LiteFold/InterPro · Datasets at Hugging Face

IPR023582

23,582

Impact family

Impact

Family

25,213

false

The Impact protein is a translational regulator that ensures constant high levels of translation under amino acid starvation. It acts by interacting with Gcn1/Gcn1L1, thereby preventing activation of Gcn2 protein kinases (EIF2AK1 to 4) and subsequent down-regulation of protein synthesis. It is evolutionary conserved fr...

[]

0

[ "PANTHER" ]

[ "PTHR16301" ]

[ "" ]

[ 25213 ]

1

[ "REACTOME" ]

[ "R-HSA-9633012" ]

[ "REACTOME:R-HSA-9633012" ]

1

[ "1vi7", "2cve", "6bqi", "6u1l", "6u1o" ]

5

[ "PUB00046141" ]

[ "11116084" ]

[ "Comparative genome analysis of the mouse imprinted gene impact and its nonimprinted human homolog IMPACT: toward the structural basis for species-specific imprinting." ]

[ 2000 ]

1

[]

[ "IPR015796" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "Microviridae sp. ctNWS1", "unclassified sequences" ]

[ 492, 18477, 6103, 1, 140 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae ...

[ 7, 1, 12, 1, 5, 6, 2, 2, 6, 2, 2, 6 ]

12

true

Family

Impact family

Impact

3

IPR023584

23,584

Ribosome recycling factor domain

Ribosome_recyc_fac_dom

Domain

30,485

false

The ribosome recycling factor or ribosome release factor (RRF) dissociates ribosomes from mRNA after termination of translation, and is essential for bacterial growth [ ]. Thus ribosomes are 'recycled' and ready for another round of protein synthesis. This entry represents a domain found in ribosome recycling factors.

[]

0

[ "PFAM" ]

[ "PF01765" ]

[ "RRF" ]

[ 30485 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-CEL-5419276", "R-HSA-5419276", "R-MMU-5419276", "R-RNO-5419276" ]

[ "REACTOME:R-CEL-5419276", "REACTOME:R-HSA-5419276", "REACTOME:R-MMU-5419276", "REACTOME:R-RNO-5419276" ]

4

[ "1dd5", "1eh1", "1ek8", "1ge9", "1is1", "1ise", "1t1m", "1wih", "1wqf", "1wqg", "1wqh", "1y69", "1zn0", "1zn1", "2rdo", "3j0d", "3j0e", "3lf9", "3lhp", "4gfq", "4kaw", "4kb2", "4kb4", "4kc6", "4kdd", "4l8i", "4v54", "4v55", "4v5a", "4v5y", "4v9c", "4v9d"...

45

[ "PUB00004841" ]

[ "8183897" ]

[ "Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth." ]

[ 1994 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Myoviridae sp. ctj4n23", "Thermococcus litoralis", "unclassified sequences" ]

[ 24364, 5526, 1, 1, 593 ]

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",...

[ 8, 1, 2, 2, 1, 2, 1, 1, 4, 4, 1, 1, 19 ]

13

true

Domain

Ribosome recycling factor domain

Ribosome_recyc_fac_dom

8

IPR023585

23,585

Isoleucine-tRNA ligase, type 1

Ile-tRNA-ligase_type1

Family

18,081

false

Isoleucine-tRNA ligase (also known as Isoleucyl-tRNA synthetase)( ) is an alpha monomer that belongs to class Ia. The enzyme, isoleucine-tRNA ligase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the l...

[ "GO:0004822" ]

[ "isoleucine-tRNA ligase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_02002" ]

[ "Ile_tRNA_synth_type1" ]

[ 18081 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1.5", "R-DDI-9837999", "R-HSA-379726", "R-HSA-9837999", "R-MMU-9837999", "R-SPO-9837999" ]

[ "EC:6.1.1.5", "REACTOME:R-DDI-9837999", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-9837999", "REACTOME:R-SPO-9837999" ]

6

[ "1ffy", "1qu2", "1qu3", "8c9e", "8c9f", "8c9g", "8wnf", "8wng", "8wni", "8wnj", "8wo2", "8wo3" ]

12

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006404", "PUB00006454", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873", "PUB00080139" ]

[ "8364025", "8274143", "1852601", "2053131", "9554847", "10446055", "10673435", "2203971", "10447505", "10704480", "12458790", "7607232" ]

[ "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, 1998, 1999, 2000, 1990, 1999, 2000, 2002, 1995 ]

12

[ "IPR002301" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 15905, 2053, 123 ]

3

[ "Arabidopsis thaliana", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 6, 1, 1, 2, 1, 2, 1, 1, 5 ]

9

true

Family

Isoleucine-tRNA ligase, type 1

Ile-tRNA-ligase_type1

4

IPR023586

23,586

Isoleucine-tRNA ligase, type 2

Ile-tRNA-ligase_type2

Family

21,827

false

Isoleucine-tRNA ligase (also known as Isoleucyl-tRNA synthetase)( ) is an alpha monomer that belongs to class Ia. The enzyme, isoleucine-tRNA ligase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the l...

[ "GO:0004822" ]

[ "isoleucine-tRNA ligase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "PANTHER" ]

[ "MF_02003", "PTHR42780" ]

[ "Ile_tRNA_synth_type2", "" ]

[ 15025, 21814 ]

2

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1.5", "R-DDI-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-9856649", "R-MMU-9856649" ]

[ "EC:6.1.1.5", "REACTOME:R-DDI-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649" ]

6

[ "1ile", "1jzq", "1jzs", "6ldk", "7d5c", "7wrs", "8c8u", "8c8v", "8c8w", "8c9d", "8wnd", "8z1p" ]

12

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006404", "PUB00006454", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873", "PUB00080139" ]

[ "8364025", "8274143", "1852601", "2053131", "9554847", "10446055", "10673435", "2203971", "10447505", "10704480", "12458790", "7607232" ]

[ "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, 1998, 1999, 2000, 1990, 1999, 2000, 2002, 1995 ]

12

[ "IPR002301" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 1000, 12019, 8056, 39, 713 ]

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...

[ 9, 1, 1, 1, 19, 4, 1, 11, 3, 1, 1, 48 ]

12

true

Family

Isoleucine-tRNA ligase, type 2

Ile-tRNA-ligase_type2

3

IPR023587

23,587

Metallothionein domain superfamily, vertebrate

Metalthion_dom_sf_vert

Homologous_superfamily

2,456

false

Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , ]. An empirical classification into three classes has been proposed by Fowler and coworkers [ ] and K...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:4.10.10.10" ]

[ "" ]

[ 2456 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-5661231", "R-CFA-5661231", "R-DRE-5661231", "R-GGA-5661231", "R-HSA-5661231", "R-HSA-877300", "R-MMU-5661231", "R-RNO-5661231", "R-SSC-5661231" ]

[ "REACTOME:R-BTA-5661231", "REACTOME:R-CFA-5661231", "REACTOME:R-DRE-5661231", "REACTOME:R-GGA-5661231", "REACTOME:R-HSA-5661231", "REACTOME:R-HSA-877300", "REACTOME:R-MMU-5661231", "REACTOME:R-RNO-5661231", "REACTOME:R-SSC-5661231" ]

9

[ "1dfs", "1dft", "1ji9", "1m0g", "1mhu", "1mrb", "1mrt", "2f5h", "2fj4", "2fj5", "2mhu", "2mrb", "2mrt", "4mt2" ]

14

[ "PUB00001490", "PUB00003570", "PUB00003571", "PUB00005944", "PUB00042525", "PUB00078698" ]

[ "2959513", "1779825", "1779826", "2959504", "1438200", "21633816" ]

[ "Chemistry and biochemistry of metallothionein.", "Overview of metallothionein.", "Definitions and nomenclature of metallothioneins.", "Nomenclature of metallothionein.", "Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.", "Metallothionein protein evolutio...

[ 1987, 1991, 1991, 1987, 1992, 2011 ]

6

[]

0

null

[ "Vertebrata" ]

[ 2456 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 4, 35, 13, 14 ]

4

true

Homologous_superfamily

Metallothionein domain superfamily, vertebrate

Metalthion_dom_sf_vert

4

IPR023589

23,589

Processive diacylglycerol beta-glucosyltransferase

Pro_diacylglycrl_glcsylTrfase

Family

339

false

This entry represents a family of bacterial processive diacylglycerol glucosyltransferases. This enzyme is involved in the synthesis of bilayer and non-bilayer-forming membrane biolipids. It successively transfers up to three glycosyl residues to diacylglycerol, forming mono-, di- and triglycosyldiacylglycerol. Diglyco...

[ "GO:0047228" ]

[ "1,2-diacylglycerol 3-glucosyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01280" ]

[ "Diacylglyc_glucosyltr" ]

[ 339 ]

1

[ "EC", "METACYC" ]

[ "2.4.1.315", "PWY-7817" ]

[ "EC:2.4.1.315", "METACYC:PWY-7817" ]

2

[]

0

[ "PUB00054595" ]

[ "9720862" ]

[ "A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products." ]

[ 1998 ]

1

[]

0

null

[ "Bacillales", "human gut metagenome" ]

[ 338, 1 ]

2

[]

0

true

Family

Processive diacylglycerol beta-glucosyltransferase

Pro_diacylglycrl_glcsylTrfase

3

IPR023590

23,590

Digeranylgeranylglycerophospholipid reductase

DGGGPL_reductase

Family

385

false

This entry represents a family of archaeal geranylgeranyl glycerophospholipid reductases. They are responsible for the reduction of 2,3-digeranylgeranylglycerophospholipids into 2,3-diphytanylglycerophospholipids during the biosynthesis of archaeal membrane lipids [ , , ]. They are also able to catalyse the reduction o...

[ "GO:0016628", "GO:0045550", "GO:0008610" ]

[ "oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor", "geranylgeranyl reductase activity", "lipid biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP" ]

[ "MF_01287" ]

[ "DGGGPL_reductase" ]

[ 385 ]

1

[]

0

[ "3oz2" ]

1

[ "PUB00054596", "PUB00054597", "PUB00058057" ]

[ "16788058", "17275067", "17288560" ]

[ "Biosynthesis of archaeal membrane lipids: digeranylgeranylglycerophospholipid reductase of the thermoacidophilic archaeon Thermoplasma acidophilum.", "Stereochemistry of reduction in digeranylgeranylglycerophospholipid reductase involved in the biosynthesis of archaeal membrane lipids from Thermoplasma acidophil...

[ 2006, 2007, 2007 ]

3

[ "IPR011777" ]

[]

1

0

1

[ "Candidatus Kryptoniota", "Methanobacteriati", "unclassified sequences" ]

[ 4, 371, 10 ]

3

[]

0

true

Family

Digeranylgeranylglycerophospholipid reductase

DGGGPL_reductase

1

IPR023592

23,592

D-galactonate dehydratase

Galactonate_deHydtase

Family

5,314

false

This entry represents a family of bacterial D-galactonate dehydratases which catalyse the dehydration of D-galactonate to 2-keto-3-deoxy-D-galactonate [ ].

