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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR004306 | 4,306 | Domain of unknown function DUF237 | DUF237 | Domain | 51 | false | false | This is a domain of unknown function found in mycoplasma. It is found at the C-terminal region. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03072"
] | [
"DUF237"
] | [
51
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
51
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF237 | Domain of unknown function DUF237 | DUF237 | 2 |
IPR004307 | 4,307 | TspO/MBR-related protein | TspO_MBR | Family | 15,271 | false | false | Members of this group are involved in transmembrane signalling. In both prokaryotes and mitochondria they are localized to the outer membrane, and have been shown to bind and transport dicarboxylic tetrapyrrole intermediates of the haem biosynthetic pathway [ , ]. They are associated with the major outer membrane porin... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PIRSF",
"PANTHER",
"CDD"
] | [
"PF03073",
"PIRSF005859",
"PTHR10057",
"cd15904"
] | [
"TspO_MBR",
"PBR",
"",
"TSPO_MBR"
] | [
15248,
10880,
13676,
13557
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196108",
"R-MMU-196108",
"R-RNO-196108"
] | [
"REACTOME:R-HSA-196108",
"REACTOME:R-MMU-196108",
"REACTOME:R-RNO-196108"
] | 3 | [
"2mgy",
"2n02",
"4ryi",
"4ryj",
"4rym",
"4ryn",
"4ryo",
"4ryq",
"4ryr",
"4uc1",
"4uc2",
"4uc3",
"5duo",
"8e7w",
"8e7x",
"8e7y",
"8e7z",
"8vgu"
] | 18 | [
"PUB00007483",
"PUB00015672",
"PUB00015711",
"PUB00015778",
"PUB00015782",
"PUB00015861",
"PUB00071816",
"PUB00071817"
] | [
"7673149",
"1373486",
"10409680",
"8114671",
"11591680",
"11097914",
"23518318",
"22364127"
] | [
"A sensory transducer homologous to the mammalian peripheral-type benzodiazepine receptor regulates photosynthetic membrane complex formation in Rhodobacter sphaeroides 2.4.1.",
"Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide... | [
1995,
1992,
1999,
1994,
2001,
2000,
2013,
2012
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
392,
9672,
5035,
25,
147
] | 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",
"Schizosaccharomyces pombe (stra... | [
3,
2,
1,
1,
8,
5,
1,
2,
5,
1,
3
] | 11 | true | Family | TspO/MBR-related protein | TspO/MBR-related protein | TspO_MBR | 8 |
IPR004308 | 4,308 | Glutamate-cysteine ligase catalytic subunit | GCS | Family | 5,656 | false | false | This family represents the catalytic subunit of glutamate-cysteine ligase ( ), also known as gamma-glutamylcysteine synthetase (GCS). This enzyme catalyses the rate limiting step in the biosynthesis of glutathione. The eukaryotic enzyme is a dimer of a heavy chain and a light chain with all the catalytic activity exhib... | [
"GO:0004357",
"GO:0006750"
] | [
"glutamate-cysteine ligase activity",
"glutathione biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PANTHER"
] | [
"PF03074",
"PTHR11164"
] | [
"GCS",
""
] | [
5656,
5618
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.2.2",
"GenProp0030",
"GenProp1359",
"GenProp1664",
"PWY-6840",
"PWY-7255",
"PWY-8043",
"R-CEL-174403",
"R-DME-174403",
"R-HSA-174403",
"R-HSA-5578999",
"R-HSA-9818027",
"R-MMU-174403",
"R-RNO-174403",
"R-SPO-174403"
] | [
"EC:6.3.2.2",
"GP:GenProp0030",
"GP:GenProp1359",
"GP:GenProp1664",
"METACYC:PWY-6840",
"METACYC:PWY-7255",
"METACYC:PWY-8043",
"REACTOME:R-CEL-174403",
"REACTOME:R-DME-174403",
"REACTOME:R-HSA-174403",
"REACTOME:R-HSA-5578999",
"REACTOME:R-HSA-9818027",
"REACTOME:R-MMU-174403",
"REACTOME:... | 15 | [
"3ig5",
"3ig8",
"3lvv",
"3lvw"
] | 4 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5656
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
1,
1,
2,
8,
4,
1,
5,
1,
1
] | 9 | true | Family | Glutamate-cysteine ligase catalytic subunit | Glutamate-cysteine ligase catalytic subunit | GCS | 1 |
IPR004310 | 4,310 | Equine arteritis virus Gp3 | EAV_Gp3 | Family | 207 | false | false | This entry contains proteins encoded by ORF3 of Equine arteritis virus. They are possible envelope glcoproteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03076"
] | [
"GP3"
] | [
207
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Equine arteritis virus"
] | [
207
] | 1 | [] | [] | 0 | true | Family | Equine arteritis virus Gp3 | Equine arteritis virus Gp3 | EAV_Gp3 | 7 |
IPR004311 | 4,311 | Vacuolating cytotoxin, putative | Vacuolating_cytotoxin_put | Domain | 359 | false | false | Proteins containing this domain include a number of Helicobacter pylori outer membrane proteins with multiple copies of this small conserved region. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03077"
] | [
"VacA2"
] | [
359
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Helicobacter"
] | [
359
] | 1 | [] | [] | 0 | true | Domain | Vacuolating cytotoxin, putative | Vacuolating cytotoxin, putative | Vacuolating_cytotoxin_put | 3 |
IPR004313 | 4,313 | Acireductone dioxygenase ARD family | ARD | Family | 10,302 | false | false | The two acireductone dioxygenase enzymes (ARD and ARD', previously known as E-2 and E-2') from Klebsiella pneumoniae share the same amino acid sequence , but bind different metal ions: ARD binds Ni2+, ARD' binds Fe2+ [ ]. ARD and ARD' can be experimentally interconverted by removal of the bound metal ion and reconstitu... | [
"GO:0010308",
"GO:0010309"
] | [
"acireductone dioxygenase (Ni2+-requiring) activity",
"acireductone dioxygenase [iron(II)-requiring] activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PANTHER",
"CDD"
] | [
"PF03079",
"PTHR23418",
"cd02232"
] | [
"ARD",
"",
"cupin_ARD"
] | [
10270,
9746,
9665
] | 3 | [
"EC",
"EC",
"GP",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.13.11.53",
"1.13.11.54",
"GenProp0729",
"PWY-4361",
"PWY-5389",
"R-BTA-1237112",
"R-DDI-1237112",
"R-DME-1237112",
"R-DRE-1237112",
"R-GGA-1237112",
"R-HSA-1237112",
"R-MMU-1237112",
"R-RNO-1237112",
"R-SCE-1237112",
"R-SPO-1237112"
] | [
"EC:1.13.11.53",
"EC:1.13.11.54",
"GP:GenProp0729",
"METACYC:PWY-4361",
"METACYC:PWY-5389",
"REACTOME:R-BTA-1237112",
"REACTOME:R-DDI-1237112",
"REACTOME:R-DME-1237112",
"REACTOME:R-DRE-1237112",
"REACTOME:R-GGA-1237112",
"REACTOME:R-HSA-1237112",
"REACTOME:R-MMU-1237112",
"REACTOME:R-RNO-12... | 15 | [
"1vr3",
"1zrr",
"2hji",
"4qgl",
"4qgm",
"4qgn",
"5i8s",
"5i8t",
"5i8y",
"5i91",
"5i93",
"7jxg"
] | 12 | [
"PUB00007489",
"PUB00007490",
"PUB00064756",
"PUB00075695"
] | [
"9880484",
"11371200",
"15938715",
"16297065"
] | [
"One protein, two enzymes.",
"Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae.",
"Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway.",
... | [
1999,
2001,
2005,
2005
] | 4 | [] | [
"IPR023956",
"IPR027496"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Thermoplasmatales",
"metagenomes"
] | [
4604,
5679,
2,
17
] | 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... | [
24,
4,
1,
2,
3,
1,
1,
8,
4,
1,
1,
26
] | 12 | true | Family | Acireductone dioxygenase ARD family | Acireductone dioxygenase ARD family | ARD | 9 |
IPR004314 | 4,314 | Neprosin | Neprosin | Domain | 13,160 | false | false | Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is Neprosin, characterised from the pitcher plant Nepenthes ventrata. This is a glutamic endopeptidase that preferentially cleaves peptide bonds on the C-terminal ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF03080",
"PS52045"
] | [
"Neprosin",
"NEPROSIN_PEP_CD"
] | [
12902,
12908
] | 2 | [] | [] | [] | 0 | [
"7zu8",
"7zva",
"7zvb",
"7zvc",
"9qr8"
] | 5 | [
"PUB00081922",
"PUB00151161",
"PUB00151162",
"PUB00160246",
"PUB00160247"
] | [
"27481162",
"28404794",
"35915115",
"35537348",
"36461675"
] | [
"Addressing proteolytic efficiency in enzymatic degradation therapy for celiac disease.",
"Neprosin, a Selective Prolyl Endoprotease for Bottom-up Proteomics and Histone Mapping.",
"Molecular and in vivo studies of a glutamate-class prolyl-endopeptidase for coeliac disease therapy.",
"Neprosin belongs to a ne... | [
2016,
2017,
2022,
2022,
2023
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
253,
12907
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
264,
107,
73
] | 3 | true | Domain | Neprosin | Neprosin | Neprosin | 3 |
IPR004315 | 4,315 | Male Drosophila accessory gland secretory protein | Male_ac_gland_sc | Family | 40 | false | false | The accessory gland of male insects is a genital tissue that secretes many components of the ejaculatory fluid, some of which affect the female's receptivity to courtship and her rate of oviposition. The protein is expressed exclusively in the male accessory glands of adult Drosophila melanogaster. During copulation it... | [
"GO:0007618",
"GO:0005576"
] | [
"mating",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF03082"
] | [
"MAGSP"
] | [
40
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007491"
] | [
"3142802"
] | [
"Structure and expression of a Drosophila male accessory gland gene whose product resembles a peptide pheromone precursor."
] | [
1988
] | 1 | [] | [] | 0 | 0 | null | [
"Photobacterium atrarenae",
"melanogaster group"
] | [
1,
39
] | 2 | [
"Drosophila melanogaster"
] | [
1
] | 1 | true | Family | Male Drosophila accessory gland secretory protein | Male Drosophila accessory gland secretory protein | Male_ac_gland_sc | 1 |
IPR004316 | 4,316 | Sugar transporter SWEET repeat | SWEET_rpt | Repeat | 19,703 | false | false | This entry includes Sugar Will Eventually be Exported Transporters (SWEETs) which are specific sugar efflux transporters essential for the maintenance of animal blood glucose levels, plant nectar production, and plant seed and pollen development [ , ]. They can carry mono- and disaccharides across a membrane following ... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF03083"
] | [
"MtN3_slv"
] | [
19703
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-189200",
"R-DRE-189200",
"R-HSA-189200",
"R-MMU-189200",
"R-RNO-189200",
"R-XTR-189200"
] | [
"REACTOME:R-DDI-189200",
"REACTOME:R-DRE-189200",
"REACTOME:R-HSA-189200",
"REACTOME:R-MMU-189200",
"REACTOME:R-RNO-189200",
"REACTOME:R-XTR-189200"
] | 6 | [
"5ctg",
"5cth",
"5uhq",
"5xpd"
] | 4 | [
"PUB00007493",
"PUB00007494",
"PUB00059211",
"PUB00076333",
"PUB00105491",
"PUB00151012",
"PUB00151013"
] | [
"8634476",
"8630032",
"21107422",
"24027245",
"29872447",
"26479032",
"28878024"
] | [
"Use of a subtractive hybridization approach to identify new Medicago truncatula genes induced during root nodule development.",
"Molecular cloning and characterization of a novel stromal cell-derived cDNA encoding a protein that facilitates gene activation of recombination activating gene (RAG)-1 in human lympho... | [
1996,
1996,
2010,
2013,
2018,
2015,
2017
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
76,
2026,
2,
17556,
43
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
65,
9,
3,
3,
6,
4,
41,
7,
102
] | 9 | true | Repeat | Sugar transporter SWEET repeat | Sugar transporter SWEET repeat | SWEET_rpt | 5 |
IPR004317 | 4,317 | Sigma1/sigma2, reoviral | Sigma_1_2_reovir | Family | 392 | false | false | Reoviruses are double-stranded RNA viruses that lack a membrane envelope. Their capsid is organised in two concentric icosahedral layers: an inner core and an outer capsid layer. The sigma1 protein is found in the outer capsid, and the sigma2 protein is found in the core. There are four other kinds of protein (besides ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03084"
] | [
"Sigma_1_2"
] | [
392
] | 1 | [] | [] | [] | 0 | [
"1ej6",
"2cse",
"2vak",
"3iyl",
"3k1q",
"5zvt",
"6xf8",
"6ztz",
"8fjk",
"8fjl",
"9cyx",
"9cyy"
] | 12 | [
"PUB00007495",
"PUB00007496",
"PUB00007497",
"PUB00007498",
"PUB00007499"
] | [
"9971813",
"11438552",
"11239401",
"11287552",
"9311901"
] | [
"The reovirus mutant tsA279 L2 gene is associated with generation of a spikeless core particle: implications for capsid assembly.",
"Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein.",
"Junction adhesion molecule is a receptor for reovirus.",
"Reovi... | [
1999,
2001,
2001,
2001,
1997
] | 5 | [] | [] | 0 | 0 | null | [
"Reovirales"
] | [
392
] | 1 | [] | [] | 0 | true | Family | Sigma1/sigma2, reoviral | Sigma1/sigma2, reoviral | Sigma_1_2_reovir | 7 |
IPR004318 | 4,318 | Rhoptry-associated protein 1 | RAP-1 | Family | 332 | false | false | Members of this family are found in the parasite Babesia bigemina. Other rhoptry-associated proteins are found in Plasmodium falciparum but these do not belong to this family. Animal infection with B. bigemina may produce a pattern similar to human malaria [ ]. Rhoptry organelles form part of the apical complex in apic... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03085"
] | [
"RAP-1"
] | [
332
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007500",
"PUB00007501",
"PUB00007502",
"PUB00007503",
"PUB00007504"
] | [
"10614497",
"9662706",
"9476795",
"9529082",
"10364599"
] | [
"Modulation of host immune responses by protozoal DNA.",
"Structure, sequence, and transcriptional analysis of the Babesia bovis rap-1 multigene locus.",
"Genetic variation in the dimorphic regions of RAP-1 genes and rap-1 loci of Babesia bigemina.",
"Helper T-cell epitopes encoded by the Babesia bigemina rap... | [
1999,
1998,
1997,
1998,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Piroplasmida"
] | [
332
] | 1 | [] | [] | 0 | true | Family | Rhoptry-associated protein 1 | Rhoptry-associated protein 1 | RAP-1 | 5 |
IPR004319 | 4,319 | Domain of unknown function DUF240 | DUF240 | Domain | 50 | false | false | This is a domain of unknown function found in mycoplasma. It is found at the N-terminal region. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03086"
] | [
"DUF240"
] | [
50
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Mycoplasmoides",
"Parnassius apollo"
] | [
49,
1
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function DUF240 | Domain of unknown function DUF240 | DUF240 | 2 |
IPR004320 | 4,320 | Protein BPS1, chloroplastic | BPS1_pln | Family | 10,342 | false | false | This family includes BPS1 (Protein BYPASS 1) from plants, a protein required for normal root and shoot development. It prevents constitutive production of a root mobile carotenoid-derived signalling compound that is capable of arresting shoot and leaf development [ , ]. | [
"GO:0048364",
"GO:0048367"
] | [
"root development",
"shoot system development"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF03087"
] | [
"BPS1"
] | [
10342
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053689",
"PUB00053690"
] | [
"15458645",
"17217459"
] | [
"BYPASS1 negatively regulates a root-derived signal that controls plant architecture.",
"Dissecting the biosynthetic pathway for the bypass1 root-derived signal."
] | [
2004,
2007
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
10342
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
80,
91,
51
] | 3 | true | Family | Protein BPS1, chloroplastic | Protein BPS1, chloroplastic | BPS1_pln | 3 |
IPR004321 | 4,321 | V-D-J recombination activating protein 2 | RAG2 | Family | 14,393 | false | false | The variable portion of the genes encoding immunoglobulins and T cell receptors are assembled from component V, D, and J DNA segments by a site-specific recombination reaction termed V(D)J recombination. V(D)J recombination is targeted to specific sites on the chromosome by recombination signal sequences (RSSs) that fl... | [
"GO:0003677",
"GO:0006310",
"GO:0005634"
] | [
"DNA binding",
"DNA recombination",
"nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF03089",
"PTHR10960"
] | [
"RAG2",
""
] | [
14385,
14386
] | 2 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-1266695",
"R-HSA-5687128"
] | [
"REACTOME:R-HSA-1266695",
"REACTOME:R-HSA-5687128"
] | 2 | [
"2jwo",
"2v83",
"2v85",
"2v86",
"2v87",
"2v88",
"2v89",
"3jbw",
"3jbx",
"3jby",
"4wwx",
"5zdz",
"5ze0",
"5ze1",
"5ze2",
"6cg0",
"6cij",
"6cik",
"6cil",
"6cim",
"6dbi",
"6dbj",
"6dbl",
"6dbo",
"6dbq",
"6dbr",
"6dbt",
"6dbu",
"6dbv",
"6dbw",
"6dbx",
"6oem"... | 49 | [
"PUB00007505"
] | [
"11961538"
] | [
"DNA repair: breaking the seal."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
14393
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
5,
6,
4
] | 4 | true | Family | V-D-J recombination activating protein 2 | V-D-J recombination activating protein 2 | RAG2 | 4 |
IPR004322 | 4,322 | Plasmid replicase, bacterial | Plasmid_replicase_bac | Family | 1,714 | false | false | This is a family of bacterial plasmid DNA replication initiator proteins. These RepA proteins exist as monomers and dimers in equilibrium: monomers bind directly to repeated DNA sequences and thus activate replication; dimers repress repA transcription by binding an inversely repeated DNA operator. Dimer dissociation c... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03090"
] | [
"Replicase"
] | [
1714
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Plasmid pEP2",
"unclassified sequences"
] | [
1683,
8,
1,
22
] | 4 | [] | [] | 0 | true | Family | Plasmid replicase, bacterial | Plasmid replicase, bacterial | Plasmid_replicase_bac | 5 |
IPR004323 | 4,323 | Divalent ion tolerance protein, CutA | Ion_tolerance_CutA | Family | 12,415 | false | false | The CutA family of proteins which exhibit ion tolerance are found in a large variety of species [ ]. In E.Coli, two operons on the cutA locus contain genes that encode three proteins, CutA1, CutA2 and CutA3. CutA1 proteins are found in the cytoplasm while CutA2 (50kDa) and CutA3 (24kDa) are located in the inner membran... | [
"GO:0010038"
] | [
"response to metal ion"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF03091",
"PTHR23419"
] | [
"CutA1",
""
] | [
12406,
11846
] | 2 | [] | [] | [] | 0 | [
"1j2v",
"1kr4",
"1naq",
"1nza",
"1o5j",
"1osc",
"1p1l",
"1uku",
"1umj",
"1v6h",
"1vhf",
"1xk8",
"2e66",
"2nuh",
"2zfh",
"2zom",
"3aa8",
"3aa9",
"3ah6",
"3ahp",
"3gsd",
"3opk",
"3x3u",
"4e98",
"4iyq",
"4nyo",
"4nyp",
"4y65",
"4y6i",
"4zk7",
"6gdu",
"6gdv"... | 43 | [
"PUB00007507",
"PUB00014093",
"PUB00022783",
"PUB00028855",
"PUB00056052"
] | [
"9260936",
"12949080",
"15351719",
"14705033",
"10954708"
] | [
"A Salmonella typhimurium genetic locus which confers copper tolerance on copper-sensitive mutants of Escherichia coli.",
"The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction.",
"Structural evidence for guanidine-protein side chain interactions: crystal struc... | [
1997,
2003,
2004,
2004,
2000
] | 5 | [] | [
"IPR023700"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
616,
8353,
3266,
180
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
6,
2,
1,
4,
6,
6,
11,
4
] | 10 | true | Family | Divalent ion tolerance protein, CutA | Divalent ion tolerance protein, CutA | Ion_tolerance_CutA | 2 |
IPR004324 | 4,324 | Folate-biopterin transporter | FBT | Family | 4,141 | false | false | This entry includes folate-biopterin transporters (FBTs) from blue-green algae and plants, including Slr0642 protein from Synechocystis and its plastidial orthologue At2g32040 from Arabidopsis [ ]. Both Slr0642 protein and At2g32040 mediate folate monoglutamate transport involved in tetrahydrofolate biosynthesis. Howev... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00788"
] | [
"fbt"
] | [
4141
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00071846"
] | [
"19923217"
] | [
"Identification of transport-critical residues in a folate transporter from the folate-biopterin transporter (FBT) family."
