13672,
14355
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00006126"
] | [
"7568110"
] | [
"Molecular cloning and sequence analysis of expansins--a highly conserved, multigene family of proteins that mediate cell wall extension in plants."
] | [
1995
] | 1 | [
"IPR007118"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Streptomyces"
] | [
14460,
4
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
108,
67,
120
] | 3 | true | Family | Expansin | Expansin | Expansin | 4 |
IPR002967 | 2,967 | Delta tubulin | Delta_tubulin | Family | 2,057 | false | false | Microtubules are polymers of tubulin, a dimer of two 55kDa subunits, designated alpha and beta [ , ]. Within the microtubule lattice, α-β heterodimers associate in a head-to-tail fashion, giving rise to microtubule polarity. Fluorescent labelling studies have suggested that tubulin is oriented in microtubules with beta... | [
"GO:0005200",
"GO:0005525",
"GO:0007017",
"GO:0005874"
] | [
"structural constituent of cytoskeleton",
"GTP binding",
"microtubule-based process",
"microtubule"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01224"
] | [
"DELTATUBULIN"
] | [
2057
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000039",
"PUB00000721",
"PUB00000978",
"PUB00002443",
"PUB00006112"
] | [
"3896122",
"8274140",
"2194680",
"3680207",
"8102497"
] | [
"Molecular biology and genetics of tubulin.",
"Gamma-tubulin: the hub of cellular microtubule assemblies.",
"Diversity among tubulin subunits: toward what functional end?",
"Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate.",
"Localization of an exchangeable GT... | [
1985,
1993,
1990,
1987,
1993
] | 5 | [
"IPR000217"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2057
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
3,
4,
5,
6,
1
] | 5 | true | Family | Delta tubulin | Delta tubulin | Delta_tubulin | 3 |
IPR002968 | 2,968 | Alpha-1-microglobulin | A1-microglobln | Family | 1,631 | false | false | The lipocalin family can be subdivided into kernal and outlier sets. The kernal lipocalins form the largest self consistent group, comprising the subfamily of alpha-1-microglobulins. The outlier lipocalins form several smaller distinct subgroups: the OBPs, the von Ebner's gland proteins, alpha-1-acid glycoproteins, tic... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR01215"
] | [
"A1MCGLOBULIN"
] | [
1631
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-166665",
"R-HSA-2168880",
"R-HSA-977606",
"R-MMU-166665",
"R-MMU-2168880",
"R-MMU-977606",
"R-RNO-2168880"
] | [
"REACTOME:R-HSA-166665",
"REACTOME:R-HSA-2168880",
"REACTOME:R-HSA-977606",
"REACTOME:R-MMU-166665",
"REACTOME:R-MMU-2168880",
"REACTOME:R-MMU-977606",
"REACTOME:R-RNO-2168880"
] | 7 | [
"1iw2",
"1lf7",
"2ova",
"2ovd",
"2ove",
"2qos",
"2rd7",
"3ojy",
"3qkg",
"4es7",
"6h03",
"6h04",
"7nyc",
"7nyd",
"8b0f",
"8b0g",
"8b0h"
] | 17 | [
"PUB00006100"
] | [
"1696404"
] | [
"An intriguing member of the lipocalin protein family: alpha 1-microglobulin."