[ "GO:0008869", "GO:0034194" ]

[ "galactonate dehydratase activity", "D-galactonate catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "SFLD", "CDD" ]

[ "MF_01289", "SFLDF00003", "cd03325" ]

[ "Galacton_dehydrat", "D-galactonate_dehydratase", "D-galactonate_dehydratase" ]

[ 883, 5170, 4958 ]

3

[ "EC" ]

[ "4.2.1.6" ]

[ "EC:4.2.1.6" ]

1

[ "3rr1", "3rra" ]

2

[ "PUB00054598" ]

[ "324806" ]

[ "D-Galactonate utilisation by enteric bacteria. The catabolic pathway in Escherichia coli." ]

[ 1977 ]

1

[ "IPR034593" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]

[ 3821, 1230, 253, 10 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-galactonate dehydratase

Galactonate_deHydtase

1

IPR023593

23,593

2-keto-3-deoxy-L-rhamnonate aldolase

KDR_aldolase

Family

431

false

This entry represents a family of bacterial 2-keto-3-deoxy-L-rhamnonate aldolases. They are responsible for reversible retro-aldol cleavage of 2-keto-3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde [ , ].

[ "GO:0016832" ]

[ "aldehyde-lyase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01290" ]

[ "KDR_aldolase" ]

[ 431 ]

1

[ "EC", "METACYC" ]

[ "4.1.2.53", "PWY-6713" ]

[ "EC:4.1.2.53", "METACYC:PWY-6713" ]

2

[ "2vws", "2vwt" ]

2

[ "PUB00047672", "PUB00049940" ]

[ "18754693", "18754683" ]

[ "Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase.", "Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12." ]

[ 2008, 2008 ]

2

[]

0

null

[ "Enterobacteriaceae" ]

[ 431 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

2-keto-3-deoxy-L-rhamnonate aldolase

KDR_aldolase

6

IPR023594

23,594

Haloalkane dehalogenase, subfamily 2

Haloalkane_dehalogenase_2

Family

361

false

This entry represents the subfamily 2 haloalkane dehalogenases. Haloalkane dehalogenases catalyse the hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons [ ]. These enzymes can be divided into two subfami...

[ "GO:0018786" ]

[ "haloalkane dehalogenase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01231" ]

[ "Haloalk_dehal_type2" ]

[ 361 ]

1

[ "EC" ]

[ "3.8.1.5" ]

[ "EC:3.8.1.5" ]

1

[ "1bn6", "1bn7", "1cqw", "1cv2", "1d07", "1g42", "1g4h", "1g5f", "1iz7", "1iz8", "1k5p", "1k63", "1k6e", "1mj5", "2bfn", "2o2h", "2o2i", "2qvb", "2v9z", "3a2l", "3a2m", "3a2n", "3afi", "3fbw", "3fwh", "3g9x", "3rk4", "3sk0", "3wi7", "3wib", "4e46", "4f5z"...

117

[ "PUB00054255" ]

[ "4019411" ]

[ "Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10." ]

[ 1985 ]

1

[ "IPR000639" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta", "unclassified sequences" ]

[ 312, 37, 12 ]

3

[]

0

true

Family

Haloalkane dehalogenase, subfamily 2

Haloalkane_dehalogenase_2

2

IPR023596

23,596

Peptidase PrsW, archaeal/bacterial

Peptidase_PrsW_arch/bac

Family

2,113

false

This entry represents the archaeal and bacterial peptidase PrsW, which is involved in intramembrane proteolysis and antimicrobial peptide resistance [ , ].

[ "GO:0008233" ]

[ "peptidase activity" ]

[ "molecular_function" ]

1

[ "PIRSF" ]

[ "PIRSF016933" ]

[ "PrsW" ]

[ 2113 ]

1

[]

0

[]

0

[ "PUB00054608", "PUB00054609" ]

[ "16816000", "17020587" ]

[ "Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis.", "YpdC determines site-1 degradation in regulated intramembrane proteolysis of the RsiW anti-sigma factor of Bacillus subtilis." ]

[ 2006, 2006 ]

2

[ "IPR026898" ]

[]

1

0

1

[ "Bacteria", "Methanobacteriota", "Phytophthora kernoviae 00238/432", "metagenomes" ]

[ 2029, 65, 1, 18 ]

4

[]

0

true

Family

Peptidase PrsW, archaeal/bacterial

Peptidase_PrsW_arch/bac

8

IPR023597

23,597

Flagellar regulator Flk

Flagellar_regulator_Flk

Family

1,398

false

This group represents a flagellar regulator Flk. It is involved in coupling flgM translation to flagellar ring assembly [ , ].

[ "GO:0010468", "GO:0016020" ]

[ "regulation of gene expression", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "NCBIFAM", "PFAM", "PIRSF" ]

[ "NF007987", "PF27202", "PIRSF020588" ]

[ "PRK10715.1", "Flk_N", "Flk" ]

[ 1215, 1398, 991 ]

3

[]

0

[]

0

[ "PUB00054610", "PUB00054611", "PUB00161965" ]

[ "9765570", "16629666", "9079927" ]

[ "Flk couples flgM translation to flagellar ring assembly in Salmonella typhimurium.", "Flk prevents premature secretion of the anti-sigma factor FlgM into the periplasm.", "The flk gene of Salmonella typhimurium couples flagellar P- and L-ring assembly to flagellar morphogenesis." ]

[ 1998, 2006, 1997 ]

3

[]

0

null

[ "Bacteria", "Beauveria bassiana D1-5", "bioreactor metagenome" ]

[ 1396, 1, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Flagellar regulator Flk

Flagellar_regulator_Flk

2

IPR023599

23,599

Membrane-associated protein TcaA

Mem_prot_TcaA

Family

289

false

TcaA is a bacterial membrane protein that plays a role in resistance to glycopeptide antibiotics [ ].

[ "GO:0046677", "GO:0016020" ]

[ "response to antibiotic", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PIRSF" ]

[ "PIRSF032522" ]

[ "TcaA" ]

[ 289 ]

1

[]

0

[]

0

[ "PUB00054615" ]

[ "15155184" ]

[ "tcaA inactivation increases glycopeptide resistance in Staphylococcus aureus." ]

[ 2004 ]

1

[]

0

null

[ "Bacillota" ]

[ 289 ]

1

[]

0

true

Family

Membrane-associated protein TcaA

Mem_prot_TcaA

8

IPR023600

23,600

Folylpolyglutamate synthase, eukaryota

Folylpolyglutamate_synth_euk

Family

4,568

false

Folylpolyglutamate synthase (FPGS) is an ATP-dependent enzyme that is responsible for the addition of a polyglutamate tail to folate and folate derivatives [ ]. It plays a key role in the retention of the intracellular folate pool. In some bacteria, such as Escherichia coli, the addition of L-glutamate to dihydropteroa...

[ "GO:0004326", "GO:0005524", "GO:0009396" ]

[ "tetrahydrofolylpolyglutamate synthase activity", "ATP binding", "folic acid-containing compound biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "PIRSF" ]

[ "PIRSF038895" ]

[ "FPGS" ]

[ 4568 ]

1

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.3.2.17", "PWY-2161", "R-CEL-196757", "R-HSA-196757", "R-MMU-196757", "R-SCE-196757", "R-SPO-196757" ]

[ "EC:6.3.2.17", "METACYC:PWY-2161", "REACTOME:R-CEL-196757", "REACTOME:R-HSA-196757", "REACTOME:R-MMU-196757", "REACTOME:R-SCE-196757", "REACTOME:R-SPO-196757" ]

7

[]

0

[ "PUB00006413", "PUB00032198" ]

[ "9618466", "15705579" ]

[ "Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase.", "Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy." ]

[ 1998, 2005 ]

2

[ "IPR001645" ]

[]

1

0

1

[ "Eukaryota" ]

[ 4568 ]

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...

[ 12, 1, 1, 3, 1, 1, 2, 6, 5, 1, 1, 10 ]

12

true

Family

Folylpolyglutamate synthase, eukaryota

Folylpolyglutamate_synth_euk

5

IPR023602

23,602

Riboflavin kinase domain, CTP-dependent

Riboflavin_kinase_CTP-dep

Domain

1,033

false

This entry represents a CTP-dependent riboflavin kinase domain, found primarily in archaea, that catalyses the phosphorylation of riboflavin to form flavin mononucleotide in riboflavin biosynthesis. Its structure resembles a RIFT barrel, structurally similar to but topologically distinct from bacterial and eukaryotic e...

[ "GO:0016773" ]

[ "phosphotransferase activity, alcohol group as acceptor" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF01982" ]

[ "CTP-dep_RFKase" ]

[ 1033 ]

1

[ "EC", "METACYC" ]

[ "2.7.1.161", "PWY-6167" ]

[ "EC:2.7.1.161", "METACYC:PWY-6167" ]

2

[ "2oyn", "2p3m", "2vbs", "2vbt", "2vbu", "2vbv", "3cta", "5trd" ]

8

[ "PUB00010127", "PUB00030175", "PUB00035657", "PUB00042719" ]

[ "12517446", "14580199", "17049878", "18073108" ]

[ "A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer.", "Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism.", "Over-expression in Escherichia coli, purification and characterization of isoform 2 ...

[ 2003, 2003, 2007, 2007 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Metazoa", "ecological metagenomes" ]

[ 916, 71, 2, 44 ]

4

[]

0

true

Domain

Riboflavin kinase domain, CTP-dependent

Riboflavin_kinase_CTP-dep

9

IPR023603

23,603

Low specificity L-threonine aldolase-like

Low_specificity_L-TA-like

Family

14,599

false

This group represents Low specificity threonine aldolases ( ) which catalyse the conversion of L-threonine or L-allo-threonine into glycine and acetaldehyde. Pyridoxal 5'-phosphate is a cofactor in the reaction [ ]. The entry also includes L-allo-threonine aldolase which acts on L-allo-threonine but not L-threonine or ...

[]

0

[ "NCBIFAM", "PIRSF" ]

[ "NF041359", "PIRSF017617" ]

[ "GntG_guanitoxin", "Thr_aldolase" ]

[ 14213, 13589 ]

2

[]

0

[ "1jg8", "1lw4", "1lw5", "1m6s", "2fm1", "3wgb", "3wgc", "3wlx", "4lnj", "4lnl", "4lnm", "4rjy", "8pum", "8pus", "9e97", "9e9j" ]

16

[ "PUB00080692", "PUB00080693", "PUB00080716", "PUB00113271" ]

[ "9692922", "9228760", "20534346", "10671527" ]

[ "Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli.", "Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39.", "Identification of the viridicatumtoxin and griseofulvin gene cluster...

[ 1998, 1997, 2010, 2000 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 281, 8944, 5133, 241 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces ...

[ 10, 2, 3, 1, 1, 1, 1, 3, 3, 1, 1, 24 ]

12

true

Family

Low specificity L-threonine aldolase-like

Low_specificity_L-TA-like

1

IPR023604

23,604

Uncharacterised protein family SanA

Uncharacterised_SanA

Family

1,129

false

Members of this entry have no known function and contains the protein SanA.