] | [
2010
] | 1 | [
"IPR039309"
] | [] | 1 | 0 | 1 | [
"Cyanobacteriota",
"Eukaryota",
"Virus NIOZ-UU159"
] | [
317,
3823,
1
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
29,
17,
33
] | 3 | true | Family | Folate-biopterin transporter | Folate-biopterin transporter | FBT | 2 |
IPR004327 | 4,327 | Phosphotyrosyl phosphatase activator, PTPA | Phstyr_phstse_ac | Family | 7,352 | false | false | Phosphotyrosyl phosphatase activator (PTPA, also known as protein phosphatase 2A activator) proteins stimulate the phosphotyrosyl phosphatase (PTPase) activity of the dimeric form of protein phosphatase 2A (PP2A). PTPase activity in PP2A (in vitro) is relatively low when compared to the better recognised phosphoserine/... | [
"GO:0019211"
] | [
"phosphatase activator activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PIRSF",
"PANTHER",
"CDD"
] | [
"PF03095",
"PIRSF016325",
"PTHR10012",
"cd04087"
] | [
"PTPA",
"Phstyr_phstse_ac",
"",
"PTPA"
] | [
7348,
4458,
7271,
6295
] | 4 | [
"EC"
] | [
"5.2.1.8"
] | [
"EC:5.2.1.8"
] | 1 | [
"2g62",
"2hv6",
"2hv7",
"2ixm",
"2ixn",
"2ixo",
"2ixp",
"4lac",
"4ny3"
] | 9 | [
"PUB00007513",
"PUB00041513",
"PUB00041812",
"PUB00047494",
"PUB00080993",
"PUB00080994",
"PUB00080995"
] | [
"11171037",
"16916641",
"16885030",
"16782712",
"16380387",
"15447631",
"12952889"
] | [
"Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling.",
"Structure and mechanism of the phosphotyrosyl phosphatase activator.",
"Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity.",
"T... | [
2001,
2006,
2006,
2006,
2006,
2005,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
7352
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
2,
1,
6,
19,
7,
2,
3,
10,
2,
2,
4
] | 12 | true | Family | Phosphotyrosyl phosphatase activator, PTPA | Phosphotyrosyl phosphatase activator, PTPA | Phstyr_phstse_ac | 4 |
IPR004328 | 4,328 | BRO1 domain | BRO1_dom | Domain | 18,300 | false | false | The BRO1 domain is a protein domain of ~390 residues in length. It occurs in a number of eukaryotic proteins, such as yeast BRO1 and human PDCD6IP/Alix, which are involved in protein targeting to the vacuole or lysosome. The BRO1 domain of fungal and mammalian proteins binds with multivesicular body components (ESCRT-I... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF03097",
"PS51180",
"SM01041"
] | [
"BRO1",
"BRO1",
"BRO1"
] | [
17058,
17232,
17083
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC51180",
"R-BTA-5666185",
"R-BTA-8980692",
"R-DRE-5666185",
"R-DRE-8980692",
"R-HSA-162588",
"R-HSA-5210891",
"R-HSA-5213460",
"R-HSA-5666185",
"R-HSA-5675482",
"R-HSA-8980692",
"R-HSA-9008059",
"R-HSA-9013026",
"R-MMU-5213460",
"R-MMU-5666185",
"R-MMU-5675482",
"R-MMU-8980692",
... | [
"PROSITEDOC:PDOC51180",
"REACTOME:R-BTA-5666185",
"REACTOME:R-BTA-8980692",
"REACTOME:R-DRE-5666185",
"REACTOME:R-DRE-8980692",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-5210891",
"REACTOME:R-HSA-5213460",
"REACTOME:R-HSA-5666185",
"REACTOME:R-HSA-5675482",
"REACTOME:R-HSA-8980692",
"REACTOME:R... | 20 | [
"1zb1",
"2oev",
"2oew",
"2r02",
"2r03",
"2r05",
"2xs1",
"2xs8",
"3c3o",
"3c3q",
"3c3r",
"3r9m",
"3rau",
"3uly",
"3um0",
"3um1",
"3um2",
"3um3",
"3zxp",
"5cru",
"5crv",
"5mjy",
"5mjz",
"5mk0",
"5mk1",
"5mk2",
"5mk3",
"5v3r",
"5wa1",
"6kp3"
] | 30 | [
"PUB00019524",
"PUB00021037",
"PUB00033714"
] | [
"14583093",
"15935782",
"15944343"
] | [
"Structure and function of human Vps20 and Snf7 proteins.",
"Structural basis for endosomal targeting by the Bro1 domain.",
"Mutational analysis of the pH signal transduction component PalC of Aspergillus nidulans supports distant similarity to BRO1 domain family members."
] | [
2004,
2005,
2005
] | 3 | [] | [
"IPR042715",
"IPR047902"
] | 0 | 2 | 0 | [
"Eukaryota",
"Plectonema cf. radiosum LEGE 06105",
"bird metagenome"
] | [
18298,
1,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
22,
5,
19,
4,
24,
11,
3,
15,
14,
2,
2,
32
] | 12 | true | Domain | BRO1 domain | BRO1 domain | BRO1_dom | 6 |
IPR004329 | 4,329 | CcmE/CycJ protein | CcmE | Family | 11,086 | false | false | CcmE is the product of a cluster of Ccm genes that are necessary for cytochrome c biosynthesis in many prokaryotes [ , ] and plant mitochondria [ ]. In E. coli, expression of these proteins is induced when the organisms are grown under anaerobic conditions with nitrate or nitrite as the final electron acceptor [ ]. | [
"GO:0020037",
"GO:0017003",
"GO:0017004"
] | [
"heme binding",
"protein-heme linkage",
"cytochrome complex assembly"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP",
"PFAM",
"PANTHER"
] | [
"MF_01959",
"PF03100",
"PTHR34128"
] | [
"CcmE",
"CcmE",
""
] | [
8574,
11033,
9290
] | 3 | [
"GP"
] | [
"GenProp0678"
] | [
"GP:GenProp0678"
] | 1 | [
"1j6q",
"1lm0",
"1sr3",
"2kct",
"8ce8"
] | 5 | [
"PUB00002274",
"PUB00088174",
"PUB00088177",
"PUB00088178"
] | [
"7635817",
"11069919",
"9712585",
"22497251"
] | [
"Escherichia coli genes required for cytochrome c maturation.",
"CCME, a nuclear-encoded heme-binding protein involved in cytochrome c maturation in plant mitochondria.",
"Prototype of a heme chaperone essential for cytochrome c maturation.",
"Solution NMR structure, backbone dynamics, and heme-binding proper... | [
1995,
2001,
1998,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
10018,
649,
129,
290
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
1,
3,
4
] | 4 | true | Family | CcmE/CycJ protein | CcmE/CycJ protein | CcmE | 7 |
IPR004330 | 4,330 | FAR1, DNA binding domain | FAR1_DNA_bnd_dom | Domain | 25,806 | false | false | Phytochrome A is the primary photoreceptor for mediating various far-red light-induced responses in higher plants. It has been found that the proteins governing this response, which include FAR-RED ELONGATED HYPOCOTYL3 (FHY3) and FAR-RED-IMPAIRED RESPONSE1 (FAR1), are a pair of homologous proteins sharing significant s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03101"
] | [
"FAR1"
] | [
25806
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00044720",
"PUB00044721",
"PUB00161280",
"PUB00161281"
] | [
"18715961",
"15591448",
"37384577",
"29930561"
] | [
"Discrete and essential roles of the multiple domains of Arabidopsis FHY3 in mediating phytochrome A signal transduction.",
"Arabidopsis FHY3/FAR1 gene family and distinct roles of its members in light control of Arabidopsis development.",
"Emerging Roles of FHY3 and FAR1 as System Integrators in Plant Developm... | [
2008,
2004,
2023,
2018
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
25806
] | 1 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
92,
3,
234,
89
] | 4 | true | Domain | FAR1, DNA binding domain | FAR1, DNA binding domain | FAR1_DNA_bnd_dom | 3 |
IPR004331 | 4,331 | SPX domain | SPX_dom | Domain | 28,467 | false | false | The SPX domain is named after SYG1/Pho81/XPR1 proteins. This 180 residue length domain is found at the amino terminus of a variety of proteins. In the yeast protein SYG1, the N terminus directly binds to the G- protein beta subunit and inhibits transduction of the mating pheromone signal [ ] suggesting that all the mem... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF03105",
"PS51382"
] | [
"SPX",
"SPX"
] | [
21504,
28320
] | 2 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1352",
"GenProp1575",
"R-SCE-204005",
"R-SCE-3295583",
"R-SCE-983168"
] | [
"GP:GenProp1352",
"GP:GenProp1575",
"REACTOME:R-SCE-204005",
"REACTOME:R-SCE-3295583",
"REACTOME:R-SCE-983168"
] | 5 | [
"5iig",
"5iiq",
"5iit",
"5ijh",
"5ijj",
"5ijp",
"5lnc",
"7d3y",
"7e40",
"7ytj",
"8i6v",
"8r33",
"8r34",
"8r35",
"8tyu",
"8tyv",
"8x5f",
"8yet",
"8yfu",
"8yfw",
"8zto",
"9ckz",
"9cl0",
"9dvj",
"9dvk",
"9dvl",
"9dvm",
"9dvn",
"9dvo",
"9dvp",
"9ijy",
"9ijz"... | 59 | [
"PUB00007515",
"PUB00007516",
"PUB00007517",
"PUB00007518",
"PUB00007519",
"PUB00043762",
"PUB00043763",
"PUB00043764"
] | [
"7592711",
"9990033",
"8918192",
"11069666",
"9927670",
"16905115",
"18315545",
"18055586"
] | [
"Truncated forms of a novel yeast protein suppress the lethality of a G protein alpha subunit deficiency by interacting with the beta subunit.",
"A human cell-surface receptor for xenotropic and polytropic murine leukemia viruses: possible role in G protein-coupled signal transduction.",
"Signaling phosphate st... | [
1995,
1999,
1996,
2000,
1999,
2006,
2008,
2008
] | 8 | [] | [
"IPR034092",
"IPR045264"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
8,
28457,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
99,
1,
3,
7,
1,
5,
8,
20,
6,
10,
6,
73
] | 12 | true | Domain | SPX domain | SPX domain | SPX_dom | 6 |
IPR004332 | 4,332 | Transposase, MuDR, plant | Transposase_MuDR | Domain | 16,559 | false | false | The plant MuDR transposase domain is present in plant (and some fungal) proteins that are presumed to be the transposases for Mutator transposable elements [ , ]. The function of these proteins is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03108"
] | [
"DBD_Tnp_Mut"
] | [
16559
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007520",
"PUB00007521"
] | [
"7672579",
"1661256"
] | [
"Characterization of the major transcripts encoded by the regulatory MuDR transposable element of maize.",
"Cloning of the Mutator transposable element MuA2, a putative regulator of somatic mutability of the a1-Mum2 allele in maize."
] | [
1995,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Robertmurraya kyonggiensis"
] | [
16558,
1
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
139,
395,
23
] | 3 | true | Domain | Transposase, MuDR, plant | Transposase, MuDR, plant | Transposase_MuDR | 5 |
IPR004333 | 4,333 | SBP domain | SBP_dom | Domain | 12,856 | false | false | SBP (for SQUAMOSA-pROMOTER BINDING PROTEIN) domain is a sequence specific DNA-binding domain found in plant proteins [ ]. Members of family probably function as transcription factors involved in the control of early flower development [ ]. They share a highly conserved DNA-binding domain that contains two zinc-binding ... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF03110",
"PS51141"
] | [
"SBP",
"ZF_SBP"
] | [
12713,
12816
] | 2 | [
"PROSITEDOC"
] | [
"PDOC51141"
] | [
"PROSITEDOC:PDOC51141"
] | 1 | [
"1ul4",
"1ul5",
"1wj0",
"8j49",
"8j4b",
"8pfc"
] | 6 | [
"PUB00007522",
"PUB00018582",
"PUB00018583"
] | [
"8569690",
"15001351",
"10524240"
] | [
"A new family of DNA binding proteins includes putative transcriptional regulators of the Antirrhinum majus floral meristem identity gene SQUAMOSA.",
"A novel zinc-binding motif revealed by solution structures of DNA-binding domains of Arabidopsis SBP-family transcription factors.",
"Molecular characterisation ... | [
1996,
2004,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"uncultured Caudovirales phage"
] | [
8,
12847,
1
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
78,
48,
169
] | 3 | true | Domain | SBP domain | SBP domain | SBP_dom | 6 |
IPR004334 | 4,334 | Poxvirus E5R | Poxvirus_E5R | Family | 112 | false | false | This family of poxvirus proteins includes Protein OPG067 (also known as Protein E5). It is found in cytoplasmic sites of viral DNA replication [ ]. The presence of BEN domains suggests a possible role in organisation of viral DNA during replication or transcription [ ]. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF015691"
] | [
"VAC_E5R"
] | [
112
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007523",
"PUB00044170"
] | [
"10854161",
"18203771"
] | [
"Identification by mass spectroscopy of three major early proteins associated with virosomes in vaccinia virus-infected cells.",
"BEN: a novel domain in chromatin factors and DNA viral proteins."
] | [
1999,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Chordopoxvirinae"
] | [
112
] | 1 | [] | [] | 0 | true | Family | Poxvirus E5R | Poxvirus E5R | Poxvirus_E5R | 6 |
IPR004335 | 4,335 | Protein of unknown function DUF244 | DUF244 | Family | 209 | false | false | Many of the proteins in this entry are Borrelia burgdorferi plasmid proteins of unknown function. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03112"
] | [
"DUF244"
] | [
209
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)",
"Pseudomonadati"
] | [
1,
208
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF244 | Protein of unknown function DUF244 | DUF244 | 2 |
IPR004336 | 4,336 | Respiratory synctial virus non-structural protein NS2 | RSV_NS2 | Family | 377 | false | false | The molecular structure and function of the NS2 protein is not known. However, mutants lacking the NS2 grow at slower rates when compared to the wild-type yet NS2 is not essential for viral replication [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03113"
] | [
"RSV_NS2"
] | [
377
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-9828721",
"R-HSA-9828806",
"R-HSA-9833109",
"R-HSA-9833110"
] | [
"REACTOME:R-HSA-9828721",
"REACTOME:R-HSA-9828806",
"REACTOME:R-HSA-9833109",
"REACTOME:R-HSA-9833110"
] | 4 | [
"7ldk"
] | 1 | [
"PUB00007524"
] | [
"9847328"
] | [
"Generation of bovine respiratory syncytial virus (BRSV) from cDNA: BRSV NS2 is not essential for virus replication in tissue culture, and the human RSV leader region acts as a functional BRSV genome promoter."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Pneumoviridae"
] | [
377
] | 1 | [] | [] | 0 | true | Family | Respiratory synctial virus non-structural protein NS2 | Respiratory synctial virus non-structural protein NS2 | RSV_NS2 | 9 |
IPR004338 | 4,338 | Ion-translocating oxidoreductase NqrB/RnfD | NqrB/RnfD | Family | 13,382 | false | false | This family of proteins describes the Nqr2 (NqrB) subunit of the bacterial 6-subunit sodium-translocating NADH-ubiquinone oxidoreductase (i.e. a respiration linked sodium pump). In Vibrio cholerae, it negatively regulates the expression of virulence factors through inhibiting (by an unknown mechanism) the transcription... | [
"GO:0055085",
"GO:0016020"
] | [
"transmembrane transport",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PANTHER"
] | [
"PF03116",
"PTHR30578"
] | [
"NQR2_RnfD_RnfE",
""
] | [
13346,
13210
] | 2 | [] | [] | [] | 0 | [
"7xk3",
"7xk4",
"7xk5",
"7xk6",
"7xk7",
"7zc6",
"8a1t",
"8a1u",
"8a1v",
"8a1w",
"8a1x",
"8a1y",
"8acw",
"8acy",
"8ad0",
"8ahx",
"8evu",
"8ew3",
"8rb8",
"8rb9",
"8rbm",
"8rbq",
"9eri",
"9erj",
"9erk",
"9erl",
"9lrr",
"9u5g",
"9ud2",
"9ud3",
"9ud4",
"9ud5"... | 39 | [
"PUB00007527",
"PUB00007528",
"PUB00087510"
] | [
"10077658",
"9154934",
"27114876"
] | [
"Effects of changes in membrane sodium flux on virulence gene expression in Vibrio cholerae.",
"Membrane localization, topology, and mutual stabilization of the rnfABC gene products in Rhodobacter capsulatus and implications for a new family of energy-coupling NADH oxidoreductases.",
"The role of Rnf in ion gra... | [
1999,
1997,
2016
] | 3 | [] | [
"IPR010966",
"IPR011303",
"IPR049685"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
43,
12994,
16,
329
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ion-translocating oxidoreductase NqrB/RnfD | Ion-translocating oxidoreductase NqrB/RnfD | NqrB/RnfD | 1 |
IPR004341 | 4,341 | CAT RNA-binding domain | CAT_RNA-bd_dom | Domain | 9,133 | false | false | This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram-positive and Gram-negative bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a d... | [
"GO:0003723"
] | [
"RNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF03123",
"SM01061"
] | [
"CAT_RBD",
"CAT_RBD"
] | [
9130,
9114
] | 2 | [] | [] | [] | 0 | [
"1auu",
"1l1c",
"3rio",
"6twr"
] | 4 | [
"PUB00007531",
"PUB00007532",
"PUB00022043"
] | [
"9305644",
"10610766",
"11953318"
] | [
"Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis.",
"RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT.",
"Solution structure of the LicT-RNA antiterminatio... | [
1997,
1999,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
9111,
8,
14
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | CAT RNA-binding domain | CAT RNA-binding domain | CAT_RNA-bd_dom | 1 |
IPR004343 | 4,343 | Plus-3 domain | Plus-3_dom | Domain | 9,503 | false | false | The yeast Paf1 complex consists of Pfa1, Rtf1, Cdc73, Ctr9, and Leo1. The complex regulates histone H2B ubiquitination, histone H3 methylation, RNA polymerase II carboxy-terminal domain (CTD) Ser2 phosphorylation, and RNA 3' end processing. The conservation of Paf1 complex function in higher eukaryotes has been confirm... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF03126",
"PS51360",
"SM00719"
] | [
"Plus-3",
"PLUS3",
"Plus3"
] | [
9298,
9034,
9072
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-112382",
"R-HSA-674695",
"R-HSA-75955",
"R-HSA-8866654"
] | [
"REACTOME:R-HSA-112382",
"REACTOME:R-HSA-674695",
"REACTOME:R-HSA-75955",
"REACTOME:R-HSA-8866654"
] | 4 | [
"2bze",
"2db9",
"3u1u",
"4l1p",
"4l1u",
"6ted",
"7unc",
"7und",
"7xn7",
"7xse",
"7xsx",
"7xsz",
"7xt7",
"7xtd",
"7xti",
"8a3y",
"9egx",
"9egy",
"9egz",
"9eh0",
"9eh1",
"9eh2",
"9s0u",
"9s3g"
] | 24 | [
"PUB00007534",
"PUB00043810"
] | [
"11014804",
"18184592"
] | [
"Synthetic lethal interactions suggest a role for the Saccharomyces cerevisiae Rtf1 protein in transcription elongation.",
"Structure and DNA binding of the human Rtf1 Plus3 domain."
