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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR022778 | 22,778 | CDKN3 domain | CDKN3 | Domain | 1,446 | false | false | This entry represents a domain found in cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates Cdk2 on threonine 160 in a cy... | [
"GO:0004721",
"GO:0004725"
] | [
"phosphoprotein phosphatase activity",
"protein tyrosine phosphatase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF05706"
] | [
"CDKN3"
] | [
1446
] | 1 | [
"EC",
"EC",
"REACTOME"
] | [
"3.1.3.16",
"3.1.3.48",
"R-DDI-8873719"
] | [
"EC:3.1.3.16",
"EC:3.1.3.48",
"REACTOME:R-DDI-8873719"
] | 3 | [
"1fpz",
"1fq1"
] | 2 | [
"PUB00011549",
"PUB00011550"
] | [
"8127873",
"10987270"
] | [
"KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases.",
"Aberrant transcripts of the cyclin-dependent kinase-associated protein phosphatase in hepatocellular carcinoma."
] | [
1994,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
126,
1320
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
17,
2,
4
] | 4 | true | Domain | CDKN3 domain | CDKN3 domain | CDKN3 | 6 |
IPR022780 | 22,780 | Dynein family light intermediate chain | Dynein_light_int_chain | Family | 7,483 | false | false | This entry consists of several eukaryotic dynein light intermediate chain proteins. The light intermediate chains (LICs) of cytoplasmic dynein consist of multiple isoforms, which undergo post-translational modification to produce a large number of species. DLIC1 is known to be involved in assembly, organisation, and fu... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF05783"
] | [
"DLIC"
] | [
7483
] | 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-5620924",
"R-DDI-6798695",
"R-DDI-6807878",
"R-DDI-9646399",
"R-GGA-141444",
"R-GGA-2467813",
"R-GGA-2500257",
"R-GGA-3371497",
"R-GGA-5663220",
"R-GGA-6798695",
"R-GGA-6807878",
"R-GGA-6811436",
"R-GGA-9646399",
"R-GGA-9648025",
"R-HSA-141444",
"R-HSA-2132295",
"R-HSA-2467813... | [
"REACTOME:R-BTA-5620924",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-6807878",
"REACTOME:R-DDI-9646399",
"REACTOME:R-GGA-141444",
"REACTOME:R-GGA-2467813",
"REACTOME:R-GGA-2500257",
"REACTOME:R-GGA-3371497",
"REACTOME:R-GGA-5663220",
"REACTOME:R-GGA-6798695",
"REACTOME:R-GGA-6807878",
"REACTOME... | 54 | [
"4w7g",
"6b9h",
"6f1t",
"6f1y",
"6f38",
"6f3a",
"6psd",
"6pse",
"6rlb",
"6sc2",
"7z8f",
"7z8i",
"7z8j",
"7z8k",
"7z8l",
"8pr0",
"8pr1",
"8pr2",
"8pr3",
"8ptk",
"8rgh",
"9bly",
"9dgq",
"9dgr",
"9dgt",
"9dgu",
"9e12",
"9e13",
"9e14",
"9e23",
"9e28"
] | 31 | [
"PUB00011311",
"PUB00019418",
"PUB00019419"
] | [
"11907264",
"10545494",
"10893222"
] | [
"Identification of a novel light intermediate chain (D2LIC) for mammalian cytoplasmic dynein 2.",
"Direct interaction of pericentrin with cytoplasmic dynein light intermediate chain contributes to mitotic spindle organization.",
"Light intermediate chain 1 defines a functional subfraction of cytoplasmic dynein ... | [
2002,
1999,
2000
] | 3 | [] | [
"IPR008467",
"IPR040045"
] | 0 | 2 | 0 | [
"Bacillota",
"Eukaryota",
"Mimiviridae sp. ChoanoV1"
] | [
4,
7478,
1
] | 3 | [
"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)"
] | [
3,
16,
4,
17,
9,
1,
19,
1
] | 8 | true | Family | Dynein family light intermediate chain | Dynein family light intermediate chain | Dynein_light_int_chain | 6 |
IPR022781 | 22,781 | Flagellar biosynthesis protein, FliO | Flagellar_biosynth_FliO | Family | 10,613 | false | false | FliO is an essential component of the flagellum-specific protein export apparatus [ ]. It is an integral membrane protein that acts as an assembly chaperone for the flagellar protein FliP. It is crucial, although not strictly required, for efficient FliP assembly and, thus flagellar assembly and function [ ]. FliO is a... | [
"GO:0044781",
"GO:0016020"
] | [
"bacterial-type flagellum organization",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"NCBIFAM"
] | [
"PF04347",
"TIGR03500"
] | [
"FliO",
"FliO_TIGR"
] | [
10613,
5805
] | 2 | [
"GP"
] | [
"GenProp0879"
] | [
"GP:GenProp0879"
] | 1 | [] | 0 | [
"PUB00009956",
"PUB00095779"
] | [
"10049367",
"28771474"
] | [
"Components of the Salmonella flagellar export apparatus and classification of export substrates.",
"A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum."
] | [
1999,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
10490,
7,
116
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flagellar biosynthesis protein, FliO | Flagellar biosynthesis protein, FliO | Flagellar_biosynth_FliO | 7 |
IPR022782 | 22,782 | Actin interacting protein 3-like, C-terminal | AIP3-like_C | Domain | 7,796 | false | false | This entry represents the C-terminal domain of actin interacting protein 3 (also known as Bud6 in budding yeasts). Bud6 is an actin- and formin-interacting protein. The N-terminal half of Bud6 is a microtubule binding domain required for its localisation and for its function in cortical capture of astral microtubule en... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03915"
] | [
"AIP3"
] | [
7796
] | 1 | [] | [] | [] | 0 | [
"3okq",
"3onx",
"4wyb"
] | 3 | [
"PUB00063966"
] | [
"23161908"
] | [
"Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6."
] | [
2012
] | 1 | [] | [
"IPR005613"
] | 0 | 1 | 0 | [
"Eukaryota",
"Haloferacaceae",
"Mycobacterium malmoense"
] | [
7790,
5,
1
] | 3 | [
"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,
120,
12,
11,
14,
1,
24,
1,
1
] | 9 | true | Domain | Actin interacting protein 3-like, C-terminal | Actin interacting protein 3-like, C-terminal | AIP3-like_C | 6 |
IPR022783 | 22,783 | GCF, C-terminal | GCFC_dom | Domain | 8,455 | false | false | This entry represents the C-terminal domain of GCF2 its homologues [ , ], as well as in a number of other proteins including Tuftelin-interacting protein 11 [ ]. While the function of the domain is unknown, some of the proteins it is found in are reported to be involved in pre-mRNA splicing [ , ]. This domain is also f... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07842"
] | [
"GCFC"
] | [
8455
] | 1 | [
"REACTOME"
] | [
"R-HSA-72163"
] | [
"REACTOME:R-HSA-72163"
] | 1 | [
"8ro0",
"8ro1",
"8ro2",
"9esh",
"9esi",
"9l5r"
] | 6 | [
"PUB00035473",
"PUB00077472",
"PUB00088153",
"PUB00088154",
"PUB00088155"
] | [
"11884525",
"22862948",
"24304693",
"19103666",
"25568310"
] | [
"Identification of septin-interacting proteins and characterization of the Smt3/SUMO-conjugation system in Drosophila.",
"Pax3/7BP is a Pax7- and Pax3-binding protein that regulates the proliferation of muscle precursor cells by an epigenetic mechanism.",
"Identification of a novel component C2ORF3 in the laria... | [
2002,
2012,
2014,
2009,
2015
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Paludifilum halophilum"
] | [
8454,
1
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (stra... | [
18,
3,
8,
4,
11,
7,
1,
15,
7,
1,
16
] | 11 | true | Domain | GCF, C-terminal | GCF, C-terminal | GCFC_dom | 7 |
IPR022784 | 22,784 | Ribosome biogenesis protein Alb1 | Ribosome_bgen_Alb1 | Family | 1,305 | false | false | Alb1 is a nuclear shuttling factor involved in ribosome biogenesis [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09135"
] | [
"Alb1"
] | [
1305
] | 1 | [] | [] | [] | 0 | [
"6ylg",
"6ylh",
"7ug6",
"7uoo",
"7uqb",
"7uqz",
"7v08",
"8hfr"
] | 8 | [
"PUB00035355"
] | [
"16651379"
] | [
"A functional network involved in the recycling of nucleocytoplasmic pre-60S factors."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1305
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
2,
1
] | 3 | true | Family | Ribosome biogenesis protein Alb1 | Ribosome biogenesis protein Alb1 | Ribosome_bgen_Alb1 | 7 |
IPR022787 | 22,787 | D-proline reductase (dithiol), PrdB protein | D_pro_red_PrdB | Family | 257 | false | false | Members of this family form the PrdB subunit, usually a selenoprotein, in the D-proline reductase complex. The usual pathway is conversion of L-protein to D-proline by a racemase, then use of D-proline as an electron acceptor coupled to ATP generation under anaerobic conditions [ ]. | [
"GO:0050002"
] | [
"D-proline reductase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR04483"
] | [
"D_pro_red_PrdB"
] | [
257
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00074344"
] | [
"23222730"
] | [
"Proline-dependent regulation of Clostridium difficile Stickland metabolism."
] | [
2013
] | 1 | [
"IPR010187"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"human gut metagenome"
] | [
256,
1
] | 2 | [] | [] | 0 | true | Family | D-proline reductase (dithiol), PrdB protein | D-proline reductase (dithiol), PrdB protein | D_pro_red_PrdB | 2 |
IPR022789 | 22,789 | Antitoxin ParD | ParD | Family | 9,789 | false | false | ParD is the antitoxin of a bacterial toxin-antitoxin gene pair. The cognate toxin is ParE in . The family contains several related antitoxins from Cyanobacteria, Proteobacteria and Actinobacteria. Antitoxins of this class carry an N-terminal ribbon-helix-helix domain, RHH, that is highly conserved across all type II ba... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"PF03693",
"PF09386",
"PTHR36582",
"TIGR02606"
] | [
"ParD_antitoxin",
"ParD",
"",
"antidote_CC2985"
] | [
8860,
410,
7916,
7311
] | 4 | [
"GP",
"GP"
] | [
"GenProp0321",
"GenProp0323"
] | [
"GP:GenProp0321",
"GP:GenProp0323"
] | 2 | [
"2an7",
"3kxe",
"5ceg",
"6x0a",
"7b22",
"7r5a",
"7ycs",
"7ycu",
"7ycv",
"7ycw",
"8c24"
] | 11 | [
"PUB00056596",
"PUB00061502",
"PUB00068089"
] | [
"15718296",
"20143871",
"20487277"
] | [
"Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes.",
"A conserved mode of protein recognition and binding in a ParD-ParE toxin-antitoxin complex.",
"Interaction specificity, toxicity and regulation of a paralogous set of ParE/RelE-family toxin-antitoxin systems."... | [
2005,
2010,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
13,
9645,
9,
7,
2,
113
] | 6 | [] | [] | 0 | true | Family | Antitoxin ParD | Antitoxin ParD | ParD | 2 |
IPR022790 | 22,790 | Glycosyl hydrolase family 26 domain | GH26_dom | Domain | 10,339 | false | false | This entry represents a domain found in the glycosyl hydrolase family 26 members. Glycoside hydrolases (GHs) play a critical role in both eukaryotes and prokaryotes, where they fulfill numerous important functions such as substrate acquisition and the remote remodelling of cell walls and the glycan decorations of glyco... | [
"GO:0004553"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF02156",
"PS51764"
] | [
"Glyco_hydro_26",
"GH26"
] | [
8819,
10287
] | 2 | [
"EC",
"METACYC"
] | [
"3.2.1.78",
"PWY-7456"
] | [
"EC:3.2.1.78",
"METACYC:PWY-7456"
] | 2 | [
"1gvy",
"1gw1",
"1j9y",
"1odz",
"1r7o",
"2bv9",
"2bvd",
"2bvt",
"2bvy",
"2cip",
"2cit",
"2ddx",
"2qha",
"2v3g",
"2vi0",
"2vx4",
"2vx5",
"2vx6",
"2vx7",
"2whk",
"2whm",
"2x2y",
"3cbw",
"3tp4",
"3vpl",
"3wdq",
"3wdr",
"3zm8",
"4cd4",
"4cd5",
"4yn5",
"4zxo"... | 51 | [
"PUB00037007",
"PUB00039771",
"PUB00039781",
"PUB00077754"
] | [
"11382747",
"15987675",
"16171384",
"20372022"
] | [
"Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding.",
"How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides: structure and activity of a Clostridium thermocellum lichenase, CtLic26A.",
"The structure and characte... | [
2001,
2005,
2005,
2010
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
87,
8814,
1348,
1,
89
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Glycosyl hydrolase family 26 domain | Glycosyl hydrolase family 26 domain | GH26_dom | 3 |
IPR022791 | 22,791 | Lysylphosphatidylglycerol synthetase/glycosyltransferase AglD | L-PG_synthase/AglD | Family | 32,868 | false | false | This family contains proteins involved in the addition of lysine to phosphatidylglycerol (lysylphosphatidylglycerol synthetase, L-PG synthase) [ ]. L-PG synthase produces lysyl-phosphatidylglycerol (L-PG), the major component of the bacterial membrane and responsible for its positive charge. L-PG synthesis contributes ... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF03706",
"TIGR00374"
] | [
"LPG_synthase_TM",
""
] | [
32849,
13695
] | 2 | [] | [] | [] | 0 | [
"9goe",
"9j8q",
"9j8r",
"9j8s"
] | 4 | [
"PUB00057883",
"PUB00057884",
"PUB00057886"
] | [
"17996897",
"20585355",
"14702396"
] | [
"Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer.",
"Identification of residues important for the activity of Haloferax volcanii AglD, a component of the archaeal N-glycosylation pathway.",
"Characterization of the Staphylococ... | [
2007,
2010,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
2077,
30055,
21,
2,
713
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
1
] | 2 | true | Family | Lysylphosphatidylglycerol synthetase/glycosyltransferase AglD | Lysylphosphatidylglycerol synthetase/glycosyltransferase AglD | L-PG_synthase/AglD | 5 |
IPR022792 | 22,792 | Type II secretion system protein GspN | T2SS_protein-GspN | Family | 3,342 | false | false | GspN is a cytoplasmic membrane component of the type II secretion system (T2SS). It is present in T2SS operons of a subset of Gram-negative speciesI, such as Aeromonas hydrophila (gene exeN); Erwinia carotovora (gene outN); Klebsiella pneumoniae (gene pulN); or Vibrio cholerae (gene epsN) [ ]. The size of the 'N' prote... | [
"GO:0015628",
"GO:0015627"
] | [
"protein secretion by the type II secretion system",
"type II protein secretion system complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF01203"
] | [
"T2SSN"
] | [
3342
] | 1 | [
"GP"
] | [
"GenProp0053"
] | [
"GP:GenProp0053"
] | 1 | [] | 0 | [
"PUB00051842",
"PUB00093998",
"PUB00094002",
"PUB00094004"
] | [
"19217396",
"30767847",
"28258547",
"22523076"
] | [
"Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.",
"Architecture, Function, and Substrates of the Type II Secretion System.",
"1H, 15N and 13C resonance assignments and secondary structure of PulG, the major pseudopilin from Klebsiella oxyt... | [
2009,
2019,
2017,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3282,
2,
58
] | 3 | [] | [] | 0 | true | Family | Type II secretion system protein GspN | Type II secretion system protein GspN | T2SS_protein-GspN | 6 |
IPR022793 | 22,793 | RNA polymerase I-specific transcription initiation factor Rrn10 | Rrn10 | Family | 1,155 | false | false | The protein Rrn10 has been identified as a component of the Upstream Activating Factor (UAF), an RNA polymerase I (pol I) specific transcription stimulatory factor [ ]. | [
"GO:0006360"
] | [
"transcription by RNA polymerase I"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF05234",
"PTHR28054"
] | [
"UAF_Rrn10",
""
] | [
248,
1142
] | 2 | [] | [] | [] | 0 | [
"7z0o"
] | 1 | [
"PUB00010432"
] | [
"12490702"
] | [
"Characterization of the fission yeast ribosomal DNA binding factor: components share homology with Upstream Activating Factor and with SWI/SNF subunits."