[]

0

[ "NCBIFAM", "PIRSF" ]

[ "NF008092", "PIRSF005011" ]

[ "PRK10834.1", "SanA" ]

[ 1129, 1097 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 1125, 4 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family SanA

Uncharacterised_SanA

1

IPR023606

23,606

CoA-transferase family III domain 1 superfamily

CoA-Trfase_III_dom_1_sf

Homologous_superfamily

91,414

false

CoA-transferases are found in organisms from all kingdoms of life. They catalyse reversible transfer reactions of coenzyme A groups from CoA-thioesters to free acids. There are at least three families of CoA-transferases, which differ in sequence and reaction mechanism: Family I consists of CoA-transferases for 3-oxoac...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.40.50.10540", "SSF89796" ]

[ "", "" ]

[ 90919, 91406 ]

2

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.8.3", "R-HSA-193368", "R-HSA-193775", "R-HSA-389887", "R-HSA-9033241", "R-MMU-193368", "R-MMU-193775", "R-MMU-389887", "R-MMU-9033241", "R-RNO-193368", "R-RNO-193775", "R-RNO-389887", "R-RNO-9033241" ]

[ "EC:2.8.3", "REACTOME:R-HSA-193368", "REACTOME:R-HSA-193775", "REACTOME:R-HSA-389887", "REACTOME:R-HSA-9033241", "REACTOME:R-MMU-193368", "REACTOME:R-MMU-193775", "REACTOME:R-MMU-389887", "REACTOME:R-MMU-9033241", "REACTOME:R-RNO-193368", "REACTOME:R-RNO-193775", "REACTOME:R-RNO-389887", "RE...

13

[ "1p5h", "1p5r", "1pqy", "1pt5", "1pt7", "1pt8", "1q6y", "1q7e", "1t3z", "1t4c", "1vgq", "1vgr", "1x74", "1xa3", "1xa4", "1xk6", "1xk7", "1xvt", "1xvu", "1xvv", "2g04", "2gce", "2gci", "2gd0", "2gd2", "2gd6", "2vjk", "2vjl", "2vjm", "2vjn", "2vjo", "2vjp"...

62

[ "PUB00019325", "PUB00031320", "PUB00032440", "PUB00035619", "PUB00035620", "PUB00093662" ]

[ "11749953", "15213226", "15823031", "11418570", "10849007", "28932214" ]

[ "A new family of CoA-transferases.", "Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes.", "Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA.", "Succinyl-CoA:(R)-benzylsucc...

[ 2001, 2004, 2005, 2001, 2000, 2017 ]

6

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Viruses", "unclassified sequences" ]

[ 1080, 74946, 12829, 3, 3, 2553 ]

6

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]

[ 3, 24, 3, 3, 17, 6, 4, 13 ]

8

true

Homologous_superfamily

CoA-transferase family III domain 1 superfamily

CoA-Trfase_III_dom_1_sf

9

IPR023607

23,607

Exodeoxyribonuclease I

Exodeoxyribonuclease_I

Family

5,648

false

This entry represents exodeoxyribonuclease I. It functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease AP lyase; exonucleolytic cleavage in the 3'- to 5'-direction yields nucleoside 5'-phos...

[ "GO:0004529" ]

[ "DNA exonuclease activity" ]

[ "molecular_function" ]

1

[ "PIRSF" ]

[ "PIRSF000977" ]

[ "Exodeoxyribonuclease_I" ]

[ 5648 ]

1

[ "EC" ]

[ "3.1.11.1" ]

[ "EC:3.1.11.1" ]

1

[ "1fxx", "2qxf", "3c94", "3c95", "3hl8", "3hp9", "4hcb", "4hcc", "4jrp", "4jrq", "4js4", "4js5", "4rg8" ]

13

[ "PUB00020975" ]

[ "1329027" ]

[ "DNA deoxyribophosphodiesterase of Escherichia coli is associated with exonuclease I." ]

[ 1992 ]

1

[ "IPR022894" ]

[]

1

0

1

[ "Aphis craccivora", "Bacteria", "metagenomes" ]

[ 1, 5602, 45 ]

3

[ "Escherichia coli (strain K12)" ]

[ 4 ]

1

true

Family

Exodeoxyribonuclease I

Exodeoxyribonuclease_I

6

IPR023608

23,608

Protein-glutamine gamma-glutamyltransferase, animal

Transglutaminase_animal

Family

10,115

false

This entry includes a group of transglutaminases from animals.

[ "GO:0003810", "GO:0018149" ]

[ "protein-glutamine gamma-glutamyltransferase activity", "peptide cross-linking" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF" ]

[ "PIRSF000459" ]

[ "TGM_EBP42" ]

[ 10115 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.3.2.13", "R-HSA-114608", "R-HSA-140875", "R-HSA-6785807", "R-HSA-6809371", "R-MMU-114608", "R-MMU-140875", "R-MMU-6809371", "R-RNO-114608", "R-RNO-140875", "R-RNO-6809371" ]

[ "EC:2.3.2.13", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-140875", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-6809371", "REACTOME:R-MMU-114608", "REACTOME:R-MMU-140875", "REACTOME:R-MMU-6809371", "REACTOME:R-RNO-114608", "REACTOME:R-RNO-140875", "REACTOME:R-RNO-6809371" ]

11

[ "1evu", "1ex0", "1f13", "1fie", "1g0d", "1ggt", "1ggu", "1ggy", "1kv3", "1l9m", "1l9n", "1nud", "1nuf", "1nug", "1qrk", "2q3z", "3ly6", "3s3j", "3s3p", "3s3s", "4kty", "4pyg", "5mhl", "5mhm", "5mhn", "5mho", "6a8p", "6kzb", "7tvz", "7tw0", "7tw1", "7tw3"...

50

[ "PUB00001513", "PUB00002570", "PUB00010639", "PUB00095164", "PUB00095165" ]

[ "1683845", "1974250", "10411627", "15692067", "19269200" ]

[ "Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues.", "Structure of transglutaminases.", "The structural basis for the regulation of tissue transglutaminase by calcium ions.", "Protein-4.2 association with band 3 (AE1, SLCA4) in Xenopus oocytes: effects of three natural protein-4...

[ 1991, 1990, 1999, 2005, 2009 ]

5

[]

0

null

[ "Eukaryota" ]

[ 10115 ]

1

[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 45, 3, 30, 21, 23 ]

5

true

Family

Protein-glutamine gamma-glutamyltransferase, animal

Transglutaminase_animal

4

IPR023609

23,609

Transcription regulator HTH, RhaS

Tscrpt_reg_HTH_RhaS

Family

1,127

false

This entry represents the HTH transcriptional activator RhaS. It is responsible for activation of rhaBAD and rhaT operons and therefore is involved in the control of rhamnose metabolism.

[ "GO:0003700", "GO:0006355" ]

[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01534", "NF010028" ]

[ "HTH_type_RhaS", "PRK13503.1" ]

[ 935, 1127 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Pseudomonadota", "human gut metagenome" ]

[ 1126, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Transcription regulator HTH, RhaS

Tscrpt_reg_HTH_RhaS

7

IPR023610

23,610

Phosphatidylinositol-4/5-phosphate 5/4-kinase

PInositol-4/5-P-5/4-kinase

Family

25,280

false

This entry includes type I and type II phosphatidylinositol-phosphate-kinases (PIPKs) [ ]. Type I (phosphatidylinositol-4-phosphate 5-kinase/PIP5K) and type II (phosphatidylinositol-5-phosphate 4-kinase/PIP4K) PIPKs catalyse the formation of phosphoinositol-4,5-bisphosphate via the phosphorylation of phosphatidylinosit...

[]

0

[ "PANTHER" ]

[ "PTHR23086" ]

[ "" ]

[ 25280 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "2.7.1", "R-BTA-1660499", "R-BTA-6811555", "R-BTA-6811558", "R-BTA-8847453", "R-DDI-1660499", "R-DDI-6811555", "R-DDI-6811558", "R-DDI-8847453", "R-DDI-8856828", "R-DME-1660499", "R-DME-201688", "R-DME-6811558", "R-DRE-1660499", "R-DRE-6811555", "R-DRE-6811558", "R-DRE-8847453", "R...

[ "EC:2.7.1", "REACTOME:R-BTA-1660499", "REACTOME:R-BTA-6811555", "REACTOME:R-BTA-6811558", "REACTOME:R-BTA-8847453", "REACTOME:R-DDI-1660499", "REACTOME:R-DDI-6811555", "REACTOME:R-DDI-6811558", "REACTOME:R-DDI-8847453", "REACTOME:R-DDI-8856828", "REACTOME:R-DME-1660499", "REACTOME:R-DME-201688...

60

[ "1bo1", "2gk9", "2ybx", "3wzz", "3x01", "3x02", "3x03", "3x04", "3x05", "3x06", "3x07", "3x08", "3x09", "3x0a", "3x0b", "3x0c", "4tz7", "5e3s", "5e3t", "5e3u", "6cmw", "6cn2", "6cn3", "6k4g", "6k4h", "6osp", "6ux9", "6ym3", "6ym4", "6ym5", "7em1", "7em2"...

53

[ "PUB00003041", "PUB00101345", "PUB00113217", "PUB00153073", "PUB00153074" ]

[ "9535851", "22942276", "27439870", "23326584", "31091439" ]

[ "Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family.", "Phosphatidylinositol-4-phosphate 5-kinase isoforms exhibit acyl chain selectivity for both substrate and lipid activator.", "Mechanism of substrate...

[ 1998, 2012, 2016, 2013, 2019 ]

5

[]

[ "IPR017163" ]

0

1

0

[ "Eukaryota", "organismal metagenomes" ]

[ 25278, 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...

[ 52, 2, 33, 10, 31, 16, 2, 33, 29, 1, 1, 79 ]

12

true

Family

Phosphatidylinositol-4/5-phosphate 5/4-kinase

PInositol-4/5-P-5/4-kinase

9

IPR023611

23,611

Small ribosomal subunit protein mS23, conserved domain, metazoa

mS23_dom_met

Domain

1,607

false

This entry represents a domain found in the animal mitochondrial small ribosomal subunit protein mS23. The function of this conserved region is not known.

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PFAM" ]

[ "PF10484" ]

[ "MRP-S23" ]

[ 1607 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-CEL-5389840", "R-CEL-5419276", "R-CEL-9937383", "R-HSA-5368286", "R-HSA-5389840", "R-HSA-5419276", "R-HSA-9937383", "R-MMU-5389840", "R-MMU-5419276", "R-MMU-9937383" ]

[ "REACTOME:R-CEL-5389840", "REACTOME:R-CEL-5419276", "REACTOME:R-CEL-9937383", "REACTOME:R-HSA-5368286", "REACTOME:R-HSA-5389840", "REACTOME:R-HSA-5419276", "REACTOME:R-HSA-9937383", "REACTOME:R-MMU-5389840", "REACTOME:R-MMU-5419276", "REACTOME:R-MMU-9937383" ]

10

[ "3j9m", "3jd5", "5aj3", "5aj4", "6gaw", "6gaz", "6neq", "6nf8", "6nu2", "6nu3", "6rw4", "6rw5", "6vlz", "6vmi", "6ydp", "6ydw", "6zm5", "6zm6", "6zs9", "6zsa", "6zsb", "6zsc", "6zsd", "6zse", "6zsg", "7a5f", "7a5g", "7a5i", "7a5k", "7l08", "7nqh", "7nql"...