] | [
2000,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
23,
9480
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
41,
1,
1,
9,
3,
2,
1,
22,
3,
1,
1,
122
] | 12 | true | Domain | Plus-3 domain | Plus-3 domain | Plus-3_dom | 4 |
IPR004344 | 4,344 | Tubulin-tyrosine ligase/Tubulin polyglutamylase | TTL/TTLL_fam | Family | 30,964 | false | false | Tubulins and microtubules are subjected to several post-translational modifications of the carboxy-terminal end of most major forms of tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL) and the tubulin polyglutamylas... | [
"GO:0036211"
] | [
"protein modification process"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF03133",
"PS51221"
] | [
"TTL",
"TTL"
] | [
30841,
30008
] | 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"... | [
"6.3.2.-",
"PWY-6289",
"PWY-6374",
"PWY-6378",
"PWY-6379",
"PWY-6409",
"PWY-6574",
"PWY-7510",
"PWY-7533",
"PWY-7542",
"PWY-7543",
"PWY-7549",
"PWY-7555",
"PWY-7556",
"PWY-7561",
"PWY-7563",
"PWY-7565",
"PWY-7569",
"PWY-7570",
"PWY-7571",
"PWY-7577",
"PWY-7600",
"PWY-7605... | [
"EC:6.3.2.-",
"METACYC:PWY-6289",
"METACYC:PWY-6374",
"METACYC:PWY-6378",
"METACYC:PWY-6379",
"METACYC:PWY-6409",
"METACYC:PWY-6574",
"METACYC:PWY-7510",
"METACYC:PWY-7533",
"METACYC:PWY-7542",
"METACYC:PWY-7543",
"METACYC:PWY-7549",
"METACYC:PWY-7555",
"METACYC:PWY-7556",
"METACYC:PWY-7... | 47 | [
"3tig",
"3tii",
"3tin",
"4i4t",
"4i50",
"4i55",
"4ihj",
"4iij",
"4o2a",
"4o2b",
"4o4h",
"4o4i",
"4o4j",
"4o4l",
"4tuy",
"4tv8",
"4tv9",
"4yj2",
"4yj3",
"4ylr",
"4yls",
"4zhq",
"4zi7",
"4zol",
"5bmv",
"5c8y",
"5ca0",
"5ca1",
"5cb4",
"5ezy",
"5fnv",
"5gon"... | 305 | [
"PUB00007535",
"PUB00066565",
"PUB00066571"
] | [
"10685598",
"15890843",
"19524510"
] | [
"Tubulin-tyrosine ligase, a long-lasting enigma.",
"Tubulin polyglutamylase enzymes are members of the TTL domain protein family.",
"Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
] | [
2000,
2005,
2009
] | 3 | [] | [
"IPR027746",
"IPR027749",
"IPR027752"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
2,
179,
30726,
18,
39
] | 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... | [
5,
6,
50,
22,
62,
45,
1,
5,
57,
1,
1,
6
] | 12 | true | Family | Tubulin-tyrosine ligase/Tubulin polyglutamylase | Tubulin-tyrosine ligase/Tubulin polyglutamylase | TTL/TTLL_fam | 9 |
IPR004345 | 4,345 | TB2/DP1/HVA22 | TB2_DP1_HVA22 | Family | 23,806 | false | false | This family includes members from a wide variety of eukaryotes and includes Receptor expression-enhancing proteins (REEPs), its homologues from fungi Yop1 and similar sequences from plants. REEP/DP1/Yop1 family of proteins are involved in the control of endoplasmic reticulum organisation and mutations in some members o... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF03134",
"PTHR12300"
] | [
"TB2_DP1_HVA22",
""
] | [
23767,
21978
] | 2 | [
"REACTOME"
] | [
"R-HSA-9752946"
] | [
"REACTOME:R-HSA-9752946"
] | 1 | [] | 0 | [
"PUB00020410",
"PUB00020411",
"PUB00095230",
"PUB00155129",
"PUB00155130",
"PUB00155131"
] | [
"10805953",
"8226892",
"24388663",
"20200447",
"32075961",
"8647449"
] | [
"Familial adenomatous polyposis.",
"Hormone response complex in a novel abscisic acid and cycloheximide-inducible barley gene.",
"Loss of association of REEP2 with membranes leads to hereditary spastic paraplegia.",
"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule ... | [
2000,
1993,
2014,
2010,
2020,
1996
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mimiviridae",
"metagenomes"
] | [
23799,
5,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
48,
7,
14,
58,
40,
17,
2,
53,
26,
1,
3,
96
] | 12 | true | Family | TB2/DP1/HVA22 | TB2/DP1/HVA22 | TB2_DP1_HVA22 | 2 |
IPR004346 | 4,346 | Type IV secretion system ATPase VirB4/TrbE | VirB4_CagE | Family | 3,232 | false | false | CagE ( ) is the ATPase component of the Cag type IV secretion system (Cag-T4SS), encoded by the cag pathogenicity island (PAI). It functions as a molecular motor, providing the energy required for protein export. CagE is essential for pathogenesis in Helicobacter pylori-induced gastritis and peptic ulceration [ ]. It i... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00929"
] | [
"VirB4_CagE"
] | [
3232
] | 1 | [
"EC",
"GP"
] | [
"3.6.4.6",
"GenProp0485"
] | [
"EC:3.6.4.6",
"GP:GenProp0485"
] | 2 | [
"7o41",
"7o42",
"7o43",
"7oiu",
"8rtb",
"8rtd"
] | 6 | [
"PUB00007538",
"PUB00007539",
"PUB00076811",
"PUB00097878",
"PUB00097879",
"PUB00163229",
"PUB00163230"
] | [
"11104802",
"11447179",
"22745169",
"31088930",
"26565397",
"34424036",
"21118511"
] | [
"Virulence factors of Helicobacter pylori responsible for gastric diseases in Mongolian gerbil.",
"Epithelial intestinal cell apoptosis induced by Helicobacter pylori depends on expression of the cag pathogenicity island phenotype.",
"Structure of the VirB4 ATPase, alone and bound to the core complex of a type ... | [
2000,
2001,
2012,
2019,
2015,
2021,
2010
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"hydrothermal vent metagenome",
"plasmids"
] | [
3209,
13,
2,
8
] | 4 | [] | [] | 0 | true | Family | Type IV secretion system ATPase VirB4/TrbE | Type IV secretion system ATPase VirB4/TrbE | VirB4_CagE | 7 |
IPR004347 | 4,347 | Pup ligase/deamidase | Pup_ligase/deamidase | Family | 8,708 | false | false | Pupylation is a novel protein modification system found in some bacteria [ ]. This entry represents two related groups of proteins involved in this system. Pup ligases, such as PafA, conjugate the prokaryotic ubiquitin-like protein Pup to lysine residues in target proteins, marking them for degradation [ ]. Pup deamida... | [
"GO:0010498",
"GO:0019941"
] | [
"proteasomal protein catabolic process",
"modification-dependent protein catabolic process"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF03136",
"PIRSF018077",
"PTHR42307"
] | [
"Pup_ligase",
"UCP018077",
""
] | [
8708,
7131,
8687
] | 3 | [
"EC",
"GP",
"METACYC"
] | [
"6.3.1.19",
"GenProp1317",
"PWY-7893"
] | [
"EC:6.3.1.19",
"GP:GenProp1317",
"METACYC:PWY-7893"
] | 3 | [
"4b0r",
"4b0s",
"4b0t",
"4bjr",
"5lrt",
"7oxv",
"7oxy",
"7oy3",
"7oyf",
"7oyh",
"9cku"
] | 11 | [
"PUB00053382",
"PUB00053383",
"PUB00053572"
] | [
"18980670",
"18832610",
"19448618"
] | [
"Unraveling the biochemistry and provenance of pupylation: a prokaryotic analog of ubiquitination.",
"Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis.",
"Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes."
... | [
2008,
2008,
2009
] | 3 | [] | [
"IPR022279",
"IPR022366"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
15,
8451,
14,
228
] | 4 | [] | [] | 0 | true | Family | Pup ligase/deamidase | Pup ligase/deamidase | Pup_ligase/deamidase | 7 |
IPR004349 | 4,349 | Vanadium/alternative nitrogenase delta subunit | V/Nase_d_su | Family | 288 | false | false | The nitrogenase complex catalyses the conversion of molecular nitrogen to ammonia (nitrogen fixation). The complex is hexameric, consisting of 2 alpha, 2 beta, and 2 delta subunits. | [
"GO:0016163",
"GO:0009399"
] | [
"nitrogenase activity",
"nitrogen fixation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF03139"
] | [
"AnfG_VnfG"
] | [
288
] | 1 | [
"EC"
] | [
"1.18.6.1"
] | [
"EC:1.18.6.1"
] | 1 | [
"5n6y",
"6fea",
"7adr",
"7ady",
"7aiz",
"8boq",
"8oie"
] | 7 | [] | [] | [] | [] | 0 | [] | [
"IPR014278",
"IPR014279"
] | 0 | 2 | 0 | [
"Bacteria",
"Methanobacteriota",
"metagenomes"
] | [
263,
22,
3
] | 3 | [] | [] | 0 | true | Family | Vanadium/alternative nitrogenase delta subunit | Vanadium/alternative nitrogenase delta subunit | V/Nase_d_su | 9 |
IPR004350 | 4,350 | Potassium channel, voltage dependent, Kv2.1 | K_chnl_volt-dep_Kv2.1 | Family | 844 | false | false | Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr... | [
"GO:0005249",
"GO:0006813",
"GO:0016020"
] | [
"voltage-gated potassium channel activity",
"potassium ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01514"
] | [
"KV21CHANNEL"
] | [
844
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1296072",
"R-HSA-381676",
"R-MMU-1296072",
"R-MMU-381676",
"R-RNO-1296072",
"R-RNO-381676"
] | [
"REACTOME:R-HSA-1296072",
"REACTOME:R-HSA-381676",
"REACTOME:R-MMU-1296072",
"REACTOME:R-MMU-381676",
"REACTOME:R-RNO-1296072",
"REACTOME:R-RNO-381676"
] | 6 | [
"8sd3",
"8sda",
"9o10",
"9o11",
"9o12",
"9o13"
] | 6 | [
"PUB00001055",
"PUB00001622",
"PUB00002771",
"PUB00004011",
"PUB00004020",
"PUB00006577",
"PUB00008322",
"PUB00009378",
"PUB00009391",
"PUB00036045"
] | [
"1772658",
"1879548",
"1373731",
"2448635",
"2451788",
"2555158",
"9305895",
"11178249",
"10712896",
"15950285"
] | [
"The molecular biology of K+ channels.",
"Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.",
"Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.",
"Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Droso... | [
1991,
1991,
1992,
1988,
1988,
1989,
1997,
2000,
2000,
2005
] | 10 | [
"IPR003973"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
844
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
2,
3
] | 4 | true | Family | Potassium channel, voltage dependent, Kv2.1 | Potassium channel, voltage dependent, Kv2.1 | K_chnl_volt-dep_Kv2.1 | 9 |
IPR004352 | 4,352 | Glycoside-hydrolase family GH114, TIM-barrel domain | GH114_TIM-barrel | Domain | 7,083 | false | false | Proteins in this entry are recognised as members of a glycosyl-hydrolase family, number 114. It is endo-alpha-1,4-polygalactosaminidase, a rare enzyme. It is proposed to be TIM-barrel, the most common structure amongst the catalytic domains of glycosyl-hydrolases [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03537"
] | [
"Glyco_hydro_114"
] | [
7083
] | 1 | [] | [] | [] | 0 | [
"2aam",
"5tcb",
"5tsy",
"6oj1",
"6ojb",
"9cgy",
"9ep5",
"9ep6",
"9eux",
"9euz"
] | 10 | [
"PUB00066755"
] | [
"21954604"
] | [
"[Endo-alpha-1-4-polygalactosaminidases and their homologues: structure and evolution]."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes",
"virus sp. ctr1v16"
] | [
49,
4777,
2203,
53,
1
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Glycoside-hydrolase family GH114, TIM-barrel domain | Glycoside-hydrolase family GH114, TIM-barrel domain | GH114_TIM-barrel | 7 |
IPR004353 | 4,353 | Vacuolar fusion protein Mon1 | Mon1 | Family | 6,746 | false | false | Members of this family have been called SAND proteins [ ] although these proteins do not contain a SAND domain. In Saccharomyces cerevisiae, Mon1 is part of the Mon1-Ccz1 complex that acts as the guanine nucleotide exchange factor (GEF) of the yeast Rab7 GTPase Ypt7 [ , ]. The Mon1/Ccz1 complex is conserved in eukaryot... | [
"GO:0006623"
] | [
"protein targeting to vacuole"
] | [
"biological_process"
] | 1 | [
"PRINTS",
"PANTHER"
] | [
"PR01546",
"PTHR13027"
] | [
"YEAST73DUF",
""
] | [
6533,
6632
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8876198",
"R-DME-8876198",
"R-HSA-8876198",
"R-MMU-8876198",
"R-SCE-8876198"
] | [
"REACTOME:R-BTA-8876198",
"REACTOME:R-DME-8876198",
"REACTOME:R-HSA-8876198",
"REACTOME:R-MMU-8876198",
"REACTOME:R-SCE-8876198"
] | 5 | [
"5ldd",
"7qla",
"8c7g",
"8jbe",
"9l0d",
"9rs6",
"9rs7"
] | 7 | [
"PUB00019469",
"PUB00019470",
"PUB00044732",
"PUB00083120",
"PUB00083121"
] | [
"10025966",
"15647795",
"17075139",
"24413168",
"24623720"
] | [
"Three receptor genes for plasminogen related growth factors in the genome of the puffer fish Fugu rubripes.",
"Molecular characterisation of the SAND protein family: a study based on comparative genomics, structural bioinformatics and phylogeny.",
"Longin-like folds identified in CHiPS and DUF254 proteins: ves... | [
1999,
2004,
2006,
2014,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"metagenomes"
] | [
6744,
2
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
1,
5,
2,
9,
4,
1,
1,
5,
1,
1,
12
] | 12 | true | Family | Vacuolar fusion protein Mon1 | Vacuolar fusion protein Mon1 | Mon1 | 1 |
IPR004354 | 4,354 | Meiotic recombination protein Rec114 | Meiotic_Rec114 | Family | 756 | false | false | This entry includes budding yeast Rec114 protein and its homologue, Rec7, from S. pombe. They are required for meiotic intragenic recombination but not for mitotic recombination [ , ]. | [
"GO:0007131"
] | [
"reciprocal meiotic recombination"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF03525",
"PR01548"
] | [
"Meiotic_rec114",
"MEIOTICR114"
] | [
756,
46
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007666",
"PUB00007667",
"PUB00074981",
"PUB00074982"
] | [
"9267437",
"8385581",
"1339382",
"10526232"
] | [
"Examination of the intron in the meiosis-specific recombination gene REC114 in Saccharomyces.",
"Genetic and molecular analysis of REC114, an early meiotic recombination gene in yeast.",
"Meiotically induced rec7 and rec8 genes of Schizosaccharomyces pombe.",
"High copy number suppression of the meiotic arre... | [
1997,
1993,
1992,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
756
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1
] | 2 | true | Family | Meiotic recombination protein Rec114 | Meiotic recombination protein Rec114 | Meiotic_Rec114 | 8 |
IPR004356 | 4,356 | Adhesin operon regulatory protein | Adhesin_operon_reg_prot | Family | 705 | false | false | Proteins in this family include PapB, DaaA, FanA, FanB and AfaA. P pili, or fimbriae, are ~68A in diameter and 1 micron in length, the bulk of which is a fibre composed of the main structural protein PapA [ ]. At its tip, the pilus is terminated by a fibrillum consisting of repeating units of the PapE protein. This, in... | [
"GO:0006355"
] | [
"regulation of DNA-templated transcription"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF03333",
"PR01554"
] | [
"PapB",
"FIMREGULATRY"
] | [
698,
493
] | 2 | [] | [] | [] | 0 | [
"3m8j"
] | 1 | [
"PUB00007359",
"PUB00007360",
"PUB00007671",
"PUB00007672"
] | [
"1348107",
"7816100",
"1357526",
"2568258"
] | [
"P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips.",
"Structural polymorphism of bacterial adhesion pili.",
"Horizontal gene transfer of the Escherichia coli pap and prs pili operons as a mechanism for the development of tissue-specific adhesive properties.",
"Autoreg... | [
1992,
1995,
1992,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Shewanella phage X14",
"organismal metagenomes"
] | [
702,
1,
2
] | 3 | [] | [] | 0 | true | Family | Adhesin operon regulatory protein | Adhesin operon regulatory protein | Adhesin_operon_reg_prot | 9 |
IPR004357 | 4,357 | Type IV secretion system CagX conjugation protein | IVSec_CagX | Family | 209 | false | false | Helicobacter pylori makes use of a type IV secretion system similar in mechanism to the conjugation machine of Agrobacterium tumefaciens [ ]. These machines secrete three different types of substrate: DNA conjugation intermediates, as in A. tumefaciens; multimeric proteins such as the pertussis toxin of Bordetella pert... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR01556"
] | [
"TYPE4SSCAGX"
] | [
209
] | 1 | [] | [] | [] | 0 | [
"5h3v",
"6oeg",
"6x6j",
"6x6k",
"6x6l",
"6x6s",
"8cb2"
] | 7 | [
"PUB00007668",
"PUB00007669",
"PUB00007670"
] | [
"10920394",
"10684851",
"10684850"
] | [
"Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells.",
"Helicobacter pylori CagA protein can be tyrosine phosphorylated in gastric epithelial cells.",
"Tyrosine-phosphorylated bacterial proteins: Trojan horses for the host cell."