] | [
1990
] | 1 | [] | [
"IPR029856"
] | 0 | 1 | 0 | [
"Bilateria"
] | [
1631
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
5,
3,
11
] | 4 | true | Family | Alpha-1-microglobulin | Alpha-1-microglobulin | A1-microglobln | 1 |
IPR002969 | 2,969 | Apolipoprotein D | ApolipopD | Family | 1,825 | false | false | Apolipoprotein D is a member of the lipocalin family with a high degree of sequence conservation from insects to mammals. It is a small, soluble carrier protein of lipophilic molecules mostly expressed in neurons and glial cells within the central and peripheral nervous system [ ]. It may have a role in anti-aging mech... | [
"GO:0008289",
"GO:0006869",
"GO:0007420",
"GO:0042246"
] | [
"lipid binding",
"lipid transport",
"brain development",
"tissue regeneration"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process"
] | 4 | [
"PRINTS"
] | [
"PR01219"
] | [
"APOLIPOPROTD"
] | [
1825
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-804914",
"R-HSA-9029569",
"R-MMU-804914",
"R-RNO-804914"
] | [
"REACTOME:R-HSA-804914",
"REACTOME:R-HSA-9029569",
"REACTOME:R-MMU-804914",
"REACTOME:R-RNO-804914"
] | 4 | [
"2hzq",
"2hzr"
] | 2 | [
"PUB00087210",
"PUB00087212",
"PUB00087213"
] | [
"24612673",
"25868396",
"21688324"
] | [
"Apolipoprotein D takes center stage in the stress response of the aging and degenerative brain.",
"Aging without Apolipoprotein D: Molecular and cellular modifications in the hippocampus and cortex.",
"Apolipoprotein D mediates autocrine protection of astrocytes and controls their reactivity level, contributin... | [
2014,
2015,
2011
] | 3 | [
"IPR022271"
] | [
"IPR026222"
] | 1 | 1 | 0 | [
"Eukaryota"
] | [
1825
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
4,
1,
5
] | 4 | true | Family | Apolipoprotein D | Apolipoprotein D | ApolipopD | 8 |
IPR002970 | 2,970 | Tick histamine-binding protein | Tick_his-bd | Family | 3,737 | false | false | null | [
"GO:0043176",
"GO:0030682"
] | [
"amine binding",
"symbiont-mediated perturbation of host defenses"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF02098"
] | [
"His_binding"
] | [
3737
] | 1 | [] | [] | [] | 0 | [
"1qft",
"1qfv",
"2x45",
"2x46",
"3brn",
"3bs2",
"3bu1",
"3bu9",
"3g7x",
"3gaq"
] | 10 | [
"PUB00000545",
"PUB00003448",
"PUB00005094",
"PUB00006145"
] | [
"8761444",
"8573354",
"2580349",
"10360182"
] | [
"The lipocalin protein family: structure and function.",
"Multiple molecular recognition properties of the lipocalin protein family.",
"Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC.",
"Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure."
] | [
1996,
1995,
1985,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Arthropoda",
"Peptoanaerobacter stomatis"
] | [
3735,
2
] | 2 | [] | [] | 0 | true | Family | Tick histamine-binding protein | Tick histamine-binding protein | Tick_his-bd | 4 |
IPR002971 | 2,971 | Major urinary protein | Maj_urinary | Family | 593 | false | false | Rodent urinary proteins (mouse major urinary proteins or MUPs and rat alpha-2u globulins) are the major protein components of rodent urine and transport pheromones [ ]. Rodent urine contains an unusually large amount of protein. The major site of MUP synthesis is the liver; the protein is secreted by the liver into ser... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR01221"
] | [
"MAJORURINARY"
] | [
593
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-804914",
"R-MMU-804914"
] | [
"REACTOME:R-HSA-804914",
"REACTOME:R-MMU-804914"
] | 2 | [
"1df3",
"1ew3",
"1gm6",
"1i04",
"1i05",
"1i06",
"1jv4",
"1mup",
"1qy0",
"1qy1",
"1qy2",
"1yp6",
"1yp7",
"1znd",
"1zne",
"1zng",
"1znh",
"1znk",
"1znl",
"2a2g",
"2a2u",
"2dm5",
"2l9c",
"2lb6",
"2nnd",
"2nne",
"2ozq",
"2r73",
"2r74",
"2ra6",
"3kff",
"3kfg"... | 42 | [
"PUB00006111"
] | [
"1279439"
] | [
"Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography."