77

[ "PUB00019866", "PUB00044434" ]

[ "11278769", "16823961" ]

[ "Identification of 12 new yeast mitochondrial ribosomal proteins including 6 that have no prokaryotic homologues.", "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics." ]

[ 2001, 2006 ]

2

[ "IPR059242" ]

[]

1

0

1

[ "Eukaryota" ]

[ 1607 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 2, 2, 2, 7, 4 ]

6

true

Domain

Small ribosomal subunit protein mS23, conserved domain, metazoa

mS23_dom_met

5

IPR023613

23,613

Nitrophorin

Family

29

false

Nitrophorins are haemoproteins found in saliva of blood-feeding insects [ , ]. Saliva of the blood-sucking bug Rhodnius prolixus (Triatomid bug) contains four homologous nitrophorins, designated NP1 to NP4 in order of their relative abundance in the glands [ ]. As isolated, nitrophorins contain nitric oxide (NO) ligate...

[ "GO:0051381", "GO:0070026" ]

[ "histamine binding", "nitric oxide binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PRINTS" ]

[ "PR00788" ]

[ "NITROPHORIN" ]

[ 29 ]

1

[]

0

[ "1d2u", "1d3s", "1eqd", "1erx", "1euo", "1ike", "1ikj", "1koi", "1ml7", "1np1", "1np4", "1pee", "1pm1", "1sxu", "1sxw", "1sxx", "1sxy", "1sy0", "1sy1", "1sy2", "1sy3", "1t68", "1u0x", "1u17", "1u18", "1x8n", "1x8o", "1x8p", "1x8q", "1ywa", "1ywb", "1ywc"...

76

[ "PUB00000545", "PUB00008042", "PUB00008043", "PUB00008044", "PUB00008045" ]

[ "8761444", "10093938", "11058753", "7721773", "9716517" ]

[ "The lipocalin protein family: structure and function.", "Novel nitric oxide-liberating heme proteins from the saliva of bloodsucking insects.", "Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods.", "Purification, partial characterization, and cloning...

[ 1996, 1999, 2000, 1995, 1998 ]

5

[]

0

null

[ "Rhodnius" ]

[ 29 ]

1

[]

0

true

Family

Nitrophorin

9

IPR023614

23,614

Porin domain superfamily

Porin_dom_sf

Homologous_superfamily

106,082

false

This superfamily represents the structural domain found in porins. Porins are found in the outer membranes of Gram-negative bacteria, mitochondria and chloroplasts, where they form ion-selective channels for small hydrophilic molecules (up to ~600 D) [ , ]. X-ray structure analyses of several bacterial porins [ , , ] h...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:2.40.160.10" ]

[ "" ]

[ 106082 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-5205685", "R-BTA-5689880", "R-BTA-70268", "R-CEL-5205685", "R-CEL-5689880", "R-CEL-70268", "R-DDI-5205685", "R-DDI-70268", "R-DME-5205685", "R-DME-5689880", "R-DME-70268", "R-HSA-1236974", "R-HSA-1268020", "R-HSA-166058", "R-HSA-168179", "R-HSA-3000484", "R-HSA-5205685", "R-...

[ "REACTOME:R-BTA-5205685", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-70268", "REACTOME:R-CEL-5205685", "REACTOME:R-CEL-5689880", "REACTOME:R-CEL-70268", "REACTOME:R-DDI-5205685", "REACTOME:R-DDI-70268", "REACTOME:R-DME-5205685", "REACTOME:R-DME-5689880", "REACTOME:R-DME-70268", "REACTOME:R-HSA-...

36

[ "1bh3", "1bt9", "1e54", "1gfm", "1gfn", "1gfo", "1gfp", "1gfq", "1h6s", "1hxt", "1hxu", "1hxx", "1mpf", "1opf", "1osm", "1pho", "1prn", "2fgq", "2fgr", "2j1n", "2j4u", "2jk4", "2k4t", "2o4v", "2odj", "2omf", "2por", "2prn", "2qtk", "2xe1", "2xe2", "2xe3"...

227

[ "PUB00001604", "PUB00003334", "PUB00003475", "PUB00003829", "PUB00005073" ]

[ "1707373", "7525973", "1725488", "1373213", "2178269" ]

[ "The structure of porin from Rhodobacter capsulatus at 1.8 A resolution.", "Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus.", "A common channel-forming motif in evolutionarily distant porins.", "Porins and specific channels of bacterial out...

[ 1991, 1994, 1991, 1992, 1990 ]

5

[]

0

null

[ "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 84853, 20360, 26, 843 ]

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",...

[ 39, 2, 19, 13, 11, 24, 21, 2, 23, 22, 3, 2, 100 ]

13

true

Homologous_superfamily

Porin domain superfamily

Porin_dom_sf

8

IPR023616

23,616

Cytochrome c oxidase-like, subunit I domain

Cyt_c_oxase-like_su1_dom

Domain

1,770,370

false

Cytochrome c oxidase ( ) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxida...

[ "GO:0004129" ]

[ "cytochrome-c oxidase activity" ]

[ "molecular_function" ]

1

[ "PROFILE" ]

[ "PS50855" ]

[ "COX1" ]

[ 1770370 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "7.1.1.9", "PWY-3781", "PWY-4521", "PWY-6692", "PWY-7279", "PWY-7429", "PWY-8271", "R-CEL-5419276", "R-CEL-9837999", "R-CEL-9864848", "R-DDI-9837999", "R-DME-5419276", "R-DME-5628897", "R-DME-611105", "R-DME-9707564", "R-DME-9837999", "R-DME-9864848", "R-DRE-5628897", "R-DRE-6111...

[ "EC:7.1.1.9", "METACYC:PWY-3781", "METACYC:PWY-4521", "METACYC:PWY-6692", "METACYC:PWY-7279", "METACYC:PWY-7429", "METACYC:PWY-8271", "REACTOME:R-CEL-5419276", "REACTOME:R-CEL-9837999", "REACTOME:R-CEL-9864848", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-5419276", "REACTOME:R-DME-5628897", ...

52

[ "1ar1", "1ehk", "1fft", "1m56", "1m57", "1occ", "1oco", "1ocr", "1ocz", "1qle", "1v54", "1v55", "1xme", "2dyr", "2dys", "2eij", "2eik", "2eil", "2eim", "2ein", "2gsm", "2occ", "2qpd", "2qpe", "2y69", "2ybb", "2yev", "2zxw", "3abk", "3abl", "3abm", "3ag1"...

261

[ "PUB00000581", "PUB00001153", "PUB00001256", "PUB00002253", "PUB00006485" ]

[ "6307356", "2824194", "8013452", "8083153", "8049679" ]

[ "Structure of cytochrome c oxidase.", "Structural models of the redox centres in cytochrome oxidase.", "Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen.", "The superfamily of heme-copper respiratory oxidases.", "The proton pump of heme-copper oxidases." ]

[ 1983, 1987, 1994, 1994, 1994 ]

5

[]

[ "IPR033944" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "Flavobacterium phage 6H", "unclassified sequences" ]

[ 1667, 49897, 1717750, 1, 1055 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 4, 8, 2, 57, 1, 1118, 53, 1, 4, 37, 5, 1, 3 ]

13

true

Domain

Cytochrome c oxidase-like, subunit I domain

Cyt_c_oxase-like_su1_dom

6

IPR023617

23,617

Tyrosine-tRNA ligase, archaeal/eukaryotic-type

Tyr-tRNA-ligase_arc/euk-type

Family

3,990

false

Tyrosine-tRNA ligases (TyrRS; also known as Tyrosyl-tRNA synthetases) ( ) are widely distributed, being found in archaea, bacteria and eukaryotes. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tR...

[ "GO:0004831" ]

[ "tyrosine-tRNA ligase activity" ]

[ "molecular_function" ]

1

[ "PIRSF" ]

[ "PIRSF006588" ]

[ "TyrRS_arch_euk" ]

[ 3990 ]

1

[ "EC" ]

[ "6.1.1.1" ]

[ "EC:6.1.1.1" ]

1

[ "1j1u", "1n3l", "1q11", "1u7d", "1u7x", "1zh0", "1zh6", "2ag6", "2cya", "2cyb", "2cyc", "2dlc", "2hgz", "2j5b", "2pxh", "2zp1", "3d6u", "3d6v", "3n2y", "3qe4", "3vgj", "4hjr", "4hjx", "4hk4", "4hpw", "4nd6", "4nd7", "4nda", "4nx2", "4pbr", "4pbs", "4pbt"...

60

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006465", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10630994", "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, 2000, 1990, 1999, 2000, 2002 ]

10

[ "IPR002307" ]

[ "IPR023678", "IPR023684" ]

1

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 957, 105, 2854, 36, 38 ]

5

[ "Arabidopsis thaliana", "Homo sapiens", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 2, 2, 1, 15, 1, 1, 15 ]

7

true

Family

Tyrosine-tRNA ligase, archaeal/eukaryotic-type

Tyr-tRNA-ligase_arc/euk-type

7

IPR023618

23,618

Photosystem I PsaG/PsaK domain, chloroplastic

PSI_PsaG/PsaK_dom

Homologous_superfamily

1,284

false

Photosystem I (PSI) [ ] is an integral membrane protein complex that uses light energy to mediate electron transfer from plastocyanin to ferredoxin. It is found in the chloroplasts of plants and cyanobacteria. PSI is composed of at least 14 different subunits, two of which are small hydrophobic proteins of about 7 to 9...

[ "GO:0015979", "GO:0009522" ]

[ "photosynthesis", "photosystem I" ]

[ "biological_process", "cellular_component" ]

2

[ "CATHGENE3D" ]

[ "G3DSA:1.10.286.40" ]

[ "" ]

[ 1284 ]

1

[]

0

[ "2o01", "2wsc", "2wse", "2wsf", "3lw5", "4rku", "4xk8", "4y28", "5l8r", "5zji", "6igz", "6ijj", "6ijo", "6jo5", "6jo6", "6l35", "6sl5", "6yac", "6yez", "6zoo", "6zxs", "7bgi", "7blx", "7d0j", "7dkz", "7dz7", "7dz8", "7ew6", "7ewk", "7f9o", "7ksq", "7kux"...