] | [
2000,
2000,
2000
] | 3 | [
"IPR010258"
] | [] | 1 | 0 | 1 | [
"Helicobacter pylori"
] | [
209
] | 1 | [] | [] | 0 | true | Family | Type IV secretion system CagX conjugation protein | Type IV secretion system CagX conjugation protein | IVSec_CagX | 4 |
IPR004358 | 4,358 | Signal transduction histidine kinase-related protein, C-terminal | Sig_transdc_His_kin-like_C | Domain | 766,157 | false | false | This domain is present in many sensor proteins that respond to extra-cytoplasmic stimuli in bacteria, but is also found in many proteins of metazoan origin. Sensors are usually linked to a 2-component regulatory system consisting of the sensor and a cytoplasmic regulator protein [ ]. The cytoplasmic C-terminal portions... | [
"GO:0016772",
"GO:0016310"
] | [
"transferase activity, transferring phosphorus-containing groups",
"phosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00344"
] | [
"BCTRLSENSOR"
] | [
766157
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.13.3",
"R-BTA-70895",
"R-HSA-70895",
"R-HSA-9912481",
"R-MMU-70895",
"R-RNO-70895",
"R-SPO-204174",
"R-SPO-5362517",
"R-SPO-9837999"
] | [
"EC:2.7.13.3",
"REACTOME:R-BTA-70895",
"REACTOME:R-HSA-70895",
"REACTOME:R-HSA-9912481",
"REACTOME:R-MMU-70895",
"REACTOME:R-RNO-70895",
"REACTOME:R-SPO-204174",
"REACTOME:R-SPO-5362517",
"REACTOME:R-SPO-9837999"
] | 9 | [
"1b3q",
"1bxd",
"1gjv",
"1gkx",
"1gkz",
"1i58",
"1i59",
"1i5a",
"1i5b",
"1i5c",
"1i5d",
"1id0",
"1r62",
"1ys3",
"1ysr",
"2c2a",
"2ch4",
"3a0r",
"3a0t",
"3a0w",
"3a0x",
"3a0y",
"3a0z",
"3cgy",
"3cgz",
"3d36",
"3dge",
"3ja6",
"3jz3",
"3sl2",
"3tz0",
"3tz2"... | 144 | [
"PUB00000966",
"PUB00003792",
"PUB00004626",
"PUB00007866",
"PUB00010651",
"PUB00011096",
"PUB00013246",
"PUB00013247",
"PUB00013562",
"PUB00013563",
"PUB00020801",
"PUB00042804",
"PUB00042805",
"PUB00042806",
"PUB00042807"
] | [
"9989504",
"2559300",
"3020561",
"11406410",
"12372152",
"10966457",
"8868347",
"10426948",
"8029829",
"1482126",
"11145881",
"16176121",
"18076326",
"11934609",
"11489844"
] | [
"Structure of CheA, a signal-transducing histidine kinase.",
"Families of bacterial signal-transducing proteins.",
"Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and ntrC.",
"Histidine kinases and resp... | [
1999,
1989,
1986,
2001,
2002,
2000,
1996,
1999,
1994,
1992,
2000,
2005,
2007,
2002,
2001
] | 15 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
10996,
714352,
33096,
39,
2,
7672
] | 6 | [
"Arabidopsis thaliana",
"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",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)... | [
47,
1,
24,
1,
5,
11,
24,
2,
2,
3,
113
] | 11 | true | Domain | Signal transduction histidine kinase-related protein, C-terminal | Signal transduction histidine kinase-related protein, C-terminal | Sig_transdc_His_kin-like_C | 7 |
IPR004360 | 4,360 | Glyoxalase/fosfomycin resistance/dioxygenase domain | Glyas_Fos-R_dOase_dom | Domain | 285,176 | false | false | Glyoxalase I ( ) (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid [ ]. Glyoxalase I is an ubiquitous enzyme which binds one mole of zinc per subunit. The bacterial and yeast enzymes are monomeric while the mammalian one is... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00903"
] | [
"Glyoxalase"
] | [
285176
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8963684",
"R-CEL-8963684",
"R-DDI-2142789",
"R-DDI-8963684",
"R-HSA-70268",
"R-HSA-8963684",
"R-MMU-70268",
"R-MMU-8963684",
"R-RNO-70268",
"R-RNO-8963684",
"R-SCE-70268",
"R-SPO-70268"
] | [
"REACTOME:R-BTA-8963684",
"REACTOME:R-CEL-8963684",
"REACTOME:R-DDI-2142789",
"REACTOME:R-DDI-8963684",
"REACTOME:R-HSA-70268",
"REACTOME:R-HSA-8963684",
"REACTOME:R-MMU-70268",
"REACTOME:R-MMU-8963684",
"REACTOME:R-RNO-70268",
"REACTOME:R-RNO-8963684",
"REACTOME:R-SCE-70268",
"REACTOME:R-SPO-... | 12 | [
"1bh5",
"1cjx",
"1dhy",
"1ecs",
"1eil",
"1eiq",
"1eir",
"1ewj",
"1f1r",
"1f1u",
"1f1v",
"1f1x",
"1f9z",
"1fa5",
"1fa6",
"1fa7",
"1fa8",
"1fro",
"1han",
"1kll",
"1kmy",
"1kmz",
"1knd",
"1knf",
"1kw3",
"1kw6",
"1kw8",
"1kw9",
"1kwb",
"1kwc",
"1lgt",
"1lkd"... | 410 | [
"PUB00002779",
"PUB00043234",
"PUB00053914",
"PUB00055578"
] | [
"7684374",
"17567049",
"11244082",
"15741169"
] | [
"Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida.",
"Structure and mechanism of the genomically encoded fosfomycin resistance protein, FosX, from Listeria monocytogenes.",
"FosB, a cysteine-dependent fosfomycin resistance protein under the control of... | [
1993,
2007,
2001,
2005
] | 4 | [
"IPR037523"
] | [
"IPR037478"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
3532,
253604,
25650,
16,
6,
2368
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
52,
3,
11,
4,
3,
9,
8,
3,
44,
8,
1,
1,
73
] | 13 | true | Domain | Glyoxalase/fosfomycin resistance/dioxygenase domain | Glyoxalase/fosfomycin resistance/dioxygenase domain | Glyas_Fos-R_dOase_dom | 8 |
IPR004361 | 4,361 | Glyoxalase I | Glyoxalase_1 | Family | 13,632 | false | false | Glyoxalase I (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway in the following reaction: glutathione + methylglyoxal = (R)-S-lactoylglutathione S-lactoylglutathione is then converted by glyoxalase II to lactic acid [ ]. Glyoxalase I is a ubiquitous enzyme which binds one mole of zinc per subun... | [
"GO:0004462",
"GO:0046872"
] | [
"lactoylglutathione lyase activity",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR00068"
] | [
"glyox_I"
] | [
13632
] | 1 | [
"EC",
"GP",
"GP",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.4.1.5",
"GenProp0744",
"GenProp1578",
"PWY-5386",
"PDOC00720",
"R-HSA-70268",
"R-MMU-70268",
"R-RNO-70268",
"R-SCE-70268",
"R-SPO-70268"
] | [
"EC:4.4.1.5",
"GP:GenProp0744",
"GP:GenProp1578",
"METACYC:PWY-5386",
"PROSITEDOC:PDOC00720",
"REACTOME:R-HSA-70268",
"REACTOME:R-MMU-70268",
"REACTOME:R-RNO-70268",
"REACTOME:R-SCE-70268",
"REACTOME:R-SPO-70268"
] | 10 | [
"1bh5",
"1f9z",
"1fa5",
"1fa6",
"1fa7",
"1fa8",
"1fro",
"1qin",
"1qip",
"2c21",
"2za0",
"3vw9",
"3w0t",
"3w0u",
"4kyh",
"4kyk",
"4mtq",
"4mtr",
"4mts",
"4mtt",
"4opn",
"4pv5",
"4x2a",
"5d7z",
"6bnn",
"6bnx",
"6bnz",
"6l0u",
"7vq6",
"7wsz",
"7wt0",
"7wt1"... | 38 | [
"PUB00002779"
] | [
"7684374"
] | [
"Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Penaeus monodon majanivirus B",
"Thermoproteati",
"unclassified sequences"
] | [
7151,
6385,
1,
2,
93
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae... | [
15,
2,
1,
1,
3,
3,
1,
15,
2,
1,
1,
28
] | 12 | true | Family | Glyoxalase I | Glyoxalase I | Glyoxalase_1 | 2 |
IPR004363 | 4,363 | Methylglyoxal synthase | Methylgl_synth | Family | 12,511 | false | false | Methylglyoxal synthase (MGS) catalyses the conversion of dihydroxyacetone phosphate (DHAP) to methylglyoxal and phosphate: Glycerone phosphate = methylglyoxal + phosphate The first part of the catalytic mechanism is believed to be similar to TIM (triosephosphate isomerase) in that both enzymes utilise DHAP to form an e... | [
"GO:0008929",
"GO:0019242"
] | [
"methylglyoxal synthase activity",
"methylglyoxal biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"PIRSF",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00549",
"NF003559",
"PIRSF006614",
"PTHR30492",
"TIGR00160",
"cd01422"
] | [
"Methylglyoxal_synth",
"PRK05234.1",
"Methylglyox_syn",
"",
"MGSA",
"MGS"
] | [
9122,
9714,
8834,
12495,
8360,
8649
] | 6 | [
"EC",
"PROSITEDOC"
] | [
"4.2.3.3",
"PDOC01037"
] | [
"EC:4.2.3.3",
"PROSITEDOC:PDOC01037"
] | 2 | [
"1b93",
"1egh",
"1ik4",
"1s89",
"1s8a",
"1vmd",
"1wo8",
"2x8w",
"2xw6",
"5h3l",
"6f2c",
"6phe",
"8u2v"
] | 13 | [
"PUB00006181",
"PUB00028433"
] | [
"10368300",
"10715115"
] | [
"The crystal structure of methylglyoxal synthase from Escherichia coli.",
"Mirroring perfection: the structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate."
] | [
1999,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
263,
11969,
170,
108,
1
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Methylglyoxal synthase | Methylglyoxal synthase | Methylgl_synth | 5 |
IPR004364 | 4,364 | Aminoacyl-tRNA synthetase, class II (D/K/N) | Aa-tRNA-synt_II | Domain | 108,620 | false | false | This entry includes the asparagine, aspartic acid and lysine tRNA synthetases. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligome... | [
"GO:0000166",
"GO:0004812",
"GO:0005524",
"GO:0006418"
] | [
"nucleotide binding",
"aminoacyl-tRNA ligase activity",
"ATP binding",
"tRNA aminoacylation for protein translation"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF00152"
] | [
"tRNA-synt_2"
] | [
108620
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1",
"R-CEL-9856649",
"R-DDI-9856649",
"R-HSA-2408522",
"R-HSA-379716",
"R-HSA-379726",
"R-HSA-9856649",
"R-MMU-9856649",
"R-RNO-9856649",
"R-SCE-9856649",
"R-SPO-9856649"
] | [
"EC:6.1.1",
"REACTOME:R-CEL-9856649",
"REACTOME:R-DDI-9856649",
"REACTOME:R-HSA-2408522",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-9856649",
"REACTOME:R-RNO-9856649",
"REACTOME:R-SCE-9856649",
"REACTOME:R-SPO-9856649"
] | 11 | [
"1asy",
"1asz",
"1b8a",
"1bbu",
"1bbw",
"1c0a",
"1e1o",
"1e1t",
"1e22",
"1e24",
"1efw",
"1eov",
"1eqr",
"1g51",
"1il2",
"1l0w",
"1lyl",
"1n9w",
"1nnh",
"1wyd",
"1x54",
"1x55",
"1x56",
"2xgt",
"2xti",
"3a5y",
"3a5z",
"3a74",
"3bju",
"3e9h",
"3e9i",
"3g1z"... | 147 | [
"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 | [
"IPR006195"
] | [
"IPR018149",
"IPR047090"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1504,
72211,
32914,
74,
1917
] | 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",... | [
50,
6,
10,
9,
5,
43,
25,
8,
27,
29,
6,
6,
70
] | 13 | true | Domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | Aminoacyl-tRNA synthetase, class II (D/K/N) | Aa-tRNA-synt_II | 2 |
IPR004365 | 4,365 | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | NA-bd_OB_tRNA | Domain | 138,072 | false | false | The OB-fold (oligonucleotide/oligosaccharide-binding fold) is found in all three kingdoms and its common architecture presents a binding face that has adapted to bind different ligands. The OB-fold is a five/six-stranded closed β-barrel formed by 70-80 amino acid residues. The strands are connected by loops of varying ... | [
"GO:0003676"
] | [
"nucleic acid binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01336"
] | [
"tRNA_anti-codon"
] | [
138072
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"6.1.1",
"R-CEL-9856649",
"R-DME-110312",
"R-DME-110314",
"R-DME-110320",
"R-DME-176187",
"R-DME-3108214",
"R-DME-3371453",
"R-DME-5358565",
"R-DME-5651801",
"R-DME-5655862",
"R-DME-5656121",
"R-DME-5656169",
"R-DME-5693607",
"R-DME-5696395",
"R-DME-5696397",
"R-DME-5696400",
"R-DM... | [
"EC:6.1.1",
"REACTOME:R-CEL-9856649",
"REACTOME:R-DME-110312",
"REACTOME:R-DME-110314",
"REACTOME:R-DME-110320",
"REACTOME:R-DME-176187",
"REACTOME:R-DME-3108214",
"REACTOME:R-DME-3371453",
"REACTOME:R-DME-5358565",
"REACTOME:R-DME-5651801",
"REACTOME:R-DME-5655862",
"REACTOME:R-DME-5656121",
... | 172 | [
"1asy",
"1asz",
"1b8a",
"1bbu",
"1bbw",
"1c0a",
"1e1o",
"1e1t",
"1e22",
"1e24",
"1efw",
"1eov",
"1eqr",
"1fgu",
"1g51",
"1il2",
"1jmc",
"1krs",
"1krt",
"1l0w",
"1lyl",
"1n9w",
"1wyd",
"1x54",
"1x55",
"1x56",
"1ynx",
"2hpi",
"2hpm",
"2k50",
"2k5v",
"2xgt"... | 192 | [
"PUB00007673",
"PUB00007674",
"PUB00007675"
] | [
"10829230",
"7760808",
"8990123"
] | [
"Protein fold recognition using sequence profiles and its application in structural genomics.",
"Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex.",
"Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA."
] | [
2000,
1995,
1997
] | 3 | [] | [
"IPR044136",
"IPR047089"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3545,
101840,
30477,
97,
2113
] | 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",... | [
60,
6,
10,
10,
5,
46,
25,
8,
25,
30,
7,
8,
57
] | 13 | true | Domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | NA-bd_OB_tRNA | 9 |
IPR004367 | 4,367 | Cyclin, C-terminal domain | Cyclin_C-dom | Domain | 47,873 | false | false | Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [ ], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essenti... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF02984",
"SM01332"
] | [
"Cyclin_C",
"Cyclin_C"
] | [
45260,
43116
] | 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-1538133",
"R-BTA-174048",
"R-BTA-176408",
"R-BTA-176412",
"R-BTA-176417",
"R-BTA-187577",
"R-BTA-2299718",
"R-BTA-2500257",
"R-BTA-2559586",
"R-BTA-2565942",
"R-BTA-2980767",
"R-BTA-2995383",
"R-BTA-3301854",
"R-BTA-4419969",
"R-BTA-6804114",
"R-BTA-6804116",
"R-BTA-68875",
... | [
"REACTOME:R-BTA-1538133",
"REACTOME:R-BTA-174048",
"REACTOME:R-BTA-176408",
"REACTOME:R-BTA-176412",
"REACTOME:R-BTA-176417",
"REACTOME:R-BTA-187577",
"REACTOME:R-BTA-2299718",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-2559586",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-2980767",
"REACTOME:R-B... | 288 | [
"1e9h",
"1fin",
"1fvv",
"1gy3",
"1h1p",
"1h1q",
"1h1r",
"1h1s",
"1h24",
"1h25",
"1h26",
"1h27",
"1h28",
"1jst",
"1jsu",
"1ogu",
"1oi9",
"1oiu",
"1oiy",
"1okv",
"1okw",
"1ol1",
"1ol2",
"1p5e",
"1pkd",
"1qmz",
"1urc",
"1vin",
"1vyw",
"1w98",
"2b9r",
"2bkz"... | 205 | [
"PUB00014101",
"PUB00014103"
] | [
"11056549",
"12910258"
] | [
"Cyclin' on the viral path to destruction.",
"Cell cycle regulation and neural differentiation."
] | [
2000,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Aeromonas piscicola",
"Eukaryota",
"Viruses",
"viral metagenome"
] | [
1,
47864,
5,
3
] | 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... | [
143,
7,
63,
22,
64,
48,
3,
74,
64,
6,
5,
215
] | 12 | true | Domain | Cyclin, C-terminal domain | Cyclin, C-terminal domain | Cyclin_C-dom | 6 |
IPR004368 | 4,368 | Translation initiation factor IF-1 | TIF_IF1 | Family | 33,686 | false | false | null | [
"GO:0003743",
"GO:0006413"
] | [
"translation initiation factor activity",
"translational initiation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00075",
"PTHR33370",
"TIGR00008",
"cd04451"
] | [
"IF_1",
"",
"infA",
"S1_IF1"
] | [
32123,
33662,
33149,
32103
] | 4 | [
"GP"
] | [
"GenProp0740"
] | [
"GP:GenProp0740"
] | 1 | [
"1ah9",
"1hr0",
"1zo1",
"2n3s",
"2n78",
"2n8n",
"2nch",
"3i4o",
"4ql5",
"5lmn",
"5lmo",
"5lmp",
"5lmq",
"5lmr",
"5lms",
"5lmt",
"5lmv",
"5me0",
"5me1",
"6c00",
"6o7k",
"8wrc",
"9dcn",
"9fco",
"9fda",
"9fib",
"9g06",
"9h9h",
"9h9j"
] | 29 | [
"PUB00000944",
"PUB00025767",
"PUB00028173",
"PUB00081032",
"PUB00081033",
"PUB00081034"
] | [
"9008164",
"11228145",
"9135158",
"16938378",
"10860719",
"14600024"
] | [
"The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.",
"Crystal structure of an initiation factor bound to the 30S ribosomal subunit.",
"The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif.",
"RNA chaperone ... | [
1997,
2001,
1997,
2006,
2000,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"candidate division MSBL1 archaeon SCGC-AAA382N08",
"unclassified sequences"
] | [
24471,
12,
8752,
1,
450
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
5,
1,
6,
2
] | 4 | true | Family | Translation initiation factor IF-1 | Translation initiation factor IF-1 | TIF_IF1 | 7 |
IPR004369 | 4,369 | Prolyl-tRNA editing protein, YbaK/EbsC | Prolyl-tRNA_editing_YbaK/EbsC | Family | 15,406 | false | false | This entry represents the YbaK family, bacterial proteins whose full length sequence is homologous to an insertion domain in proline--tRNA ligases. They deacylate mischarged tRNAs. YbaK functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity [ , ]. YbaK ha... | [] | [] | [] | 0 | [
"PIRSF",
"NCBIFAM",
"CDD"
] | [
"PIRSF006181",
"TIGR00011",
"cd00002"
] | [
"EbsC_YbaK",
"YbaK_EbsC",
"YbaK_deacylase"
] | [
15313,
13278,
14968
] | 3 | [] | [] | [] | 0 | [
"1dbu",
"1dbx",
"2dxa"
] | 3 | [
"PUB00017205",
"PUB00063636",
"PUB00063637",
"PUB00063639"
] | [
"8226689",
"15886196",
"23185990",
"14663147"
] | [
"Cloning and molecular analysis of genes affecting expression of binding substance, the recipient-encoded receptor(s) mediating mating aggregate formation in Enterococcus faecalis.",
"The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase.",
"Aminoacyl-tRNA Substrate and Enzyme Backbone Atoms Co... | [
1993,
2005,
2012,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomethylophilus alvi",
"Myoviridae sp. ctVCj30",
"metagenomes"
] | [
15275,
10,
2,
1,
118
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Prolyl-tRNA editing protein, YbaK/EbsC | Prolyl-tRNA editing protein, YbaK/EbsC | Prolyl-tRNA_editing_YbaK/EbsC | 5 |
IPR004370 | 4,370 | 4-oxalocrotonate tautomerase-like domain | 4-OT-like_dom | Domain | 14,227 | false | false | 4-oxalocrotonate tautomerase (4-OT, also known as 2-hydroxymuconate tautomerase) is an enzyme that converts 2-hydroxymuconate to the α-β-unsaturated ketone, 2-oxo-3-hexenedioate [ ]. This enzyme forms part of a bacterial metabolic pathway that oxidatively catabolizes toluene, o-xylene, 3-ethyltoluene, and 1,2,4-trimeth... | [
"GO:0016853"
] | [
"isomerase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01361"
] | [
"Tautomerase"
] | [
14227
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"5.3.2.-",
"PWY-5642",
"PWY-6550"
] | [
"EC:5.3.2.-",
"METACYC:PWY-5642",
"METACYC:PWY-6550"
] | 3 | [
"1bjp",
"1gyj",
"1gyx",
"1gyy",
"1otf",
"1s0y",
"2fm7",
"2op8",
"2opa",
"2orm",
"2x4k",
"3abf",
"3ej3",
"3ej7",
"3ej9",
"3m20",
"3m21",
"3mb2",
"3ry0",
"4faz",
"4fdx",
"4ota",
"4otb",
"4otc",
"4x19",
"4x1c",
"5cln",
"5clo",
"5tig",
"5unq",
"6bgn",
"6blm"... | 48 | [
"PUB00007676",
"PUB00019310",
"PUB00025426",
"PUB00066780"
] | [
"12051677",
"8547259",
"12356301",
"1339435"
] | [
"The 4-oxalocrotonate tautomerase family of enzymes: how nature makes new enzymes using a beta-alpha-beta structural motif.",
"Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases.",
"The crystal structure of YdcE, a 4-oxalocrotonate tau... | [
2002,
1996,
2002,
1992
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
276,
13781,
20,
2,
148
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | 4-oxalocrotonate tautomerase-like domain | 4-oxalocrotonate tautomerase-like domain | 4-OT-like_dom | 3 |
IPR004372 | 4,372 | Acetate/propionate kinase | Ac/propionate_kinase | Family | 25,660 | false | false | This entry represents proteins which transfer phosphate from ATP to a short chain aliphatic acid. For example, Acetate kinase catalyses the reaction ATP + acetate = ADP + acetyl phosphate and propionate kinase which utilizes propionate as substrate [ , ]. | [
"GO:0016301",
"GO:0016774",
"GO:0006082"
] | [
"kinase activity",
"phosphotransferase activity, carboxyl group as acceptor",
"organic acid metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PIRSF",
"NCBIFAM"
] | [
"MF_00020",
"PIRSF000722",
"TIGR00016"
] | [
"Acetate_kinase",
"Acetate_prop_kin",
"ackA"
] | [
25658,
24421,
24569
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.2.1",
"GenProp0478",
"GenProp0754",
"GenProp1267",
"GenProp1345",
"GenProp1543",
"GenProp1749",
"GenProp1762",
"PWY-5482",
"PWY-5485",
"PWY-5497",
"PWY-8015",
"PWY-8086",
"PWY-8303",
"PWY-8377"
] | [
"EC:2.7.2.1",
"GP:GenProp0478",
"GP:GenProp0754",
"GP:GenProp1267",
"GP:GenProp1345",
"GP:GenProp1543",
"GP:GenProp1749",
"GP:GenProp1762",
"METACYC:PWY-5482",
"METACYC:PWY-5485",
"METACYC:PWY-5497",
"METACYC:PWY-8015",
"METACYC:PWY-8086",
"METACYC:PWY-8303",
"METACYC:PWY-8377"
] | 15 | [
"1g99",
"1tuu",
"1tuy",
"1x3m",
"1x3n",
"2e1y",
"2e1z",
"2e20",
"2iir",
"3khy",
"3p4i",
"3r9p",
"3sk3",
"3slc",
"4dq8",
"4fwk",
"4fwl",
"4fwm",
"4fwn",
"4fwo",
"4fwp",
"4fwq",
"4fwr",
"4fws",
"4h0o",
"4h0p",
"4ijn",
"4iz9",
"4xh1",
"4xh4",
"4xh5",
"6ioy"... | 39 | [
"PUB00016056",
"PUB00065155"
] | [
"9484901",
"23031654"
] | [
"Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate.",
"Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the d... | [
1998,
2012
] | 2 | [
"IPR000890"
] | [
"IPR024896",
"IPR024917"
] | 1 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctX581",
"Stenosarchaea group",
"unclassified sequences"
] | [
23898,
1498,
1,
36,
227
] | 5 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2,
1
] | 2 | true | Family | Acetate/propionate kinase | Acetate/propionate kinase | Ac/propionate_kinase | 4 |
IPR004373 | 4,373 | Peptide chain release factor 1 | RF-1 | Family | 25,526 | false | false | This entry represents peptide chain release factor 1 (PrfA, RF-1), and excludes the related peptide chain release factor 2 (PrfB, RF-2). RF-1 helps recognise and terminate translation at UAA and UAG stop codons [ ]. This entry also includes chloroplast release factor APG3, which is an orthologue of E. coli RF1 and is e... | [
"GO:0016149",
"GO:0006415"
] | [
"translation release factor activity, codon specific",
"translational termination"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00093",
"TIGR00019"
] | [
"Rel_fac_1",
"prfA"
] | [
25010,
25452
] | 2 | [
"GP"
] | [
"GenProp0746"
] | [
"GP:GenProp0746"
] | 1 | [
"1rq0",
"1zbt",
"2b3t",
"2fvo",
"4v4r",
"4v63",
"4v7p",
"5j30",
"5j3c",
"5j4d",
"5o2r",
"6b4v",
"6boh",
"6bok",
"6dnc",
"6gwt",
"6gxm",
"6gxn",
"6gxo",
"6orl",
"6osk",
"6osq",
"7m5d",
"8akn",
"8fzd",
"8fze",
"8fzg",
"8fzh",
"9d7r",
"9d7s",
"9d7t",
"9mtp"... | 37 | [
"PUB00085731",
"PUB00085732"
] | [
"17450416",
"4879404"
] | [
"Chloroplast ribosome release factor 1 (AtcpRF1) is essential for chloroplast development.",
"Release factors differing in specificity for terminator codons."