] | [
2002
] | 1 | [] | [
"IPR007898"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
1155
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Family | RNA polymerase I-specific transcription initiation factor Rrn10 | RNA polymerase I-specific transcription initiation factor Rrn10 | Rrn10 | 4 |
IPR022794 | 22,794 | Bul1, C-terminal | Bul1_C | Domain | 799 | false | false | This domain contains the C terminus of Saccharomyces cerevisiae Bul1 and Bul2. Bul1 binds the ubiquitin ligase Rsp5, via an N-terminal PPSY motif (157-160 in ) [ ]. The complex containing Bul1 and Rsp5 is involved in intracellular trafficking of the general amino acid permease Gap1 [ ], degradation of Rog1 in cooperati... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF04426"
] | [
"Bul1_C"
] | [
799
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009998",
"PUB00009999",
"PUB00010000",
"PUB00010116"
] | [
"9931424",
"10958669",
"10366593",
"11500494"
] | [
"The PY-motif of Bul1 protein is essential for growth of Saccharomyces cerevisiae under various stress conditions.",
"Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5.",
"A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisia... | [
1998,
2000,
1999,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
799
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
3
] | 1 | true | Domain | Bul1, C-terminal | Bul1, C-terminal | Bul1_C | 3 |
IPR022797 | 22,797 | Type III secretion system regulator LcrR/Chaperone CesD2 | LcrR/CesD2 | Family | 186 | false | false | LcrR proteins are encoded within type III secretion operons and have been characterised in Yersinia as a regulator of the Low-Calcium Response (LCR). CesD2 of enteropathogenic Escherichia coli is a chaperone for the Type III Secretion Translocator Protein EspD. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09621"
] | [
"LcrR"
] | [
186
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [
"IPR013405"
] | 0 | 1 | 0 | [
"Bacteria"
] | [
186
] | 1 | [] | [] | 0 | true | Family | Type III secretion system regulator LcrR/Chaperone CesD2 | Type III secretion system regulator LcrR/Chaperone CesD2 | LcrR/CesD2 | 8 |
IPR022798 | 22,798 | Cellulose synthase operon protein D, bacterial | BcsD_bac | Family | 868 | false | false | This entry represents Cellulose synthase operon protein D from Komagataeibacter xylinus and similar proteins from Proteobacteria. BcsD has been related with the level of crystalline structure of cellulose [ ]. The protein have a octamer pore-like structure with four inner passageways [ ]. An operon encoding 4 proteins ... | [
"GO:0030244"
] | [
"cellulose biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF03500"
] | [
"Cellsynth_D"
] | [
868
] | 1 | [] | [] | [] | 0 | [
"3a8e",
"3aj1",
"3aj2",
"7zzq",
"7zzy",
"8pkd",
"8poc",
"8pog"
] | 8 | [
"PUB00007624",
"PUB00008351",
"PUB00054683",
"PUB00100100"
] | [
"2146681",
"8901635",
"20921370",
"28573539"
] | [
"Genetic organization of the cellulose synthase operon in Acetobacter xylinum.",
"Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase.",
"Structure of bacterial cellulose synthase subunit D octamer with four inner passageways.",
"Enhancement of cryst... | [
1990,
1996,
2010,
2017
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"organismal metagenomes"
] | [
863,
5
] | 2 | [] | [] | 0 | true | Family | Cellulose synthase operon protein D, bacterial | Cellulose synthase operon protein D, bacterial | BcsD_bac | 4 |
IPR022800 | 22,800 | Spt4/RpoE2 zinc finger | Spt4/RpoE2_Znf | Domain | 5,225 | false | false | This entry consists of several eukaryotic transcription elongation Spt4 proteins as well as archaebacterial RpoE2 [ ]. Three transcription-elongation factors Spt4, Spt5, and Spt6 are conserved among eukaryotes and are essential for transcription via the modulation of chromatin structure. Spt4 and Spt5 are tightly assoc... | [] | [] | [] | 0 | [
"PFAM",
"SMART",
"CDD"
] | [
"PF06093",
"SM01389",
"cd07973"
] | [
"Spt4",
"Spt4",
"Spt4"
] | [
5221,
5060,
4131
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-112382",
"R-CEL-113418",
"R-CEL-674695",
"R-CEL-6796648",
"R-CEL-75955",
"R-DME-112382",
"R-DME-113418",
"R-DME-674695",
"R-DME-6796648",
"R-DME-6807505",
"R-DME-75955",
"R-DRE-674695",
"R-DRE-6796648",
"R-HSA-112382",
"R-HSA-113418",
"R-HSA-167152",
"R-HSA-167158",
"R-HSA-1... | [
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-113418",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-75955",
"REACTOME:R-DME-112382",
"REACTOME:R-DME-113418",
"REACTOME:R-DME-674695",
"REACTOME:R-DME-6796648",
"REACTOME:R-DME-6807505",
"REACTOME:R-DME-75955",
"REACTOME:R-DRE-67... | 40 | [
"1ryq",
"2exu",
"3h7h",
"3lpe",
"3p8b",
"3qqc",
"4zn1",
"4zn3",
"5oik",
"5xon",
"6gmh",
"6gml",
"6ir9",
"6j4w",
"6j4x",
"6j4y",
"6j4z",
"6j50",
"6j51",
"6ted",
"7nkx",
"7nky",
"7oky",
"7und",
"7wbv",
"7wbw",
"7wbx",
"7xn7",
"7xse",
"7xsx",
"7xsz",
"7xt7"... | 69 | [
"PUB00010582",
"PUB00012261",
"PUB00053827"
] | [
"8127719",
"11182892",
"19000817"
] | [
"A subunit of an archaeal DNA-dependent RNA polymerase contains the S1 motif.",
"Control of eukaryotic transcription elongation.",
"Core structure of the yeast spt4-spt5 complex: a conserved module for regulation of transcription elongation."
] | [
1994,
2001,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria candidate phyla",
"Eukaryota",
"Proteus phage Myduc",
"unclassified sequences"
] | [
877,
2,
4304,
1,
41
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
1,
1,
2,
3,
4,
1,
3,
6,
1,
1,
6
] | 12 | true | Domain | Spt4/RpoE2 zinc finger | Spt4/RpoE2 zinc finger | Spt4/RpoE2_Znf | 2 |
IPR022801 | 22,801 | Small ribosomal subunit protein uS4 | Ribosomal_uS4 | Family | 64,899 | false | false | This family includes the small ribosomal subunit protein uS4, also known as S9. U3 small nucleolar ribonucleoprotein protein IMP3, a component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP), is also included in this entry. It is required for the early cleavages during pre-18S ribosomal RNA processing [ ... | [
"GO:0019843"
] | [
"rRNA binding"
] | [
"molecular_function"
] | 1 | [
"PANTHER"
] | [
"PTHR11831"
] | [
""
] | [
64899
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-6791226",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-179933... | 98 | [
"1c05",
"1c06",
"1eg0",
"1fjg",
"1fka",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1qd7",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xmo"... | 1,834 | [
"PUB00001317",
"PUB00004390",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00095723",
"PUB00151110"
] | [
"9707415",
"2041737",
"11297922",
"11290319",
"11114498",
"12655004",
"34516797"
] | [
"The crystal structure of ribosomal protein S4 reveals a two-domain molecule with an extensive RNA-binding surface: one domain shows structural homology to the ETS DNA-binding motif.",
"Yeast ribosomal proteins: XII. YS11 of Saccharomyces cerevisiae is a homologue to E. coli S4 according to the gene analysis.",
... | [
1998,
1991,
2001,
2001,
2000,
2003,
2021
] | 7 | [] | [
"IPR005709",
"IPR005710"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctNZc11",
"unclassified sequences"
] | [
920,
24976,
38479,
1,
523
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
19,
2,
2,
4,
1,
8,
7,
3,
21,
7,
4,
4,
38
] | 13 | true | Family | Small ribosomal subunit protein uS4 | Small ribosomal subunit protein uS4 | Ribosomal_uS4 | 5 |
IPR022802 | 22,802 | Small ribosomal subunit protein uS4, archaea | Ribosomal_uS4_arc | Family | 905 | false | false | This entry represents archaeal ribosomal S4 proteins, also known as uS4. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain... | [
"GO:0019843",
"GO:0006412"
] | [
"rRNA binding",
"translation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_01306_A"
] | [
"Ribosomal_uS4_A"
] | [
905
] | 1 | [] | [] | [] | 0 | [
"4v4n",
"4v6u",
"5jb3",
"5jbh",
"6skf",
"6skg",
"6sw9",
"6swc",
"6swd",
"6th6",
"6tmf",
"7zag",
"7zah",
"7zai",
"7zhg",
"8hkx",
"8hky",
"8hkz",
"8hl1",
"8hl2",
"8hl3",
"8hl4",
"8hl5",
"8wkp",
"8wq2",
"8wq4",
"9e71",
"9e7f",
"9fhl",
"9fny",
"9fnz",
"9fo0"... | 43 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [
"IPR005710"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Geodia barretti",
"unclassified sequences",
"uncultured marine bacterium MedDCM-OCT-S05-C222"
] | [
876,
1,
27,
1
] | 4 | [] | [] | 0 | true | Family | Small ribosomal subunit protein uS4, archaea | Small ribosomal subunit protein uS4, archaea | Ribosomal_uS4_arc | 7 |
IPR022803 | 22,803 | Large ribosomal subunit protein uL5 domain superfamily | Ribosomal_uL5_dom_sf | Homologous_superfamily | 38,348 | false | false | This superfamily represents the structural domain of uL5, which forms a 2 layer, mainly antiparallel β-sheet. Large ribosomal subunit protein uL5, previously known as Ribosomal protein L5, is ~180 amino acids in length. In Escherichia coli, uL5 is known to be involved in binding 5S RNA to the large ribosomal subunit [ ... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.30.1440.10",
"SSF55282"
] | [
"",
""
] | [
38277,
38310
] | 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-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",
"R-DDI-975956",
"R-DDI-975957",
"R-DME-156827",
"R-DME-1799339",
"R-DME-72689",
"R-DME-72706",
"R-DME-975956",
"R-DME-975957... | [
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-975956",
"REACTOME:R-CEL-975957",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-1799339",
"REACTOME:R-DDI-72689",
"REACTOME:R-DDI-72706",
"REACTOME:R-DDI-975956",
"REACTOME:R-DDI-97595... | 57 | [
"1ffk",
"1iq4",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1mji",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9"... | 1,756 | [
"PUB00000599",
"PUB00000693",
"PUB00001802",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00104042"
] | [
"2198942",
"1840500",
"2016059",
"11297922",
"11290319",
"11114498",
"11866091"
] | [
"Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui.",
"The structure of the gene for ribosomal protein L5 in the archaebacterium Sulfolobus acidocaldarius.",
"Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21... | [
1990,
1991,
1991,
2001,
2001,
2000,
2002
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2567,
23784,
11444,
553
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
15,
3,
1,
3,
1,
4,
3,
2,
15,
5,
3,
3,
52
] | 13 | true | Homologous_superfamily | Large ribosomal subunit protein uL5 domain superfamily | Large ribosomal subunit protein uL5 domain superfamily | Ribosomal_uL5_dom_sf | 7 |
IPR022804 | 22,804 | Large ribosomal subunit protein uL5, archaea | Ribosomal_uL5_arc | Family | 873 | false | false | This entry represents the archaeal uL5 proteins. Large ribosomal subunit protein uL5, previously known as Ribosomal protein L5, is ~180 amino acids in length. In Escherichia coli, uL5 is known to be involved in binding 5S RNA to the large ribosomal subunit [ ]. Ribosomes are the particles that catalyse mRNA-directed pr... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP"
] | [
"MF_01333_A"
] | [
"Ribosomal_uL5_A"
] | [
873
] | 1 | [] | [] | [] | 0 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp"... | 98 | [
"PUB00000599",
"PUB00000693",
"PUB00001802",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00104042"
] | [
"2198942",
"1840500",
"2016059",
"11297922",
"11290319",
"11114498",
"11866091"
] | [
"Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui.",
"The structure of the gene for ribosomal protein L5 in the archaebacterium Sulfolobus acidocaldarius.",
"Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21... | [
1990,
1991,
1991,
2001,
2001,
2000,
2002
] | 7 | [
"IPR057266"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Fungi",
"ecological metagenomes"
] | [
862,
3,
8
] | 3 | [] | [] | 0 | true | Family | Large ribosomal subunit protein uL5, archaea | Large ribosomal subunit protein uL5, archaea | Ribosomal_uL5_arc | 6 |
IPR022805 | 22,805 | Phosphoenolpyruvate carboxylase, bacterial/plant-type | PEP_COase_bac/pln-type | Family | 14,949 | false | false | Phosphoenolpyruvate carboxylase (PEPCase), an enzyme found in all multicellular plants, catalyses the formation of oxaloacetate from phosphoenolpyruvate (PEP) and a hydrocarbonate ion [ ]. This reaction is harnessed by C4 plants to capture and concentrate carbon dioxide into the photosynthetic bundle sheath cells. It a... | [
"GO:0008964",
"GO:0006099",
"GO:0015977"
] | [
"phosphoenolpyruvate carboxylase activity",
"tricarboxylic acid cycle",
"carbon fixation"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP"
] | [
"MF_00595"
] | [
"PEPcase_type1"
] | [
14949
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.1.31",
"PWY-1622",
"PWY-241",
"PWY-5913",
"PWY-6142",
"PWY-6146",
"PWY-6549",
"PWY-7115",
"PWY-7117",
"PWY-7124"
] | [
"EC:4.1.1.31",
"METACYC:PWY-1622",
"METACYC:PWY-241",
"METACYC:PWY-5913",
"METACYC:PWY-6142",
"METACYC:PWY-6146",
"METACYC:PWY-6549",
"METACYC:PWY-7115",
"METACYC:PWY-7117",
"METACYC:PWY-7124"
] | 10 | [
"1fiy",
"1jqn",
"1jqo",
"1qb4",
"3zgb",
"3zge",
"4bxc",
"4bxh",
"5fdn",
"5vyj",
"6mgi",
"6u2t",
"6v3o",
"8cj5",
"8cj8",
"8oj9",
"8oje",
"8ojf",
"8ojq",
"8ojy",
"8ojz",
"8qtm",
"8qx1",
"8qx3"
] | 24 | [
"PUB00003734",
"PUB00003752",
"PUB00004559",
"PUB00004561"
] | [
"2779518",
"1508152",
"1421147",
"1450389"
] | [
"The phosphoenolpyruvate carboxylase gene of Corynebacterium glutamicum: molecular cloning, nucleotide sequence, and expression.",
"Homologous genes for the C4 isoform of phosphoenolpyruvate carboxylase in a C3 and a C4 Flaveria species.",
"Alfalfa root nodule phosphoenolpyruvate carboxylase: characterization o... | [
1989,
1992,
1992,
1992
] | 4 | [
"IPR021135"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
11851,
2635,
311,
152
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
1,
17,
24
] | 4 | true | Family | Phosphoenolpyruvate carboxylase, bacterial/plant-type | Phosphoenolpyruvate carboxylase, bacterial/plant-type | PEP_COase_bac/pln-type | 7 |
IPR022812 | 22,812 | Dynamin | Dynamin | Family | 50,156 | false | false | Membrane transport between compartments in eukaryotic cells requires proteins that allow the budding and scission of nascent cargo vesicles from one compartment and their targeting and fusion with another. Dynamins are large GTPases that belong to a protein superfamily [ ] that, in eukaryotic cells, includes classical ... | [] | [] | [] | 0 | [
"PRINTS",
"PANTHER"
] | [
"PR00195",
"PTHR11566"
] | [
"DYNAMIN",
""
] | [
44973,
48731
] | 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-1169408",
"R-BTA-166016",
"R-BTA-190873",
"R-BTA-196025",
"R-BTA-2132295",
"R-BTA-437239",
"R-BTA-75153",
"R-BTA-8856828",
"R-CEL-190873",
"R-CEL-196025",
"R-CEL-3928665",
"R-CEL-432720",
"R-CEL-432722",
"R-CEL-437239",
"R-CEL-75153",
"R-CEL-8856828",
"R-CFA-1169408",
"R-DDI... | [
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-190873",
"REACTOME:R-BTA-196025",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-437239",
"REACTOME:R-BTA-75153",
"REACTOME:R-BTA-8856828",
"REACTOME:R-CEL-190873",
"REACTOME:R-CEL-196025",
"REACTOME:R-CEL-3928665",
"REACTOME:R-CEL-... | 79 | [
"1jwy",
"1jx2",
"2aka",
"2x2e",
"2x2f",
"3l43",
"3ljb",
"3snh",
"3szr",
"3t34",
"3t35",
"3w6n",
"3w6o",
"3w6p",
"3zvr",
"3zyc",
"3zys",
"4bej",
"4h1u",
"4h1v",
"4p4s",
"4p4t",
"4p4u",
"4uud",
"4uuk",
"4whj",
"4x0r",
"5a3f",
"5d3q",
"5gtm",
"5owv",
"5oxf"... | 72 | [
"PUB00000075",
"PUB00000836",
"PUB00001910",
"PUB00003186",
"PUB00014977"
] | [
"2142876",
"2112425",
"1532158",
"2607176",
"15040446"
] | [
"Motor proteins of cytoplasmic microtubules.",
"A putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting.",
"Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin.",
... | [
1990,
1990,
1992,
1989,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermoproteati",
"Viruses",
"metagenomes"
] | [
231,
49885,
4,
26,
10
] | 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... | [
73,
4,
98,
22,
85,
49,
8,
49,
58,
3,
3,
128
] | 12 | true | Family | Dynamin | Dynamin | Dynamin | 6 |
IPR022813 | 22,813 | Protein-export membrane protein SecD/SecF, archaeal and bacterial | SecD/SecF_arch_bac | Family | 46,767 | false | false | This entry represents archaeal and bacterial SecD and SecF protein export membrane proteins and their archaeal homologues [ ]. It is found in association with SecD and SecF proteins are part of the multimeric protein export complex comprising SecA, D, E, F, G, Y, and YajC [ ]. SecD and SecF are required to maintain a p... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR30081"
] | [
""
] | [
46767
] | 1 | [
"REACTOME"
] | [
"R-HSA-1222387"
] | [
"REACTOME:R-HSA-1222387"
] | 1 | [
"3aqo",
"3aqp",
"5mg3",
"5xam",
"5xan",
"5xap",
"5yhf"
] | 7 | [
"PUB00007064",
"PUB00007065",
"PUB00007066",
"PUB00007187",
"PUB00008120",
"PUB00020319",
"PUB00053868"
] | [
"2202721",
"11336818",
"10418149",