59

[ "PUB00000583", "PUB00002802", "PUB00100153" ]

[ "3333014", "8360180", "11687207" ]

[ "Structure, function and organization of the Photosystem I reaction center complex.", "The PSI-K subunit of photosystem I from barley (Hordeum vulgare L.). Evidence for a gene duplication of an ancestral PSI-G/K gene.", "Role of subunits in eukaryotic Photosystem I." ]

[ 1987, 1993, 2001 ]

3

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 5, 1279 ]

2

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 9, 5, 6 ]

3

true

Homologous_superfamily

Photosystem I PsaG/PsaK domain, chloroplastic

PSI_PsaG/PsaK_dom

4

IPR023620

23,620

Small protein B

SmpB

Homologous_superfamily

25,211

false

This entry represents SsrA-binding protein (aka small protein B or SmpB), which is a unique RNA-binding protein that is conserved throughout the bacterial kingdom and is an essential component of the SsrA quality-control system. Tight recognition of codon-anticodon pairings by the ribosome ensures the accuracy and fide...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:2.40.280.10", "SSF74982" ]

[ "", "" ]

[ 25187, 25211 ]

2

[]

0

[ "1j1h", "1k8h", "1p6v", "1wjx", "1zc8", "2czj", "2ob7", "3iyq", "3iyr", "3iz4", "4v6t", "4v8q", "5zey", "6q95", "6q97", "6q98", "6q9a", "7abz", "7ac7", "7acj", "7acr", "7ljp", "8vs9", "8vsa" ]

24

[ "PUB00006449", "PUB00026223", "PUB00045920" ]

[ "10393194", "12560085", "19132006" ]

[ "SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA).", "Solution structure of a tmRNA-binding protein, SmpB, from Thermus thermophilus.", "Ribosome hijacking: a role for small protein B during trans-translation." ]

[ 1999, 2003, 2009 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "Viruses", "candidate division MSBL1 archaeon SCGC-AAA382A20", "unclassified sequences" ]

[ 24457, 200, 15, 1, 538 ]

5

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Homologous_superfamily

Small protein B

SmpB

3

IPR023621

23,621

Large ribosomal subunit protein eL31 domain superfamily

Ribosomal_eL31_dom_sf

Homologous_superfamily

7,555

false

This superfamily represents the structural domain found in ribosomal proteins belonging to the eL31 family. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.10.440.10", "SSF54575" ]

[ "", "" ]

[ 7551, 7511 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72706", "R-DDI-975956", "R-DDI-975957", "R-DME-156827", "R-DME-1799339", "R-DME-72689", "R-DME-72706", "R-DME-975956", "R-DME-975957...

[ "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-975956", "REACTOME:R-CEL-975957", "REACTOME:R-DDI-156827", "REACTOME:R-DDI-1799339", "REACTOME:R-DDI-72689", "REACTOME:R-DDI-72706", "REACTOME:R-DDI-975956", "REACTOME:R-DDI-97595...

64

[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...

655

[ "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "11297922", "11290319", "11114498" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 2001, 2001, 2000 ]

3

[]

0

null

[ "Archaea", "Eukaryota", "Pseudomonadota", "unclassified sequences" ]

[ 894, 6624, 3, 34 ]

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...

[ 11, 1, 1, 1, 9, 6, 1, 7, 15, 2, 1, 14 ]

12

true

Homologous_superfamily

Large ribosomal subunit protein eL31 domain superfamily

Ribosomal_eL31_dom_sf

6

IPR023623

23,623

Antenna complex, beta subunit, conserved site

Antenna_beta_CS

Conserved_site

947

false

The antenna complexes of photosynthetic bacteria function as light-harvesting systems that absorb light and transfer the excitation energy to the reaction centres. The antenna complexes usually comprise 2 polypeptides (alpha- and beta-chains), 2-3 bacteriochlorophyll molecules and some carotenoids [ , , , ]. The alpha-...

[]

0

[ "PROSITE" ]

[ "PS00969" ]

[ "ANTENNA_COMP_BETA" ]

[ 947 ]

1

[]

0

[ "1dx7", "1ijd", "1jo5", "1kzu", "1lgh", "1nkz", "1wrg", "2fkw", "4v9g", "6et5", "6z5r", "6z5s", "7ddq", "7eqd", "7f0l", "7o0u", "7o0v", "7o0w", "7o0x", "7oy8", "7pbw", "7pil", "7pqd", "7tuw", "7tv3", "7va9", "7vb9", "7vnm", "7vny", "7vor", "7vot", "7voy"...

65

[ "PUB00001417", "PUB00003468", "PUB00153105", "PUB00153106" ]

[ "1577009", "1460542", "36738736", "36792596" ]

[ "The primary structure of the antenna polypeptides of Ectothiorhodospira halochloris and Ectothiorhodospira halophila. Four core-type antenna polypeptides in E. halochloris and E. halophila.", "Structure, function and organization of antenna polypeptides and antenna complexes from the three families of Rhodospiri...

[ 1992, 1992, 2023, 2023 ]

4

[]

0

null

[ "Bacteria", "Mycena maculata", "freshwater sediment metagenome" ]

[ 945, 1, 1 ]

3

[]

0

true

Conserved_site

Antenna complex, beta subunit, conserved site

Antenna_beta_CS

5

IPR023624

23,624

Antenna complex, beta domain superfamily

Antenna_beta_dom_sf

Homologous_superfamily

1,185

false

The antenna complexes of photosynthetic bacteria function as light-harvesting systems that absorb light and transfer the excitation energy to the reaction centres. The antenna complexes usually comprise 2 polypeptides (alpha- and beta-chains), 2-3 bacteriochlorophyll molecules and some carotenoids [ , , , ]. The alpha-...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.20.5.250" ]

[ "" ]

[ 1185 ]

1

[]

0

[ "1dx7", "1ijd", "1jmm", "1jo5", "1kzu", "1lgh", "1nkz", "1wrg", "2fkw", "3wmm", "4v8k", "4v9g", "5b5m", "5b5n", "5y5s", "5yq7", "6e36", "6et5", "6q53", "6tzl", "6ubv", "6z5r", "6z5s", "6zxa", "7c52", "7c9r", "7ddq", "7eqd", "7f0l", "7o0u", "7o0v", "7o0w"...

94

[ "PUB00001417", "PUB00003468", "PUB00153105", "PUB00153106" ]

[ "1577009", "1460542", "36738736", "36792596" ]

[ "The primary structure of the antenna polypeptides of Ectothiorhodospira halochloris and Ectothiorhodospira halophila. Four core-type antenna polypeptides in E. halochloris and E. halophila.", "Structure, function and organization of antenna polypeptides and antenna complexes from the three families of Rhodospiri...

[ 1992, 1992, 2023, 2023 ]

4

[]

0

null

[ "Bacteria", "Oryza", "freshwater sediment metagenome" ]

[ 1175, 9, 1 ]

3

[ "Oryza sativa subsp. japonica" ]

[ 3 ]

1

true

Homologous_superfamily

Antenna complex, beta domain superfamily

Antenna_beta_dom_sf

9

IPR023626

23,626

Large ribosomal subunit protein eL39 domain superfamily

Ribosomal_eL39_dom_sf

Homologous_superfamily

4,901

false

This superfamily represents the structural domain found in ribosomal proteins belonging to the eL39 family, which includes eukaryotic and archaeal proteins. A number of eukaryotic and archaebacterial large subunit ribosomal proteins can be grouped on the basis of sequence similarities. This entry represents the large r...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.10.1620.10", "SSF48662" ]

[ "", "" ]

[ 4897, 4869 ]

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-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DME-156827", "R-DME-1799339", "R-DME-72689", "R-DME-72706", "R-DME-97595...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-9759...

63

[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...

633

[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00151098", "PUB00151099" ]

[ "11297922", "11290319", "11114498", "34428590", "36517592" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Deletion of ribosomal paralogs Rpl39 and Rpl39l compromises cell proliferation via protein synthesis and mitochondrial activity.", "A male germ-cell-specific ...

[ 2001, 2001, 2000, 2021, 2022 ]

5

[]

0

null

[ "Archaea", "Eukaryota", "Pantoea vagans", "unclassified sequences" ]

[ 819, 4068, 1, 13 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 7, 1, 1, 2, 3, 3, 1, 3, 9, 1, 1, 13 ]

12

true

Homologous_superfamily

Large ribosomal subunit protein eL39 domain superfamily

Ribosomal_eL39_dom_sf

9

IPR023627

23,627

Recombination protein RecR

Rcmb_RecR

Homologous_superfamily

24,785

false

The bacterial protein RecR is an important regulator in the RecFOR homologous recombination pathway during DNA repair [ , , , ]. It acts with RecF and RecO forming a complex that facilitates the loading of RecA onto ssDNA [ , ]. RecR is a zinc metalloprotein consisting of a N-terminal helix-hairpin-helix (HhH) motif, a...

[]

0

[ "SSF" ]

[ "SSF111304" ]

[ "" ]

[ 24785 ]

1

[]

0

[ "1vdd", "2v1c", "3vdp", "3vdu", "3ve5", "4jcv", "4o6o", "4o6p", "5z2v", "5zvq", "8a93", "8ab0", "8bpr", "8k3f" ]

14

[ "PUB00004365", "PUB00032061", "PUB00064122", "PUB00101156" ]

[ "2674903", "15116069", "23019218", "29633970" ]

[ "The recR locus of Escherichia coli K-12: molecular cloning, DNA sequencing and identification of the gene product.", "Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair.", "RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssD...

[ 1989, 2004, 2012, 2018 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]

[ 7, 24083, 70, 1, 624 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]

[ 1, 1 ]

2

true

Homologous_superfamily

Recombination protein RecR

Rcmb_RecR

2

IPR023631

23,631

Amidase signature domain

Amidase_dom

Domain

133,598

false

The amidase signature enzymes consist structurally of a core domain that is covered by α-helices [ ]. Amidase signature (AS) enzymes are a large group of hydrolytic enzymes that contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being found in both prokaryotes an...

[]

0

[ "PFAM" ]

[ "PF01425" ]

[ "Amidase" ]

[ 133598 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.3.5.7", "R-CEL-2142753", "R-DRE-2142753", "R-HSA-2142753", "R-MMU-2142753", "R-RNO-2142753", "R-SSC-2142753" ]

[ "EC:6.3.5.7", "REACTOME:R-CEL-2142753", "REACTOME:R-DRE-2142753", "REACTOME:R-HSA-2142753", "REACTOME:R-MMU-2142753", "REACTOME:R-RNO-2142753", "REACTOME:R-SSC-2142753" ]

7

[ "1m21", "1m22", "1mt5", "1o9n", "1o9o", "1o9p", "1o9q", "1obi", "1obj", "1obk", "1obl", "1och", "1ock", "1ocl", "1ocm", "2dc0", "2df4", "2dqn", "2f2a", "2g5h", "2g5i", "2gi3", "2vya", "2wap", "2wj1", "2wj2", "3a1i", "3a1k", "3a2p", "3a2q", "3al0", "3h0l"...

90

[ "PUB00027199", "PUB00035563", "PUB00035564", "PUB00035565", "PUB00035566" ]

[ "12367528", "15595822", "17015445", "12032064", "12521300" ]

[ "An alternative mechanism for amidase signature enzymes.", "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.", "Structu...