] | [
1992
] | 1 | [
"IPR002345"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
593
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
44,
37
] | 3 | true | Family | Major urinary protein | Major urinary protein | Maj_urinary | 6 |
IPR002974 | 2,974 | Cytochrome P450, E-class, CYP52, ascomycetes | Cyt_P450_E_CYP52_ascomycetes | Family | 4,285 | false | false | This entry includes members of the CYP52 family from class E, cytochrome P450 proteins, found in ascomycetes. These enzymes should be classed as sequence cluster group II [ ]. Group II proteins are distributed widely amongst the kingdoms of life, but the CYP52 family has been first described only amongst Candida-relate... | [
"GO:0004497",
"GO:0005506",
"GO:0016712",
"GO:0020037"
] | [
"monooxygenase activity",
"iron ion binding",
"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen",
"heme binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function"
] | 4 | [
"PRINTS"
] | [
"PR01239"
] | [
"EP450IICYP52"
] | [
4285
] | 1 | [
"EC"
] | [
"1.14.14"
] | [
"EC:1.14.14"
] | 1 | [] | 0 | [
"PUB00033965",
"PUB00033966",
"PUB00033967",
"PUB00033969",
"PUB00033972",
"PUB00097866"
] | [
"16042601",
"17023115",
"15128046",
"8637843",
"14532053",
"24242247"
] | [
"Biodiversity of cytochrome P450 redox systems.",
"Cytochrome P450--redox partner fusion enzymes.",
"Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.",
"Structural domains of P450-containi... | [
2005,
2007,
2004,
1995,
2003,
2014
] | 6 | [
"IPR047146"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
4285
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Family | Cytochrome P450, E-class, CYP52, ascomycetes | Cytochrome P450, E-class, CYP52, ascomycetes | Cyt_P450_E_CYP52_ascomycetes | 7 |
IPR002975 | 2,975 | Fungal G-protein, alpha subunit | Fungi_Gprotein_alpha | Family | 5,339 | false | false | This family consists of the fungal class of G-protein alpha subunits. In Saccharomyces cerevisiae, two GTP-binding alpha subunits of the heterotrimeric G protein have been identified, Gpa1 and Gpa2. Gpa1 interacts with yeast pheromone receptors (Ste2 or Ste3) that initiate the signalling response leading to mating betw... | [
"GO:0001664",
"GO:0003924",
"GO:0005525",
"GO:0007186",
"GO:0005834"
] | [
"G protein-coupled receptor binding",
"GTPase activity",
"GTP binding",
"G protein-coupled receptor signaling pathway",
"heterotrimeric G-protein complex"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR01241"
] | [
"GPROTEINAFNG"
] | [
5339
] | 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-DDI-112043",
"R-DDI-170660",
"R-DDI-170670",
"R-DDI-202040",
"R-DDI-399997",
"R-DDI-416476",
"R-DDI-416482",
"R-DDI-418592",
"R-DDI-434316",
"R-DDI-9013148",
"R-DDI-9013149",
"R-DDI-9856530",
"R-SCE-112043",
"R-SCE-202040",
"R-SCE-2514859",
"R-SCE-399997",
"R-SCE-416476",
"R-SCE... | [
"REACTOME:R-DDI-112043",
"REACTOME:R-DDI-170660",
"REACTOME:R-DDI-170670",
"REACTOME:R-DDI-202040",
"REACTOME:R-DDI-399997",
"REACTOME:R-DDI-416476",
"REACTOME:R-DDI-416482",
"REACTOME:R-DDI-418592",
"REACTOME:R-DDI-434316",
"REACTOME:R-DDI-9013148",
"REACTOME:R-DDI-9013149",
"REACTOME:R-DDI-9... | 33 | [] | 0 | [
"PUB00005142",
"PUB00015166",
"PUB00015168",
"PUB00015169",
"PUB00015170",
"PUB00015171",
"PUB00015172",
"PUB00077802",
"PUB00077803",
"PUB00077810"
] | [
"1902986",
"15294442",
"15119945",
"14762218",
"11313912",
"9278091",
"11882385",
"14536090",
"12150916",
"7796906"
] | [
"Diversity of G proteins in signal transduction.",
"G protein activation by G protein coupled receptors: ternary complex formation or catalyzed reaction?",
"Biochemistry of transmembrane signaling mediated by trimeric G proteins.",
"G protein signaling: insights from new structures.",
"Regulation of G prote... | [
1991,
2004,
2004,
2004,
2001,
1997,
2002,
2003,
2002,