"12167867",
"9694879",
"8112309",
"16452406"
] | [
"The sec and prl genes of Escherichia coli.",
"SecB, a molecular chaperone with two faces.",
"Effects of pre-protein overexpression on SecB synthesis in Escherichia coli.",
"Three-dimensional structure of the bacterial protein-translocation complex SecYEG.",
"SecDF of Bacillus subtilis, a molecular Siamese ... | [
1990,
2001,
1999,
2002,
1998,
1994,
2006
] | 7 | [] | [
"IPR022645",
"IPR024912",
"IPR024921"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctJ0s2",
"unclassified sequences"
] | [
1318,
44054,
109,
1,
1285
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | Protein-export membrane protein SecD/SecF, archaeal and bacterial | Protein-export membrane protein SecD/SecF, archaeal and bacterial | SecD/SecF_arch_bac | 8 |
IPR022815 | 22,815 | Protease inhibitor | Inh | Family | 601 | false | false | This family of proteins represent monomeric serralysin inhibitors of about 125 residues, which interact with specific metalloprotease which are synthesised by serralysin secretors and characterised by being plant, insect and animal pathogens. It is probable that the serralysin inhibitors protect the host from proteolys... | [
"GO:0008191",
"GO:0010951"
] | [
"metalloendopeptidase inhibitor activity",
"negative regulation of endopeptidase activity"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR01274"
] | [
"MPTASEINHBTR"
] | [
601
] | 1 | [] | [] | [] | 0 | [
"1jiw",
"1smp",
"2rn4"
] | 3 | [
"PUB00000545",
"PUB00005013",
"PUB00006323",
"PUB00015040"
] | [
"8761444",
"7684291",
"7752231",
"10770939"
] | [
"The lipocalin protein family: structure and function.",
"Structure and sequence relationships in the lipocalins and related proteins.",
"Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi.",
"Alkaline proteinase inhibitor of Pseudomonas aeru... | [
1996,
1993,
1995,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
601
] | 1 | [] | [] | 0 | true | Family | Protease inhibitor | Protease inhibitor | Inh | 1 |
IPR022816 | 22,816 | Condensin complex subunit 2/barren | Condensin_barren_su2 | Family | 5,629 | false | false | This entry represents eukaryotic condensin complex subunit 2 proteins. Included in this group are several Barren protein homologues from several eukaryotic organisms. In Drosophila Barren (barr) is required for sister-chromatid segregation in mitosis. barr encodes a novel protein that is present in proliferating cells ... | [
"GO:0007076",
"GO:0000796"
] | [
"mitotic chromosome condensation",
"condensin complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF05786",
"PIRSF017126",
"PTHR13108"
] | [
"Cnd2",
"Condensin_H",
""
] | [
5569,
3542,
5559
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2514853",
"R-MMU-2514853",
"R-SCE-2514853",
"R-SPO-2514853"
] | [
"REACTOME:R-HSA-2514853",
"REACTOME:R-MMU-2514853",
"REACTOME:R-SCE-2514853",
"REACTOME:R-SPO-2514853"
] | 4 | [
"5oqn",
"5oqo",
"5oqp",
"5oqq",
"5oqr",
"6igx",
"6q6e",
"6qj2",
"6qj3",
"6qj4",
"6yvd",
"6yvu",
"6yvv",
"7q2x",
"7q2y",
"7q2z",
"7qen",
"7qfw"
] | 18 | [
"PUB00011266"
] | [
"8978614"
] | [
"Chromatid segregation at anaphase requires the barren product, a novel chromosome-associated protein that interacts with Topoisomerase II."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5629
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
5,
1,
2,
7,
2,
1,
4,
4,
1,
1,
9
] | 11 | true | Family | Condensin complex subunit 2/barren | Condensin complex subunit 2/barren | Condensin_barren_su2 | 2 |
IPR022818 | 22,818 | Photosystem I Ycf3, assembly | PSI_Ycf3_assembly | Family | 13,991 | false | false | Photosystem I (PSI) is a large protein complex embedded within the photosynthetic thylakoid membrane formed by a core complex, peripheral light-harvesting complexes (LHCIs) and cofactors. It consists of 15 core and 4 LHCI subunits, ~150 chlorophylls (a and b) molecules, 2 phylloquinones, and 3 Fe4S4-clusters [ ]. The t... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00439",
"NF002725"
] | [
"Ycf3",
"PRK02603.1"
] | [
13413,
13991
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009534",
"PUB00014955",
"PUB00015098",
"PUB00015099",
"PUB00015100",
"PUB00015101",
"PUB00096753"
] | [
"9321389",
"10806238",
"11418848",
"9045660",
"9314531",
"10103064",
"29934511"
] | [
"The chloroplast ycf3 and ycf4 open reading frames of Chlamydomonas reinhardtii are required for the accumulation of the photosystem I complex.",
"The BtpA protein stabilizes the reaction center proteins of photosystem I in the cyanobacterium Synechocystis sp. PCC 6803 at low temperature.",
"Three-dimensional s... | [
1997,
2000,
2001,
1997,
1997,
1999,
2018
] | 7 | [] | [] | 0 | 0 | null | [
"Cyanobacteriota",
"Eukaryota"
] | [
370,
13621
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
5,
3,
2
] | 3 | true | Family | Photosystem I Ycf3, assembly | Photosystem I Ycf3, assembly | PSI_Ycf3_assembly | 1 |
IPR022819 | 22,819 | Poxvirus Bcl-2-like | Poxvirus_Bcl-2-like | Family | 857 | false | false | This family represents a group of Poxvirus Bcl-2-like proteins that function as immunomodulators to evade the host innate immune response through the inhibition of apoptosis or blocking the activation of pro-inflammatory transcription factors, such as interferon (IFN) regulatory factor-3 (IRF-3) and nuclear factor-kapp... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06227"
] | [
"Poxv_Bcl-2-like"
] | [
857
] | 1 | [] | [] | [] | 0 | [
"2i39",
"2k36",
"2uxe",
"2vvw",
"2vvx",
"2vvy",
"3jrv",
"4bbb",
"4bbc",
"4bbd",
"4lqk",
"4m0s",
"8xy1",
"8xy2",
"8xy3",
"8xy4"
] | 16 | [
"PUB00061428",
"PUB00062445",
"PUB00097497",
"PUB00097498",
"PUB00097499",
"PUB00097500",
"PUB00097501"
] | [
"19913487",
"22194685",
"27907166",
"23138003",
"29748387",
"27973613",
"23761407"
] | [
"Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7.",
"Inhibition of apoptosis and NF-κB activation by vaccinia protein N1 occur via distinct binding surfaces and make different contributions to virulence.",
"Vaccinia Virus Protein C6 Inhibits Type I IFN Signalling in the Nucleus ... | [
2009,
2011,
2016,
2013,
2018,
2016,
2013
] | 7 | [] | [
"IPR008724",
"IPR009174",
"IPR009353",
"IPR011212"
] | 0 | 4 | 0 | [
"Chordopoxvirinae",
"Chryseobacterium hagamense"
] | [
856,
1
] | 2 | [] | [] | 0 | true | Family | Poxvirus Bcl-2-like | Poxvirus Bcl-2-like | Poxvirus_Bcl-2-like | 5 |
IPR022820 | 22,820 | Uncharacterised protein family UPF0758, YicR subfamily | UPF0758_YicR | Family | 1,135 | false | false | UPF0758 was previously known as the radC family. The name was assigned according to the radC102 mutant of E. coli which was later demonstrated to be an allele of the transcription-repair-coupling factor recG [ , ]. It has been described as a putative JAMM-family deubiquitinating enzyme, but its function remains to be d... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00018"
] | [
"UPF0758_YicR"
] | [
1135
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00037483",
"PUB00044698",
"PUB00044699"
] | [
"14737182",
"11053371",
"18556794"
] | [
"JAMM: a metalloprotease-like zinc site in the proteasome and signalosome.",
"radC102 of Escherichia coli is an allele of recG.",
"RadC, a misleading name?"
] | [
2004,
2000,
2008
] | 3 | [
"IPR001405"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota"
] | [
1135
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Uncharacterised protein family UPF0758, YicR subfamily | Uncharacterised protein family UPF0758, YicR subfamily | UPF0758_YicR | 7 |
IPR022821 | 22,821 | HTH-type transcriptional regulator MurR | Tscrpt_reg_HTH_MurR | Family | 169 | false | false | This entry contains MurR, which represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid (MurNAc). It binds to two adjacent inverted repeats within the operator region. MurNAc 6-phosphate and GlcNAc-6-phosphate can bind to MurR and weaken the DNA binding ability of Mur... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_02108",
"NF012026"
] | [
"HTH_type_MurR",
"PRK15482.1"
] | [
156,
169
] | 2 | [] | [] | [] | 0 | [
"7en5",
"7en6",
"7en7"
] | 3 | [
"PUB00053898",
"PUB00151033"
] | [
"18723630",
"35640608"
] | [
"The transcriptional factors MurR and catabolite activator protein regulate N-acetylmuramic acid catabolism in Escherichia coli.",
"Molecular basis for cell-wall recycling regulation by transcriptional repressor MurR in Escherichia coli."
] | [
2008,
2022
] | 2 | [
"IPR047640"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
169
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | HTH-type transcriptional regulator MurR | HTH-type transcriptional regulator MurR | Tscrpt_reg_HTH_MurR | 9 |
IPR022822 | 22,822 | Lactate utilization protein A | LutA | Family | 874 | false | false | This entry represents lactate utilization protein A, which is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. | [
"GO:0006089"
] | [
"lactate metabolic process"
] | [
"biological_process"
] | 1 | [
"HAMAP"
] | [
"MF_02105"
] | [
"LutA"
] | [
874
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
874
] | 1 | [] | [] | 0 | true | Family | Lactate utilization protein A | Lactate utilization protein A | LutA | 5 |
IPR022823 | 22,823 | Lactate utilization protein C | LutC | Family | 829 | false | false | This entry represents lactate utilization protein C, which is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source [ ]. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_02104"
] | [
"LutC"
] | [
829
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053899"
] | [
"19201793"
] | [
"A widely conserved gene cluster required for lactate utilization in Bacillus subtilis and its involvement in biofilm formation."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
829
] | 1 | [] | [] | 0 | true | Family | Lactate utilization protein C | Lactate utilization protein C | LutC | 8 |
IPR022824 | 22,824 | Multidrug resistance protein MdtA | Multidrug-R_MdtA | Family | 1,524 | false | false | This entry represents the multidrug resistance protein MdtA. MdtA is one subunit of the MdtABC tripartite complex which is a RND-type drug exporter. The complex consists of MdtB/C, which form a transmembrane heteromultimer and MdtA which is a membrane fusion protein [ ]. The mdtABC complex confers resistance against no... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_01422"
] | [
"MdtA"
] | [
1524
] | 1 | [
"REACTOME"
] | [
"R-HSA-9638334"
] | [
"REACTOME:R-HSA-9638334"
] | 1 | [] | 0 | [
"PUB00053900",
"PUB00053915"
] | [
"12107133",
"12107134"
] | [
"The putative response regulator BaeR stimulates multidrug resistance of Escherichia coli via a novel multidrug exporter system, MdtABC.",
"The baeSR two-component regulatory system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobi... | [
2002,
2002
] | 2 | [
"IPR006143"
] | [] | 1 | 0 | 1 | [
"Beauveria bassiana D1-5",
"Pseudomonadota"
] | [
1,
1523
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Multidrug resistance protein MdtA | Multidrug resistance protein MdtA | Multidrug-R_MdtA | 7 |
IPR022825 | 22,825 | Lactate utilization protein B | LutB | Family | 789 | false | false | This entry represents lactate utilization protein B, which is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source [ ]. It is thought to function as an electron transporter during oxidation of L-lactate. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_02103"
] | [
"LutB"
] | [
789
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053899"
] | [
"19201793"
] | [
"A widely conserved gene cluster required for lactate utilization in Bacillus subtilis and its involvement in biofilm formation."
] | [
2009
] | 1 | [
"IPR004452"
] | [] | 1 | 0 | 1 | [
"Bacillales"
] | [
789
] | 1 | [] | [] | 0 | true | Family | Lactate utilization protein B | Lactate utilization protein B | LutB | 4 |
IPR022826 | 22,826 | 3-deoxy-D-manno-octulosonic acid kinase | KDO_kinase | Family | 2,084 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0016773"
] | [
"phosphotransferase activity, alcohol group as acceptor"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00521",
"NF002475"
] | [
"KDO_kinase",
"PRK01723.1"
] | [
2071,
2083
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.1.166",
"PWY-7675",
"PWY-7676",
"PWY-8284"
] | [
"EC:2.7.1.166",
"METACYC:PWY-7675",
"METACYC:PWY-7676",
"METACYC:PWY-8284"
] | 4 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00019761",
"PUB00020114",
"PUB00034898",
"PUB00034899"
] | [
"3291115",
"12368087",
"10531340",
"12471243",
"15078142",
"15320712"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"A Haemophilus influenzae gene that encodes a membrane bound 3-deoxy-D-manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo phosphorylation in ... | [
1988,
2002,
1999,
2002,
2004,
2004
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Knufia peltigerae",
"metagenomes"
] | [
2047,
1,
36
] | 3 | [] | [] | 0 | true | Family | 3-deoxy-D-manno-octulosonic acid kinase | 3-deoxy-D-manno-octulosonic acid kinase | KDO_kinase | 6 |
IPR022827 | 22,827 | Phycoerythrobilin:ferredoxin oxidoreductase | Phycoerythrobilin_Fdx_Rdtase | Family | 140 | false | false | This entry represents bacterial phycoerythrobilin:ferredoxin oxidoreductases. They are involved in the biosynthesis of photosynthetic antennae of cyanobacteria. | [
"GO:0050618",
"GO:0010024"
] | [
"phycoerythrobilin:ferredoxin oxidoreductase activity",
"phytochromobilin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_00793"
] | [
"PebB"
] | [
140
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.3.7.3",
"PWY-5915",
"PWY-7579"
] | [
"EC:1.3.7.3",
"METACYC:PWY-5915",
"METACYC:PWY-7579"
] | 3 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR009249"
] | [] | 1 | 0 | 1 | [
"Cyanobacteriota",
"Rhodophyta"
] | [
137,
3
] | 2 | [] | [] | 0 | true | Family | Phycoerythrobilin:ferredoxin oxidoreductase | Phycoerythrobilin:ferredoxin oxidoreductase | Phycoerythrobilin_Fdx_Rdtase | 7 |
IPR022828 | 22,828 | Thiazole biosynthetic enzyme, prokaryotic | Thi4_prok | Family | 1,113 | false | false | This entry represents bacterial and archaeal proteins related to eukaryotic THI4, involved in the biosynthesis of the thiamine precursor thiazole. Archaea harbour structural homologues of both the bacterial (ThiS-ThiF) and eukaryotic (THI4) proteins for thiazole synthesis. Most archaea have homologues that cluster to t... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00304"
] | [
"Thi4"
] | [
1113
] | 1 | [
"EC",
"METACYC"
] | [
"2.4.2.59",
"PWY-8308"
] | [
"EC:2.4.2.59",
"METACYC:PWY-8308"
] | 2 | [
"4y4m",
"4y4n",
"6hk1",
"7rk0"
] | 4 | [
"PUB00059231",
"PUB00072882"
] | [
"15375115",
"25348237"
] | [
"Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea.",
"Conserved active site cysteine residue of archaeal THI4 homolog is essential for thiamine biosynthesis in Haloferax volcanii."
] | [
2004,
2014
] | 2 | [
"IPR002922"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"unclassified sequences"
] | [
722,
368,
23
] | 3 | [] | [] | 0 | true | Family | Thiazole biosynthetic enzyme, prokaryotic | Thiazole biosynthetic enzyme, prokaryotic | Thi4_prok | 8 |
IPR022829 | 22,829 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase | DHNA_CoA_hydrolase | Family | 341 | false | false | This entry contains 1,4-dihydroxy-2-naphthoyl-CoA hydrolase, which catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA), a reaction involved in phylloquinone (vitamin K1) biosynthesis. | [
"GO:0016790"
] | [
"thiolester hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_02101"
] | [
"DHNA_CoA_hydrolase"
] | [
341
] | 1 | [
"EC",
"METACYC"
] | [
"3.1.2.28",
"PWY-5837"
] | [
"EC:3.1.2.28",
"METACYC:PWY-5837"
] | 2 | [
"2hx5",
"4k00"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Paulinella",
"mine drainage metagenome"
] | [
336,
4,
1
] | 3 | [] | [] | 0 | true | Family | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase | DHNA_CoA_hydrolase | 3 |
IPR022830 | 22,830 | Indigoidine synthase A-like | Indigdn_synthA-like | Homologous_superfamily | 10,487 | false | false | The crystal structure of indigoidine synthase A (IndA)-like protein (TM1464) from Thermotoga maritima represents a new fold [ ]. This protein has been shown to act also as a pseudouridine-5'-phosphate glycosidase [ ]. | [
"GO:0004730"
] | [
"pseudouridylate synthase activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.40.1790.10",
"SSF110581"
] | [
"",
""
] | [
10481,
10477
] | 2 | [
"EC",
"METACYC"
] | [
"4.2.1.70",
"PWY-6019"
] | [
"EC:4.2.1.70",
"METACYC:PWY-6019"
] | 2 | [
"1vkm",
"4ex8",
"4ex9",
"4gij",
"4gik",
"4gil",
"4gim",
"8k05",
"8k06",
"8k07"
] | 10 | [
"PUB00032105",
"PUB00068113"
] | [
"15822122",
"18591240"
] | [
"Crystal structure of an indigoidine synthase A (IndA)-like protein (TM1464) from Thermotoga maritima at 1.90 A resolution reveals a new fold.",
"Molecular identification of pseudouridine-metabolizing enzymes."