[ 2002, 2004, 2006, 2002, 2002 ]

5

[]

[ "IPR014085" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "unclassified sequences" ]

[ 1456, 81819, 48308, 2, 2013 ]

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...

[ 31, 13, 15, 12, 8, 5, 8, 59, 6, 3, 4, 95 ]

12

true

Domain

Amidase signature domain

Amidase_dom

1

IPR023632

23,632

ATP synthase, F1 complex, gamma subunit conserved site

ATP_synth_F1_gsu_CS

Conserved_site

24,890

false

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ...

[]

0

[ "PROSITE" ]

[ "PS00153" ]

[ "ATPASE_GAMMA" ]

[ 24890 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-163210", "R-BTA-8949613", "R-BTA-9837999", "R-DDI-9837999", "R-DME-163210", "R-DME-8949613", "R-DME-9837999", "R-HSA-163210", "R-HSA-8949613", "R-HSA-9837999", "R-MMU-163210", "R-MMU-8949613", "R-MMU-9837999", "R-RNO-163210", "R-RNO-8949613", "R-RNO-9837999", "R-SCE-9837999", ...

[ "REACTOME:R-BTA-163210", "REACTOME:R-BTA-8949613", "REACTOME:R-BTA-9837999", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-163210", "REACTOME:R-DME-8949613", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-163210", "REACTOME:R-...

18

[ "1bmf", "1cow", "1e1q", "1e1r", "1e79", "1efr", "1h8e", "1h8h", "1mab", "1nbm", "1ohh", "1qo1", "1w0j", "1w0k", "2ck3", "2f43", "2hld", "2jdi", "2jiz", "2jj1", "2jj2", "2qe7", "2v7q", "2w6e", "2w6f", "2w6g", "2w6h", "2w6i", "2w6j", "2wpd", "2wss", "2xnd"...

314

[ "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020605", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]

[ "11309608", "15473999", "15078220", "16154570", "20450191", "18937357", "1385979", "9741106" ]

[ "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disciplinary approach.", "Regulation of the F0F1-ATP ...

[ 2001, 2004, 2004, 2005, 2010, 2008, 1992, 1998 ]

8

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences", "uncultured marine thaumarchaeote KM3_41_D11" ]

[ 18948, 5614, 327, 1 ]

4

[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae...

[ 12, 2, 1, 1, 3, 7, 1, 7, 8, 1, 1, 19 ]

12

true

Conserved_site

ATP synthase, F1 complex, gamma subunit conserved site

ATP_synth_F1_gsu_CS

3

IPR023634

23,634

Reovirus, outer capsid sigma-3 domain superfamily

Reovirus_capsid_sigma-3_dom_sf

Homologous_superfamily

400

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 outer capsid is made up of the major proteins mu1 and sigma3, and the minor protein sigma1. The inner core structure is composed of the m...

[]

0

[ "SSF" ]

[ "SSF64465" ]

[ "" ]

[ 400 ]

1

[]

0

[ "1fn9", "1jmu", "2cse", "6xf8", "6zty", "6ztz", "7lup", "9cyt", "9cyy" ]

9

[ "PUB00007495", "PUB00024942" ]

[ "9971813", "11230122" ]

[ "The reovirus mutant tsA279 L2 gene is associated with generation of a spikeless core particle: implications for capsid assembly.", "Structure of the reovirus outer capsid and dsRNA-binding protein sigma3 at 1.8 A resolution." ]

[ 1999, 2001 ]

2

[]

0

null

[ "Protostomia", "Pseudomonadota", "Reovirales" ]

[ 2, 6, 392 ]

3

[]

0

true

Homologous_superfamily

Reovirus, outer capsid sigma-3 domain superfamily

Reovirus_capsid_sigma-3_dom_sf

1

IPR023635

23,635

Peptide deformylase

Peptide_deformylase

Family

46,531

false

Peptide deformylase (PDF) is an essential metalloenzyme required for the removal of the formyl group at the N terminus of nascent polypeptide chains in eubacteria: [ ]. The enzyme acts as a monomer and binds a single metal ion, catalysing the reaction: N-formyl-L-methionine + H 2 O = formate + methionyl peptide Catalyt...

[ "GO:0042586" ]

[ "peptide deformylase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "PFAM", "PIRSF", "PRINTS", "PANTHER", "NCBIFAM", "CDD" ]

[ "MF_00163", "PF01327", "PIRSF004749", "PR01576", "PTHR10458", "TIGR00079", "cd00487" ]

[ "Pep_deformylase", "Pep_deformylase", "Pep_def", "PDEFORMYLASE", "", "pept_deformyl", "Pep_deformylase" ]

[ 43182, 46527, 41225, 45635, 46097, 38230, 44404 ]

7

[ "EC" ]

[ "3.5.1.88" ]

[ "EC:3.5.1.88" ]

1

[ "1bs4", "1bs5", "1bs6", "1bs7", "1bs8", "1bsj", "1bsk", "1bsz", "1def", "1dff", "1g27", "1g2a", "1icj", "1ix1", "1jym", "1lm4", "1lm6", "1lme", "1lmh", "1lqw", "1lqy", "1lru", "1lry", "1n5n", "1q1y", "1rl4", "1rqc", "1s17", "1sv2", "1szz", "1v3y", "1vev"...

178

[ "PUB00003371", "PUB00003388", "PUB00007062", "PUB00007063", "PUB00022096", "PUB00027108", "PUB00079662", "PUB00079663" ]

[ "8845003", "9665852", "9846875", "9565550", "12823970", "12126617", "11738381", "10931273" ]

[ "A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase.", "Solution structure of nickel-peptide deformylase.", "Iron center, substrate recognition and mechanism of peptide deformylase.", "Structure of peptide deformylase and identification of the sub...

[ 1996, 1998, 1998, 1998, 2003, 2002, 2001, 2000 ]

8

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 15, 42386, 3148, 41, 941 ]

5

[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 8, 1, 4, 1, 1, 1, 7, 2, 6 ]

9

true

Family

Peptide deformylase

Peptide_deformylase

8

IPR023636

23,636

Urocanase conserved site

Urocanase_CS

Conserved_site

15,613

false

This entry represents a conserved site found in the C-terminal part of Urocanase. It is found also in S-methyl thiourocanate hydratase which cannot use urocanate or thiourocanate as substrate and catalyses the conversion of S-methyl thiourocanate, to S-methyl-thiohydantoin-5-propanoate [ ]. Urocanase [ ] (also known as...

[ "GO:0016153" ]

[ "urocanate hydratase activity" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS01233" ]

[ "UROCANASE" ]

[ 15613 ]

1

[ "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME" ]

[ "4.2.1.49", "PWY-5028", "PWY-5030", "R-CEL-70921", "R-HSA-70921", "R-MMU-70921" ]

[ "EC:4.2.1.49", "METACYC:PWY-5028", "METACYC:PWY-5030", "REACTOME:R-CEL-70921", "REACTOME:R-HSA-70921", "REACTOME:R-MMU-70921" ]

6

[ "1uwl", "1x87", "2fkn", "2v7g", "6uek", "7jfz", "8q9v" ]

7

[ "PUB00000161", "PUB00070322", "PUB00155448" ]

[ "7944380", "4990470", "38389448" ]

[ "The urocanase story: a novel role of NAD+ as electrophile.", "Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway.", "Structure and Substrate Specificity of <i>S</i>-Methyl Thiourocanate Hydratase." ]

[ 1994, 1970, 2024 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 228, 13937, 1288, 160 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 1, 1, 2, 2 ]

5

true

Conserved_site

Urocanase conserved site

Urocanase_CS

2

IPR023637

23,637

Urocanase-like

Family

17,320

false

Urocanase [ ] (also known as imidazolonepropionate hydrolase or urocanate hydratase) is the enzyme that catalyses the second step in the degradation of histidine, the hydration of urocanate into imidazolonepropionate: urocanate + H 2 O = 4,5-dihydro-4-oxo-5-imidazolepropanoate Urocanase is found in some bacteria (gene ...

[]

0

[ "HAMAP", "NCBIFAM", "PIRSF", "PANTHER", "NCBIFAM" ]

[ "MF_00577", "NF003820", "PIRSF001423", "PTHR12216", "TIGR01228" ]

[ "HutU", "PRK05414.1", "Urocanate_hydrat", "", "hutU" ]

[ 15549, 15715, 15833, 17320, 14094 ]

5

[ "EC", "GP", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "4.2.1.49", "GenProp1619", "PWY-5028", "PWY-5030", "R-CEL-70921", "R-DDI-70921", "R-HSA-70921", "R-MMU-70921" ]

[ "EC:4.2.1.49", "GP:GenProp1619", "METACYC:PWY-5028", "METACYC:PWY-5030", "REACTOME:R-CEL-70921", "REACTOME:R-DDI-70921", "REACTOME:R-HSA-70921", "REACTOME:R-MMU-70921" ]

8

[ "1uwk", "1uwl", "1w1u", "1x87", "2fkn", "2v7g", "6uek", "7jfz", "7ned", "8q9u", "8q9v" ]

11

[ "PUB00000161", "PUB00031924", "PUB00070322", "PUB00155448" ]

[ "7944380", "15313616", "4990470", "38389448" ]

[ "The urocanase story: a novel role of NAD+ as electrophile.", "Structure and action of urocanase.", "Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway.", "Structure and Substrate Specificity of <i>S</i>-Methyl Thiourocanate Hydratas...

[ 1994, 2004, 1970, 2024 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 233, 15017, 1793, 277 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 1, 1, 2, 2 ]

5

true

Family

Urocanase-like

5

IPR023638

23,638

Large ribosomal subunit protein eL19, conserved site

Ribosomal_eL19_CS

Conserved_site

5,846

false

This entry represents a conserved site in the ribosomal protein eL19 from eukaryotes and archaea [ ]; it is part of the large ribosomal subunit. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This lead...

[]

0

[ "PROSITE" ]

[ "PS00526" ]

[ "RIBOSOMAL_L19E" ]

[ 5846 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-CFA-156827", "R-CFA-1799339", "R-CFA-6791226", "R-CFA-72689", "R-CFA-727...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-9759...

70

[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...

589

[ "PUB00006505", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "10381320", "11297922", "11290319", "11114498" ]

[ "The structure and evolution of the ribosomal proteins encoded in the spc operon of the archaeon (Crenarchaeota) Sulfolobus acidocaldarius.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 1999, 2001, 2001, 2000 ]

4

[]

0

null

[ "Archaea", "Eukaryota", "Nocardioides antri", "ecological metagenomes" ]

[ 612, 5226, 1, 7 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 9, 1, 1, 1, 9, 3, 1, 4, 4, 2, 11 ]

11

true

Conserved_site

Large ribosomal subunit protein eL19, conserved site

Ribosomal_eL19_CS

3

IPR023639

23,639

DNA primase small subunit PriS

DNA_primase_ssu_PriS

Family

918

false

This family represents sequences of the DNA primase small subunit PriS from archaea. DNA primase synthesises the RNA primers for the Okazaki fragments in lagging strand DNA synthesis. DNA primase is a heterodimer of large and small subunits [ ].