1995
] | 10 | [
"IPR001019"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
5339
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
3,
2,
1
] | 3 | true | Family | Fungal G-protein, alpha subunit | Fungal G-protein, alpha subunit | Fungi_Gprotein_alpha | 3 |
IPR002977 | 2,977 | Anion exchange protein 1 | Anion_exchange_1 | Family | 544 | false | false | Bicarbonate (HCO 3 - ) transport mechanisms are the principal regulators of pH in animal cells. Such transport also plays a vital role in acid-base movements in the stomach, pancreas, intestine, kidney, reproductive organs and the central nervous system. Functional studies have suggested four different HCO 3 - transpor... | [
"GO:0005452",
"GO:0006820",
"GO:0016020"
] | [
"solute:inorganic anion antiporter activity",
"monoatomic anion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01187"
] | [
"ANIONEXHNGR1"
] | [
544
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1237044",
"R-HSA-1247673",
"R-HSA-425381",
"R-HSA-5619050",
"R-MMU-1237044",
"R-MMU-1247673",
"R-MMU-425381",
"R-RNO-1237044",
"R-RNO-1247673",
"R-RNO-425381"
] | [
"REACTOME:R-HSA-1237044",
"REACTOME:R-HSA-1247673",
"REACTOME:R-HSA-425381",
"REACTOME:R-HSA-5619050",
"REACTOME:R-MMU-1237044",
"REACTOME:R-MMU-1247673",
"REACTOME:R-MMU-425381",
"REACTOME:R-RNO-1237044",
"REACTOME:R-RNO-1247673",
"REACTOME:R-RNO-425381"
] | 10 | [
"4yzf",
"7tvz",
"7tw0",
"7tw1",
"7tw2",
"7tw3",
"7tw5",
"7tw6",
"7ty4",
"7ty6",
"7ty7",
"7ty8",
"7tya",
"7uz3",
"7uzu",
"7uzv",
"7v07",
"7v0k",
"7v0m",
"7v0t",
"7v0u",
"7v0y",
"7v19",
"8crq",
"8crr",
"8crt",
"8cs9",
"8csl",
"8csv",
"8csy",
"8ct3",
"8cte"... | 40 | [
"PUB00005997",
"PUB00005998",
"PUB00005999",
"PUB00006000",
"PUB00006023",
"PUB00018713"
] | [
"2289848",
"2042971",
"9491367",
"10353704",
"9235899",
"9261985"
] | [
"Molecular biology of the anion exchanger gene family.",
"The band 3-related anion exchanger (AE) gene family.",
"The structure and function of band 3 (AE1): recent developments (review).",
"The association between familial distal renal tubular acidosis and mutations in the red cell anion exchanger (band 3, A... | [
1990,
1991,
1997,
1998,
1997,
1997
] | 6 | [
"IPR001717"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
544
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
7,
5
] | 4 | true | Family | Anion exchange protein 1 | Anion exchange protein 1 | Anion_exchange_1 | 4 |
IPR002978 | 2,978 | Anion exchange protein 2 | Anion_exchange_2 | Family | 510 | false | false | Bicarbonate (HCO 3 - ) transport mechanisms are the principal regulators of pH in animal cells. Such transport also plays a vital role in acid-base movements in the stomach, pancreas, intestine, kidney, reproductive organs and the central nervous system. Functional studies have suggested four different HCO 3 - transpor... | [
"GO:0005452",
"GO:0006820",
"GO:0016020"
] | [
"solute:inorganic anion antiporter activity",
"monoatomic anion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01188"
] | [
"ANIONEXHNGR2"
] | [
510
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-425381",
"R-MMU-425381",
"R-RNO-425381"
] | [
"REACTOME:R-HSA-425381",
"REACTOME:R-MMU-425381",
"REACTOME:R-RNO-425381"
] | 3 | [
"8gv8",
"8gv9",
"8gva",
"8gvc",
"8gve",
"8gvf",
"8gvh",
"8jni",
"8jnj"
] | 9 | [
"PUB00005997",
"PUB00005998",
"PUB00005999",
"PUB00006001",
"PUB00006002",
"PUB00006023",
"PUB00018713"
] | [
"2289848",
"2042971",
"9491367",
"2371270",
"8631828",
"9235899",
"9261985"
] | [
"Molecular biology of the anion exchanger gene family.",
"The band 3-related anion exchanger (AE) gene family.",
"The structure and function of band 3 (AE1): recent developments (review).",
"Functional expression and subcellular localization of an anion exchanger cloned from choroid plexus.",
"Three N-termi... | [
1990,
1991,