] | [
2005,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanocrinis alkalitolerans",
"Eukaryota",
"metagenomes"
] | [
6030,
1,
4251,
205
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
... | [
7,
1,
2,
2,
1,
1,
5,
1,
11
] | 9 | true | Homologous_superfamily | Indigoidine synthase A-like | Indigoidine synthase A-like | Indigdn_synthA-like | 1 |
IPR022831 | 22,831 | Multidrug resistance protein MdtB | Multidrug-R_MdtB | Family | 1,715 | false | false | This entry represents the multidrug resistance protein MdtB. MdtA is one subunit of the MdtABC tripartate complex which is a RND-type drug exporter. The complex consists of MdtB/C, which form a transmembrane heteromultimer and MdtA which is a membrane fusion protein [ ]. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_01423"
] | [
"MdtB"
] | [
1715
] | 1 | [
"GP",
"REACTOME"
] | [
"GenProp1199",
"R-HSA-9638334"
] | [
"GP:GenProp1199",
"REACTOME:R-HSA-9638334"
] | 2 | [] | 0 | [
"PUB00053900"
] | [
"12107133"
] | [
"The putative response regulator BaeR stimulates multidrug resistance of Escherichia coli via a novel multidrug exporter system, MdtABC."
] | [
2002
] | 1 | [
"IPR001036"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta"
] | [
1713,
2
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Multidrug resistance protein MdtB | Multidrug resistance protein MdtB | Multidrug-R_MdtB | 2 |
IPR022832 | 22,832 | Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF | Flippase_ArnF | Family | 1,633 | false | false | This entry represents ArnF, which is a an integral membrane component of the ArnE/ArnF (heterodimer) undecaprenyl-phosphate-alpha-L-Ara4N flippase. This flippase translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner mem... | [
"GO:1901505",
"GO:0009103"
] | [
"carbohydrate derivative transmembrane transporter activity",
"lipopolysaccharide biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00538",
"NF002816"
] | [
"Flippase_ArnF",
"PRK02971.1-2"
] | [
1566,
1633
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053903"
] | [
"17928292"
] | [
"An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli."
] | [
2007
] | 1 | [
"IPR000390"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Beauveria bassiana D1-5",
"bioreactor metagenome"
] | [
1631,
1,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF | Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF | Flippase_ArnF | 3 |
IPR022833 | 22,833 | Uncharacterised protein family UPF0757, YmgG | UPF0757_YmgG | Family | 82 | false | false | This entry contains proteins of unknown function, which include YmgG from Escherichia coli. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_01455"
] | [
"UPF0757"
] | [
82
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
82
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Uncharacterised protein family UPF0757, YmgG | Uncharacterised protein family UPF0757, YmgG | UPF0757_YmgG | 8 |
IPR022835 | 22,835 | Chaperone modulatory protein CbpM | CbpM | Family | 563 | false | false | This entry represents Chaperone modulatory protein CbpM from Escherichia coli and similar proteins from Gammaproteobacteria. CbpM (named after "CbpA modulator", [ ]) interacts with the N-terminal J-domain of CbpA, forms a stable complex and specifically inhibits its activity [ , ]. Together with CbpA, it modulates the ... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_01155"
] | [
"CbpM"
] | [
563
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00100094",
"PUB00100096",
"PUB00100097",
"PUB00100098"
] | [
"20226195",
"15184371",
"17337578",
"24945826"
] | [
"Structural basis of the regulation of the CbpA co-chaperone by its specific modulator CbpM.",
"CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM.",
"In vivo modulation of a DnaJ homolog, CbpA, by CbpM.",
"Structure of CbpA J-domain bound to the regulatory protein Cbpm explai... | [
2010,
2004,
2007,
2014
] | 4 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
563
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Chaperone modulatory protein CbpM | Chaperone modulatory protein CbpM | CbpM | 1 |
IPR022837 | 22,837 | Protein-methionine-sulfoxide reductase subunit MsrQ-like | MsrQ-like | Family | 7,393 | false | false | MsrPQ is an enzymatic system that repairs proteins containing methionine sulfoxide in the bacterial cell envelope. MsrP, a molybdo-enzyme, and MsrQ, a haem-binding membrane protein, are widely conserved throughout Gram-negative bacteria. MsrPQ uses electrons from the respiratory chain, which represents a novel mechanis... | [] | [] | [] | 0 | [
"HAMAP",
"PANTHER"
] | [
"MF_01207",
"PTHR36964"
] | [
"MsrQ",
""
] | [
6602,
7382
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00078613",
"PUB00093603"
] | [
"26641313",
"23889511"
] | [
"Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons.",
"The magnetosome proteins MamX, MamZ and MamH are involved in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense."
] | [
2015,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Nanobdellati",
"unclassified sequences"
] | [
7287,
6,
10,
90
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Protein-methionine-sulfoxide reductase subunit MsrQ-like | Protein-methionine-sulfoxide reductase subunit MsrQ-like | MsrQ-like | 1 |
IPR022838 | 22,838 | GTP cyclohydrolase FolE2 | GTP_cyclohydrolase_FolE2 | Family | 5,083 | false | false | This entry contains proteins belonging to the GTP cyclohydrolase IV family. GTP cyclohydrolase FolE2 converts GTP to 7,8-dihydroneopterin triphosphate [ ]. | [
"GO:0003933",
"GO:0003934"
] | [
"GTP cyclohydrolase activity",
"GTP cyclohydrolase I activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"HAMAP"
] | [
"MF_01527_B"
] | [
"GTP_cyclohydrol_B"
] | [
5083
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.5.4.16",
"PWY-5663",
"PWY-6147",
"PWY-6703",
"PWY-6983",
"PWY-7442",
"PWY-7852"
] | [
"EC:3.5.4.16",
"METACYC:PWY-5663",
"METACYC:PWY-6147",
"METACYC:PWY-6703",
"METACYC:PWY-6983",
"METACYC:PWY-7442",
"METACYC:PWY-7852"
] | 7 | [
"2r5r",
"3d2o",
"5k95",
"5k9g",
"8g6c",
"8g8v",
"8tcc"
] | 7 | [
"PUB00051207"
] | [
"17032654"
] | [
"Discovery of a new prokaryotic type I GTP cyclohydrolase family."
] | [
2006
] | 1 | [
"IPR003801"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4992,
8,
83
] | 3 | [] | [] | 0 | true | Family | GTP cyclohydrolase FolE2 | GTP cyclohydrolase FolE2 | GTP_cyclohydrolase_FolE2 | 5 |
IPR022839 | 22,839 | ArnT | ArnT | Family | 2,346 | false | false | This entry represents the bacterial undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferases. This family of proteins are a subset of the glycosyltransferase 39 family and are responsible for the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. Th... | [
"GO:0016763"
] | [
"pentosyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01165",
"NF009784"
] | [
"ArnT_transfer",
"PRK13279.1"
] | [
2245,
2343
] | 2 | [
"EC"
] | [
"2.4.2.43"
] | [
"EC:2.4.2.43"
] | 1 | [] | 0 | [
"PUB00053907"
] | [
"16226890"
] | [
"Purification and characterization of the L-Ara4N transferase protein ArnT from Salmonella typhimurium."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
2344,
2
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | ArnT | ArnT | ArnT | 9 |
IPR022840 | 22,840 | GTP cyclohydrolase MptA | GTP_cyclohydrolase_MptA | Family | 708 | false | false | This entry represents GTP cyclohydrolases belonging to family IV. In archaea, GTP cyclohydrolase MptA converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin [ ]. | [
"GO:0003933"
] | [
"GTP cyclohydrolase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01527_A",
"TIGR00294"
] | [
"GTP_cyclohydrol_A",
""
] | [
694,
677
] | 2 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.5.4.39",
"PWY-6797",
"PWY-7853"
] | [
"EC:3.5.4.39",
"METACYC:PWY-6797",
"METACYC:PWY-7853"
] | 3 | [] | 0 | [
"PUB00057463"
] | [
"17497938"
] | [
"Characterization of an Fe(2+)-dependent archaeal-specific GTP cyclohydrolase, MptA, from Methanocaldococcus jannaschii."
] | [
2007
] | 1 | [
"IPR003801"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
644,
46,
18
] | 3 | [] | [] | 0 | true | Family | GTP cyclohydrolase MptA | GTP cyclohydrolase MptA | GTP_cyclohydrolase_MptA | 5 |
IPR022841 | 22,841 | 5-dehydro-2-deoxygluconokinase, Firmicutes | DKG_kinase_firmi | Family | 972 | false | false | Bacterial 5-dehydro-2-deoxygluconokinase is responsible for catalysing the phosphorylation of 5-dehydro-2-deoxy-D-gluconate (2-deoxy-5-keto-D-gluconate or DKG) to 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP), the fifth step in the inositol catabolic pathway [ ]. This entry consists of Gram-positive (Firmicutes) enzym... | [
"GO:0047590",
"GO:0016310"
] | [
"5-dehydro-2-deoxygluconokinase activity",
"phosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_01668"
] | [
"IolC"
] | [
972
] | 1 | [
"EC"
] | [
"2.7.1.92"
] | [
"EC:2.7.1.92"
] | 1 | [
"2qcv"
] | 1 | [
"PUB00053908"
] | [
"18310071"
] | [
"myo-Inositol catabolism in Bacillus subtilis."
] | [
2008
] | 1 | [
"IPR030830"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
972
] | 1 | [] | [] | 0 | true | Family | 5-dehydro-2-deoxygluconokinase, Firmicutes | 5-dehydro-2-deoxygluconokinase, Firmicutes | DKG_kinase_firmi | 2 |
IPR022842 | 22,842 | DNA-directed RNA polymerase subunit Rpo3/Rpb3/RPAC1 | RNAP_Rpo3/Rpb3/RPAC1 | Family | 9,908 | false | false | DNA-directed RNA polymerases, also known as DNA-dependent RNA polymerases, are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. Eukaryotes have three different DNA-directed RNA polymerases (RNAPs), Pol I, II, and III, whereas Archaea and Bacteria have single enzym... | [
"GO:0003899",
"GO:0006351"
] | [
"DNA-directed RNA polymerase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_00320"
] | [
"RNApol_arch_Rpo3"
] | [
9908
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.6",
"R-BTA-112382",
"R-BTA-113418",
"R-BTA-5250924",
"R-BTA-5578749",
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-6803529",
"R-BTA-6807505",
"R-BTA-72086",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-72203",
"R-BTA-73762",
"R-BTA-73772... | [
"EC:2.7.7.6",
"REACTOME:R-BTA-112382",
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-5250924",
"REACTOME:R-BTA-5578749",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-6803529",
"REACTOME:R-BTA-6807505... | 168 | [
"1i3q",
"1i50",
"1i6h",
"1k83",
"1nik",
"1nt9",
"1pqv",
"1r5u",
"1r9s",
"1r9t",
"1sfo",
"1twa",
"1twc",
"1twf",
"1twg",
"1twh",
"1wcm",
"1y1v",
"1y1w",
"1y1y",
"1y77",
"2b63",
"2b8k",
"2e2h",
"2e2i",
"2e2j",
"2ja5",
"2ja6",
"2ja7",
"2ja8",
"2nvq",
"2nvt"... | 533 | [
"PUB00045896",
"PUB00059148",
"PUB00059149",
"PUB00079994"
] | [
"18235446",
"19419240",
"19880312",
"11839495"
] | [
"The X-ray crystal structure of RNA polymerase from Archaea.",
"Evolution of Complex RNA Polymerases: The Complete Archaeal RNA Polymerase Structure.",
"Archaeal RNA polymerase.",
"Multisubunit RNA polymerases."
] | [
2008,
2009,
2009,
2002
] | 4 | [] | [
"IPR033901"
] | 0 | 1 | 0 | [
"Archaea",
"Eukaryota",
"Pithoviruses",
"unclassified sequences",
"uncultured marine bacterium MedDCM-OCT-S05-C222"
] | [
916,
8956,
2,
33,
1
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
19,
2,
3,
2,
8,
6,
2,
5,
7,
2,
2,
8
] | 12 | true | Family | DNA-directed RNA polymerase subunit Rpo3/Rpb3/RPAC1 | DNA-directed RNA polymerase subunit Rpo3/Rpb3/RPAC1 | RNAP_Rpo3/Rpb3/RPAC1 | 3 |
IPR022843 | 22,843 | Formamidase | Formamidase | Family | 959 | false | false | This entry represents formamidase. Formamidase is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide [ ]. | [
"GO:0004328"
] | [
"formamidase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01243",
"NF009803"
] | [
"Formamidase",
"PRK13287.1"
] | [
859,
959
] | 2 | [
"EC",
"METACYC"
] | [
"3.5.1.49",
"PWY-7142"
] | [
"EC:3.5.1.49",
"METACYC:PWY-7142"
] | 2 | [
"2dyu",
"2dyv",
"2e2k",
"2e2l",
"5g3o",
"5g3p"
] | 6 | [
"PUB00053909"
] | [
"11359566"
] | [
"The AmiE aliphatic amidase and AmiF formamidase of Helicobacter pylori: natural evolution of two enzyme paralogues."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
877,
78,
4
] | 3 | [] | [] | 0 | true | Family | Formamidase | Formamidase | Formamidase | 6 |
IPR022845 | 22,845 | Small ribosomal subunit protein eS31, archaea | Ribosomal_eS31_arc | Family | 734 | false | false | This entry represents the archaeal Small ribosomal subunit protein eS31 (S27ae), which is a component of the 30S subunit. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation ... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00777"
] | [
"Ribosomal_eS31"
] | [
734
] | 1 | [] | [] | [] | 0 | [
"2k4x",
"4v4n",
"4v6u",
"5jb3",
"5jbh",
"6sw9",
"6swc",
"6swe",
"6tmf",
"7zag",
"7zah",
"7zai",
"7zhg",
"8hkx",
"8hky",
"8hkz",
"8hl1",
"8hl2",
"8hl3",
"8hl4",
"8hl5",
"8wkp",
"8wq2",
"8wq4",
"9fhl",
"9fny",
"9fnz",
"9fo0",
"9fra",
"9frk",
"9frl",
"9fs6"... | 35 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Neocallimastigaceae",
"ecological metagenomes"
] | [
712,
4,
18
] | 3 | [] | [] | 0 | true | Family | Small ribosomal subunit protein eS31, archaea | Small ribosomal subunit protein eS31, archaea | Ribosomal_eS31_arc | 8 |
IPR022846 | 22,846 | Xaa-Pro dipeptidase | X_Pro_dipept | Family | 2,783 | false | false | This entry represents Xaa-Pro dipeptidase, also known as proline dipeptidase. This enzyme splits dipeptides with a prolyl residue in the C-terminal position. | [
"GO:0016795"
] | [
"phosphoric triester hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01279",
"NF010133"
] | [
"X_Pro_dipeptid",
"PRK13607.1"
] | [
2691,
2782
] | 2 | [
"EC"
] | [
"3.4.13.9"
] | [
"EC:3.4.13.9"
] | 1 | [
"3l24",
"3l7g",
"3rva",
"4qr8",
"4zwo",
"4zwp",
"4zwu",
"6ah7",
"6ah8",
"7e5c"
] | 10 | [] | [] | [] | [] | 0 | [
"IPR052433"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
2764,
5,
14
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Xaa-Pro dipeptidase | Xaa-Pro dipeptidase | X_Pro_dipept | 7 |
IPR022847 | 22,847 | Translation elongation factor IF5A, archaeal | Transl_elong_IF5A_arc | Family | 891 | false | false | This entry represents the archaeal IF-5A proteins. Eukaryotic eIF-5A was initially thought to function as a translation initiation factor, based on its ability to stimulate methionyl-puromycin synthesis. However, subsequent work revealed a role for eIF5A in translation elongation [ , ]. Depletion or inactivation of eIF... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00085",
"NF003076"
] | [
"eIF_5A",
"PRK03999.1"
] | [
856,
891
] | 2 | [] | [] | [] | 0 | [
"1bkb",
"1eif",
"1iz6",
"2eif",
"8put"
] | 5 | [
"PUB00000742",
"PUB00003672",
"PUB00005808",
"PUB00010716",
"PUB00046010",
"PUB00082267",
"PUB00090482"
] | [
"8347280",
"1903841",
"9493264",
"9753699",
"19424157",
"23727016",
"28392174"
] | [
"Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation.",
"Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.",
"Crystal structure of the NAD complex of human... | [
1993,
1991,
1998,
1998,
2009,
2013,
2017
] | 7 | [
"IPR001884"
] | [] | 1 | 0 | 1 | [
"Archaea",
"ecological metagenomes"
] | [
865,
26
] | 2 | [] | [] | 0 | true | Family | Translation elongation factor IF5A, archaeal | Translation elongation factor IF5A, archaeal | Transl_elong_IF5A_arc | 8 |
IPR022849 | 22,849 | Peptidase S12, YfeW/YbbE-like | Pept_S12_YfeW/YbbE-like | Family | 692 | false | false | This entry represents unassigned peptidases that belong to MEROPS peptidase family S12 (D-Ala-D-Ala carboxypeptidase B family, clan SE). Proteins in this entry include Bacillus subtilis YbbE, also known as AmiE, an amidase that hydrolyzes the N-acetylmuramyl-L-Ala bond of MurNAc peptides [ ]. This entry also includes Y... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_01034"
] | [
"S12_YfeW"
] | [
692
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.4.16.4",
"PWY-5265",
"PWY-6471"
] | [
"EC:3.4.16.4",
"METACYC:PWY-5265",
"METACYC:PWY-6471"
] | 3 | [] | 0 | [
"PUB00091111",
"PUB00093751"
] | [
"20400549",
"16402224"
] | [
"Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase.",
"The DD-carboxypeptidase activity encoded by pbp4B is not essential for the cell growth of Escherichia coli."