[ "GO:0003899" ]

[ "DNA-directed RNA polymerase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00700" ]

[ "DNA_primase_sml_arc" ]

[ 918 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "2.7.7.-", "PWY-6322", "PWY-6626", "PWY-6749", "PWY-6955", "PWY-6998", "PWY-7127", "PWY-7419", "PWY-7529", "PWY-7706", "PWY-7719", "PWY-7735", "PWY-7737", "PWY-7769", "PWY-7888", "PWY-7904", "PWY-8117", "PWY-8179" ]

[ "EC:2.7.7.-", "METACYC:PWY-6322", "METACYC:PWY-6626", "METACYC:PWY-6749", "METACYC:PWY-6955", "METACYC:PWY-6998", "METACYC:PWY-7127", "METACYC:PWY-7419", "METACYC:PWY-7529", "METACYC:PWY-7706", "METACYC:PWY-7719", "METACYC:PWY-7735", "METACYC:PWY-7737", "METACYC:PWY-7769", "METACYC:PWY-7...

18

[ "1g71", "1v33", "1v34", "1zt2", "5of3", "5ofn", "9f26", "9f28" ]

8

[ "PUB00005693" ]

[ "2023935" ]

[ "Mutations in conserved yeast DNA primase domains impair DNA replication in vivo." ]

[ 1991 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Metazoa", "unclassified sequences" ]

[ 893, 2, 2, 21 ]

4

[]

0

true

Family

DNA primase small subunit PriS

DNA_primase_ssu_PriS

6

IPR023642

23,642

DNA primase large subunit PriL

DNA_primase_lsu_PriL

Family

941

false

This family consists of DNA primase large subunit PriL from archaea. DNA primase is the polymerase that synthesises small RNA primers for the Okazaki fragments made during discontinuous DNA replication. Primases are grouped into two classes, bacteria/bacteriophage and archaeal/eukaryotic. The proteins in the two classe...

[ "GO:0003899" ]

[ "DNA-directed RNA polymerase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "CDD" ]

[ "MF_00701", "cd06560" ]

[ "DNA_primase_lrg_arc", "PriL" ]

[ 882, 865 ]

2

[]

0

[ "1zt2", "2dla", "5of3", "5ofn", "9f26", "9f28" ]

6

[ "PUB00005693", "PUB00009835", "PUB00009837", "PUB00039010" ]

[ "2023935", "2528682", "8026492", "16273105" ]

[ "Mutations in conserved yeast DNA primase domains impair DNA replication in vivo.", "A single essential gene, PRI2, encodes the large subunit of DNA primase in Saccharomyces cerevisiae.", "DNA replication in vitro by recombinant DNA-polymerase-alpha-primase.", "Structure of the heterodimeric core primase." ]

[ 1991, 1989, 1994, 2005 ]

4

[ "IPR007238" ]

[]

1

0

1

[ "Archaea", "Bacteria", "ecological metagenomes" ]

[ 902, 2, 37 ]

3

[]

0

true

Family

DNA primase large subunit PriL

DNA_primase_lsu_PriL

7

IPR023643

23,643

3-phenylpropionate-dihydrodiol/cinnamic acid-dihydrodiol dehydrogenase HcaB

Dihydrodiol_DH_HcaB

Family

103

false

The HcaB protein is a dehydrogenase which converts 3-phenylpropionate-dihydrodiol and cinnamic acid-dihydrodiol into 3-(2,3-dihydroxylphenyl)propanoic acid and 2,3-dihydroxicinnamic acid, respectively [ ]. This protein functions in the dioxygenolytic pathway for catabolism of phenylpropanoid compounds such as cinnamic ...

[ "GO:0016491" ]

[ "oxidoreductase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01647" ]

[ "HcaB" ]

[ 103 ]

1

[ "EC", "METACYC" ]

[ "1.3.1.87", "PWY-6690" ]

[ "EC:1.3.1.87", "METACYC:PWY-6690" ]

2

[]

0

[ "PUB00054929", "PUB00054961" ]

[ "9603882", "11729263" ]

[ "Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12.", "Biodegradation of aromatic compounds by Escherichia coli." ]

[ 1998, 2001 ]

2

[ "IPR047950" ]

[]

1

0

1

[ "Enterobacterales" ]

[ 103 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

3-phenylpropionate-dihydrodiol/cinnamic acid-dihydrodiol dehydrogenase HcaB

Dihydrodiol_DH_HcaB

9

IPR023644

23,644

Nitrous-oxide reductase

NO_Rdtase

Family

1,709

false

Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide. NosZ, one of the members of this family, is the nitrous-oxide reductase structural protein, with an N-terminal twin-arginine translocation (TAT) signal sequence. T...

[ "GO:0005507", "GO:0005509", "GO:0050304" ]

[ "copper ion binding", "calcium ion binding", "nitrous-oxide reductase activity" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00716", "TIGR04244" ]

[ "NosZ", "nitrous_NosZ_RR" ]

[ 964, 1709 ]

2

[ "EC", "METACYC", "METACYC" ]

[ "1.7.2.4", "PWY-6748", "PWY-7084" ]

[ "EC:1.7.2.4", "METACYC:PWY-6748", "METACYC:PWY-7084" ]

3

[ "1fwx", "1qni", "2iwf", "2iwk", "3sbp", "3sbq", "3sbr", "5i5i", "5i5j", "5i5m", "6rkz", "6rl0", "6y6y", "6y71", "6y72", "6y77", "6y7d", "6y7e", "7apy", "7aq0", "7aq2", "7aq3", "7aq4", "7aq5", "7aq6", "7aq7", "7aq8", "7aq9", "7aqa", "7qba", "9f8x" ]

31

[ "PUB00060453" ]

[ "11160097" ]

[ "Role of the Tat ransport system in nitrous oxide reductase translocation and cytochrome cd1 biosynthesis in Pseudomonas stutzeri." ]

[ 2001 ]

1

[]

0

null

[ "Bacteria", "Halobacteriales", "unclassified sequences" ]

[ 1489, 101, 119 ]

3

[]

0

true

Family

Nitrous-oxide reductase

NO_Rdtase

7

IPR023646

23,646

Primosomal replication protein PriB

Prisomal_replication_PriB

Family

3,214

false

PriB, also known as Primosomal replication protein N, is a component of the preprimosomal complex. The preprimosomal complex is composed of one monomer of PriC and DnaT, two monomers of PriA, two dimers of PriB and one hexamer of DnaB. Upon transient interaction with DnaG it forms the primosome [ ]. PriB binds single-s...

[ "GO:0003697", "GO:0006260", "GO:0030894" ]

[ "single-stranded DNA binding", "DNA replication", "replisome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "PFAM", "PIRSF", "NCBIFAM" ]

[ "MF_00720", "PF22657", "PIRSF003135", "TIGR04418" ]

[ "PriB", "SSB_1", "Primosomal_n", "PriB_gamma" ]

[ 2772, 3174, 3059, 3071 ]

4

[ "GP", "GP" ]

[ "GenProp1081", "GenProp1130" ]

[ "GP:GenProp1081", "GP:GenProp1130" ]

2

[ "1txy", "1v1q", "1woc", "2ccz", "2pnh", "3en2", "3fhw", "3k8a", "3klw", "4apv", "4fdb", "5wqv", "8fak" ]

13

[ "PUB00004912", "PUB00022695", "PUB00024637", "PUB00024697", "PUB00031014", "PUB00054930", "PUB00054931", "PUB00054932", "PUB00054933" ]

[ "9192620", "15169953", "10731701", "10932248", "15159541", "8663106", "1856227", "1646811", "8366072" ]

[ "Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution.", "The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA.", "Ro...

[ 1997, 2004, 2000, 2000, 2004, 1996, 1991, 1991, 1993 ]

9

[ "IPR000424" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta", "unclassified sequences" ]

[ 3194, 2, 18 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Primosomal replication protein PriB

Prisomal_replication_PriB

8

IPR023649

23,649

Deoxyribose-phosphate aldolase type II

DeoC_typeII

Family

1,702

false

Deoxyribose-phosphate aldolase is a widely distributed enzyme, which catalyses the following reversible reaction: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde While the physiological role of this enzyme remains unknown in eukaryotes, in prokaroytes it is thought to function in the cataboli...

[ "GO:0004139", "GO:0009264", "GO:0005737" ]

[ "deoxyribose-phosphate aldolase activity", "deoxyribonucleotide catabolic process", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_00592" ]

[ "DeoC_type2" ]

[ 1702 ]

1

[ "EC", "METACYC", "METACYC" ]

[ "4.1.2.4", "PWY-7180", "PWY-8060" ]

[ "EC:4.1.2.4", "METACYC:PWY-7180", "METACYC:PWY-8060" ]

3

[ "1jcj", "1jcl", "1ktn", "1p1x", "5c6m", "5eky", "5el1", "5emu", "6z9h", "6z9i", "6z9j", "7p75", "7p76", "9fd7", "9fd8", "9fd9" ]

16

[ "PUB00000628", "PUB00016149", "PUB00021873", "PUB00027586", "PUB00028044" ]

[ "1730028", "11598300", "15388928", "12529358", "4923156" ]

[ "Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties.", "Observation of covalent intermediates in an enzyme mechanism at atomic resolution.", "Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability.", "The first crystal ...

[ 1992, 2001, 2004, 2003, 1970 ]

5

[ "IPR011343" ]

[]

1

0

1

[ "Bacteria", "Panagrolaimus superbus" ]

[ 1701, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Deoxyribose-phosphate aldolase type II

DeoC_typeII

6

IPR023650

23,650

Beta-lactamase, class-A active site

Beta-lactam_class-A_AS

Active_site

11,363

false

This entry represents a short region that contains the active site serine residue [ ] in the class A beta-lactamases that belong to MEROPS peptidase family S11 (D-Ala-D-Ala carboxypeptidase A family, clan SE). Beta-lactamase catalyses the opening and hydrolysis of the beta-lactam ring of beta-lactam antibiotics such as...

[]

0

[ "PROSITE" ]

[ "PS00146" ]

[ "BETA_LACTAMASE_A" ]

[ 11363 ]

1

[ "EC", "REACTOME" ]

[ "3.5.2.6", "R-HSA-9913143" ]

[ "EC:3.5.2.6", "REACTOME:R-HSA-9913143" ]

2

[ "1alq", "1axb", "1blc", "1blh", "1blp", "1bsg", "1bt5", "1btl", "1bza", "1ci8", "1ci9", "1ck3", "1e25", "1erm", "1ero", "1erq", "1esu", "1fqg", "1g68", "1g6a", "1ghi", "1ghm", "1ghp", "1htz", "1hzo", "1i2s", "1i2w", "1iyo", "1iyp", "1iyq", "1iys", "1jtd"...

563

[ "PUB00000464", "PUB00000477", "PUB00003270" ]

[ "3128280", "2788410", "1856867" ]

[ "The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.", "The phototrophic bacterium Rhodopseudomonas capsulata sp108 encodes an indigenous class A beta-lactamase.", "Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis...