1997,
1990,
1996,
1997,
1997
] | 7 | [
"IPR001717"
] | [] | 1 | 0 | 1 | [
"Amniota"
] | [
510
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
9,
9
] | 3 | true | Family | Anion exchange protein 2 | Anion exchange protein 2 | Anion_exchange_2 | 2 |
IPR002980 | 2,980 | Sodium:neurotransmitter symporter, GABA, GAT-1 | Na/ntran_symport_GABA_GAT1 | Family | 2,203 | false | false | Neurotransmitter transport systems are integral to the release, re-uptake and recycling of neurotransmitters at synapses. High affinity transport proteins found in the plasma membrane of presynaptic nerve terminals and glial cells are responsible for the removal from the extracellular space of released-transmitters, th... | [
"GO:0005332",
"GO:0006836",
"GO:0005886",
"GO:0016020"
] | [
"gamma-aminobutyric acid:sodium:chloride symporter activity",
"neurotransmitter transport",
"plasma membrane",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS",
"CDD"
] | [
"PR01195",
"cd11506"
] | [
"GAT1TRNSPORT",
"SLC6sbd_GAT1"
] | [
2202,
515
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-442660",
"R-HSA-888593",
"R-MMU-442660",
"R-MMU-888593",
"R-RNO-442660",
"R-RNO-888593"
] | [
"REACTOME:R-HSA-442660",
"REACTOME:R-HSA-888593",
"REACTOME:R-MMU-442660",
"REACTOME:R-MMU-888593",
"REACTOME:R-RNO-442660",
"REACTOME:R-RNO-888593"
] | 6 | [
"7sk2",
"7y7v",
"7y7w",
"7y7y",
"7y7z",
"8gnk"
] | 6 | [
"PUB00001020",
"PUB00006006",
"PUB00006007",
"PUB00006008",
"PUB00006010",
"PUB00006011"
] | [
"15336049",
"8811182",
"8103691",
"7823024",
"8774941",
"7472524"
] | [
"Cloners quick on the uptake.",
"Molecular biology of mammalian amino acid transporters.",
"Neurotransmitter transporters: three distinct gene families.",
"Neurotransmitter transporters: three important gene families for neuronal function.",
"Localization of messenger RNAs encoding three GABA transporters i... | [
1992,
1996,
1993,
1994,
1995,
1995
] | 6 | [
"IPR000175"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
2203
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
8,
5,
3
] | 4 | true | Family | Sodium:neurotransmitter symporter, GABA, GAT-1 | Sodium:neurotransmitter symporter, GABA, GAT-1 | Na/ntran_symport_GABA_GAT1 | 3 |
IPR002981 | 2,981 | Sodium:neurotransmitter symporter, GABA, GAT-2 | Na/ntran_symport_GABA_GAT2 | Family | 654 | false | false | Neurotransmitter transport systems are integral to the release, re-uptake and recycling of neurotransmitters at synapses. High affinity transport proteins found in the plasma membrane of presynaptic nerve terminals and glial cells are responsible for the removal from the extracellular space of released-transmitters, th... | [
"GO:0005332",
"GO:0006836",
"GO:0005886",
"GO:0016020"
] | [
"gamma-aminobutyric acid:sodium:chloride symporter activity",
"neurotransmitter transport",
"plasma membrane",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01196"
] | [
"GAT2TRNSPORT"
] | [
654
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-442660",
"R-BTA-888593",
"R-HSA-442660",
"R-HSA-888593",
"R-MMU-442660",
"R-MMU-888593",
"R-RNO-442660",
"R-RNO-888593"
] | [
"REACTOME:R-BTA-442660",
"REACTOME:R-BTA-888593",
"REACTOME:R-HSA-442660",
"REACTOME:R-HSA-888593",
"REACTOME:R-MMU-442660",
"REACTOME:R-MMU-888593",
"REACTOME:R-RNO-442660",
"REACTOME:R-RNO-888593"
] | 8 | [] | 0 | [
"PUB00001020",
"PUB00006006",
"PUB00006007",
"PUB00006008",
"PUB00006010",
"PUB00006012"
] | [
"15336049",
"8811182",
"8103691",
"7823024",
"8774941",
"10379832"
] | [
"Cloners quick on the uptake.",
"Molecular biology of mammalian amino acid transporters.",
"Neurotransmitter transporters: three distinct gene families.",
"Neurotransmitter transporters: three important gene families for neuronal function.",
"Localization of messenger RNAs encoding three GABA transporters i... | [
1992,
1996,