] | [
2010,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Enterobacteriaceae"
] | [
692
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Peptidase S12, YfeW/YbbE-like | Peptidase S12, YfeW/YbbE-like | Pept_S12_YfeW/YbbE-like | 9 |
IPR022851 | 22,851 | Translation factor SUI1 homolog, archaea | SUI1_arc | Family | 824 | false | false | This entry represents protein translation factor SUI1 homolog, involved in translation regulation. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00604"
] | [
"SUI1"
] | [
824
] | 1 | [] | [] | [] | 0 | [
"4mo0",
"5jb3",
"5jbh",
"5zcy"
] | 4 | [] | [] | [] | [] | 0 | [
"IPR005872"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Geodia barretti",
"ecological metagenomes"
] | [
811,
2,
1,
10
] | 4 | [] | [] | 0 | true | Family | Translation factor SUI1 homolog, archaea | Translation factor SUI1 homolog, archaea | SUI1_arc | 1 |
IPR022852 | 22,852 | Carnitinyl-CoA dehydratase | Carnitinyl_CoA_dehydratase | Family | 744 | false | false | The CaiD protein is a carnitinyl-CoA dehydratase enzyme which, together with carnitine-CoA transferase enzyme CaiB, is responsible for the transfomation of L-carnitine to crotonobetaine [ ]. Many enterobacteria are able to convert carnitine, via crotonobetaine, to gamma-butyrobetaine in the presence of carbon and nitro... | [
"GO:0016836"
] | [
"hydro-lyase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01051",
"NF002936"
] | [
"CaiD",
"PRK03580.1"
] | [
703,
744
] | 2 | [
"EC",
"METACYC"
] | [
"4.2.1.149",
"PWY-8339"
] | [
"EC:4.2.1.149",
"METACYC:PWY-8339"
] | 2 | [] | 0 | [
"PUB00003866",
"PUB00035966",
"PUB00053911",
"PUB00054253"
] | [
"7815937",
"11551212",
"9037756",
"12081978"
] | [
"Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli.",
"Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli.",
"Bacterial carnitine metabolism.",... | [
1994,
2001,
1997,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
744
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Carnitinyl-CoA dehydratase | Carnitinyl-CoA dehydratase | Carnitinyl_CoA_dehydratase | 4 |
IPR022853 | 22,853 | Flotillin-like protein FloA | FloA | Family | 3,458 | false | false | This entry represents flotillin-like protein FloA from bacteria. Bacterial flotillin-like proteins are found in membrane microdomains that may be equivalent to eukaryotic membrane rafts [ ]. Similarly to eukaryotic flotillin proteins, flotillins in bacteria play an essential role in organizing and maintaining the corre... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM",
"PFAM"
] | [
"MF_01562",
"NF010186",
"PF12127"
] | [
"FloA",
"PRK13665.1",
"FloA"
] | [
3226,
3296,
3458
] | 3 | [] | [] | [] | 0 | [] | 0 | [
"PUB00076123",
"PUB00099631",
"PUB00099632",
"PUB00099653",
"PUB00104908"
] | [
"22882210",
"20713508",
"25652542",
"27362352",
"22753055"
] | [
"The biofilm formation defect of a Bacillus subtilis flotillin-defective mutant involves the protease FtsH.",
"Functional microdomains in bacterial membranes.",
"Exploring the existence of lipid rafts in bacteria.",
"Super Resolution Fluorescence Microscopy and Tracking of Bacterial Flotillin (Reggie) Paralog... | [
2012,
2010,
2015,
2016,
2012
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctnR613",
"metagenomes"
] | [
3322,
4,
1,
131
] | 4 | [] | [] | 0 | true | Family | Flotillin-like protein FloA | Flotillin-like protein FloA | FloA | 2 |
IPR022854 | 22,854 | Transcriptional regulator GfcR | GfcR-like | Family | 595 | false | false | This entry represents Transcriptional regulator GfcR and related proteins from archaea. They share protein sequence similarity to the PyrE protein (Orotate phosphoribosyltransferase) from Salmonella typhimurium [ ]. GfcR is a DNA-binding transcriptional regulator that functions as a regulator of central sugar catabolic... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01214",
"NF002620"
] | [
"GfcR",
"PRK02277.1"
] | [
562,
595
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00066199",
"PUB00066200",
"PUB00153518"
] | [
"12533452",
"2271660",
"37387308"
] | [
"Development of a gene knockout system for the halophilic archaeon Haloferax volcanii by use of the pyrE gene.",
"Kinetic mechanism of orotate phosphoribosyltransferase from Salmonella typhimurium.",
"Discovery of a novel transcriptional regulator of sugar catabolism in archaea."
] | [
2003,
1990,
2023
] | 3 | [] | [
"IPR053401"
] | 0 | 1 | 0 | [
"Archaea",
"ecological metagenomes"
] | [
583,
12
] | 2 | [] | [] | 0 | true | Family | Transcriptional regulator GfcR | Transcriptional regulator GfcR | GfcR-like | 2 |
IPR022855 | 22,855 | Multidrug resistance protein MdtH | Multidrug-R_MdtH | Family | 1,381 | false | false | Multidrug resistance protein MdtH confers resistance to norfloxacin and enoxacin [ ]. | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01529",
"NF008650"
] | [
"MFS_MdtH",
"PRK11646.1"
] | [
1275,
1381
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053912"
] | [
"11566977"
] | [
"Analysis of a complete library of putative drug transporter genes in Escherichia coli."
] | [
2001
] | 1 | [
"IPR011701"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta",
"termite gut metagenome"
] | [
1378,
2,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Multidrug resistance protein MdtH | Multidrug resistance protein MdtH | Multidrug-R_MdtH | 5 |
IPR022856 | 22,856 | Large ribosomal subunit protein eL21, archaea | Ribosomal_eL21_arc | Family | 894 | false | false | This entry represents the archaeal 50S ribosomal eL21 family of proteins. The eL21 family contains proteins from a number of eukaryotic and archaebacterial organisms which include mammalian eL21, Entamoeba histolytica eL21, Caenorhabditis elegans eL21 (C14B9.7), Saccharomyces cerevisiae (Baker's yeast) eL21 (URP1) and ... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00369",
"NF003303"
] | [
"Ribosomal_eL21",
"PRK04306.1"
] | [
894,
825
] | 2 | [] | [] | [] | 0 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 92 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00028498"
] | [
"11297922",
"11290319",
"11114498",
"10937989"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The complete atomic structure of the large ribosomal subunit at 2.4 A resolution."
] | [
2001,
2001,
2000,
2000
] | 4 | [
"IPR001147"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_01_FULL_39_8b",
"Mesangiospermae",
"unclassified sequences"
] | [
868,
1,
3,
22
] | 4 | [] | [] | 0 | true | Family | Large ribosomal subunit protein eL21, archaea | Large ribosomal subunit protein eL21, archaea | Ribosomal_eL21_arc | 1 |
IPR022857 | 22,857 | Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase | ArnC_tfrase | Family | 1,627 | false | false | This entry represents the bacterial undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase family. This enzymes catalyse the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic ... | [
"GO:0016757",
"GO:0016780",
"GO:0009245",
"GO:0046677"
] | [
"glycosyltransferase activity",
"phosphotransferase activity, for other substituted phosphate groups",
"lipid A biosynthetic process",
"response to antibiotic"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"HAMAP"
] | [
"MF_01164"
] | [
"ArnC_transfer"
] | [
1627
] | 1 | [
"EC"
] | [
"2.4.2.53"
] | [
"EC:2.4.2.53"
] | 1 | [
"8vxh",
"9asc",
"9b77",
"9bhc",
"9bhe"
] | 5 | [
"PUB00054283"
] | [
"15695810"
] | [
"A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5"
] | [
1626,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase | Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase | ArnC_tfrase | 7 |
IPR022858 | 22,858 | Metallothiol transferase FosB | Metallothiol_Trafse_FosB | Family | 1,000 | false | false | FosB is a metallothiol transferase which confers resistance to the antiobiotic fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin [ ]. L-cysteine is thought to be the physiological thiol donor. | [
"GO:0016765",
"GO:0046677"
] | [
"transferase activity, transferring alkyl or aryl (other than methyl) groups",
"response to antibiotic"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01512",
"NF003152"
] | [
"FosB",
"PRK04101.1"
] | [
921,
1000
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.5.1.-",
"PWY-4502",
"PWY-4681",
"PWY-5802",
"PWY-5815",
"PWY-5816",
"PWY-5817",
"PWY-5893",
"PWY-5979",
"PWY-6262",
"PWY-6403",
"PWY-6659",
"PWY-6681",
"PWY-6936",
"PWY-7372",
"PWY-7405",
"PWY-7407",
"PWY-7493",
"PWY-7520",
"PWY-7529",
"PWY-7532",
"PWY-7540",
"PWY-7543... | [
"EC:2.5.1.-",
"METACYC:PWY-4502",
"METACYC:PWY-4681",
"METACYC:PWY-5802",
"METACYC:PWY-5815",
"METACYC:PWY-5816",
"METACYC:PWY-5817",
"METACYC:PWY-5893",
"METACYC:PWY-5979",
"METACYC:PWY-6262",
"METACYC:PWY-6403",
"METACYC:PWY-6659",
"METACYC:PWY-6681",
"METACYC:PWY-6936",
"METACYC:PWY-7... | 43 | [
"4ir0",
"4jd1",
"4jh1",
"4jh2",
"4jh3",
"4jh4",
"4jh5",
"4jh6",
"4jh7",
"4jh8",
"4jh9",
"4nay",
"4naz",
"4nb0",
"4nb1",
"4nb2",
"5f6q",
"7n7g",
"8dtd",
"8e7q",
"8e7r",
"8g7f",
"8g7g",
"8g7h",
"8g7i"
] | 25 | [
"PUB00053914"
] | [
"11244082"
] | [
"FosB, a cysteine-dependent fosfomycin resistance protein under the control of sigma(W), an extracytoplasmic-function sigma factor in Bacillus subtilis."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Phytophthora kernoviae 00238/432",
"human gut metagenome"
] | [
998,
1,
1
] | 3 | [] | [] | 0 | true | Family | Metallothiol transferase FosB | Metallothiol transferase FosB | Metallothiol_Trafse_FosB | 9 |
IPR022859 | 22,859 | Alginate lyase | Alginate_lyase | Family | 757 | false | false | This entry represents alginate lyase or poly (beta-D-mannuronate) lyase. It depolymerises alginate by cleaving the beta-1,4 glycosidic bond. Alginate is a family of 1-4-linked copolymers of beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G). It is produced by brown algae and by some bacteria belonging to the gen... | [
"GO:0045135",
"GO:0042122",
"GO:0042597"
] | [
"poly(beta-D-mannuronate) lyase activity",
"alginic acid catabolic process",
"periplasmic space"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_00557",
"NF001467",
"cd00244"
] | [
"Alginate_lyase",
"PRK00325.1-2",
"AlgLyase"
] | [
694,
757,
677
] | 3 | [
"EC",
"METACYC"
] | [
"4.2.2.3",
"PWY-6986"
] | [
"EC:4.2.2.3",
"METACYC:PWY-6986"
] | 2 | [
"1hv6",
"1qaz",
"4ozv",
"4ozw",
"7sa8"
] | 5 | [
"PUB00011248"
] | [
"9683471"
] | [
"Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
757
] | 1 | [] | [] | 0 | true | Family | Alginate lyase | Alginate lyase | Alginate_lyase | 4 |
IPR022861 | 22,861 | Glutamine-tRNA ligase, bacterial | Gln_tRNA_ligase_bac | Family | 9,872 | false | false | This entry represents bacterial glutamine-tRNA ligases. Glutamine-tRNA ligase ( ) is a class Ic aminoacyl-tRNA ligase and shows several similarities with glutamine-tRNA ligase concerning structure and catalytic properties. It is an alpha2 dimer. Glutamine-tRNA ligase is a relatively rare ligase, found in the cytosolic ... | [
"GO:0004819"
] | [
"glutamine-tRNA ligase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_00126"
] | [
"Gln_tRNA_synth"
] | [
9872
] | 1 | [
"EC"
] | [
"6.1.1.18"
] | [
"EC:6.1.1.18"
] | 1 | [
"1euq",
"1euy",
"1exd",
"1gsg",
"1gtr",
"1gts",
"1nyl",
"1o0b",
"1o0c",
"1qrs",
"1qrt",
"1qru",
"1qtq",
"1zjw",
"2hz7",
"2rd2",
"2re8",
"4jxx",
"4jxz",
"4jyz",
"5bnz"
] | 21 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [
"IPR004514"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Candidatus Heimdallarchaeum",
"Eukaryota",
"Myoviridae sp. ctKhy9",
"metagenomes"
] | [
9739,
2,
29,
1,
101
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glutamine-tRNA ligase, bacterial | Glutamine-tRNA ligase, bacterial | Gln_tRNA_ligase_bac | 1 |
IPR022863 | 22,863 | Ribosomal protein uS12, archaea | Ribosomal_uS12_arc | Family | 867 | false | false | This entry represents archaeal 30S subunit ribosomal protein uS12. With S4 and S5, uS12 plays an important role in translational accuracy. It is located at the interface of the 30S and 50S subunits. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are ex... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00403_A"
] | [
"Ribosomal_uS12_A"
] | [
867
] | 1 | [] | [] | [] | 0 | [
"4v4n",
"4v6u",
"5jb3",
"5jbh",
"6skf",
"6skg",
"6sw9",
"6swc",
"6swd",
"6th6",
"6tmf",
"7zag",
"7zah",
"7zai",
"7zhg",
"8hkx",
"8hky",
"8hkz",
"8hl1",
"8hl2",
"8hl3",
"8hl4",
"8hl5",
"8wkp",
"8wq2",
"8wq4",
"9e71",
"9e7f",
"9fhl",
"9fny",
"9fnz",
"9fo0"... | 43 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [
"IPR005680"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Geodia barretti",
"unclassified sequences"
] | [
842,
2,
23
] | 3 | [] | [] | 0 | true | Family | Ribosomal protein uS12, archaea | Ribosomal protein uS12, archaea | Ribosomal_uS12_arc | 1 |
IPR022864 | 22,864 | DnaA regulatory inactivator Hda, Enterobacteriaceae | Hda_Enterobact | Family | 1,056 | false | false | This entry represents the Hda (Homologous to DnaA) proteins, which are about half the length of DnaA and homologous over the entire length of Hda. In Escherichia coli, the initiation of DNA replication requires DnaA bound to ATP rather than ADP; Hda helps facilitate the conversion of DnaA-ATP to DnaA-ADP, thus inhibiti... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_01158"
] | [
"Hda"
] | [
1056
] | 1 | [] | [] | [] | 0 | [
"5x06"
] | 1 | [
"PUB00042952"
] | [
"16882985"
] | [
"Hda-mediated inactivation of the DnaA protein and dnaA gene autoregulation act in concert to ensure homeostatic maintenance of the Escherichia coli chromosome."
] | [
2006
] | 1 | [
"IPR017788"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Beauveria bassiana D1-5",
"bioreactor metagenome"
] | [
1054,
1,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | DnaA regulatory inactivator Hda, Enterobacteriaceae | DnaA regulatory inactivator Hda, Enterobacteriaceae | Hda_Enterobact | 2 |
IPR022865 | 22,865 | DNA ligase, ATP-dependent, bacterial/archaeal | DNA_ligae_ATP-dep_bac/arc | Family | 3,538 | false | false | This entry represents bacterial and archaeal ATP-dependent DNA ligases. DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalysing the formation of an internucleotide ester bond between phosphate and deoxyribose. It is active during DNA replication, DNA repair and DNA recombi... | [
"GO:0003910"
] | [
"DNA ligase (ATP) activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_00407"
] | [
"DNA_ligase"
] | [
3538
] | 1 | [
"EC",
"EC"
] | [
"6.5.1",
"6.5.1.1"
] | [
"EC:6.5.1",
"EC:6.5.1.1"
] | 2 | [
"2cfm",
"2hiv",
"2hix",
"3gde",
"3rr5",
"4eq5",
"6wbo",
"7rpo",
"7rpw",
"7rpx"
] | 10 | [
"PUB00000083",
"PUB00004738"
] | [
"1497311",
"1988940"
] | [
"Mammalian DNA ligases.",
"Location of the active site for enzyme-adenylate formation in DNA ligases."