] | [
2007,
1968
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctPyh10",
"unclassified sequences"
] | [
23896,
1201,
1,
428
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
1,
7,
7
] | 4 | true | Family | Peptide chain release factor 1 | Peptide chain release factor 1 | RF-1 | 9 |
IPR004374 | 4,374 | Peptide chain release factor 2 | PrfB | Family | 25,906 | false | false | Peptide chain release factors (RFs) are required for the termination of protein biosynthesis [ ]. At present two classes of RFs can be distinguished. Class I RFs bind to ribosomes that have encountered a stop codon at their decoding site and induce release of the nascent polypeptide. Class II RFs are GTP-binding protei... | [
"GO:0016149",
"GO:0006415",
"GO:0005737"
] | [
"translation release factor activity, codon specific",
"translational termination",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00094",
"TIGR00020"
] | [
"Rel_fac_2",
"prfB"
] | [
25182,
25845
] | 2 | [
"GP"
] | [
"GenProp0746"
] | [
"GP:GenProp0746"
] | 1 | [
"1gqe",
"1mi6",
"1ml5",
"2ihr",
"4v4s",
"4v5e",
"4v5j",
"4v67",
"4v9n",
"5czp",
"5dfe",
"5h5u",
"5mdv",
"5mdw",
"5mdy",
"5mgp",
"5u4i",
"5u4j",
"5u9f",
"5u9g",
"6c4h",
"6c4i",
"6c5l",
"6og7",
"6ogf",
"6ogg",
"6ost",
"6ot3",
"6ouo",
"6szs",
"7o1c",
"7oj0"... | 37 | [
"PUB00003804",
"PUB00004407",
"PUB00004944",
"PUB00085742"
] | [
"2215213",
"1408743",
"8821264",
"12468741"
] | [
"Recent advances in peptide chain termination.",
"Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure.",
"Hidden infidelities of the translational stop signal.",
"A peptide chain release facto... | [
1990,
1992,
1996,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
24166,
5,
1288,
447
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
10,
1,
6,
8
] | 4 | true | Family | Peptide chain release factor 2 | Peptide chain release factor 2 | PrfB | 9 |
IPR004375 | 4,375 | NanQ anomerase/TabA/YiaL family | NanQ/TabA/YiaL | Family | 8,674 | false | false | This protein family consists of bacterial proteins. N-acetylneuraminate anomerase NanQ (NanQ, previously known as YhcH) plays a role in sialic acid catabolism by opening both the alpha- and beta-forms of N-acetylneuraminate (sialic acid; Neu5Ac) to provide aceneuramate, the preferred substrate for the sialic acid aldol... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"PF04074",
"PTHR34986",
"TIGR00022"
] | [
"DUF386",
"",
""
] | [
8672,
8602,
8077
] | 3 | [] | [] | [] | 0 | [
"1jop",
"1s4c",
"4tsd",
"9jrr"
] | 4 | [
"PUB00054289",
"PUB00078078",
"PUB00099659"
] | [
"16077096",
"19060153",
"33895133"
] | [
"Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism.",
"Toxin-antitoxin systems in Escherichia coli influence biofilm formation through YjgK (TabA) and fimbriae.",
"The metalloprotein YhcH is an anomerase providing N-acetylneuraminate aldolase with the open form of its su... | [
2005,
2009,
2021
] | 3 | [] | [
"IPR049827"
] | 0 | 1 | 0 | [
"Bacteria",
"Eumetazoa",
"unclassified sequences"
] | [
8594,
5,
75
] | 3 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Family | NanQ anomerase/TabA/YiaL family | NanQ anomerase/TabA/YiaL family | NanQ/TabA/YiaL | 7 |
IPR004376 | 4,376 | Phosphoesterase MJ0037 | Pesterase_MJ0037 | Family | 261 | false | false | This entry represents a group of poorly uncharacterised archaeal proteins, such as MJ0037 from Methanocaldococcus jannaschii, that share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11. SbcD is a subunit of the SbcCD nuclease of Escherichia coli ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00024"
] | [
"SbcD_rel_arch"
] | [
261
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR024173"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"unclassified sequences"
] | [
255,
3,
3
] | 3 | [] | [] | 0 | true | Family | Phosphoesterase MJ0037 | Phosphoesterase MJ0037 | Pesterase_MJ0037 | 1 |
IPR004377 | 4,377 | ABC transporter, permease protein DrrB/DrrC | ABC_transpt_DrrB/DrrC | Family | 1,545 | false | false | DrrB and DrrC are part of the ABC transporter complex drrABC involved in doxorubicin and daunorubicin resistance [ ]. The members of this family are found mainly in mycobacteria. They are paralogous to proteins of the resistance efflux system of Streptomyces peucetius [ ]. In mycobacteria this pump confers resistance t... | [
"GO:0043215",
"GO:0046677",
"GO:1900753"
] | [
"daunorubicin transport",
"response to antibiotic",
"doxorubicin transport"
] | [
"biological_process",
"biological_process",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00025"
] | [
"Mtu_efflux"
] | [
1545
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00061723",
"PUB00061726"
] | [
"12057006",
"19651502"
] | [
"Overexpression and functional characterization of an ABC (ATP-binding cassette) transporter encoded by the genes drrA and drrB of Mycobacterium tuberculosis.",
"Self-resistance mechanism in Streptomyces peucetius: overexpression of drrA, drrB and drrC for doxorubicin enhancement."
] | [
2002,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Actinomycetes",
"ecological metagenomes"
] | [
1542,
3
] | 2 | [] | [] | 0 | true | Family | ABC transporter, permease protein DrrB/DrrC | ABC transporter, permease protein DrrB/DrrC | ABC_transpt_DrrB/DrrC | 3 |
IPR004378 | 4,378 | F420H(2)-dependent quinone reductase | F420H2_quin_Rdtase | Family | 20,674 | false | false | This entry represents a family of proteins found in paralogous families in the genera Mycobacterium and Streptomyces. Seven members are in Mycobacterium tuberculosis. Member protein Rv3547 has been characterised as a deazaflavin-dependent nitroreductase [ , ]. Rv1558 is an F420H(2)-dependent quinone reductase involved ... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"NCBIFAM"
] | [
"PF04075",
"TIGR00026"
] | [
"F420H2_quin_red",
"hi_GC_TIGR00026"
] | [
19903,
18394
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.1.98.-",
"GenProp0002",
"PWY-5922",
"PWY-5923",
"PWY-5924",
"PWY-5927",
"PWY-8445"
] | [
"EC:1.1.98.-",
"GP:GenProp0002",
"METACYC:PWY-5922",
"METACYC:PWY-5923",
"METACYC:PWY-5924",
"METACYC:PWY-5927",
"METACYC:PWY-8445"
] | 7 | [
"3h96",
"3r5l",
"3r5p",
"3r5r",
"3r5w",
"3r5y",
"3r5z",
"4y9i",
"6wta",
"6xri",
"7kl8",
"8d4w"
] | 12 | [
"PUB00054201",
"PUB00054202",
"PUB00077109"
] | [
"16387854",
"19039139",
"23240649"
] | [
"Identification of a nitroimidazo-oxazine-specific protein involved in PA-824 resistance in Mycobacterium tuberculosis.",
"PA-824 kills nonreplicating Mycobacterium tuberculosis by intracellular NO release.",
"A novel F(420) -dependent anti-oxidant mechanism protects Mycobacterium tuberculosis against oxidative... | [
2006,
2008,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
94,
20300,
10,
270
] | 4 | [] | [] | 0 | true | Family | F420H(2)-dependent quinone reductase | F420H(2)-dependent quinone reductase | F420H2_quin_Rdtase | 5 |
IPR004379 | 4,379 | UDP-galactopyranose mutase | UDP-GALP_mutase | Family | 8,540 | false | false | UDP-galactopyranose mutase ( ) is involved in the conversion of UDP-GALP into UDP-GALF through a 2-keto intermediate, and contains FAD as a cofactor. The gene is known as glf, ceoA, and rfbD. It is known experimentally in Escherichia coli, Mycobacterium tuberculosis, and Klebsiella pneumoniae. | [
"GO:0008767"
] | [
"UDP-galactopyranose mutase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00031"
] | [
"UDP-GALP_mutase"
] | [
8540
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.4.99.9",
"PWY-6397",
"PWY-7328",
"PWY-7622"
] | [
"EC:5.4.99.9",
"METACYC:PWY-6397",
"METACYC:PWY-7328",
"METACYC:PWY-7622"
] | 4 | [
"1i8t",
"1v0j",
"1wam",
"2bi7",
"2bi8",
"3gf4",
"3hdq",
"3hdy",
"3he3",
"3inr",
"3int",
"3kyb",
"3mj4",
"4mo2",
"4rpg",
"4rph",
"4rpj",
"4rpk",
"4rpl",
"4xgk",
"5br7",
"5eqd",
"5eqf",
"5er9",
"5f3r",
"6d2e",
"6d2g",
"6d99",
"6d9a",
"6d9b",
"6d9c",
"6d9d"... | 33 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
42,
8362,
49,
17,
70
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | UDP-galactopyranose mutase | UDP-galactopyranose mutase | UDP-GALP_mutase | 2 |
IPR004380 | 4,380 | Aspartate racemase | Asp_race | Family | 14,437 | false | false | Asparate racemases ( ) and some close homologues of function are related to the more common glutamate racemases, but form a distinct evolutionary branch [ ]. Members of this family are the aspartate racemase-related subset of amino acid racemases. Aspartate racemases act as homodimers and catalyse the conversion of L-a... | [
"GO:0047661"
] | [
"amino-acid racemase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00035"
] | [
"asp_race"
] | [
14437
] | 1 | [
"EC"
] | [
"5.1.1.13"
] | [
"EC:5.1.1.13"
] | 1 | [
"1iu9",
"1jfl",
"2dx7",
"2zsk",
"3ojc",
"3s7z",
"3s81",
"5b19",
"5ell",
"5elm",
"5evc",
"5hqt",
"5hra",
"5hrc",
"9lyd"
] | 15 | [
"PUB00021860",
"PUB00047294"
] | [
"12297289",
"17847084"
] | [
"Structural insight into gene duplication, gene fusion and domain swapping in the evolution of PLP-independent amino acid racemases.",
"Structure of aspartate racemase complexed with a dual substrate analogue, citric acid, and implications for the reaction mechanism."
] | [
2002,
2008
] | 2 | [
"IPR015942"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctjdk2",
"unclassified sequences"
] | [
170,
13448,
688,
1,
130
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Aspartate racemase | Aspartate racemase | Asp_race | 1 |
IPR004383 | 4,383 | Ribosomal RNA large subunit methyltransferase RlmN/Cfr | rRNA_lsu_MTrfase_RlmN/Cfr | Family | 27,361 | false | false | This entry represents the RlmN family, that includes dual-specificity RNA methyltransferase RlmN and ribosomal RNA large subunit methyltransferase Cfr. Dual-specificity RNA methyltransferase RlmN specifically methylates position 2 of adenine 2503 in 23S rRNA [ ]. This nucleotide is located in a functionally important r... | [
"GO:0008173",
"GO:0006364"
] | [
"RNA methyltransferase activity",
"rRNA processing"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"SFLD"
] | [
"PIRSF006004",
"SFLDF00275"
] | [
"CHP00048",
"adenosine_C2_methyltransferase"
] | [
26209,
27028
] | 2 | [
"EC",
"EC"
] | [
"2.1.1",
"2.1.1.192"
] | [
"EC:2.1.1",
"EC:2.1.1.192"
] | 2 | [
"3rf9",
"3rfa",
"4pl1",
"4pl2",
"5hr6",
"5hr7",
"6fz6",
"9p0p"
] | 8 | [
"PUB00017347",
"PUB00046147",
"PUB00064728",
"PUB00064729",
"PUB00064730"
] | [
"10952608",
"18025251",
"21415317",
"22891362",
"19144912"
] | [
"Identification of a plasmid-borne chloramphenicol-florfenicol resistance gene in Staphylococcus sciuri.",
"The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA.",
"A radically different mechanism for S-adenosylmethionine-dependent methyltransferases.",
"The Escherichi... | [
2000,
2008,
2011,
2012,
2009
] | 5 | [
"IPR040072"
] | [
"IPR022881",
"IPR027492"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
55,
24746,
2105,
7,
448
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
1,
8,
12
] | 4 | true | Family | Ribosomal RNA large subunit methyltransferase RlmN/Cfr | Ribosomal RNA large subunit methyltransferase RlmN/Cfr | rRNA_lsu_MTrfase_RlmN/Cfr | 9 |
IPR004384 | 4,384 | RNA methyltransferase TrmJ/LasT | RNA_MeTrfase_TrmJ/LasT | Family | 15,505 | false | false | This entry includes TrmJ and LasT from E.coli. TrmJ is a tRNA methyltransferase that catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA [ , , ]. The function of LasT is not clear. | [
"GO:0008173",
"GO:0006396"
] | [
"RNA methyltransferase activity",
"RNA processing"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"PIRSF004808",
"PTHR42786",
"TIGR00050"
] | [
"LasT",
"",
"rRNA_methyl_1"
] | [
12665,
15499,
11105
] | 3 | [
"EC"
] | [
"2.1.1.200"
] | [
"EC:2.1.1.200"
] | 1 | [
"3ic6",
"3ilk",
"3kty",
"3onp",
"4cnd",
"4cne",
"4cnf",
"4cng",
"4xbo",
"5gm8",
"5gmb",
"5gmc",
"5gra"
] | 13 | [
"PUB00043004",
"PUB00090189",
"PUB00090190"
] | [
"16848900",
"24951554",
"26202969"
] | [
"The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase.",
"Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates.",
"tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily."
... | [
2006,
2014,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
789,
14100,
390,
226
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | RNA methyltransferase TrmJ/LasT | RNA methyltransferase TrmJ/LasT | RNA_MeTrfase_TrmJ/LasT | 5 |
IPR004385 | 4,385 | Nucleoside diphosphate pyrophosphatase | NDP_pyrophosphatase | Family | 12,842 | false | false | This entry describes a family of proteins which appear to catalyse the hydrolysis of phosphorus-containing acid anhydrides such as nucleoside diphosphate, for example ADP-mannose and UDP-glucose [ ]. Some of these enzymes play a key role in glycogen biosynthesis. | [
"GO:0016818",
"GO:0046872"
] | [
"hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR00052"
] | [
""
] | [
12842
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.1",
"3.6.1.-",
"PWY-5757",
"PWY-6147",
"PWY-6383",
"PWY-6797",
"PWY-7206",
"PWY-7419",
"PWY-7539",
"PWY-7719",
"PWY-7821",
"PWY-8289",
"R-BTA-480985",
"R-HSA-480985",
"R-MMU-480985"
] | [
"EC:3.6.1",
"EC:3.6.1.-",
"METACYC:PWY-5757",
"METACYC:PWY-6147",
"METACYC:PWY-6383",
"METACYC:PWY-6797",
"METACYC:PWY-7206",
"METACYC:PWY-7419",
"METACYC:PWY-7539",
"METACYC:PWY-7719",
"METACYC:PWY-7821",
"METACYC:PWY-8289",
"REACTOME:R-BTA-480985",
"REACTOME:R-HSA-480985",
"REACTOME:R-... | 15 | [
"1g0s",
"1g9q",
"1ga7",
"1khz",
"1viq",
"1viu",
"3o52",
"3o61",
"3o69",
"3o6z",
"3q91",
"8otv",
"8wv3",
"8zr8",
"9b1z",
"9b20",
"9b21",
"9b22",
"9drd",
"9dre",
"9drf",
"9dsz",
"9dt6",
"9dt7",
"9dt8",
"9dtc",
"9du6",
"9du8",
"9du9",
"9dua",
"9dud",
"9duf"... | 35 | [
"PUB00014894"
] | [
"12429023"
] | [
"Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermoproteati",
"unclassified sequences",
"uncultured marine phage"
] | [
11432,
1334,
7,
68,
1
] | 5 | [
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
2,
2,
2,
3
] | 6 | true | Family | Nucleoside diphosphate pyrophosphatase | Nucleoside diphosphate pyrophosphatase | NDP_pyrophosphatase | 3 |
IPR004386 | 4,386 | Toxin-antitoxin system, YafQ-like toxin | Toxin_YafQ-like | Family | 5,593 | false | false | YafQ is a ribosome-associated endoribonuclease that serves as part of a toxin-antitoxin system, for which DinJ is the antidote component [ ]. It associates with the ribosome and blocks translation elongation through sequence-specific and frame-dependent mRNA cleavage [ ]. | [] | [] | [] | 0 | [
"PFAM",
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"PF15738",
"PIRSF006156",
"PTHR40588",
"TIGR00053"
] | [
"YafQ_toxin",
"YafQ",
"",
""
] | [
5587,
3549,
4189,
756
] | 4 | [
"GP",
"GP"
] | [
"GenProp0321",
"GenProp1125"
] | [
"GP:GenProp0321",
"GP:GenProp1125"
] | 2 | [
"1z8m",
"2otr",
"4ls4",
"4lsy",
"4ltt",
"4ml0",
"4ml2",
"4mmg",
"4mmj",
"4nrn",
"4q2u",
"9lew"
] | 12 | [
"PUB00057354",
"PUB00060311"
] | [
"17263853",
"19210620"
] | [
"Escherichia coli dinJ-yafQ genes act as a toxin-antitoxin module.",
"Bacterial toxin YafQ is an endoribonuclease that associates with the ribosome and blocks translation elongation through sequence-specific and frame-dependent mRNA cleavage."
] | [
2007,
2009
] | 2 | [
"IPR007712"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanobacteriota",
"Sym plasmid",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
5496,
9,
2,
2,
84
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Toxin-antitoxin system, YafQ-like toxin | Toxin-antitoxin system, YafQ-like toxin | Toxin_YafQ-like | 9 |
IPR004387 | 4,387 | Peptidase M50, putative membrane-associated zinc metallopeptidase | Pept_M50_Zn | Family | 28,333 | false | false | Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase... | [
"GO:0004222",
"GO:0006508",
"GO:0016020"
] | [
"metalloendopeptidase activity",
"proteolysis",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR42837",
"TIGR00054"
] | [
"",
""
] | [
28326,
18969
] | 2 | [
"EC",
"GP",
"METACYC"
] | [
"3.4.24.-",
"GenProp1327",
"PWY-8119"
] | [
"EC:3.4.24.-",
"GP:GenProp1327",
"METACYC:PWY-8119"
] | 3 | [
"2zpm",
"3id2",
"3id3",
"3id4",
"3wkl",
"3wkm",
"6akq",
"6al0",
"6al1",
"6icc",
"6icf",
"7cqc",
"7cqd",
"7w6x",
"7w6y",
"7w6z",
"7w70",
"7w71",
"7xft",
"7xfu",
"8ipc",
"9j82",
"9j83"
] | 23 | [
"PUB00003579",
"PUB00015313"
] | [
"7674922",
"8674113"
] | [
"Evolutionary families of metallopeptidases.",
"Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ."