1993,
1994,
1995,
1999
] | 6 | [
"IPR000175"
] | [] | 1 | 0 | 1 | [
"Amniota"
] | [
654
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
4
] | 3 | true | Family | Sodium:neurotransmitter symporter, GABA, GAT-2 | Sodium:neurotransmitter symporter, GABA, GAT-2 | Na/ntran_symport_GABA_GAT2 | 5 |
IPR002982 | 2,982 | Sodium:neurotransmitter symporter, GABA, GAT-3 | Na/ntran_symport_GABA_GAT3 | Family | 316 | false | false | GABA is the major inhibitory transmitter in the mammalian brain, and is widely distributed throughout the nervous system. Molecular cloning studies have resulted in the cloning of three Na + and Cl - -coupled GABA transporters (known as GAT-1, GAT-2, GAT-3) and a betaine/GABA transporter (BGT-1). Each transporter shows... | [
"GO:0005332",
"GO:0006836",
"GO:0005886",
"GO:0016020"
] | [
"gamma-aminobutyric acid:sodium:chloride symporter activity",
"neurotransmitter transport",
"plasma membrane",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS",
"CDD"
] | [
"PR01197",
"cd11508"
] | [
"GAT3TRNSPORT",
"SLC6sbd_GAT3"
] | [
299,
164
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-442660",
"R-HSA-71288",
"R-HSA-888593",
"R-MMU-442660",
"R-MMU-71288",
"R-MMU-888593",
"R-RNO-442660",
"R-RNO-71288",
"R-RNO-888593"
] | [
"REACTOME:R-HSA-442660",
"REACTOME:R-HSA-71288",
"REACTOME:R-HSA-888593",
"REACTOME:R-MMU-442660",
"REACTOME:R-MMU-71288",
"REACTOME:R-MMU-888593",
"REACTOME:R-RNO-442660",
"REACTOME:R-RNO-71288",
"REACTOME:R-RNO-888593"
] | 9 | [
"9cp4",
"9cp5",
"9lk7",
"9lk8",
"9lk9"
] | 5 | [
"PUB00001020",
"PUB00006006",
"PUB00006007",
"PUB00006008",
"PUB00006010"
] | [
"15336049",
"8811182",
"8103691",
"7823024",
"8774941"
] | [
"Cloners quick on the uptake.",
"Molecular biology of mammalian amino acid transporters.",
"Neurotransmitter transporters: three distinct gene families.",
"Neurotransmitter transporters: three important gene families for neuronal function.",
"Localization of messenger RNAs encoding three GABA transporters i... | [
1992,
1996,
1993,
1994,
1995
] | 5 | [
"IPR000175"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
316
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
2
] | 3 | true | Family | Sodium:neurotransmitter symporter, GABA, GAT-3 | Sodium:neurotransmitter symporter, GABA, GAT-3 | Na/ntran_symport_GABA_GAT3 | 2 |
IPR002983 | 2,983 | Sodium:neurotransmitter symporter, betaine | Na/ntran_symport_betaine | Family | 302 | false | false | Neurotransmitter transport systems are integral to the release, re-uptake and recycling of neurotransmitters at synapses. High affinity transport proteins found in the plasma membrane of presynaptic nerve terminals and glial cells are responsible for the removal from the extracellular space of released-transmitters, th... | [
"GO:0005332",
"GO:0006836",
"GO:0005886",
"GO:0016020"
] | [
"gamma-aminobutyric acid:sodium:chloride symporter activity",
"neurotransmitter transport",
"plasma membrane",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01198"
] | [
"BETTRANSPORT"
] | [
302
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CFA-352230",
"R-CFA-442660",
"R-CFA-71288",
"R-CFA-888593",
"R-HSA-352230",
"R-HSA-442660",
"R-HSA-71288",
"R-HSA-888593",
"R-MMU-352230",
"R-MMU-442660",
"R-MMU-71288",
"R-MMU-888593",
"R-RNO-352230",
"R-RNO-442660",
"R-RNO-71288",
"R-RNO-888593"
] | [
"REACTOME:R-CFA-352230",
"REACTOME:R-CFA-442660",
"REACTOME:R-CFA-71288",
"REACTOME:R-CFA-888593",
"REACTOME:R-HSA-352230",
"REACTOME:R-HSA-442660",
"REACTOME:R-HSA-71288",
"REACTOME:R-HSA-888593",
"REACTOME:R-MMU-352230",
"REACTOME:R-MMU-442660",
"REACTOME:R-MMU-71288",
"REACTOME:R-MMU-888593... | 16 | [] | 0 | [
"PUB00001020",
"PUB00006006",
"PUB00006007",
"PUB00006008",
"PUB00006013",
"PUB00006014"
] | [
"15336049",
"8811182",
"8103691",
"7823024",
"1365830",
"10358010"
] | [