] | [
1992,
1991
] | 2 | [
"IPR000977"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
943,
2550,
33,
12
] | 4 | [] | [] | 0 | true | Family | DNA ligase, ATP-dependent, bacterial/archaeal | DNA ligase, ATP-dependent, bacterial/archaeal | DNA_ligae_ATP-dep_bac/arc | 6 |
IPR022866 | 22,866 | Heat shock protein HspQ | HspQ | Family | 961 | false | false | This entry represents the bacterial heat shock protein HspQ family. They are involved in the degradation of certain denaturated proteins, including DnaA, during heat shock stress. The crystal structure of HspQ from Escherichia coli showed a trimeric structure stabilized by a large and hydrophobic interaction surface [ ... | [
"GO:0009408"
] | [
"response to heat"
] | [
"biological_process"
] | 1 | [
"HAMAP"
] | [
"MF_01194"
] | [
"HspQ"
] | [
961
] | 1 | [] | [] | [] | 0 | [
"5ycq"
] | 1 | [
"PUB00100088"
] | [
"29083032"
] | [
"X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
957,
4
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Heat shock protein HspQ | Heat shock protein HspQ | HspQ | 4 |
IPR022867 | 22,867 | Protein-methionine-sulfoxide reductase subunit MsrP | MsrP | Family | 7,253 | false | false | MsrPQ is an enzymatic system that repairs proteins containing methionine sulfoxide in the bacterial cell envelope. MsrP, a molybdo-enzyme, and MsrQ, a haem-binding membrane protein, are widely conserved throughout Gram-negative bacteria. MsrPQ uses electrons from the respiratory chain, which represents a novel mechanis... | [
"GO:0016667",
"GO:0043546",
"GO:0030091"
] | [
"oxidoreductase activity, acting on a sulfur group of donors",
"molybdopterin cofactor binding",
"protein repair"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01206",
"NF003767"
] | [
"MsrP",
"PRK05363.1"
] | [
6731,
7252
] | 2 | [
"EC"
] | [
"1.8.5.-"
] | [
"EC:1.8.5.-"
] | 1 | [
"1xdq",
"1xdy"
] | 2 | [
"PUB00032402",
"PUB00078595",
"PUB00078613"
] | [
"15355966",
"16042411",
"26641313"
] | [
"Structural and biochemical identification of a novel bacterial oxidoreductase.",
"Characterization of an Escherichia coli sulfite oxidase homologue reveals the role of a conserved active site cysteine in assembly and function.",
"Repairing oxidized proteins in the bacterial envelope using respiratory chain ele... | [
2004,
2005,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
7128,
22,
103
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Protein-methionine-sulfoxide reductase subunit MsrP | Protein-methionine-sulfoxide reductase subunit MsrP | MsrP | 9 |
IPR022870 | 22,870 | Phycocyanobilin:ferredoxin oxidoreductase | Ferredoxin_bilin_OxRdtase | Family | 417 | false | false | This entry represents phycocyanobilin:ferredoxin oxidoreductases. They are involved in the reduction of biliverdin IX-alpha. | [
"GO:0050620",
"GO:0010024"
] | [
"phycocyanobilin:ferredoxin oxidoreductase activity",
"phytochromobilin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00618",
"NF002760"
] | [
"Ferredoxin_bilin_red",
"PRK02816.1"
] | [
400,
417
] | 2 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.3.7.5",
"PWY-5917",
"PWY-7578"
] | [
"EC:1.3.7.5",
"METACYC:PWY-5917",
"METACYC:PWY-7578"
] | 3 | [
"2d1e",
"2dke",
"2g18",
"3ajg",
"3ajh",
"3f0l",
"3f0m",
"3i8u",
"3i94",
"3i95",
"3nb8",
"3nb9",
"4eoc",
"4eod",
"4eoe",
"4qcd",
"5b4h",
"5b4i",
"5b4j",
"7yk9",
"7ykb"
] | 21 | [
"PUB00040149"
] | [
"16380422"
] | [
"Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXalpha, a key enzyme in the biosynthesis of phycocyanobilin."
] | [
2006
] | 1 | [
"IPR009249"
] | [] | 1 | 0 | 1 | [
"Cyanobacteriota",
"Eukaryota",
"Kyanoviridae"
] | [
396,
12,
9
] | 3 | [] | [] | 0 | true | Family | Phycocyanobilin:ferredoxin oxidoreductase | Phycocyanobilin:ferredoxin oxidoreductase | Ferredoxin_bilin_OxRdtase | 5 |
IPR022871 | 22,871 | Para-hydroxybenzoic acid efflux pump, subunit AaeA | PHBA_efflux_pump_AaeA | Family | 1,043 | false | false | This entry represents the p-hydroxybenzoic acid efflux pump subunit AaeA. | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01544",
"NF007850"
] | [
"AaeA",
"PRK10559.1"
] | [
1011,
1043
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00054183"
] | [
"15489430"
] | [
"Characterization of the Escherichia coli AaeAB efflux pump: a metabolic relief valve?"
] | [
2004
] | 1 | [
"IPR006143"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota"
] | [
1043
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Para-hydroxybenzoic acid efflux pump, subunit AaeA | Para-hydroxybenzoic acid efflux pump, subunit AaeA | PHBA_efflux_pump_AaeA | 2 |
IPR022872 | 22,872 | Quinate/Shikimate dehydrogenase | Quinate/Shikimate_DH | Family | 473 | false | false | This entry represents a group of bifunctional enzymes , quinate/shikimate dehydrogenase [ ]. This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from ( ), in that it can use both quinate and shikimate as substrate and either NAD(+) or NADP(+) as acceptor. | [
"GO:0004764",
"GO:0030266",
"GO:0052733",
"GO:0052734"
] | [
"shikimate 3-dehydrogenase (NADP+) activity",
"quinate 3-dehydrogenase (NAD+) activity",
"quinate 3-dehydrogenase (NADP+) activity",
"shikimate 3-dehydrogenase (NAD+) activity"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function"
] | 4 | [
"HAMAP"
] | [
"MF_01578"
] | [
"Shikimate_DH_YdiB"
] | [
473
] | 1 | [
"EC",
"METACYC"
] | [
"1.1.1.282",
"PWY-6416"
] | [
"EC:1.1.1.282",
"METACYC:PWY-6416"
] | 2 | [
"1npd",
"1o9b",
"1vi2",
"3t4e"
] | 4 | [
"PUB00027835"
] | [
"12637497"
] | [
"Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities."
] | [
2003
] | 1 | [
"IPR022893"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota"
] | [
473
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Quinate/Shikimate dehydrogenase | Quinate/Shikimate dehydrogenase | Quinate/Shikimate_DH | 9 |
IPR022874 | 22,874 | Valine-tRNA ligase, type 2 | Valine-tRNA_ligase_type_2 | Family | 3,588 | false | false | This entry represents the type 2 subfamily of the valine-tRNA ligases. Valine-tRNA ligase (also known as Valyl-tRNA synthetase) ( ) is an alpha monomer that belongs to class Ia aminoacyl-tRNA ligase. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognat... | [
"GO:0004832"
] | [
"valine-tRNA ligase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_02005"
] | [
"Val_tRNA_synth_type2"
] | [
3588
] | 1 | [
"EC"
] | [
"6.1.1.9"
] | [
"EC:6.1.1.9"
] | 1 | [] | 0 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [
"IPR002303"
] | [
"IPR048044"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Tupanvirus",
"metagenomes"
] | [
696,
2794,
7,
4,
87
] | 5 | [] | [] | 0 | true | Family | Valine-tRNA ligase, type 2 | Valine-tRNA ligase, type 2 | Valine-tRNA_ligase_type_2 | 6 |
IPR022876 | 22,876 | Redox-sensing transcriptional repressor Rex | Tscrpt_rep_Rex | Family | 9,164 | false | false | This entry represents the redox-sensing transcriptional repressor Rex. Rex is thought to be responsible for modulating transcription according to changes in the cellular NADH/NAD(+) redox state and binds to the promoter of the aldehyde-alcohol dehydrogenase adhE gene [ ]. | [
"GO:0045892",
"GO:0051775"
] | [
"negative regulation of DNA-templated transcription",
"response to redox state"
] | [
"biological_process",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"PANTHER"
] | [
"MF_01131",
"NF003995",
"PTHR35786"
] | [
"Rex",
"PRK05472.2-4",
""
] | [
9012,
9032,
9161
] | 3 | [] | [] | [] | 0 | [
"1xcb",
"2dt5",
"2vt2",
"2vt3",
"3ikt",
"3ikv",
"3il2",
"3keo",
"3keq",
"3ket",
"3wg9",
"3wgg",
"3wgh",
"3wgi",
"5zz5",
"5zz6",
"5zz7",
"7wb3"
] | 18 | [
"PUB00160990"
] | [
"25312953"
] | [
"Ethanol-induced alcohol dehydrogenase E (AdhE) potentiates pneumolysin in Streptococcus pneumoniae."
] | [
2015
] | 1 | [] | [
"IPR058203",
"IPR058236"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
8915,
11,
238
] | 3 | [] | [] | 0 | true | Family | Redox-sensing transcriptional repressor Rex | Redox-sensing transcriptional repressor Rex | Tscrpt_rep_Rex | 4 |
IPR022877 | 22,877 | Protein of unknown funcion UPF0173 | UPF0173 | Family | 7,087 | false | false | This entry represents a group of uncharacterised proteins that belong to the UPF0173 family of metal-dependent hydrolases predominantly found in bacteria and archaea. | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00457",
"NF001911"
] | [
"UPF0173",
"PRK00685.1"
] | [
6316,
7087
] | 2 | [] | [] | [] | 0 | [
"3x2x",
"3x2y",
"3x2z",
"3x30",
"6hrg",
"7e3v",
"7e3w"
] | 7 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
745,
6247,
32,
63
] | 4 | [] | [] | 0 | true | Family | Protein of unknown funcion UPF0173 | Protein of unknown funcion UPF0173 | UPF0173 | 9 |
IPR022878 | 22,878 | V-type ATP synthase catalytic alpha chain | V-ATPase_asu | Family | 11,163 | false | false | This entry represents the catalytic subunit alpha of V-type ATP synthase, which is known as subunit A in eukaryotes. In bacteria and archaea it produces ATP from ADP in the presence of a proton gradient across the membrane. Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolys... | [
"GO:0046961",
"GO:0046034"
] | [
"proton-transporting ATPase activity, rotational mechanism",
"ATP metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"PANTHER"
] | [
"MF_00309",
"NF003220",
"PTHR43607"
] | [
"ATP_synth_A_arch",
"PRK04192.1",
""
] | [
8426,
9552,
11161
] | 3 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"7.1.2.2",
"PWY-7980",
"R-BTA-1222556",
"R-BTA-77387",
"R-BTA-917977",
"R-BTA-9639288",
"R-BTA-983712",
"R-CEL-1222556",
"R-CEL-77387",
"R-CEL-917977",
"R-CEL-9639288",
"R-CEL-983712",
"R-DDI-1222556",
"R-DDI-77387",
"R-DDI-917977",
"R-DDI-9639288",
"R-DME-1222556",
"R-DME-77387",
... | [
"EC:7.1.2.2",
"METACYC:PWY-7980",
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-77387",
"REACTOME:R-BTA-917977",
"REACTOME:R-BTA-9639288",
"REACTOME:R-BTA-983712",
"REACTOME:R-CEL-1222556",
"REACTOME:R-CEL-77387",
"REACTOME:R-CEL-917977",
"REACTOME:R-CEL-9639288",
"REACTOME:R-CEL-983712",
"REACT... | 43 | [
"1vdz",
"3a5c",
"3a5d",
"3gqb",
"3i4l",
"3i72",
"3i73",
"3ikj",
"3j0j",
"3j9t",
"3j9u",
"3j9v",
"3m4y",
"3mfy",
"3nd8",
"3nd9",
"3p20",
"3qg1",
"3qia",
"3qjy",
"3sdz",
"3se0",
"3vr2",
"3vr3",
"3vr4",
"3vr5",
"3vr6",
"3w3a",
"5bn3",
"5bn4",
"5bn5",
"5bw9"... | 154 | [
"PUB00007886",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789",
"PUB00160299"
] | [
"11533110",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106",
"9874757"
] | [
"Structure-function relationships of A-, F- and V-ATPases.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases.",
"New in... | [
2001,
2004,
2004,
2010,
2008,
1992,
1998,
1992
] | 8 | [] | [
"IPR005725",
"IPR005726"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
975,
3611,
6320,
257
] | 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... | [
7,
1,
2,
9,
6,
4,
1,
6,
4,
1,
1,
16
] | 12 | true | Family | V-type ATP synthase catalytic alpha chain | V-type ATP synthase catalytic alpha chain | V-ATPase_asu | 6 |
IPR022879 | 22,879 | V-type ATP synthase regulatory subunit B/beta | V-ATPase_su_B/beta | Family | 12,286 | false | false | This entry represents the beta regulatory subunit of V-type ATP synthase, known as subunit B in eukaryota. Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing t... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM",
"PIRSF",
"PANTHER"
] | [
"MF_00310",
"NF003235",
"PIRSF039114",
"PTHR43389"
] | [
"ATP_synth_B_arch",
"PRK04196.1",
"V-ATPsynth_beta/V-ATPase_B",
""
] | [
9440,
10666,
7290,
12279
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1222556",
"R-BTA-77387",
"R-BTA-917977",
"R-BTA-9639288",
"R-BTA-983712",
"R-CEL-1222556",
"R-CEL-77387",
"R-CEL-917977",
"R-CEL-9639288",
"R-CEL-983712",
"R-DDI-1222556",
"R-DDI-77387",
"R-DDI-917977",
"R-DDI-9639288",
"R-DME-1222556",
"R-DME-77387",
"R-DME-917977",
"R-DME-... | [
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-77387",
"REACTOME:R-BTA-917977",
"REACTOME:R-BTA-9639288",
"REACTOME:R-BTA-983712",
"REACTOME:R-CEL-1222556",
"REACTOME:R-CEL-77387",
"REACTOME:R-CEL-917977",
"REACTOME:R-CEL-9639288",
"REACTOME:R-CEL-983712",
"REACTOME:R-DDI-1222556",
"REACTOME:R-DDI-... | 43 | [
"2c61",
"2rkw",
"3a5c",
"3a5d",
"3b2q",
"3dsr",
"3eiu",
"3gqb",
"3j0j",
"3j9t",
"3j9u",
"3j9v",
"3ssa",
"3tgw",
"3tiv",
"3vr2",
"3vr3",
"3vr4",
"3vr5",
"3vr6",
"3w3a",
"5bn3",
"5bn4",
"5bn5",
"5bo5",
"5bw9",
"5d80",
"5gar",
"5gas",
"5knb",
"5knc",
"5knd"... | 147 | [
"PUB00007886",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789",
"PUB00160299"
] | [
"11533110",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106",
"9874757"
] | [
"Structure-function relationships of A-, F- and V-ATPases.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases.",
"New in... | [
2001,
2004,
2004,
2010,
2008,
1992,
1998,
1992
] | 8 | [] | [
"IPR005723",
"IPR005724"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1237,
3375,
7442,
232
] | 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... | [
14,
2,
4,
2,
19,
6,
1,
6,
7,
1,
1,
24
] | 12 | true | Family | V-type ATP synthase regulatory subunit B/beta | V-type ATP synthase regulatory subunit B/beta | V-ATPase_su_B/beta | 4 |
IPR022880 | 22,880 | DNA polymerase IV | DNApol_IV | Family | 35,001 | false | false | DNA polymerase IV is a poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. It copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by polIV. It exhibits no 3'-5' exonuclease (proofreading)... | [
"GO:0003887"
] | [
"DNA-directed DNA polymerase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"CDD"
] | [
"MF_01113",
"cd03586"
] | [
"DNApol_IV",
"PolY_Pol_IV_kappa"
] | [
30458,
34542
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.7",
"R-CEL-5655862",
"R-CEL-5696397",
"R-CEL-5696400",
"R-CEL-6782135",
"R-CEL-6782210",
"R-HSA-5655862",
"R-HSA-5656169",
"R-HSA-5685942",
"R-HSA-5696397",
"R-HSA-5696400",
"R-HSA-6782135",
"R-HSA-6782210",
"R-MMU-5655862",
"R-MMU-5656169",
"R-MMU-5685942",
"R-MMU-5696397",
... | [
"EC:2.7.7.7",
"REACTOME:R-CEL-5655862",
"REACTOME:R-CEL-5696397",
"REACTOME:R-CEL-5696400",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-HSA-5655862",
"REACTOME:R-HSA-5656169",
"REACTOME:R-HSA-5685942",
"REACTOME:R-HSA-5696397",
"REACTOME:R-HSA-5696400",
"REACTOME:R-HSA-6782... | 26 | [
"1im4",
"1jx4",
"1jxl",
"1k1q",
"1k1s",
"1n48",
"1n56",
"1ryr",
"1rys",
"1s0m",
"1s0n",
"1s0o",
"1s10",
"1s97",
"1s9f",
"1t94",
"2ago",
"2agp",
"2agq",
"2asd",
"2asj",
"2asl",
"2atl",
"2au0",
"2bq3",
"2bqr",
"2bqu",
"2br0",
"2c22",
"2c28",
"2c2d",
"2c2e"... | 198 | [
"PUB00053994",
"PUB00053995",
"PUB00053996",
"PUB00053997",
"PUB00053998"
] | [
"9391106",
"11080171",
"11463382",
"11751576",
"12060704"
] | [
"Multiple pathways for SOS-induced mutagenesis in Escherichia coli: an overexpression of dinB/dinP results in strongly enhancing mutagenesis in the absence of any exogenous treatment to damage DNA.",
"All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis.",
"SOS ... | [
1997,
2000,
2001,
2002,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
673,
29476,
4359,
6,
487
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe... | [
10,
1,
3,
1,
4,
10,
1,
7,
7,
1,
6
] | 11 | true | Family | DNA polymerase IV | DNA polymerase IV | DNApol_IV | 9 |
IPR022881 | 22,881 | Ribosomal RNA large subunit methyltransferase, Cfr | rRNA_lsu_MeTfrase_Cfr | Family | 254 | false | false | This entry represents the Cfr subfamily of RlmN methyltransferases. Ribosomal RNA large subunit methyltransferase Cfr specifically methylates position 8 of adenine 2503 in 23S rRNA. It can also methylate position 2 of A2503 after the primary methylation is complete, to form 2,8-dimethyladenosine. Cfr confers antibiotic... | [
"GO:0070475"
] | [
"rRNA base methylation"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"SFLD",
"NCBIFAM"
] | [
"MF_01873",
"SFLDF00296",
"TIGR04432"
] | [
"23SrRNA_methyltr_Cfr",
"adenosine_C8_methyltransferase",
"rSAM_Cfr"
] | [
219,
250,
254
] | 3 | [
"EC",
"METACYC"
] | [
"2.1.1.224",
"PWY-6828"
] | [
"EC:2.1.1.224",
"METACYC:PWY-6828"
] | 2 | [
"9p0p"
] | 1 | [
"PUB00017347",
"PUB00064730"
] | [
"10952608",
"19144912"
] | [
"Identification of a plasmid-borne chloramphenicol-florfenicol resistance gene in Staphylococcus sciuri.",
"Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria."