] | [
1995,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
8,
26716,
884,
725
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
11,
1,
6,
13
] | 4 | true | Family | Peptidase M50, putative membrane-associated zinc metallopeptidase | Peptidase M50, putative membrane-associated zinc metallopeptidase | Pept_M50_Zn | 7 |
IPR004389 | 4,389 | Large ribosomal subunit protein uL18, bacteria | Ribosomal_uL18_bact | Family | 25,010 | false | false | This entry represents the ribosomal protein uL18 from bacteria and chloroplasts. The archaebacterial type is not included in this family. The large ribosomal subunit protein uL18 is an essential component of the large subunit LSU, which is required in its formation and stabilisation. The LSU contains the ribosomal cata... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01337_B",
"TIGR00060"
] | [
"Ribosomal_uL18_B",
"L18_bact"
] | [
24797,
24939
] | 2 | [] | [] | [] | 0 | [
"1ily",
"1nkw",
"1nwx",
"1nwy",
"1ovy",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"2j28",
"2rdo",
"2zjp",
"2zjq",
"2zjr",
"3bbx",
"3cf5",
"3dll",
"3j3v",
"3j5l",
"3j7z",
"3j8g",
"3j9w",
"3j9y",
"3j9z",
"3ja1",
"3jbu",
"3jbv",
"3jcd",
"3jce"... | 1,114 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00030943",
"PUB00079485",
"PUB00097818"
] | [
"11297922",
"11290319",
"11114498",
"15184028",
"14527328",
"12962325"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit.",
"The structural basis of large ribosomal subunit fu... | [
2001,
2001,
2000,
2004,
2003,
2003
] | 6 | [
"IPR005484"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
23533,
1084,
393
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
2,
4
] | 4 | true | Family | Large ribosomal subunit protein uL18, bacteria | Large ribosomal subunit protein uL18, bacteria | Ribosomal_uL18_bact | 4 |
IPR004390 | 4,390 | Signal-recognition particle receptor FtsY | SR_rcpt_FtsY | Family | 26,760 | false | false | FtsY is involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. It acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). In E. coli, interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec tra... | [
"GO:0006614"
] | [
"SRP-dependent cotranslational protein targeting to membrane"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00920",
"TIGR00064"
] | [
"FtsY",
"ftsY"
] | [
25590,
26755
] | 2 | [
"EC"
] | [
"3.6.5.4"
] | [
"EC:3.6.5.4"
] | 1 | [
"1fts",
"1okk",
"1rj9",
"1vma",
"1zu4",
"1zu5",
"2cnw",
"2iyl",
"2j7p",
"2og2",
"2q9a",
"2q9b",
"2q9c",
"2qy9",
"2xkv",
"2xxa",
"2yhs",
"3b9q",
"3dm9",
"3dmd",
"3e70",
"3zn8",
"4ak9",
"4c7o",
"5gad",
"5l3r",
"5l3s",
"5l3w",
"5nco",
"5niy",
"6cqp",
"6cs8"... | 45 | [
"PUB00017615",
"PUB00060300",
"PUB00060301"
] | [
"11735405",
"17682051",
"15815684"
] | [
"Role of SRP RNA in the GTPase cycles of Ffh and FtsY.",
"Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation.",
"FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG t... | [
2001,
2007,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
924,
24715,
617,
504
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
5,
3
] | 4 | true | Family | Signal-recognition particle receptor FtsY | Signal-recognition particle receptor FtsY | SR_rcpt_FtsY | 5 |
IPR004391 | 4,391 | Glutamate racemase | Glu_race | Family | 22,355 | false | false | Glutamate racemase ( ) provides the (R)-glutamic acid required for cell wall biosynthesis. It converts L-glutamate to D-glutamate during peptidoglycan biosynthesis. The most closely related proteins differing in function are aspartate racemases. | [
"GO:0008881"
] | [
"glutamate racemase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00258",
"TIGR00067"
] | [
"Glu_racemase",
"glut_race"
] | [
21955,
21625
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC"
] | [
"5.1.1.3",
"GenProp1448",
"PWY-6386",
"PWY-6387"
] | [
"EC:5.1.1.3",
"GP:GenProp1448",
"METACYC:PWY-6386",
"METACYC:PWY-6387"
] | 4 | [
"1b73",
"1b74",
"1zuw",
"2dwu",
"2gzm",
"2jfn",
"2jfo",
"2jfp",
"2jfq",
"2jfu",
"2jfv",
"2jfw",
"2jfx",
"2jfy",
"2jfz",
"2ohg",
"2oho",
"2ohv",
"2vvt",
"2w4i",
"3hfr",
"3ist",
"3isv",
"3out",
"3uhf",
"3uho",
"3uhp",
"4b1f",
"5hj7",
"5ijw",
"5w16",
"5w1q"... | 37 | [] | [] | [] | [] | 0 | [
"IPR015942"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Thermoproteati",
"unclassified sequences"
] | [
21966,
28,
8,
353
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glutamate racemase | Glutamate racemase | Glu_race | 9 |
IPR004392 | 4,392 | Hydrogenase maturation factor HypB | Hyd_mat_HypB | Family | 7,973 | false | false | The hydrogenase accessory protein HypB is a GTP hydrolase required for assembly of the nickel metallocentre of hydrogenase [ ]. In Helicobacter pylori, HypB is also required for maturation of urease [ ]. The homologue guanidine hydrolase-activating protein B (GhaB) is involved in the maturation of the nickel-dependent ... | [
"GO:0003924",
"GO:0016151",
"GO:0051604"
] | [
"GTPase activity",
"nickel cation binding",
"protein maturation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"PTHR30134",
"TIGR00073",
"cd05390"
] | [
"",
"hypB",
"HypB"
] | [
7965,
7058,
5395
] | 3 | [] | [] | [] | 0 | [
"2hf8",
"2hf9",
"2wsm",
"4lps"
] | 4 | [
"PUB00015852",
"PUB00088173",
"PUB00154481"
] | [
"7601092",
"12533448",
"35264792"
] | [
"GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli.",
"Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase.",
"Discovery of a Ni<sup>2+</sup>-dependent guanidine hydrolase in bacteria."
] | [
1995,
2003,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
460,
7319,
9,
185
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Hydrogenase maturation factor HypB | Hydrogenase maturation factor HypB | Hyd_mat_HypB | 4 |
IPR004393 | 4,393 | Nicotinate-nucleotide pyrophosphorylase | NadC | Family | 23,816 | false | false | Nicotinate-nucleotide pyrophosphorylase ( ), also known as quinolinate phosphoribosyltransferase (decarboxylating), catalyses the conversion of nicotinate D-ribonucleotide, pyrophosphate and carbon dioxide into pyridine-2,3-dicarboxylate and 5-phospho-alpha-D-ribose 1-diphosphate. This enzyme is a type II phosphoribosy... | [
"GO:0004514",
"GO:0009435"
] | [
"nicotinate-nucleotide diphosphorylase (carboxylating) activity",
"NAD+ biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM",
"CDD"
] | [
"TIGR00078",
"cd01572"
] | [
"nadC",
"QPRTase"
] | [
23578,
23501
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.4.2.19",
"GenProp0057",
"PWY-5316",
"PWY-5653",
"PWY-7342",
"PWY-8277",
"PWY-8352",
"R-DDI-196807",
"R-HSA-196807",
"R-MMU-196807",
"R-RNO-196807",
"R-SCE-196807",
"R-SSC-196807"
] | [
"EC:2.4.2.19",
"GP:GenProp0057",
"METACYC:PWY-5316",
"METACYC:PWY-5653",
"METACYC:PWY-7342",
"METACYC:PWY-8277",
"METACYC:PWY-8352",
"REACTOME:R-DDI-196807",
"REACTOME:R-HSA-196807",
"REACTOME:R-MMU-196807",
"REACTOME:R-RNO-196807",
"REACTOME:R-SCE-196807",
"REACTOME:R-SSC-196807"
] | 13 | [
"1o4u",
"1qap",
"1qpn",
"1qpo",
"1qpq",
"1qpr",
"1x1o",
"2b7n",
"2b7p",
"2b7q",
"2jbm",
"3c2e",
"3c2f",
"3c2o",
"3c2r",
"3c2v",
"3gnn",
"3l0g",
"3paj",
"3tqv",
"4i9a",
"4kwv",
"4kww",
"5ayx",
"5ayy",
"5ayz",
"5hul",
"5huo",
"5hup",
"7xgl",
"7xgm",
"7xgn"... | 32 | [
"PUB00005289",
"PUB00017199",
"PUB00017200",
"PUB00017201",
"PUB00017204"
] | [
"9016724",
"6997723",
"11876660",
"9862811",
"15103640"
] | [
"A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase.",
"Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems.",
"Quinolinate phosphoribosyltransferase: kinetic mechanism for a type II PRTase.",
"Crystal s... | [
1997,
1980,
2002,
1998,
2004
] | 5 | [
"IPR027277"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
681,
19611,
3077,
447
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
6,
1,
2,
1,
2,
1,
11,
1,
1
] | 9 | true | Family | Nicotinate-nucleotide pyrophosphorylase | Nicotinate-nucleotide pyrophosphorylase | NadC | 6 |
IPR004394 | 4,394 | Protein Iojap/ribosomal silencing factor RsfS | Iojap/RsfS/C7orf30 | Family | 26,287 | false | false | This entry includes Iojap protein from plants, the ribosomal silencing factor RsfS (also known as RsfA) from bacteria and its homologue, C7orf30, from animals. | [] | [] | [] | 0 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_01477",
"PTHR21043",
"TIGR00090"
] | [
"Iojap_RsfS",
"",
"rsfS_iojap_ybeB"
] | [
25065,
26106,
25530
] | 3 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-9937383",
"R-MMU-9937383"
] | [
"REACTOME:R-HSA-9937383",
"REACTOME:R-MMU-9937383"
] | 2 | [
"2id1",
"2o5a",
"3ups",
"4wcw",
"5ool",
"5oom",
"6sj5",
"6sj6",
"6yxy",
"7a5h",
"7a5j",
"7am2",
"7aoi",
"7bl2",
"7bl3",
"7bl4",
"7bl5",
"7o9k",
"7o9m",
"7odr",
"7ods",
"7odt",
"7of0",
"7of2",
"7of3",
"7of5",
"7of7",
"7oi6",
"7oi7",
"7oi8",
"7oi9",
"7oic"... | 49 | [
"PUB00064845",
"PUB00064846",
"PUB00064847",
"PUB00074044"
] | [
"22829778",
"1382980",
"21908688",
"22238375"
] | [
"RsfA (YbeB) proteins are conserved ribosomal silencing factors.",
"Molecular cloning and characterization of iojap (ij), a pattern striping gene of maize.",
"In-depth temporal transcriptome profiling reveals a crucial developmental switch with roles for RNA processing and organelle metabolism that are essentia... | [
2012,
1992,
2011,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Myoviridae sp. ctTrm2",
"unclassified sequences"
] | [
22424,
3335,
1,
527
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
7,
1,
1,
2,
1,
1,
1,
4,
3,
9
] | 10 | true | Family | Protein Iojap/ribosomal silencing factor RsfS | Protein Iojap/ribosomal silencing factor RsfS | Iojap/RsfS/C7orf30 | 7 |
IPR004396 | 4,396 | Ribosome-binding ATPase YchF/Obg-like ATPase 1 | ATPase_YchF/OLA1 | Family | 31,191 | false | false | E. coli ribosome-binding ATPase YchF is an ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner [ ]. The mammalian homologue of YchF has been termed OLA1, for Obg-like ATPase 1 [ ]. These proteins bind and hydrolyse ATP more efficiently than GTP, therefore their na... | [
"GO:0005524",
"GO:0005525",
"GO:0016887"
] | [
"ATP binding",
"GTP binding",
"ATP hydrolysis activity"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"HAMAP",
"PIRSF",
"NCBIFAM"
] | [
"MF_00944",
"PIRSF006641",
"TIGR00092"
] | [
"YchF_OLA1_ATPase",
"CHP00092",
""
] | [
28427,
29308,
30727
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-114608",
"R-CEL-114608",
"R-DME-114608",
"R-DRE-114608",
"R-GGA-114608",
"R-HSA-114608",
"R-MMU-114608",
"R-RNO-114608",
"R-SCE-114608",
"R-SPO-114608",
"R-XTR-114608"
] | [
"REACTOME:R-BTA-114608",
"REACTOME:R-CEL-114608",
"REACTOME:R-DME-114608",
"REACTOME:R-DRE-114608",
"REACTOME:R-GGA-114608",
"REACTOME:R-HSA-114608",
"REACTOME:R-MMU-114608",
"REACTOME:R-RNO-114608",
"REACTOME:R-SCE-114608",
"REACTOME:R-SPO-114608",
"REACTOME:R-XTR-114608"
] | 11 | [
"1jal",
"1ni3",
"2dby",
"2dwq",
"2ohf",
"5ee0",
"5ee1",
"5ee3",
"5ee9",
"7y9i",
"8kie",
"8w51"
] | 12 | [
"PUB00036769",
"PUB00068863"
] | [
"17430889",
"21527254"
] | [
"Human OLA1 defines an ATPase subfamily in the Obg family of GTP-binding proteins.",
"Deciphering the catalytic machinery in a universally conserved ribosome binding ATPase YchF."
] | [
2007,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
24597,
6168,
2,
424
] | 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",... | [
5,
1,
3,
4,
1,
2,
3,
1,
4,
4,
2,
2,
11
] | 13 | true | Family | Ribosome-binding ATPase YchF/Obg-like ATPase 1 | Ribosome-binding ATPase YchF/Obg-like ATPase 1 | ATPase_YchF/OLA1 | 4 |
IPR004398 | 4,398 | RNA methyltransferase, RsmD | RNA_MeTrfase_RsmD | Family | 25,708 | false | false | This entry contains ribosomal RNA small subunit methyltransferase D as well as the putative rRNA methyltransferase YlbH. They methylate the guanosine in position 966 of 16S rRNA in the assembled 30S particle [ , ]. RsmD-like protein Rv2966 from Mycobacterium tuberculosis, also can methylate and modulate host cellular D... | [
"GO:0008168",
"GO:0031167"
] | [
"methyltransferase activity",
"rRNA methylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"PIRSF004553",
"PTHR43542",
"TIGR00095"
] | [
"CHP00095",
"",
""
] | [
23673,
25697,
21738
] | 3 | [
"EC"
] | [
"2.1.1.171"
] | [
"EC:2.1.1.171"
] | 1 | [
"1ws6",
"2esr",
"2fhp",
"2fpo",
"2ift",
"3p9n",
"6aie",
"6m1c"
] | 8 | [
"PUB00042729",
"PUB00065530",
"PUB00152823"
] | [
"17189261",
"21474448",
"25824946"
] | [
"Methyltransferase that modifies guanine 966 of the 16 S rRNA: functional identification and tertiary structure.",
"Structural and functional characterization of Rv2966c protein reveals an RsmD-like methyltransferase from Mycobacterium tuberculosis and the role of its N-terminal domain in target recognition.",
... | [
2007,
2011,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Nitrososphaerota",
"Siphoviridae sp. ctZF426",
"unclassified sequences"
] | [
24181,
930,
3,
1,
593
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
1,
6,
6
] | 4 | true | Family | RNA methyltransferase, RsmD | RNA methyltransferase, RsmD | RNA_MeTrfase_RsmD | 6 |
IPR004399 | 4,399 | Hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase domain | HMP/HMP-P_kinase_dom | Domain | 29,467 | false | false | This entry represents a bifunctional enzyme, phosphomethylpyrimidine (HMP-P) kinase ( )/Hydroxymethylpyrimidine (HMP) kinase ( ), the ThiD/J protein of thiamine biosynthesis. It catalyses two consecutive phosphorylation reactions in the thiamine phosphate biosynthesis pathway, first phosphorylating HMP to HMP-P, and th... | [
"GO:0008972",
"GO:0009228"
] | [
"phosphomethylpyrimidine kinase activity",
"thiamine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM",
"CDD"
] | [
"TIGR00097",
"cd01169"
] | [
"HMP-P_kinase",
"HMPP_kinase"
] | [
23574,
29464
] | 2 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.1.49",
"2.7.4.7",
"GenProp0253",
"GenProp1266",
"GenProp1289",
"GenProp1590",
"PWY-6890",
"PWY-6910",
"PWY-7282",
"PWY-7356",
"PWY-7357"
] | [
"EC:2.7.1.49",
"EC:2.7.4.7",
"GP:GenProp0253",
"GP:GenProp1266",
"GP:GenProp1289",
"GP:GenProp1590",
"METACYC:PWY-6890",
"METACYC:PWY-6910",
"METACYC:PWY-7282",
"METACYC:PWY-7356",
"METACYC:PWY-7357"
] | 11 | [
"1jxh",
"1jxi",
"1ub0",
"2i5b",
"3rm5",
"4c5j",
"4c5k",
"4c5l",
"4c5m",
"4c5n",
"4jjp",
"4yl5",
"4ywr",
"7l07",
"7r8y",
"7r8z",
"8g1h"
] | 17 | [
"PUB00070802"
] | [
"10075431"
] | [
"Cloning and characterization of the thiD/J gene of Escherichia coli encoding a thiamin-synthesizing bifunctional enzyme, hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase."