"Cloners quick on the uptake.",
"Molecular biology of mammalian amino acid transporters.",
"Neurotransmitter transporters: three distinct gene families.",
"Neurotransmitter transporters: three important gene families for neuronal function.",
"Osmolytes.",
"Functional characterization of the Betaine/gamma-... | [
1992,
1996,
1993,
1994,
1992,
1999
] | 6 | [
"IPR000175"
] | [] | 1 | 0 | 1 | [
"Tetrapoda"
] | [
302
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
4,
5
] | 3 | true | Family | Sodium:neurotransmitter symporter, betaine | Sodium:neurotransmitter symporter, betaine | Na/ntran_symport_betaine | 8 |
IPR002984 | 2,984 | Sodium:neurotransmitter symporter, creatine | Na/ntran_symport_creatine | Family | 270 | false | false | Neurotransmitter transport systems are integral to the release, re-uptake and recycling of neurotransmitters at synapses. High affinity transport proteins found in the plasma membrane of presynaptic nerve terminals and glial cells are responsible for the removal from the extracellular space of released-transmitters, th... | [
"GO:0005309",
"GO:0006836",
"GO:0005886",
"GO:0016020"
] | [
"creatine:sodium symporter activity",
"neurotransmitter transport",
"plasma membrane",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01199"
] | [
"CRTTRANSPORT"
] | [
270
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-71288",
"R-HSA-71288",
"R-MMU-71288",
"R-RNO-71288"
] | [
"REACTOME:R-BTA-71288",
"REACTOME:R-HSA-71288",
"REACTOME:R-MMU-71288",
"REACTOME:R-RNO-71288"
] | 4 | [
"9kr7",
"9krh",
"9kri"
] | 3 | [
"PUB00001020",
"PUB00006006",
"PUB00006007",
"PUB00006008",
"PUB00006015",
"PUB00006016",
"PUB00006017"
] | [
"15336049",
"8811182",
"8103691",
"7823024",
"7896942",
"8297374",
"7953292"
] | [
"Cloners quick on the uptake.",
"Molecular biology of mammalian amino acid transporters.",
"Neurotransmitter transporters: three distinct gene families.",
"Neurotransmitter transporters: three important gene families for neuronal function.",
"In situ hybridization analysis of CHOT1, a creatine transporter, ... | [
1992,
1996,
1993,
1994,
1995,
1994,
1994
] | 7 | [
"IPR000175"
] | [] | 1 | 0 | 1 | [
"Mammalia"
] | [
270
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
5,
4
] | 3 | true | Family | Sodium:neurotransmitter symporter, creatine | Sodium:neurotransmitter symporter, creatine | Na/ntran_symport_creatine | 7 |
IPR002985 | 2,985 | Arginine decarboxylase | Arg_decrbxlase | Family | 9,939 | false | false | null | [
"GO:0008792",
"GO:0006527",
"GO:0008295"
] | [
"arginine decarboxylase activity",
"L-arginine catabolic process",
"spermidine biosynthetic process"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP",
"PIRSF",
"PRINTS",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_01417",
"PIRSF001336",
"PR01180",
"PTHR43295",
"TIGR01273",
"cd06830"
] | [
"SpeA",
"Arg_decrbxlase",
"ARGDCRBXLASE",
"",
"speA",
"PLPDE_III_ADC"
] | [
4703,
6924,
7784,
9937,
6889,
7806
] | 6 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.1.19",
"GenProp0642",
"GenProp1253",
"GenProp1282",
"GenProp1431",
"GenProp1733",
"PWY-40",
"PWY-43",
"PWY-6834"
] | [
"EC:4.1.1.19",
"GP:GenProp0642",
"GP:GenProp1253",
"GP:GenProp1282",
"GP:GenProp1431",
"GP:GenProp1733",
"METACYC:PWY-40",
"METACYC:PWY-43",
"METACYC:PWY-6834"
] | 9 | [
"3n2o",
"3nzp",
"3nzq"
] | 3 | [
"PUB00001452",
"PUB00003632",
"PUB00006119"
] | [
"8181483",
"3143046",
"8022938"
] | [
"Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.",
"Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary relationship with other amino acid decarboxylases.",
"Cloning of tomato (Lycopersicon esculentum Mill.) arginine decarboxylase gene and its expressio... | [
1994,
1988,
1993
] | 3 | [
"IPR000183"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
29,
8273,
1509,
128