] | [
2000,
2009
] | 2 | [
"IPR004383"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Phytophthora kernoviae 00238/432"
] | [
253,
1
] | 2 | [] | [] | 0 | true | Family | Ribosomal RNA large subunit methyltransferase, Cfr | Ribosomal RNA large subunit methyltransferase, Cfr | rRNA_lsu_MeTfrase_Cfr | 3 |
IPR022882 | 22,882 | tRNA1(Val) (adenine(37)-N6)-methyltransferase | tRNA_adenine-N6_MeTrfase | Family | 4,840 | false | false | Proteins in this family specifically methylate the adenine in position 37 of tRNA (Val) [ ]. | [
"GO:0016430"
] | [
"tRNA (adenine-N6)-methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_01872"
] | [
"tRNA_methyltr_YfiC"
] | [
4840
] | 1 | [
"EC"
] | [
"2.1.1.223"
] | [
"EC:2.1.1.223"
] | 1 | [] | 0 | [
"PUB00060590"
] | [
"19383770"
] | [
"The yfiC gene of E. coli encodes an adenine-N6 methyltransferase that specifically modifies A37 of tRNA1Val(cmo5UAC)."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Siphoviridae sp. ctCCX1",
"Tetradesmus obliquus",
"metagenomes"
] | [
4809,
2,
2,
27
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | tRNA1(Val) (adenine(37)-N6)-methyltransferase | tRNA1(Val) (adenine(37)-N6)-methyltransferase | tRNA_adenine-N6_MeTrfase | 5 |
IPR022885 | 22,885 | NAD(P)H-quinone oxidoreductase subunit D/H | NDH1_su_D/H | Family | 40,795 | false | false | NAD(P)H-quinone oxidoreductase or NAD(P)H dehydrogenase 1 subunit D shuttles electrons from NADH, via FMN and iron-sulphur (Fe-S) centres, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. It couples the redox reaction to proton translocat... | [
"GO:0016651"
] | [
"oxidoreductase activity, acting on NAD(P)H"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_01358",
"PTHR11993",
"TIGR01962"
] | [
"NDH1_NuoD",
"",
"NuoD"
] | [
35886,
40745,
18735
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.1.1.-",
"GenProp0135",
"GenProp1230",
"GenProp1254",
"GenProp1341",
"GenProp1537",
"GenProp1583",
"GenProp1608",
"GenProp1637",
"GenProp1751",
"R-BTA-611105",
"R-BTA-6799198",
"R-CEL-6799198",
"R-DDI-6799198",
"R-HSA-611105",
"R-HSA-6799198",
"R-MMU-611105",
"R-MMU-6799198",
"... | [
"EC:7.1.1.-",
"GP:GenProp0135",
"GP:GenProp1230",
"GP:GenProp1254",
"GP:GenProp1341",
"GP:GenProp1537",
"GP:GenProp1583",
"GP:GenProp1608",
"GP:GenProp1637",
"GP:GenProp1751",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-CEL-6799198",
"REACTOME:R-DDI-6799198",
"REACTOME... | 20 | [
"2fug",
"2ybb",
"3i9v",
"3iam",
"3ias",
"3m9s",
"4hea",
"4wz7",
"5gpn",
"5gup",
"5lc5",
"5ldw",
"5ldx",
"5lnk",
"5o31",
"5xtb",
"5xtd",
"5xth",
"5xti",
"6g2j",
"6g72",
"6gcs",
"6h8k",
"6hum",
"6i0d",
"6i1p",
"6khi",
"6khj",
"6l7o",
"6l7p",
"6nbq",
"6nbx"... | 341 | [] | [] | [] | [] | 0 | [] | [
"IPR023062",
"IPR026662"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
976,
19030,
20075,
714
] | 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",... | [
9,
2,
2,
3,
1,
19,
4,
1,
10,
5,
5
] | 11 | true | Family | NAD(P)H-quinone oxidoreductase subunit D/H | NAD(P)H-quinone oxidoreductase subunit D/H | NDH1_su_D/H | 8 |
IPR022887 | 22,887 | Cell division suppressor protein, YneA | Cell_div_suppressor_YneA | Family | 124 | false | false | The YneA protein is responsible for cell division suppression during the SOS response in Bacillus subtilis. Localization of the FtsZ protein to the cell division site was reduced in dinR-disrupted or yneA-expressing cells, further suggesting that the YneA protein suppresses cell division through the suppression of FtsZ... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_02014"
] | [
"YneA"
] | [
124
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053936"
] | [
"12581363"
] | [
"Identification of a protein, YneA, responsible for cell division suppression during the SOS response in Bacillus subtilis."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
124
] | 1 | [] | [] | 0 | true | Family | Cell division suppressor protein, YneA | Cell division suppressor protein, YneA | Cell_div_suppressor_YneA | 9 |
IPR022889 | 22,889 | DNA-binding protein, archaeal | DNA_bind_arc | Family | 785 | false | false | This entry represents DNA binding proteins from archaea belonging to the PDCD5 family. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00026"
] | [
"dsDNA_bind"
] | [
785
] | 1 | [] | [] | [] | 0 | [
"6iqc",
"6iqo"
] | 2 | [] | [] | [] | [] | 0 | [
"IPR002836"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Geoalkalibacter subterraneus",
"ecological metagenomes"
] | [
774,
1,
10
] | 3 | [] | [] | 0 | true | Family | DNA-binding protein, archaeal | DNA-binding protein, archaeal | DNA_bind_arc | 2 |
IPR022890 | 22,890 | Ferredoxin--NADP reductase, type 2 | Fd--NADP_Rdtase_type_2 | Family | 10,359 | false | false | The function of ferredoxin--NADP reductase is to mediate the following reaction: 2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH [ ]. Although all ferredoxin-NADP+ reductases (FNRs) catalyze the same reaction, they belong to two unrelated families of proteins: the plant-type and the glutathione re... | [
"GO:0004324"
] | [
"ferredoxin-NADP+ reductase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_01685"
] | [
"FENR2"
] | [
10359
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.18.1.2",
"PWY-101",
"PWY-8271"
] | [
"EC:1.18.1.2",
"METACYC:PWY-101",
"METACYC:PWY-8271"
] | 3 | [
"2zbw",
"3ab1",
"3lzw",
"3lzx",
"5twb",
"5twc",
"5xhu",
"5ygq",
"6a4j",
"6gar",
"6gas",
"8c16",
"8c3m"
] | 13 | [
"PUB00053937",
"PUB00053987"
] | [
"15252706",
"18307973"
] | [
"Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC.",
"Structural and functional diversity of ferredoxin-NADP(+) reductases."
] | [
2004,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
78,
10196,
14,
71
] | 4 | [] | [] | 0 | true | Family | Ferredoxin--NADP reductase, type 2 | Ferredoxin--NADP reductase, type 2 | Fd--NADP_Rdtase_type_2 | 7 |
IPR022891 | 22,891 | Triosephosphate isomerase, archaeal | Triosephosphate_isomerase_arc | Family | 822 | false | false | This entry represents archaeal triosephosphate isomerases. Triosephosphate isomerase ( ) (TIM) [ ] is the glycolytic enzyme that catalyses the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient... | [
"GO:0004807",
"GO:0006094",
"GO:0006096"
] | [
"triose-phosphate isomerase activity",
"gluconeogenesis",
"glycolytic process"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP"
] | [
"MF_00147_A"
] | [
"TIM_A"
] | [
822
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.3.1.1",
"PWY-1042",
"PWY-5484",
"PWY-6142",
"PWY-7003",
"PWY-8404"
] | [
"EC:5.3.1.1",
"METACYC:PWY-1042",
"METACYC:PWY-5484",
"METACYC:PWY-6142",
"METACYC:PWY-7003",
"METACYC:PWY-8404"
] | 6 | [
"1hg3",
"1w0m",
"2h6r",
"5csr",
"5css"
] | 5 | [
"PUB00000326",
"PUB00004091",
"PUB00014239",
"PUB00027646",
"PUB00029041",
"PUB00099868"
] | [
"2204417",
"2005961",
"12023819",
"12206759",
"12509510",
"31878282"
] | [
"Structure of yeast triosephosphate isomerase at 1.9-A resolution.",
"Enzyme catalysis: not different, just better.",
"Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease.",
"One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequen... | [
1990,
1991,
2002,
2002,
2003,
2019
] | 6 | [
"IPR000652"
] | [] | 1 | 0 | 1 | [
"Archaea",
"unclassified sequences"
] | [
808,
14
] | 2 | [] | [] | 0 | true | Family | Triosephosphate isomerase, archaeal | Triosephosphate isomerase, archaeal | Triosephosphate_isomerase_arc | 5 |
IPR022892 | 22,892 | Ribonuclease HI | RNaseHI | Family | 19,071 | false | false | Ribonuclease H (RNase H) recognises and cleaves the RNA strand of RNA-DNA heteroduplexes. RNases H are classified into two types. Type 1 RNases H include prokaryotic and eukaryotic RNases H1 and retroviral RNase H. Type 2 RNases H include prokaryotic and eukaryotic RNases H2 and bacterial RNase H3 [ , ]. In prokaryotes... | [
"GO:0004523"
] | [
"RNA-DNA hybrid ribonuclease activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"CDD"
] | [
"MF_00042",
"cd09278"
] | [
"RNase_H",
"RNase_HI_prokaryote_like"
] | [
14620,
19070
] | 2 | [
"EC"
] | [
"3.1.26.4"
] | [
"EC:3.1.26.4"
] | 1 | [
"1f21",
"1g15",
"1goa",
"1gob",
"1goc",
"1jl1",
"1jl2",
"1jxb",
"1kva",
"1kvb",
"1kvc",
"1lav",
"1law",
"1rbr",
"1rbs",
"1rbt",
"1rbu",
"1rbv",
"1rch",
"1rda",
"1rdb",
"1rdc",
"1rdd",
"1ril",
"1rnh",
"1wse",
"1wsf",
"1wsg",
"1wsh",
"1wsi",
"1wsj",
"2e4l"... | 53 | [
"PUB00018345",
"PUB00080551",
"PUB00080552"
] | [
"2177653",
"16232566",
"19228197"
] | [
"Ribonuclease H: from discovery to 3D structure.",
"Molecular diversities of RNases H.",
"Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes."
] | [
1990,
1999,
2009
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5,
18297,
72,
376,
321
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ribonuclease HI | Ribonuclease HI | RNaseHI | 9 |
IPR022893 | 22,893 | Shikimate dehydrogenase family | Shikimate_DH_fam | Family | 43,015 | false | false | This entry represents shikimate dehydrogenase ( ) and quinate/shikimate dehydrogenase ( ). The latter is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from ( ), in that it can use both quinate and shikimate as substrate and either NAD(+) or NADP(+) as acceptor. | [
"GO:0004764"
] | [
"shikimate 3-dehydrogenase (NADP+) activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PANTHER"
] | [
"MF_00222",
"PTHR21089"
] | [
"Shikimate_DH_AroE",
""
] | [
23408,
42778
] | 2 | [
"EC",
"EC",
"METACYC"
] | [
"1.1.1",
"1.1.1.25",
"PWY-6163"
] | [
"EC:1.1.1",
"EC:1.1.1.25",
"METACYC:PWY-6163"
] | 3 | [
"1npd",
"1npy",
"1nvt",
"1nyt",
"1o9b",
"1p74",
"1p77",
"1vi2",
"1wxd",
"2cy0",
"2d5c",
"2egg",
"2ev9",
"2gpt",
"2hk7",
"2hk8",
"2hk9",
"2nlo",
"2o7q",
"2o7s",
"3don",
"3doo",
"3fbt",
"3jyo",
"3jyp",
"3jyq",
"3o8q",
"3pgj",
"3phg",
"3phh",
"3phi",
"3phj"... | 57 | [] | [] | [] | [] | 0 | [] | [
"IPR011342",
"IPR022872"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
858,
36224,
5207,
726
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
2,
1,
14,
29
] | 5 | true | Family | Shikimate dehydrogenase family | Shikimate dehydrogenase family | Shikimate_DH_fam | 4 |
IPR022894 | 22,894 | Oligoribonuclease | Oligoribonuclease | Family | 21,297 | false | false | Oligoribonuclease (Orn) is a DEDDh-type DnaQ-like 3'-5' exoribonuclease that is responsible for degrading small oligoribonucleotides to mononucleotides. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the ac... | [
"GO:0000175"
] | [
"3'-5'-RNA exonuclease activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM",
"PANTHER",
"CDD"
] | [
"MF_00045",
"NF003765",
"PTHR11046",
"cd06135"
] | [
"Oligoribonuclease",
"PRK05359.1",
"",
"Orn"
] | [
10580,
15678,
20925,
15504
] | 4 | [
"EC",
"REACTOME"
] | [
"3.1.15.-",
"R-HSA-9836573"
] | [
"EC:3.1.15.-",
"REACTOME:R-HSA-9836573"
] | 2 | [
"1fxx",
"1j9a",
"1yta",
"2gbz",
"2igi",
"2qxf",
"3c94",
"3c95",
"3hl8",
"3hp9",
"3tr8",
"4hcb",
"4hcc",
"4jrp",
"4jrq",
"4js4",
"4js5",
"4rg8",
"5cy4",
"6a4a",
"6a4d",
"6a4e",
"6a4f",
"6j7y",
"6j7z",
"6j80",
"6n6a",
"6n6c",
"6n6d",
"6n6e",
"6n6f",
"6n6g"... | 49 | [
"PUB00040994",
"PUB00086001",
"PUB00086002"
] | [
"17029243",
"10851236",
"16682444"
] | [
"The crystal structure of XC847 from Xanthomonas campestris: a 3'-5' oligoribonuclease of DnaQ fold family with a novel opposingly shifted helix.",
"The human homolog of Escherichia coli Orn degrades small single-stranded RNA and DNA oligomers.",
"Oligoribonuclease is a common downstream target of lithium-induc... | [
2006,
2000,
2006
] | 3 | [] | [
"IPR023607"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Viruses",
"unclassified sequences"
] | [
15127,
5839,
19,
8,
304
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
5,
1,
3,
1,
5,
5,
9,
1,
6,
10,
1,
1,
4
] | 13 | true | Family | Oligoribonuclease | Oligoribonuclease | Oligoribonuclease | 9 |
IPR022895 | 22,895 | Flap endonuclease Xni | Xni | Family | 2,031 | false | false | This entry contains the bacterial flap endonuclease Xni (also known as YgdG), which was previously identified as a 3'-5' exonuclease and named exonuclease IX (ExoIX) [ , ]. Xni was subsequently found to possess flap endonuclease activity, but not exonuclease activity [ , , ]. | [
"GO:0048256"
] | [
"flap endonuclease activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_01192"
] | [
"Xni"
] | [
2031
] | 1 | [] | [] | [] | 0 | [
"3zd8",
"3zd9",
"3zda",
"3zdb",
"3zdc",
"3zdd",
"3zde"
] | 7 | [
"PUB00053938",
"PUB00053939",
"PUB00053941",
"PUB00069558",
"PUB00069563",
"PUB00094488",
"PUB00094489",
"PUB00094492"
] | [
"9592142",
"9840179",
"17567612",
"23821668",
"19000038",
"17559871",
"23451868",
"10409700"
] | [
"Exonuclease IX of Escherichia coli.",
"Exonuclease IX of Escherichia coli removes 3' phosphoglycolate end groups from DNA.",
"Molecular interactions of Escherichia coli ExoIX and identification of its associated 3'-5' exonuclease activity.",
"The structure of Escherichia coli ExoIX--implications for DNA bind... | [
1998,
1998,
2007,
2013,
2009,
2007,
2013,
1999
] | 8 | [
"IPR038969"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
2029,
2
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flap endonuclease Xni | Flap endonuclease Xni | Xni | 1 |
IPR022896 | 22,896 | Triosephosphate isomerase, bacterial/eukaryotic | TrioseP_Isoase_bac/euk | Family | 31,735 | false | false | Triosephosphate isomerase ( ) (TIM) [ ] is the glycolytic enzyme that catalyses the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, highly conserved in prokaryotes and euk... | [
"GO:0004807",
"GO:0006096"
] | [
"triose-phosphate isomerase activity",
"glycolytic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_00147_B"
] | [
"TIM_B"
] | [
31735
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REAC... | [
"5.3.1.1",
"PWY-1042",
"PWY-5484",
"PWY-6142",
"PWY-7003",
"PWY-8404",
"R-CEL-70171",
"R-CEL-70263",
"R-DDI-70171",
"R-DDI-70263",
"R-DME-70171",
"R-DME-70263",
"R-DRE-70171",
"R-DRE-70263",
"R-GGA-352875",
"R-GGA-352882",
"R-GGA-70171",
"R-GGA-70263",
"R-HSA-70171",
"R-HSA-702... | [
"EC:5.3.1.1",
"METACYC:PWY-1042",
"METACYC:PWY-5484",
"METACYC:PWY-6142",
"METACYC:PWY-7003",
"METACYC:PWY-8404",
"REACTOME:R-CEL-70171",
"REACTOME:R-CEL-70263",
"REACTOME:R-DDI-70171",
"REACTOME:R-DDI-70263",
"REACTOME:R-DME-70171",
"REACTOME:R-DME-70263",
"REACTOME:R-DRE-70171",
"REACTOM... | 32 | [
"1ag1",
"1amk",
"1aw1",
"1aw2",
"1b9b",
"1btm",
"1ci1",
"1dkw",
"1hti",
"1i45",
"1if2",
"1iig",
"1iih",
"1kv5",
"1lyx",
"1lzo",
"1m6j",
"1m7o",
"1m7p",
"1ml1",
"1mo0",
"1mss",
"1n55",
"1ney",
"1nf0",
"1o5x",
"1qds",
"1r2r",
"1r2s",
"1r2t",
"1spq",
"1sq7"... | 254 | [
"PUB00000326",
"PUB00004091",
"PUB00014239",
"PUB00027646",
"PUB00029041",
"PUB00099868"
] | [
"2204417",
"2005961",
"12023819",
"12206759",
"12509510",
"31878282"
] | [
"Structure of yeast triosephosphate isomerase at 1.9-A resolution.",
"Enzyme catalysis: not different, just better.",
"Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease.",
"One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequen... | [
1990,
1991,
2002,
2002,
2003,
2019
] | 6 | [
"IPR000652"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"unclassified sequences"
] | [
4,
24330,
6940,
1,
460
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
5,
1,
3,
1,
1,
5,
1,
1,
6,
11,
1,
1,
25
] | 13 | true | Family | Triosephosphate isomerase, bacterial/eukaryotic | Triosephosphate isomerase, bacterial/eukaryotic | TrioseP_Isoase_bac/euk | 8 |
IPR022897 | 22,897 | HTH-type transcription regulator MntR | HTH_tscrpt_reg_MntR | Family | 1,328 | false | false | This entry contains the Bacillus subtilis YqhN (MntR), which encodes a metalloregulatory protein distantly related to the Corynebacterium diphtheriae diphtheria toxin repressor (DtxR). While DtxR mediates the iron-dependent repression of iron uptake, MntR encodes a manganese modulated regulator of manganese transport. ... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00732"
] | [
"HTH_MntR"
] | [
1328
] | 1 | [] | [] | [] | 0 | [
"1on1",
"1on2",
"2ev0",
"2ev5",
"2ev6",
"2f5c",
"2f5d",
"2f5e",
"2f5f",
"2hyf",
"2hyg",
"3r60",
"3r61",
"4hv5",
"4hv6",
"4hx4",
"4hx7",
"4hx8",
"6kta",
"6ktb",
"9c4c",
"9c4d"
] | 22 | [
"PUB00053943"
] | [
"10760146"
] | [
"Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins."