] | [
1999
] | 1 | [
"IPR013749"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
870,
25796,
2574,
227
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
3,
1,
2,
2,
3,
3,
8
] | 7 | true | Domain | Hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase domain | Hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase domain | HMP/HMP-P_kinase_dom | 4 |
IPR004401 | 4,401 | Nucleoid-associated protein YbaB/EbfC | YbaB/EbfC | Family | 30,326 | false | false | This is a family of DNA-binding proteins, mainly found in bacteria and plants. Members of this family form homodimers which bind DNA via a tweezer-like structure [ , , , ]. The conformation of the DNA is changed when bound to these proteins [ ]. In bacteria, these proteins may play a role in DNA replication-recovery fo... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM",
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"MF_00274",
"PF02575",
"PIRSF004555",
"PTHR33449",
"TIGR00103"
] | [
"DNA_YbaB_EbfC",
"YbaB_DNA_bd",
"UCP004555",
"",
"DNA_YbaB_EbfC"
] | [
20298,
30231,
20479,
21017,
20576
] | 5 | [] | [] | [] | 0 | [
"1j8b",
"1pug",
"1ybx",
"3f42",
"5yrx"
] | 5 | [
"PUB00026293",
"PUB00057452",
"PUB00057453",
"PUB00095231"
] | [
"12486730",
"19594923",
"19208644",
"22544270"
] | [
"Crystal structure of YbaB from Haemophilus influenzae (HI0442), a protein of unknown function coexpressed with the recombinational DNA repair protein RecR.",
"DNA-binding by Haemophilus influenzae and Escherichia coli YbaB, members of a widely-distributed bacterial protein family.",
"Borrelia burgdorferi EbfC ... | [
2003,
2009,
2009,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
28867,
1081,
378
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
2,
11
] | 4 | true | Family | Nucleoid-associated protein YbaB/EbfC | Nucleoid-associated protein YbaB/EbfC | YbaB/EbfC | 3 |
IPR004402 | 4,402 | Purine nucleoside phosphorylase DeoD-type | DeoD-type | Family | 9,169 | false | false | Purine nucleoside phosphorylase , also called inosine phosphorylase (pnp), catalyses the cleavage of the glycosidic bond of ribo- and deoxyribonucleosides in the presence of orthophospate [ ]. It is specific for guanosine, inosine and adenosine and cleavage results in formation of their respective bases and ribose phos... | [
"GO:0004731",
"GO:0006139"
] | [
"purine-nucleoside phosphorylase activity",
"nucleobase-containing compound metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_01627",
"TIGR00107",
"cd09006"
] | [
"Pur_nucleosid_phosp",
"deoD",
"PNP_EcPNPI-like"
] | [
8133,
9033,
9141
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.4.2.1",
"GenProp1235",
"GenProp1255",
"GenProp1278",
"GenProp1323",
"GenProp1469",
"GenProp1528",
"GenProp1741",
"GenProp1752",
"PWY-4202",
"PWY-5532",
"PWY-5695",
"PWY-6608",
"PWY-6609",
"PWY-6611",
"PWY-6620",
"PWY-6627",
"PWY-6644",
"PWY-7179",
"PWY-8440"
] | [
"EC:2.4.2.1",
"GP:GenProp1235",
"GP:GenProp1255",
"GP:GenProp1278",
"GP:GenProp1323",
"GP:GenProp1469",
"GP:GenProp1528",
"GP:GenProp1741",
"GP:GenProp1752",
"METACYC:PWY-4202",
"METACYC:PWY-5532",
"METACYC:PWY-5695",
"METACYC:PWY-6608",
"METACYC:PWY-6609",
"METACYC:PWY-6611",
"METACYC... | 20 | [
"1a69",
"1ecp",
"1k9s",
"1otx",
"1oty",
"1ou4",
"1oum",
"1ov6",
"1ovg",
"1pk7",
"1pk9",
"1pke",
"1pr0",
"1pr1",
"1pr2",
"1pr4",
"1pr5",
"1pr6",
"1pw7",
"1vhj",
"1vhw",
"1xe3",
"1z33",
"1z34",
"1z35",
"1z36",
"1z37",
"1z38",
"1z39",
"2ac7",
"2i4t",
"2isc"... | 104 | [
"PUB00053833"
] | [
"11337031"
] | [
"Purine nucleoside phosphorylases: properties, functions, and clinical aspects."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
9075,
39,
55
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
1
] | 2 | true | Family | Purine nucleoside phosphorylase DeoD-type | Purine nucleoside phosphorylase DeoD-type | DeoD-type | 2 |
IPR004403 | 4,403 | Peptide chain release factor eRF1/aRF1 | Peptide_chain-rel_eRF1/aRF1 | Family | 7,781 | false | false | This entry represents the eRF1 and aRF1 proteins. Terminating protein synthesis on the ribosome requires the presence of a class I polypeptide chain release factor (RF) to induce peptidyl-tRNA hydrolysis. Bacteria possess two class I RFs; RF1 which recognises UAG and UAA, and RF2 which recognises UGA and UAA. Mitochond... | [
"GO:0003747",
"GO:0006415"
] | [
"translation release factor activity",
"translational termination"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR10113",
"TIGR03676"
] | [
"",
"aRF1_eRF1"
] | [
7771,
6623
] | 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-72764",
"R-BTA-9629569",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-72764",
"R-CEL-9629569",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-72764",
"R-DDI-975956",
"R-DDI-975957",
"R-DME-72764",
"R-DME-9629569",
"R-DME-975956",
"R-DME-975957",
"R-HSA-72764",
"R-HSA-9010553",
"R-HSA-9629... | [
"REACTOME:R-BTA-72764",
"REACTOME:R-BTA-9629569",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-72764",
"REACTOME:R-CEL-9629569",
"REACTOME:R-CEL-975956",
"REACTOME:R-CEL-975957",
"REACTOME:R-DDI-72764",
"REACTOME:R-DDI-975956",
"REACTOME:R-DDI-975957",
"REACTOME:R-DME-7276... | 36 | [
"1dt9",
"2hst",
"2ktu",
"2ktv",
"2lgt",
"2llx",
"2mq6",
"2mq9",
"3agk",
"3e1y",
"3e20",
"3ir9",
"3j5y",
"3jag",
"3jah",
"3jai",
"3vmf",
"4af1",
"4crm",
"4crn",
"4d5n",
"4d61",
"5a8l",
"5dmq",
"5dmr",
"5lzt",
"5lzu",
"5lzv",
"6d90",
"6hcf",
"6hcm",
"6ip8"... | 42 | [
"PUB00053182",
"PUB00053183",
"PUB00053184"
] | [
"9179839",
"10788613",
"10471834"
] | [
"Polypeptide chain release factors.",
"Translation termination factor aRF1 from the archaeon Methanococcus jannaschii is active with eukaryotic ribosomes.",
"Polypeptide release factor eRF1 from Tetrahymena thermophila: cDNA cloning, purification and complex formation with yeast eRF3."
] | [
1997,
2000,
1999
] | 3 | [] | [
"IPR020918"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
1074,
48,
6539,
43,
77
] | 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... | [
8,
1,
4,
4,
5,
6,
1,
10,
2,
1,
1,
13
] | 12 | true | Family | Peptide chain release factor eRF1/aRF1 | Peptide chain release factor eRF1/aRF1 | Peptide_chain-rel_eRF1/aRF1 | 2 |
IPR004404 | 4,404 | Dihydroxy-acid dehydratase | DihydroxyA_deHydtase | Family | 29,986 | false | false | Two dehydratases, dihydroxy-acid dehydratase (gene ilvD or ILV3) and 6-phosphogluconate dehydratase (gene edd) have been shown to be evolutionary related [ ]. Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-k... | [
"GO:0004160",
"GO:0009082"
] | [
"dihydroxy-acid dehydratase activity",
"branched-chain amino acid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00012",
"TIGR00110"
] | [
"IlvD",
"ilvD"
] | [
28495,
29605
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.2.1.9",
"GenProp0162",
"GenProp0163",
"GenProp0164",
"GenProp1342",
"GenProp1405",
"PWY-5101",
"PWY-5103",
"PWY-5104",
"PWY-7111"
] | [
"EC:4.2.1.9",
"GP:GenProp0162",
"GP:GenProp0163",
"GP:GenProp0164",
"GP:GenProp1342",
"GP:GenProp1405",
"METACYC:PWY-5101",
"METACYC:PWY-5103",
"METACYC:PWY-5104",
"METACYC:PWY-7111"
] | 10 | [
"5ym0",
"5ze4",
"6nte",
"6ovt",
"8hs0",
"8ikz",
"8imu",
"9ix7",
"9jpi",
"9jsq",
"9l8r"
] | 11 | [
"PUB00001841",
"PUB00002191"
] | [
"8299945",
"1624451"
] | [
"Cloning of the dihydroxyacid dehydratase-encoding gene (ILV3) from Saccharomyces cerevisiae.",
"Molecular characterization of the Entner-Doudoroff pathway in Escherichia coli: sequence analysis and localization of promoters for the edd-eda operon."
] | [
1993,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
825,
25116,
3663,
382
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
3,
1,
2,
2,
1,
1,
7
] | 7 | true | Family | Dihydroxy-acid dehydratase | Dihydroxy-acid dehydratase | DihydroxyA_deHydtase | 9 |
IPR004405 | 4,405 | Pelota | TF_pelota | Family | 6,155 | false | false | Pelota (known as DOM34 in yeast) is a conserved protein in eukaryotes and archaea [ ] that binds Hbs1, a GTPase related to the EF1-alpha subfamily, and plays a central role in mRNA surveillance during protein synthesis [ ]. It is involved in the No-Go Decay (NGD) and Non-Stop Decay (NSD) pathways, which target mRNAs wh... | [
"GO:0070481",
"GO:0070966",
"GO:0071025"
] | [
"nuclear-transcribed mRNA catabolic process, non-stop decay",
"nuclear-transcribed mRNA catabolic process, no-go decay",
"RNA surveillance"
] | [
"biological_process",
"biological_process",
"biological_process"
] | 3 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR10853",
"TIGR00111"
] | [
"",
"pelota"
] | [
6115,
4825
] | 2 | [] | [] | [] | 0 | [
"1x52",
"2qi2",
"2vgm",
"2vgn",
"3izq",
"3j15",
"3j16",
"3mca",
"3obw",
"3oby",
"3wxm",
"5eo3",
"5lzw",
"5lzx",
"5lzy",
"5lzz",
"5m1j",
"6ji2"
] | 18 | [
"PUB00049007",
"PUB00058728",
"PUB00070080",
"PUB00070081",
"PUB00070083",
"PUB00161397",
"PUB00161398",
"PUB00161399"
] | [
"17889667",
"20682285",
"21448132",
"18022361",
"20974926",
"22358840",
"20890290",
"31611569"
] | [
"Structural and functional insights into Dom34, a key component of no-go mRNA decay.",
"Crystal structures of two archaeal Pelotas reveal inter-domain structural plasticity.",
"Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes.",
"RNA quality control in ... | [
2007,
2010,
2011,
2007,
2010,
2012,
2010,
2019
] | 8 | [] | [
"IPR023521"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Halorubrum virus BJ1",
"unclassified sequences"
] | [
923,
2,
5189,
1,
40
] | 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... | [
10,
1,
1,
1,
2,
2,
1,
5,
2,
2,
1,
4
] | 12 | true | Family | Pelota | Pelota | TF_pelota | 4 |
IPR004406 | 4,406 | Aconitase B | Aconitase_B | Family | 7,052 | false | false | This entry represents bacterial aconitase B (AcnB), which can switch between aconitase enzyme activity and post-translational gene regulation. An iron-mediated dimerisation mechanism may be responsible for switching AcnB between its catalytic and regulatory roles, as dimerisation requires iron while mRNA binding is inh... | [
"GO:0003994",
"GO:0051539",
"GO:0006099",
"GO:0005829"
] | [
"aconitate hydratase activity",
"4 iron, 4 sulfur cluster binding",
"tricarboxylic acid cycle",
"cytosol"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF036687",
"TIGR00117"
] | [
"AcnB",
"acnB"
] | [
6932,
7028
] | 2 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC"
] | [
"4.2.1.3",
"4.2.1.99",
"GenProp0033",
"GenProp1265",
"GenProp1267",
"GenProp1687",
"PWY-5747"
] | [
"EC:4.2.1.3",
"EC:4.2.1.99",
"GP:GenProp0033",
"GP:GenProp1265",
"GP:GenProp1267",
"GP:GenProp1687",
"METACYC:PWY-5747"
] | 7 | [
"1l5j"
] | 1 | [
"PUB00005471",
"PUB00036012",
"PUB00036013",
"PUB00036014",
"PUB00036015",
"PUB00036016",
"PUB00036017",
"PUB00036018",
"PUB00036019",
"PUB00036021"
] | [
"9020582",
"16850017",
"10087914",
"15877277",
"17513696",
"15882410",
"15009904",
"17185597",
"16407072",
"15604397"
] | [
"The aconitase family: three structural variations on a common theme.",
"The role of iron regulatory proteins in mammalian iron homeostasis and disease.",
"Moonlighting proteins.",
"Single-gene disorders: what role could moonlighting enzymes play?",
"Evolution of the iron-responsive element.",
"Switching ... | [
1997,
2006,
1999,
2005,
2007,
2005,
2004,
2006,
2006,
2004
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcinales",
"metagenomes"
] | [
6908,
85,
8,
51
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Aconitase B | Aconitase B | Aconitase_B | 9 |
IPR004408 | 4,408 | Biotin--acetyl-CoA-carboxylase ligase | Biotin_CoA_COase_ligase | Family | 30,093 | false | false | The biotin operon of Escherichia coli contains 5 structural genes involved in the synthesis of biotin. Transcription of the operon is regulated via one of these proteins, the biotin ligase BirA. BirA is an asymetric protein with 3 specific domains -an N-terminal DNA-binding domain, a central catalytic domain and a C-te... | [
"GO:0004077",
"GO:0036211"
] | [
"biotin--[biotin carboxyl-carrier protein] ligase activity",
"protein modification process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM",
"CDD"
] | [
"TIGR00121",
"cd16442"
] | [
"birA_ligase",
"BPL"
] | [
29338,
27904
] | 2 | [
"EC",
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.4",
"6.3.4.15",
"GenProp0036",
"R-HSA-196780",
"R-HSA-3371599",
"R-MMU-196780",
"R-SCE-196780",
"R-SPO-196780"
] | [
"EC:6.3.4",
"EC:6.3.4.15",
"GP:GenProp0036",
"REACTOME:R-HSA-196780",
"REACTOME:R-HSA-3371599",
"REACTOME:R-MMU-196780",
"REACTOME:R-SCE-196780",
"REACTOME:R-SPO-196780"
] | 8 | [
"1bia",
"1bib",
"1hxd",
"1wnl",
"1wpy",
"1wq7",
"1wqw",
"1x01",
"2cgh",
"2deq",
"2djz",
"2dkg",
"2dth",
"2dti",
"2dto",
"2dve",
"2dxt",
"2dxu",
"2dz9",
"2dzc",
"2e10",
"2e1h",
"2e41",
"2e64",
"2e65",
"2eay",
"2ej9",
"2ejf",
"2ejg",
"2ewn",
"2fyk",
"2hni"... | 77 | [
"PUB00005496"
] | [
"10470036"
] | [
"The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity."
] | [
1999
] | 1 | [] | [
"IPR030855"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
848,
24542,
4118,
585
] | 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",... | [
19,
3,
2,
4,
1,
3,
4,
1,
3,
5,
1,
1,
2
] | 13 | true | Family | Biotin--acetyl-CoA-carboxylase ligase | Biotin--acetyl-CoA-carboxylase ligase | Biotin_CoA_COase_ligase | 6 |
IPR004409 | 4,409 | Biotin operon repressor, helix-turn-helix domain | Biotin_operon_repress_HTH | Domain | 1,520 | false | false | The biotin operon of Escherichia coli contains 5 structural genes involved in the synthesis of biotin. Transcription of the operon is regulated via one of these proteins, BirA. BirA is an asymetric protein with 3 specific domains. The ligase reaction intermediate, biotinyl-5'-AMP, is the co-repressor that triggers DNA ... | [
"GO:0006355"
] | [
"regulation of DNA-templated transcription"
] | [
"biological_process"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00122"
] | [
"birA_repr_reg"
] | [
1520
] | 1 | [
"EC",
"GP"
] | [
"6.3.4.15",
"GenProp0036"
] | [
"EC:6.3.4.15",
"GP:GenProp0036"
] | 2 | [
"1bia",
"1bib",
"1hxd",
"2ewn",
"4wf2",
"8f8u",
"8fi3",
"9j8e",
"9j8f"
] | 9 | [
"PUB00005496"
] | [
"10470036"
] | [
"The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Archaeoglobus fulgidus",
"Bacteria",
"ecological metagenomes"
] | [
4,
1513,
3
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Biotin operon repressor, helix-turn-helix domain | Biotin operon repressor, helix-turn-helix domain | Biotin_operon_repress_HTH | 9 |
IPR004410 | 4,410 | Malonyl CoA-acyl carrier protein transacylase, FabD-type | Malonyl_CoA-ACP_transAc_FabD | Family | 20,826 | false | false | Malonyl CoA-acyl carrier protein transacylases transfer the malonyl moiety from coenzyme A to acyl-carrier protein. This entry represents the FabD-type enzymes, which include the fatty acid biosynthesis protein FabD and the antibiotic biosynthesis proteins PksC, PksE, BaeE/C and ThaF [ , , , ]. | [
"GO:0004314"
] | [
"[acyl-carrier-protein] S-malonyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00128"
] | [
"fabD"
] | [
20826
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.1.39",
"GenProp0681",
"GenProp1415",
"GenProp1512",
"PWY-4381",
"PWY-6799",
"PWY-8012",
"PWY-8047",
"PWY-8049",
"PWY-8438"
] | [
"EC:2.3.1.39",
"GP:GenProp0681",
"GP:GenProp1415",
"GP:GenProp1512",
"METACYC:PWY-4381",
"METACYC:PWY-6799",
"METACYC:PWY-8012",
"METACYC:PWY-8047",
"METACYC:PWY-8049",
"METACYC:PWY-8438"
] | 10 | [
"1mla",
"2cuy",
"2g1h",
"2g2o",
"2g2y",
"2g2z",
"2h1y",
"3ezo",
"3g87",
"3h0p",
"3hjv",
"3im8",
"3im9",
"3k89",
"3ptw",
"3qat",
"3r97",
"3rgi",
"3sbm",
"3tqe",
"4rr5",
"5dz6",
"5dz7",
"5ypv",
"5zk4",
"6apf",
"6apg",
"6apk",
"6mhp",
"6smd",
"6u0j"
] | 31 | [
"PUB00056817",
"PUB00056818",
"PUB00097880",
"PUB00097881"
] | [
"1314802",
"16757561",
"20853892",
"17234808"
] | [
"Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase.",
"Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-S-carrier proteins in the pksX pathway of Bacillus subtilis.",
"Induced biosynthesis of cryp... | [
1992,
2006,
2010,
2007
] | 4 | [
"IPR024925"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
19773,
772,
281
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
5,
1,
3,
3
] | 4 | true | Family | Malonyl CoA-acyl carrier protein transacylase, FabD-type | Malonyl CoA-acyl carrier protein transacylase, FabD-type | Malonyl_CoA-ACP_transAc_FabD | 5 |
IPR004411 | 4,411 | Peptidase A31, coenzyme F420-reducing hydrogenase delta subunit | Pept_A31_F420-red_hyd_d | Family | 244 | false | false | This group of sequences are classed as unassigned endopeptidases belonging to the MEROPS peptidase family A31 (HybD endopeptidase family, clan AE). The sequences in this family represent the delta subunit, FrhD, of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase, otherwise known as coenzyme F420-redu... | [
"GO:0008233",
"GO:0036211"
] | [
"peptidase activity",
"protein modification process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM",
"CDD"
] | [
"TIGR00130",
"cd06064"
] | [
"frhD",
"H2MP_F420-Reduc"
] | [
229,
205
] | 2 | [
"GP"
] | [
"GenProp0723"
] | [
"GP:GenProp0723"
] | 1 | [] | 0 | [
"PUB00009571"
] | [
"2207102"
] | [
"Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H."
] | [
1990
] | 1 | [
"IPR000671"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanobacteriota",
"ecological metagenomes"
] | [
14,
225,
5
] | 3 | [] | [] | 0 | true | Family | Peptidase A31, coenzyme F420-reducing hydrogenase delta subunit | Peptidase A31, coenzyme F420-reducing hydrogenase delta subunit | Pept_A31_F420-red_hyd_d | 2 |
IPR004412 | 4,412 | Glutamyl-tRNA(Gln) amidotransferase A subunit | GatA | Family | 25,506 | false | false | In many species, Gln-tRNA ligase is missing. tRNA(Gln) is misacylated with Glu after which a heterotrimeric amidotransferase converts Glu to Gln. This group represents the amidase chain of the heterotrimer, encoded by the gatA gene called glutamyl-tRNA(Gln) amidotransferase, A subunit . This enzyme functions as an alte... | [
"GO:0050567",
"GO:0006412",
"GO:0030956"
] | [
"glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity",
"translation",
"glutamyl-tRNA(Gln) amidotransferase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00120",
"TIGR00132"
] | [
"GatA",
"gatA"
] | [
25503,
22545
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP"
] | [
"6.3.5.7",
"GenProp0188",
"GenProp0258",
"GenProp1383",
"GenProp1660"
] | [
"EC:6.3.5.7",
"GP:GenProp0188",
"GP:GenProp0258",
"GP:GenProp1383",
"GP:GenProp1660"
] | 5 | [
"2df4",
"2dqn",
"2f2a",
"2g5h",
"2g5i",
"2gi3",
"3al0",
"3h0l",
"3h0m",
"3h0r",
"3ip4",
"3kfu",
"4n0h",
"4n0i",
"4wj3"
] | 15 | [
"PUB00035563",
"PUB00035564",
"PUB00035565",
"PUB00035566"
] | [
"15595822",
"17015445",
"12032064",
"12521300"
] | [
"Probing the Ser-Ser-Lys catalytic triad mechanism of peptide amidase: computational studies of the ground state, transition state, and intermediate.",
"A second fatty acid amide hydrolase with variable distribution among placental mammals.",
"Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalyti... | [
2004,
2006,
2002,
2002
] | 4 | [
"IPR000120"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
730,
20471,
3920,
385
] | 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... | [
4,
2,
2,
2,
2,
1,
1,
2,
3,
1,
1,
6
] | 12 | true | Family | Glutamyl-tRNA(Gln) amidotransferase A subunit | Glutamyl-tRNA(Gln) amidotransferase A subunit | GatA | 9 |
IPR004413 | 4,413 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | GatB | Family | 26,246 | false | false | This entry represents the B subunit of aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase. Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase ([ec:6.3.5.-]) allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which la... | [
"GO:0016884"
] | [
"carbon-nitrogen ligase activity, with glutamine as amido-N-donor"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00121",
"TIGR00133"
] | [
"GatB",
"gatB"
] | [
25869,
25915
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"6.3.5.-",
"GenProp0188",
"GenProp0258",
"GenProp1383",
"GenProp1660",
"PWY-5297",
"PWY-7811",
"PWY-8229",
"PDOC00948"
] | [
"EC:6.3.5.-",
"GP:GenProp0188",
"GP:GenProp0258",
"GP:GenProp1383",
"GP:GenProp1660",
"METACYC:PWY-5297",
"METACYC:PWY-7811",
"METACYC:PWY-8229",
"PROSITEDOC:PDOC00948"
] | 9 | [
"2df4",
"2dqn",
"2f2a",
"2g5h",
"2g5i",
"3al0",
"3h0l",
"3h0m",
"3h0r",
"3ip4",
"3kfu",
"4n0h",
"4n0i",
"4wj3"
] | 14 | [
"PUB00007932"
] | [
"9342321"
] | [
"Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation."