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
8,
1,
7,
7
] | 4 | true | Family | Arginine decarboxylase | Arginine decarboxylase | Arg_decrbxlase | 4 |
IPR002986 | 2,986 | Diaminopimelate decarboxylase, LysA | DAP_deCOOHase_LysA | Family | 29,292 | false | false | Pyridoxal-dependent decarboxylases that act on ornithine-, lysine-, arginine- and related substrates can be classified into different families on the basis of sequence similarity [ , ]. One of these families includes ornithine decarboxylase (ODC), which catalyses the transformation of ornithine into putrescine; prokary... | [
"GO:0008836",
"GO:0009089"
] | [
"diaminopimelate decarboxylase activity",
"L-lysine biosynthetic process via diaminopimelate"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PRINTS",
"NCBIFAM",
"CDD"
] | [
"MF_02120",
"PR01181",
"TIGR01048",
"cd06828"
] | [
"LysA",
"DAPDCRBXLASE",
"lysA",
"PLPDE_III_DapDC"
] | [
24583,
28680,
25381,
27257
] | 4 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.1.20",
"GenProp0125",
"GenProp0788",
"PWY-2941",
"PWY-2942",
"PWY-5097"
] | [
"EC:4.1.1.20",
"GP:GenProp0125",
"GP:GenProp0788",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097"
] | 6 | [
"1hkv",
"1hkw",
"1knw",
"1ko0",
"1tuf",
"1twi",
"2j66",
"2o0t",
"2p3e",
"2qgh",
"2yxx",
"3c5q",
"3n2b",
"3vab",
"4xg1",
"5x7m",
"5x7n",
"6n2a",
"6n2f",
"7jpj",
"7ru7"
] | 21 | [
"PUB00001452",
"PUB00003632",
"PUB00006113",
"PUB00014556"
] | [
"8181483",
"3143046",
"8215365",
"12637582"
] | [
"Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.",
"Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary relationship with other amino acid decarboxylases.",
"Cloning and sequence analysis of the meso-diaminopimelate decarboxylase gene from Bacillus meth... | [
1994,
1988,
1993,
2003
] | 4 | [
"IPR000183"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
660,
26867,
1150,
615
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
1,
3,
8
] | 4 | true | Family | Diaminopimelate decarboxylase, LysA | Diaminopimelate decarboxylase, LysA | DAP_deCOOHase_LysA | 8 |
IPR002987 | 2,987 | Sodium/calcium exchanger, isoform 1 | NaCa_exhngr1 | Family | 907 | false | false | Na + /Ca 2+ exchange proteins are involved in maintaining Ca 2+ homeostasis in a wide variety of cell types. They are found in both the plasma membrane and intracellular organellar membranes, where they exchange Na + for Ca 2+ in an electrogenic manner. When located in the plasma membrane, they generally utilise the tr... | [
"GO:0005432",
"GO:0006816",
"GO:0016020"
] | [
"calcium:sodium antiporter activity",
"calcium ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01260"
] | [
"NACAEXCHNGR1"
] | [
907
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CFA-418359",
"R-CFA-425561",
"R-CFA-5578775",
"R-HSA-418359",
"R-HSA-425561",
"R-HSA-5578775",
"R-MMU-418359",
"R-MMU-425561",
"R-MMU-5578775",
"R-RNO-418359",
"R-RNO-425561",
"R-RNO-5578775"
] | [
"REACTOME:R-CFA-418359",
"REACTOME:R-CFA-425561",
"REACTOME:R-CFA-5578775",
"REACTOME:R-HSA-418359",
"REACTOME:R-HSA-425561",
"REACTOME:R-HSA-5578775",
"REACTOME:R-MMU-418359",
"REACTOME:R-MMU-425561",
"REACTOME:R-MMU-5578775",
"REACTOME:R-RNO-418359",
"REACTOME:R-RNO-425561",
"REACTOME:R-RNO-... | 12 | [
"8jp0",
"8sgi",
"8sgj",
"8sgt",
"9iv8"
] | 5 | [
"PUB00002973",
"PUB00005133"
] | [
"8798769",
"1700476"
] | [
"Cloning of a third mammalian Na+-Ca2+ exchanger, NCX3.",
"Molecular cloning and functional expression of the cardiac sarcolemmal Na(+)-Ca2+ exchanger."
] | [
1996,
1990
] | 2 | [
"IPR004836"
] | [] | 1 | 0 | 1 | [
"Tetrapoda"
] | [
907
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
10,
15
] | 3 | true | Family | Sodium/calcium exchanger, isoform 1 | Sodium/calcium exchanger, isoform 1 | NaCa_exhngr1 | 2 |
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