] | [
2000
] | 1 | [
"IPR022689"
] | [] | 1 | 0 | 1 | [
"Bacillales",
"Eukaryota"
] | [
1326,
2
] | 2 | [] | [] | 0 | true | Family | HTH-type transcription regulator MntR | HTH-type transcription regulator MntR | HTH_tscrpt_reg_MntR | 1 |
IPR022898 | 22,898 | Ribonuclease HII | RNase_HII | Family | 26,522 | false | false | Ribonuclease HII is involved in the degradation of the ribonucleotide moiety on RNA-DNA hybrid molecules carrying out endonucleolytic cleavage to 5'-phospo-monoester [ , ]. This entry is specific for ribonuclease HII. Several bacteria, such as Bacillus subtilis, have two different type II RNases H, RNases HII and HIII ... | [
"GO:0004523"
] | [
"RNA-DNA hybrid ribonuclease activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_00052_B",
"NF000595",
"cd07182"
] | [
"RNase_HII_B",
"PRK00015.1-3",
"RNase_HII_bacteria_HII_like"
] | [
23215,
25888,
26445
] | 3 | [
"EC"
] | [
"3.1.26.4"
] | [
"EC:3.1.26.4"
] | 1 | [
"2etj",
"3o3f",
"3o3g",
"3o3h",
"4hht",
"5y9p",
"7uwe",
"7uwh"
] | 8 | [
"PUB00004477",
"PUB00021793",
"PUB00056173",
"PUB00079405",
"PUB00081181",
"PUB00081182"
] | [
"9241229",
"11254381",
"17322199",
"19228198",
"15978682",
"21095591"
] | [
"Comparative sequence analysis of ribonucleases HII, III, II PH and D.",
"Structural biochemistry of a type 2 RNase H: RNA primer recognition and removal during DNA replication.",
"Biochemical characterization and functional complementation of ribonuclease HII and ribonuclease HIII from Chlamydophila pneumoniae... | [
1997,
2001,
2007,
2009,
2005,
2010
] | 6 | [
"IPR001352"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Viruses",
"candidate division MSBL1 archaeon SCGC-AAA382N08",
"unclassified sequences"
] | [
25393,
386,
15,
1,
727
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ribonuclease HII | Ribonuclease HII | RNase_HII | 7 |
IPR022899 | 22,899 | Deoxyhypusine synthase, putative, archaeal | Deoxyhypus_synthase_arc | Family | 378 | false | false | This entry represents probable deoxyhypusine synthases from archaea. Eukaryotic initiation factor 5A (eIF-5A), now considered to be an elongation factor (see ), contains an unusual amino acid, hypusine [N epsilon-(4-aminobutyl-2-hydroxy)lysine]. The first step in the post-translational formation of hypusine is catalyse... | [
"GO:0034038"
] | [
"deoxyhypusine synthase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_00153"
] | [
"DHS"
] | [
378
] | 1 | [
"EC"
] | [
"2.5.1.46"
] | [
"EC:2.5.1.46"
] | 1 | [
"7cmc",
"8put"
] | 2 | [
"PUB00005808"
] | [
"9493264"
] | [
"Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site."
] | [
1998
] | 1 | [
"IPR002773"
] | [] | 1 | 0 | 1 | [
"Archaea"
] | [
378
] | 1 | [] | [] | 0 | true | Family | Deoxyhypusine synthase, putative, archaeal | Deoxyhypusine synthase, putative, archaeal | Deoxyhypus_synthase_arc | 9 |
IPR022901 | 22,901 | snRNP Sm-like, putative, archaea | snRNP_Sm-like_arc | Family | 539 | false | false | This entry represents a family of Sm-like ribonucleoproteins from archaea. | [] | [] | [] | 0 | [
"HAMAP",
"CDD"
] | [
"MF_00257",
"cd01731"
] | [
"Lsm_RuxX",
"archaeal_Sm1"
] | [
190,
537
] | 2 | [] | [] | [] | 0 | [
"1h64",
"1i4k",
"1i5l",
"1i81",
"1i8f",
"1jbm",
"1jri",
"1lnx",
"1loj",
"1m8v",
"1mgq",
"1th7",
"5mki",
"5mkn"
] | 14 | [] | [] | [] | [] | 0 | [
"IPR044641"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Candidatus Segetimicrobium genomatis",
"Eukaryota",
"ecological metagenomes"
] | [
513,
1,
3,
22
] | 4 | [] | [] | 0 | true | Family | snRNP Sm-like, putative, archaea | snRNP Sm-like, putative, archaea | snRNP_Sm-like_arc | 9 |
IPR022902 | 22,902 | N-acetyltransferase Eis | NAcTrfase_Eis | Family | 5,060 | false | false | Eis (enhanced intracellular survival) from Mycobacterium has been identified as a secretory protein that is released into the host cell to modulate inflammatory responses [ , , ]. It is an acetyltransferase of the GCN5-related family of N-acetyltransferases that initiates suppression of host immune responses by acetyla... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01812",
"NF002367"
] | [
"Eis",
"PRK01346.1-4"
] | [
4996,
4424
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.3.1.-",
"PWY-3602",
"PWY-361",
"PWY-4801",
"PWY-4922",
"PWY-5048",
"PWY-5139",
"PWY-5268",
"PWY-5284",
"PWY-5292",
"PWY-5307",
"PWY-5313",
"PWY-5317",
"PWY-5318",
"PWY-5353",
"PWY-5400",
"PWY-5473",
"PWY-5475",
"PWY-5477",
"PWY-5660",
"PWY-5679",
"PWY-5710",
"PWY-5794"... | [
"EC:2.3.1.-",
"METACYC:PWY-3602",
"METACYC:PWY-361",
"METACYC:PWY-4801",
"METACYC:PWY-4922",
"METACYC:PWY-5048",
"METACYC:PWY-5139",
"METACYC:PWY-5268",
"METACYC:PWY-5284",
"METACYC:PWY-5292",
"METACYC:PWY-5307",
"METACYC:PWY-5313",
"METACYC:PWY-5317",
"METACYC:PWY-5318",
"METACYC:PWY-53... | 220 | [
"3r1k",
"3ryo",
"3sxn",
"3sxo",
"3uy5",
"4jd6",
"4qb9",
"5ebv",
"5ec4",
"5iv0",
"5tvj",
"6b0u",
"6b3t",
"6p3t",
"6p3u",
"6p3v",
"6rft",
"6rfx",
"6rfy",
"6vur",
"6vus",
"6vut",
"6vuu",
"6vuw",
"6vux",
"6vuy",
"6vuz",
"6vv0",
"6vv1",
"6vv2",
"6vv3",
"6x10"... | 50 | [
"PUB00083897",
"PUB00083898",
"PUB00083899"
] | [
"17449476",
"17259625",
"21187903"
] | [
"Eis (enhanced intracellular survival) protein of Mycobacterium tuberculosis disturbs the cross regulation of T-cells.",
"Expression, production and release of the Eis protein by Mycobacterium tuberculosis during infection of macrophages and its effect on cytokine secretion.",
"Mycobacterium tuberculosis eis re... | [
2007,
2007,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Geodia barretti",
"ecological metagenomes"
] | [
5045,
1,
14
] | 3 | [] | [] | 0 | true | Family | N-acetyltransferase Eis | N-acetyltransferase Eis | NAcTrfase_Eis | 2 |
IPR022903 | 22,903 | Glycine cleavage system T protein, bacteria | GcvT_bac | Family | 15,153 | false | false | This entry represents GcvT from bacteria [ ]. The glycine cleavage multienzyme complex (GCV) catalyses the catabolism of glycine in eukaryotes. GCVT (aminomethyltransferase, ) is a folate-dependent enzyme that catalyses the release of ammonia and the transfer of the methylene carbon unit (C1 unit) to tetrahydrofolate (... | [
"GO:0004047",
"GO:0006546"
] | [
"aminomethyltransferase activity",
"glycine catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_00259"
] | [
"GcvT"
] | [
15153
] | 1 | [
"EC"
] | [
"2.1.2.10"
] | [
"EC:2.1.2.10"
] | 1 | [
"1v5v",
"1vlo",
"1woo",
"1wop",
"1wor",
"1wos",
"1yx2",
"3a8i",
"3a8j",
"3a8k"
] | 10 | [
"PUB00001870",
"PUB00022265",
"PUB00038140",
"PUB00069711",
"PUB00069712",
"PUB00160522"
] | [
"9047339",
"15489424",
"16051266",
"20375021",
"8219277",
"20489182"
] | [
"Cloning, and molecular characterization of the GCV1 gene encoding the glycine cleavage T-protein from Saccharomyces cerevisiae.",
"Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolism.",
"Crystal structure of human T-protein of glycine... | [
1997,
2004,
2005,
2010,
1993,
2010
] | 6 | [
"IPR006223"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
386,
14583,
9,
175
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glycine cleavage system T protein, bacteria | Glycine cleavage system T protein, bacteria | GcvT_bac | 3 |
IPR022905 | 22,905 | DNA-directed RNA polymerase subunit Rpo11-like | Rpo11-like | Family | 8,854 | false | false | DNA-directed RNA polymerases, also known as DNA-dependent RNA polymerases, are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. Eukaryotes have three different DNA-directed RNA polymerases (RNAPs), Pol I, II, and III, whereas Archaea and Bacteria have single enzym... | [
"GO:0003899",
"GO:0006351"
] | [
"DNA-directed RNA polymerase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_00261"
] | [
"RNApol_arch_Rpo11"
] | [
8854
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.6",
"R-BTA-112382",
"R-BTA-113418",
"R-BTA-5578749",
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-6803529",
"R-BTA-6807505",
"R-BTA-72086",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-72203",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-75953",... | [
"EC:2.7.7.6",
"REACTOME:R-BTA-112382",
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-5578749",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-6803529",
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-72086",... | 183 | [
"1i3q",
"1i50",
"1i6h",
"1k83",
"1nik",
"1nt9",
"1pqv",
"1r5u",
"1r9s",
"1r9t",
"1sfo",
"1twa",
"1twc",
"1twf",
"1twg",
"1twh",
"1wcm",
"1xpp",
"1y1v",
"1y1w",
"1y1y",
"1y77",
"2b63",
"2b8k",
"2e2h",
"2e2i",
"2e2j",
"2ja5",
"2ja6",
"2ja7",
"2ja8",
"2nvq"... | 534 | [
"PUB00045896",
"PUB00059148",
"PUB00059149"
] | [
"18235446",
"19419240",
"19880312"
] | [
"The X-ray crystal structure of RNA polymerase from Archaea.",
"Evolution of Complex RNA Polymerases: The Complete Archaeal RNA Polymerase Structure.",
"Archaeal RNA polymerase."
] | [
2008,
2009,
2009
] | 3 | [] | [
"IPR033898",
"IPR037685"
] | 0 | 2 | 0 | [
"Archaea",
"Candidatus Buchananbacteria bacterium RIFCSPHIGHO2_01_FULL_39_14",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
887,
1,
7929,
6,
31
] | 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,
2,
2,
9,
12,
7,
2,
5,
5,
2,
2,
15
] | 12 | true | Family | DNA-directed RNA polymerase subunit Rpo11-like | DNA-directed RNA polymerase subunit Rpo11-like | Rpo11-like | 9 |
IPR022906 | 22,906 | Uncharacterised protein family UPF0127 | UPF0127 | Family | 47 | false | false | This family represents a group of archaeal proteins that are functionally uncharacterised. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00263"
] | [
"UPF0127"
] | [
47
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR003795"
] | [] | 1 | 0 | 1 | [
"Methanobacteriota"
] | [
47
] | 1 | [] | [] | 0 | true | Family | Uncharacterised protein family UPF0127 | Uncharacterised protein family UPF0127 | UPF0127 | 4 |
IPR022907 | 22,907 | VapC family | VapC_family | Family | 27,206 | false | false | This entry represents VapC family of proteins, which are toxic components of a toxin-antitoxin (TA) module. VapC family members are ribonucleases but are unable to degrade ds- or ss-DNA [ ]. Several bacterial VapC proteins have been shown to be tRNA (fMet)-specific endonucleases [ ]. | [
"GO:0004540"
] | [
"RNA nuclease activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_00265"
] | [
"VapC_Nob1"
] | [
27206
] | 1 | [] | [] | [] | 0 | [
"1o4w",
"1v8o",
"1v8p",
"1v96",
"1w8i",
"1y82",
"1ye5",
"2bsq",
"2fe1",
"2h1c",
"2h1o",
"2lcq",
"3dbo",
"3h87",
"3tnd",
"4chg",
"4xgq",
"4xgr",
"5ecd",
"5ecw",
"5ecy",
"5ed0",
"5h4g",
"5h4h",
"5k8j",
"5l6l",
"5l6m",
"5sv2",
"5wz4",
"5wzf",
"5x3t",
"6a7v"... | 43 | [
"PUB00057856",
"PUB00085651"
] | [
"21502523",
"17496075"
] | [
"Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA.",
"VapC-1 of nontypeable Haemophilus influenzae is a ribonuclease."
] | [
2011,
2007
] | 2 | [] | [
"IPR006226",
"IPR016647"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1103,
25711,
20,
3,
369
] | 5 | [] | [] | 0 | true | Family | VapC family | VapC family | VapC_family | 4 |
IPR022908 | 22,908 | tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase | Taw3 | Family | 298 | false | false | The presence of Wyosine derivatives, such as wybutosine (yW), at position 37 of tRNA(Phe) is characteristic of Eukaryotes and Archaea. Four of the five wybutosine biosynthetic enzymes from Eukaryotes have homologues in Archaea. Taw3 is the archaeal homologue of eukaryotic Tyw3, responsible for the methylation at N4 of ... | [
"GO:0008175",
"GO:0030488",
"GO:0031591"
] | [
"tRNA methyltransferase activity",
"tRNA methylation",
"wybutosine biosynthetic process"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP"
] | [
"MF_00266"
] | [
"TYW3_archaea"
] | [
298
] | 1 | [
"EC",
"METACYC"
] | [
"2.1.1.282",
"PWY-7286"
] | [
"EC:2.1.1.282",
"METACYC:PWY-7286"
] | 2 | [
"1tlj",
"2drv",
"2dvk",
"2it2",
"2it3",
"2qg3"
] | 6 | [
"PUB00058054"
] | [
"20382657"
] | [
"Biosynthesis of wyosine derivatives in tRNA: an ancient and highly diverse pathway in Archaea."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"groundwater metagenome"
] | [
284,
12,
2
] | 3 | [] | [] | 0 | true | Family | tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase | tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase | Taw3 | 9 |
IPR022909 | 22,909 | Large ribosomal subunit protein uL10, archaea | Ribosomal_uL10_arc | Family | 885 | false | false | This entry represents the large ribosomal subunit protein uL10 found in archaea. 50S ribosomal protein uL10 forms the large subunit's ribosomal stalk, playing a central role in the interaction of the ribosome with elongation factors [ ]. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all o... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00280"
] | [
"Ribosomal_uL10_arch"
] | [
885
] | 1 | [] | [] | [] | 0 | [
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b",
"1yhq"... | 66 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00064870"
] | [
"11297922",
"11290319",
"11114498",
"17804412"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism."
] | [
2001,
2001,
2000,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Candidatus Rhodobacter oscarellae",
"ecological metagenomes"
] | [
876,
1,
8
] | 3 | [] | [] | 0 | true | Family | Large ribosomal subunit protein uL10, archaea | Large ribosomal subunit protein uL10, archaea | Ribosomal_uL10_arc | 9 |
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