] | [
1997
] | 1 | [
"IPR017959"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
768,
20709,
4360,
409
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
3,
1,
1,
2,
3,
3,
1,
2,
5,
1,
1,
4
] | 12 | true | Family | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | GatB | 5 |
IPR004414 | 4,414 | Glutamyl-tRNA(Gln) amidotransferase subunit E | GatE | Family | 1,028 | false | false | Glutamyl-tRNA(Gln) amidotransferase, subunit E (GatE) is found only in the Archaea. It is part of a heterodimer, with GatD ( ), that acts as an amidotransferase on misacylated Glu-tRNA(Gln) to produce Gln-tRNA(Gln) [ ]. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu... | [
"GO:0016884"
] | [
"carbon-nitrogen ligase activity, with glutamine as amido-N-donor"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00588",
"TIGR00134"
] | [
"GatE",
"gatE_arch"
] | [
997,
1010
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"6.3.5.-",
"GenProp0258",
"PWY-5297",
"PWY-7811",
"PWY-8229"
] | [
"EC:6.3.5.-",
"GP:GenProp0258",
"METACYC:PWY-5297",
"METACYC:PWY-7811",
"METACYC:PWY-8229"
] | 5 | [
"1zq1",
"2d6f"
] | 2 | [
"PUB00015320",
"PUB00040197",
"PUB00100077"
] | [
"10993083",
"16809540",
"20457752"
] | [
"Domain-specific recruitment of amide amino acids for protein synthesis.",
"Structural basis of RNA-dependent recruitment of glutamine to the genetic code.",
"The archaeal transamidosome for RNA-dependent glutamine biosynthesis."
] | [
2000,
2006,
2010
] | 3 | [
"IPR017959"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
965,
38,
25
] | 3 | [] | [] | 0 | true | Family | Glutamyl-tRNA(Gln) amidotransferase subunit E | Glutamyl-tRNA(Gln) amidotransferase subunit E | GatE | 3 |
IPR004416 | 4,416 | tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG | MnmG | Family | 24,305 | false | false | tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG (also known as GidA) is a tRNA modification enzyme found in bacteria and mitochondria. MnmG forms a complex with MnmE which is involved in the formation of methyluridine derivatives at the wobble uridine base in some tRNAs [ , , ]. Sequence variations in ... | [
"GO:0002098"
] | [
"tRNA wobble uridine modification"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00129",
"TIGR00136"
] | [
"MnmG_GidA",
"mnmG_gidA"
] | [
22822,
24197
] | 2 | [
"GP",
"GP"
] | [
"GenProp0704",
"GenProp1555"
] | [
"GP:GenProp0704",
"GP:GenProp1555"
] | 2 | [
"2zxh",
"2zxi",
"3ces",
"3cp2",
"3cp8",
"3g05",
"8zu0",
"9hip",
"9hiq",
"9hir"
] | 10 | [
"PUB00043571",
"PUB00043572",
"PUB00043573",
"PUB00090565"
] | [
"15509579",
"11544186",
"15542390",
"19767610"
] | [
"Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases.",
"Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift.",
"Phenotype of non-syndro... | [
2005,
2001,
2004,
2009
] | 4 | [
"IPR002218"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Candidatus Methanofastidiosum methylothiophilum",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
20286,
1,
3758,
1,
259
] | 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",... | [
6,
1,
8,
1,
1,
10,
2,
1,
3,
2,
1,
1,
6
] | 13 | true | Family | tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG | tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG | MnmG | 1 |
IPR004417 | 4,417 | Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO | TrmFO | Family | 7,271 | false | false | Proteins in this entry catalyse the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. They are closely related to GidA (glucose-inhibited division protein A, also known as MnmG), a protein involved in tRNA modification [ , ] in bacteria and mitochondria. | [
"GO:0047151",
"GO:0050660",
"GO:0008033",
"GO:0005737"
] | [
"tRNA (uracil(54)-C5)-methyltransferase activity, 5,10-methylenetetrahydrofolate-dependent",
"flavin adenine dinucleotide binding",
"tRNA processing",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01037",
"TIGR00137"
] | [
"TrmFO",
"gid_trmFO"
] | [
7247,
7196
] | 2 | [
"EC"
] | [
"2.1.1.74"
] | [
"EC:2.1.1.74"
] | 1 | [
"3g5q",
"3g5r",
"3g5s"
] | 3 | [
"PUB00043571",
"PUB00043572"
] | [
"15509579",
"11544186"
] | [
"Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases.",
"Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift."
] | [
2005,
2001
] | 2 | [
"IPR002218"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Metazoa",
"metagenomes"
] | [
7206,
6,
59
] | 3 | [] | [] | 0 | true | Family | Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO | Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO | TrmFO | 3 |
IPR004418 | 4,418 | Homoaconitase, mitochondrial | Homoaconitase_mito | Family | 1,761 | false | false | Homoaconitase (cis-homoaconitase; ) catalyses the dehydration of cis-homoaconitate to homoisocitric acid. It is an enzyme from the alpha-aminoadipate pathway of lysine biosynthesis, and has been identified in higher fungi and several archaea and one thermophilic species of bacteria, Thermus thermophilus [ ]. Like aconi... | [
"GO:0004409",
"GO:0051539",
"GO:0009085"
] | [
"homoaconitate hydratase activity",
"4 iron, 4 sulfur cluster binding",
"L-lysine biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00139"
] | [
"h_aconitase"
] | [
1761
] | 1 | [
"EC",
"METACYC"
] | [
"4.2.1.36",
"PWY-3081"
] | [
"EC:4.2.1.36",
"METACYC:PWY-3081"
] | 2 | [] | 0 | [
"PUB00036023",
"PUB00036024"
] | [
"16524361",
"9541534"
] | [
"Kinetics and product analysis of the reaction catalysed by recombinant homoaconitase from Thermus thermophilus.",
"A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms."
] | [
2006,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
18,
1739,
4
] | 3 | [
"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,
2
] | 3 | true | Family | Homoaconitase, mitochondrial | Homoaconitase, mitochondrial | Homoaconitase_mito | 1 |
IPR004419 | 4,419 | Peptidase A31, hydrogenase expression/formation protein | Pept_A31_hyd_express | Family | 2,999 | false | false | This family of peptidases consists of hydrogenase expression/formation proteins, such as HoxM from Cupriavidus necator (also known as Alcaligenes eutrophus) and HybD from E. coli. They belong to the MEROPS peptidase family A31. Nickel/iron hydrogenases are synthesized as two subunits, with the larger subunit containing... | [
"GO:0046872",
"GO:0016485"
] | [
"metal ion binding",
"protein processing"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR00140"
] | [
"hupD"
] | [
2999
] | 1 | [] | [] | [] | 0 | [
"1cfz",
"2kml"
] | 2 | [
"PUB00011020",
"PUB00011022",
"PUB00011023",
"PUB00011024"
] | [
"10727938",
"10795682",
"10331925",
"8405419"
] | [
"Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation.",
"Analysis of the cleavage site specificity of the endopeptidase involved in the maturation of the large subunit of hydrogenase 3 from Escherichia coli.",
"Crystal structure of the hydrogenase maturating e... | [
2000,
2000,
1999,
1993
] | 4 | [
"IPR000671"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"ecological metagenomes"
] | [
2976,
23
] | 2 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | Peptidase A31, hydrogenase expression/formation protein | Peptidase A31, hydrogenase expression/formation protein | Pept_A31_hyd_express | 4 |
IPR004420 | 4,420 | Peptidase A31, hydrogenase maturation protease HycI | Pept_A31_hyd_mat_HycI | Family | 1,638 | false | false | This group of metallopeptidases belong to the MEROPS peptidase family A31 (HybD endopeptidase family, clan AE). The family contains the HycI endopeptidases and their homologues. Hydrogenase 3 maturation protease (HycI) is a protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3 [ , ]... | [
"GO:0008233"
] | [
"peptidase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM",
"CDD"
] | [
"TIGR00142",
"cd06067"
] | [
"hycI",
"H2MP_MemB-H2evol"
] | [
1474,
1630
] | 2 | [] | [] | [] | 0 | [
"2e85",
"2i8l",
"3pu6",
"5zby"
] | 4 | [
"PUB00001457",
"PUB00011088"
] | [
"7851435",
"8756471"
] | [
"Characterisation of a protease from Escherichia coli involved in hydrogenase maturation.",
"Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form."
] | [
1995,
1996
] | 2 | [
"IPR000671"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Beauveria bassiana D1-5",
"unclassified sequences"
] | [
176,
1439,
1,
22
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Peptidase A31, hydrogenase maturation protease HycI | Peptidase A31, hydrogenase maturation protease HycI | Pept_A31_hyd_mat_HycI | 6 |
IPR004421 | 4,421 | Carbamoyltransferase, HypF-type | Carbamoyltransferase_HypF | Family | 7,337 | false | false | The large subunit of [NiFe]-hydrogenase, as well as other nickel metalloenzymes, is synthesized as a precursor devoid of the metalloenzyme active site. This precursor then undergoes a complex post-translational maturation process that requires a number of accessory proteins [ , , ]. Members of the HypF family are acces... | [
"GO:0016743",
"GO:0046872",
"GO:0046944"
] | [
"carboxyl- or carbamoyltransferase activity",
"metal ion binding",
"protein carbamoylation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF006256",
"TIGR00143"
] | [
"CMPcnvr_hdrg_mat",
"hypF"
] | [
7047,
7239
] | 2 | [] | [] | [] | 0 | [
"3tsp",
"3tsq",
"3tsu",
"3ttc",
"3ttd",
"3ttf",
"3vth",
"3vti",
"4g9i"
] | 9 | [
"PUB00006430",
"PUB00011083",
"PUB00011084",
"PUB00011085",
"PUB00011086",
"PUB00013568",
"PUB00013569",
"PUB00014601"
] | [
"10368269",
"11163786",
"12377778",
"12206761",
"11206077",
"11336840",
"12196162",
"10226043"
] | [
"Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center.",
"Carbamoylphosphate requirement for synthesis of the active center of [NiFe]-hydrogenases.",
"HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation."... | [
1999,
2001,
2002,
2002,
2000,
2001,
2002,
1999
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
400,
6863,
4,
70
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Carbamoyltransferase, HypF-type | Carbamoyltransferase, HypF-type | Carbamoyltransferase_HypF | 3 |
IPR004422 | 4,422 | Beta-ribofuranosylphenol 5'-phosphate synthase | RFAP_synthase | Family | 1,570 | false | false | This protein family includes Beta-ribofuranosylphenol 5'-phosphate synthase (also known as beta-ribofuranosylaminobenzene 5'-phosphate synthase, RFAP synthase) from Methanocaldococcus jannaschii and other archaeal species and similar proteins predominantly found in Proteobacteria and Planctomycetes. RFAP synthase is an... | [] | [] | [] | 0 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF004884",
"TIGR00144"
] | [
"Sugar_kin_arch",
"beta_RFAP_syn"
] | [
1493,
1437
] | 2 | [
"EC",
"METACYC"
] | [
"2.4.2.54",
"PWY-6148"
] | [
"EC:2.4.2.54",
"METACYC:PWY-6148"
] | 2 | [
"6yqq",
"8aoz",
"8ap0"
] | 3 | [
"PUB00015321",
"PUB00100271"
] | [
"12142414",
"21634403"
] | [
"Purification, overproduction, and partial characterization of beta-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway.",
"The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-D-ribitol moiety in methanopterin."
] | [
2002,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Geodia barretti",
"ecological metagenomes"
] | [
791,
753,
1,
25
] | 4 | [] | [] | 0 | true | Family | Beta-ribofuranosylphenol 5'-phosphate synthase | Beta-ribofuranosylphenol 5'-phosphate synthase | RFAP_synthase | 6 |
IPR004424 | 4,424 | 4-diphosphocytidyl-2C-methyl-D-erythritol kinase | IspE | Family | 23,556 | false | false | 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is a member of the family of GHMP kinases that were previously designated as conserved hypothetical protein YchB or as isopentenyl monophosphate kinase. In Solanum lycopersicum (Tomato) (Lycopersicon esculentum) and Escherichia coli the protein has been indentified as 4-... | [
"GO:0050515",
"GO:0016114"
] | [
"4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity",
"terpenoid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PIRSF",
"NCBIFAM"
] | [
"MF_00061",
"PIRSF010376",
"TIGR00154"
] | [
"IspE",
"IspE",
"ispE"
] | [
23178,
22311,
21797
] | 3 | [
"EC",
"GP",
"GP",
"METACYC"
] | [
"2.7.1.148",
"GenProp0048",
"GenProp1295",
"PWY-7560"
] | [
"EC:2.7.1.148",
"GP:GenProp0048",
"GP:GenProp1295",
"METACYC:PWY-7560"
] | 4 | [
"1oj4",
"1uek",
"2v2q",
"2v2v",
"2v2z",
"2v34",
"2v8p",
"2vf3",
"2ww4",
"3pyd",
"3pye",
"3pyf",
"3pyg",
"4dxl",
"4ed4",
"4emd",
"8ckh",
"8qc7",
"8qcc",
"8qcn",
"8qco"
] | 21 | [
"PUB00015669",
"PUB00015929",
"PUB00095232"
] | [
"12771135",
"10655484",
"18236010"
] | [
"Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis.",
"Biosynthesis of terpenoids: YchB protein of Escherichia coli phosphorylates the 2-hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.",
"Chloroplast localiz... | [
2003,
2000,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3,
22186,
889,
478
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
2,
1,
1,
5
] | 4 | true | Family | 4-diphosphocytidyl-2C-methyl-D-erythritol kinase | 4-diphosphocytidyl-2C-methyl-D-erythritol kinase | IspE | 4 |
IPR004425 | 4,425 | Proteasome assembly chaperone MJ0106-like | MJ0106-like | Family | 240 | false | false | This family represents one out of two closely related orthologous sets of proteins that, so far, are found only archaea. This orthologue set includes MJ0106 from Methanococcus jannaschii and AF1251 from Archaeoglobus fulgidus, but not MJ1210 or AF0525 (which are represented in . Members of this entry belong to the prot... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00161"
] | [
""
] | [
240
] | 1 | [] | [] | [] | 0 | [
"3wz2",
"5y9n"
] | 2 | [] | [] | [] | [] | 0 | [
"IPR019151"
] | [] | 1 | 0 | 1 | [
"Archaea",
"ecological metagenomes"
] | [
236,
4
] | 2 | [] | [] | 0 | true | Family | Proteasome assembly chaperone MJ0106-like | Proteasome assembly chaperone MJ0106-like | MJ0106-like | 5 |
IPR004426 | 4,426 | Proteasome assembly chaperone MJ1210-like | MJ1210-like | Family | 655 | false | false | This family represents one out of two closely related orthologous sets of proteins that, so far, are found only in but, are universal among, the Archaea. This orthologue set includes MJ1210 from Methanocaldococcus jannaschii (Methanococcus jannaschii) and AF0525 from Archaeoglobus fulgidus, but not MJ0106 or AF1251 (wh... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00162"
] | [
""
] | [
655
] | 1 | [] | [] | [] | 0 | [
"3vr0"
] | 1 | [] | [] | [] | [] | 0 | [
"IPR019151"
] | [] | 1 | 0 | 1 | [
"Archaea",
"ecological metagenomes"
] | [
643,
12
] | 2 | [] | [] | 0 | true | Family | Proteasome assembly chaperone MJ1210-like | Proteasome assembly chaperone MJ1210-like | MJ1210-like | 3 |
IPR004429 | 4,429 | Isopropylmalate dehydrogenase | Isopropylmalate_DH | Family | 22,233 | false | false | Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the dimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologues. These enzymes dehydrogenate their substates at a H-C-OH si... | [
"GO:0003862",
"GO:0009098"
] | [
"3-isopropylmalate dehydrogenase activity",
"L-leucine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_01033",
"PTHR42979",
"TIGR00169"
] | [
"LeuB_type1",
"",
"leuB"
] | [
17712,
22208,
20776
] | 3 | [
"EC",
"GP",
"METACYC"
] | [
"1.1.1.85",
"GenProp0164",
"PWY-7396"
] | [
"EC:1.1.1.85",
"GP:GenProp0164",
"METACYC:PWY-7396"
] | 3 | [
"1a05",
"1cm7",
"1cnz",
"1dpz",
"1dr0",
"1dr8",
"1g2u",
"1gc8",
"1gc9",
"1hex",
"1idm",
"1ipd",
"1osi",
"1osj",
"1v53",
"1v5b",
"1vlc",
"1wal",
"1xaa",
"1xab",
"1xac",
"1xad",
"2ayq",
"2y3z",
"2y40",
"2y41",
"2y42",
"2ztw",
"3r8w",
"3u1h",
"3udo",
"3udu"... | 53 | [
"PUB00032144",
"PUB00089640"
] | [
"15663922",
"27705900"
] | [
"The high-resolution Structure of LeuB (Rv2995c) from Mycobacterium tuberculosis.",
"Structural diversity in echinocandin biosynthesis: the impact of oxidation steps and approaches toward an evolutionary explanation."
] | [
2005,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Myoviridae sp. cta6i12",
"unclassified sequences"
] | [
13,
18075,
3759,
1,
385
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
20,
1,
1,
7,
1,
1,
8
] | 7 | true | Family | Isopropylmalate dehydrogenase | Isopropylmalate dehydrogenase | Isopropylmalate_DH | 8 |
IPR004430 | 4,430 | 3-isopropylmalate dehydratase, large subunit | 3-IsopropMal_deHydase_lsu | Family | 24,151 | false | false | 3-isopropylmalate dehydratase (or isopropylmalate isomerase; ) catalyses the stereo-specific isomerisation of 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. This enzyme performs the second step in the biosynthesis of leucine, and is present in most prokaryotes and many fungal species.... | [
"GO:0003861",
"GO:0051539",
"GO:0009098"
] | [
"3-isopropylmalate dehydratase activity",
"4 iron, 4 sulfur cluster binding",
"L-leucine biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM",
"NCBIFAM"
] | [
"MF_01026",
"NF009116",
"TIGR00170"
] | [
"LeuC_type1",
"PRK12466.1",
"leuC"
] | [
22834,
24110,
23874
] | 3 | [
"EC",
"GP"
] | [
"4.2.1.33",
"GenProp0164"
] | [
"EC:4.2.1.33",
"GP:GenProp0164"
] | 2 | [] | 0 | [
"PUB00005471",
"PUB00016210",
"PUB00032014",
"PUB00033924",
"PUB00036023",
"PUB00082326"
] | [
"9020582",
"9813279",
"15522288",
"1400210",
"16524361",
"20663849"
] | [
"The aconitase family: three structural variations on a common theme.",
"The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus.",
"Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specifici... | [
1997,
1998,
2004,
1992,
2006,
2010
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
379,
21612,
1831,
329
] | 4 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1,
1
] | 4 | true | Family | 3-isopropylmalate dehydratase, large subunit | 3-isopropylmalate dehydratase, large subunit | 3-IsopropMal_deHydase_lsu | 9 |
IPR004431 | 4,431 | 3-isopropylmalate dehydratase, small subunit | 3-IsopropMal_deHydase_ssu | Family | 23,932 | false | false | This entry represents a region of the small subunit. The structure of the Pyrococcus horikoshii small subunit ( ) has recently been determined [ ]. As expected the structure of this polypeptide is similar to that of aconitase domain 4, though one α helix is replaced by a short loop with relatively high temperature fact... | [
"GO:0003861",
"GO:0009098",
"GO:0009316"
] | [
"3-isopropylmalate dehydratase activity",
"L-leucine biosynthetic process",
"3-isopropylmalate dehydratase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM",
"NCBIFAM"
] | [
"MF_01031",
"NF002458",
"TIGR00171"
] | [
"LeuD_type1",
"PRK01641.1",
"leuD"
] | [
20937,
23809,
23788
] | 3 | [
"EC",
"GP"
] | [
"4.2.1.33",
"GenProp0164"
] | [
"EC:4.2.1.33",
"GP:GenProp0164"
] | 2 | [
"2hcu",
"3h5e",
"3h5h",
"3h5j",
"3q3w"
] | 5 | [
"PUB00005471",
"PUB00016210",
"PUB00032014",
"PUB00033924",
"PUB00036023",
"PUB00082326"
] | [
"9020582",
"9813279",
"15522288",
"1400210",
"16524361",
"20663849"
] | [
"The aconitase family: three structural variations on a common theme.",
"The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus.",
"Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specifici... | [
1997,
1998,
2004,
1992,
2006,
2010
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
385,
21295,
1867,
385
] | 4 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1,
1
] | 4 | true | Family | 3-isopropylmalate dehydratase, small subunit | 3-isopropylmalate dehydratase, small subunit | 3-IsopropMal_deHydase_ssu | 8 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.