[ 1988, 1989, 1991 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "Stenosarchaea group", "Viruses", "plasmids", "unclassified sequences" ]

[ 11122, 60, 4, 7, 5, 165 ]

6

[ "Arabidopsis thaliana", "Zea mays" ]

[ 1, 1 ]

2

true

Active_site

Beta-lactamase, class-A active site

Beta-lactam_class-A_AS

8

IPR023651

23,651

Large ribosomal subunit protein eL14, archaea

Ribosomal_eL14_arc

Family

206

false

This entry represents archaebacterial ribosomal protein eL14. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accorda...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_00721" ]

[ "Ribosomal_eL14" ]

[ 206 ]

1

[]

0

[ "2joy", "2kds", "4v4n", "4v6u", "6skf", "6skg", "6th6", "8hku", "8hkv", "8hky", "8hkz", "8hl1", "8hl2", "8hl3", "8hl4", "8hl5", "9e6q", "9e71", "9e7f", "9qf4", "9qf5", "9qf6" ]

22

[ "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "11297922", "11290319", "11114498" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 2001, 2001, 2000 ]

3

[ "IPR039660" ]

[]

1

0

1

[ "Archaea" ]

[ 206 ]

1

[]

0

true

Family

Large ribosomal subunit protein eL14, archaea

Ribosomal_eL14_arc

9

IPR023653

23,653

Acetoacetate decarboxylase, bacterial

Acetoacetate_decarboxylase_bac

Family

804

false

This entry represents bacterial acetoacetate decarboxylases. Acetoacetate decarboxylase (ADC) is involved in solventogenesis in certain bacteria, which occurs at the end of the exponential growth phase when there is a metabolic switch from classical sugar fermentation with the production of acetate and butyrate to the ...

[ "GO:0016831" ]

[ "carboxy-lyase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00597" ]

[ "ADC" ]

[ 804 ]

1

[ "EC", "METACYC", "METACYC" ]

[ "4.1.1.4", "PWY-6588", "PWY-6876" ]

[ "EC:4.1.1.4", "METACYC:PWY-6588", "METACYC:PWY-6876" ]

3

[ "3bgt", "3bh2", "3bh3" ]

3

[ "PUB00014916", "PUB00014917" ]

[ "11824611", "10972834" ]

[ "Changes in protein synthesis and identification of proteins specifically induced during solventogenesis in Clostridium acetobutylicum.", "Spo0A directly controls the switch from acid to solvent production in solvent-forming clostridia." ]

[ 2002, 2000 ]

2

[ "IPR010451" ]

[]

1

0

1

[ "Bacteria", "Phytophthora kernoviae 00238/432", "ecological metagenomes" ]

[ 797, 1, 6 ]

3

[]

0

true

Family

Acetoacetate decarboxylase, bacterial

Acetoacetate_decarboxylase_bac

5

IPR023654

23,654

Large ribosomal subunit protein eL32, archaea

Ribosomal_eL32_arc

Family

928

false

This entry represents the archaeal 50S eL32 ribosomal proteins. eL32 is a protein from the large ribosomal subunit that contains a surface-exposed globular domain and a finger-like projection that extends into the RNA core to stabilize the tertiary structure. eL32 does not appear to play a role in forming the A (aminac...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00810", "NF006332" ]

[ "Ribosomal_eL32", "PRK08562.1" ]

[ 494, 928 ]

2

[]

0

[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...

96

[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00028498", "PUB00079483", "PUB00079521", "PUB00079522", "PUB00079523", "PUB00079524" ]

[ "11297922", "11290319", "11114498", "10937989", "10937990", "12082018", "16452584", "16516201", "11904172" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.", "The structural basis of ribosome activity in peptide bond synthesis.", ...

[ 2001, 2001, 2000, 2000, 2000, 2002, 2006, 2006, 2002 ]

9

[ "IPR001515" ]

[]

1

0

1

[ "Archaea", "Candidatus Rhodobacter oscarellae", "Eukaryota", "unclassified sequences" ]

[ 894, 1, 6, 27 ]

4

[]

0

true

Family

Large ribosomal subunit protein eL32, archaea

Ribosomal_eL32_arc

1

IPR023655

23,655

Cytochrome c6

Cyt_C6

Family

1,933

false

Cytochrome c (CytC) proteins can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide r...

[ "GO:0005506", "GO:0009055" ]

[ "iron ion binding", "electron transfer activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP", "PANTHER" ]

[ "MF_00594", "PTHR34688" ]

[ "Cytc_PetJ", "" ]

[ 711, 1931 ]

2

[]

0

[ "1a2s", "1c6o", "1c6r", "1c6s", "1ced", "1ctj", "1cyi", "1cyj", "1f1f", "1gdv", "1kib", "1ls9", "2ce0", "2ce1", "2dge", "2v07", "2v08", "2zbo", "3cu4", "3dmi", "3dp5", "3dr0", "3ph2", "4eic", "4eid", "4eie", "4eif", "4gyd", "4h0j", "4h0k", "4kmg", "5mcs"...

40

[ "PUB00000610", "PUB00002343", "PUB00003350", "PUB00039983" ]

[ "1646017", "1964450", "7623381", "16815443" ]

[ "Sequence variability in bacterial cytochromes c.", "S-class cytochromes c have a variety of folding patterns: structure of cytochrome c-553 from Desulfovibrio vulgaris determined by the multi-wavelength anomalous dispersion method.", "The structure of chloroplast cytochrome c6 at 1.9 A resolution: evidence for...

[ 1991, 1990, 1995, 2006 ]

4

[ "IPR008168" ]

[]

1

0

1

[ "Bacteria", "Eukaryota" ]

[ 783, 1150 ]

2

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 3, 3 ]

3

true

Family

Cytochrome c6

Cyt_C6

1

IPR023656

23,656

IMP biosynthesis enzyme PurP

IMP_biosynth_PurP

Family

1,025

false

This entry represents the 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase also known as PurP. The last two steps of de novo purine biosynthesis are: i) conversion of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxami...

[ "GO:0016879" ]

[ "ligase activity, forming carbon-nitrogen bonds" ]

[ "molecular_function" ]

1

[ "HAMAP", "PIRSF", "PANTHER" ]

[ "MF_01163", "PIRSF004602", "PTHR38147" ]

[ "IMP_biosynth_PurP", "ATPgrasp_PurP", "" ]

[ 477, 921, 1025 ]

3

[ "EC", "METACYC" ]

[ "6.3.4.23", "PWY-7234" ]

[ "EC:6.3.4.23", "METACYC:PWY-7234" ]

2

[ "2pbz", "2r7k", "2r7l", "2r7m", "2r7n", "2r84", "2r85", "2r86", "2r87" ]

9

[ "PUB00013793", "PUB00025174", "PUB00034499", "PUB00034500" ]

[ "11844782", "11323713", "9150241", "15623504" ]

[ "New class of IMP cyclohydrolases in Methanococcus jannaschii.", "Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis.", "Purine biosynthesis in the domain Archaea without folates or modified folates.", "A Methanocaldococcus jannaschii archaeal signature gene en...

[ 2002, 2001, 1997, 2005 ]

4

[]

0

null

[ "Archaea", "Bacteria", "ecological metagenomes" ]

[ 832, 129, 64 ]

3

[]

0

true

Family

IMP biosynthesis enzyme PurP

IMP_biosynth_PurP

6

IPR023657

23,657

Large ribosomal subunit protein eL40, archaea

Ribosomal_eL40_arc

Family

824

false

This family represents the archaeal eL40 ribosomal protein [ ]. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accor...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "NCBIFAM", "PANTHER" ]

[ "MF_00788", "NF003161", "PTHR39649" ]

[ "Ribosomal_eL40", "PRK04136.1", "" ]

[ 658, 805, 823 ]

3

[]

0

[ "2ayj", "4v4n", "4v6u", "6skf", "6skg", "6th6", "7pwg", "7pwo", "8br8", "8brm", "8bsi", "8bsj", "8btd", "8btr", "8fru", "8hku", "8hkv", "8hky", "8hkz", "8hl1", "8hl2", "8hl3", "8hl4", "8hl5", "9e6q", "9e71", "9e7f", "9nri", "9nta", "9o17", "9ou7", "9qf4"...

34

[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00047050" ]

[ "11297922", "11290319", "11114498", "18218710" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus." ]

[ 2001, 2001, 2000, 2008 ]

4

[]

0

null

[ "Archaea", "Eukaryota", "candidate division WOR-3 bacterium", "ecological metagenomes" ]

[ 796, 7, 2, 19 ]

4

[]

0

true

Family

Large ribosomal subunit protein eL40, archaea

Ribosomal_eL40_arc

7

IPR023658

23,658

15,16-dihydrobiliverdin:ferredoxin oxidoreductase

DiHydbiliverdin_OxRdtase

Family

44

false

This enzyme catalyses the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge [ ].

[ "GO:0050617" ]

[ "15,16-dihydrobiliverdin:ferredoxin oxidoreductase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00792" ]

[ "PebA" ]

[ 44 ]

1

[ "EC", "METACYC", "METACYC" ]

[ "1.3.7.2", "PWY-5915", "PWY-7579" ]

[ "EC:1.3.7.2", "METACYC:PWY-5915", "METACYC:PWY-7579" ]

3

[ "2x9o" ]

1

[ "PUB00011945" ]

[ "11283349" ]

[ "Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms." ]

[ 2001 ]

1

[ "IPR009249" ]

[]

1

0

1

[ "Cyanophyceae" ]

[ 44 ]

1

[]

0

true

Family

15,16-dihydrobiliverdin:ferredoxin oxidoreductase

DiHydbiliverdin_OxRdtase

4

IPR023659

23,659

Coenzyme F420:L-glutamate ligase, archaeal

F420_ligase_CofE_arc

Family

406

false

This entry contains coenzyme F420:L-glutamate ligase (also known as F420-0:gamma-glutamyl ligase) from archaea. It catalyses the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 deriv...

[ "GO:0043773", "GO:0046872" ]

[ "coenzyme F420-0 gamma-glutamyl ligase activity", "metal ion binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP" ]

[ "MF_01258" ]

[ "F420_ligase_CofE" ]

[ 406 ]

1

[ "EC", "EC", "METACYC" ]

[ "6.3.2.31", "6.3.2.34", "PWY-5199" ]

[ "EC:6.3.2.31", "EC:6.3.2.34", "METACYC:PWY-5199" ]

3

[ "2g9i", "2phn", "7uld", "7ule", "7ulf", "8g8p" ]

6

[ "PUB00002622", "PUB00003870", "PUB00044776", "PUB00044777" ]

[ "2110564", "8577249", "12867481", "15215601" ]

[ "DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans.", "Molecular characterization of the lincomycin-production gene cluster of Streptomyces lincolnensis 78-11.", "Methanococcus jannaschii coenzyme F420 analogs contain a terminal alpha-linked glutamate.", "Identification and cloning of th...

[ 1990, 1995, 2003, 2004 ]

4

[ "IPR008225" ]

[]

1

0

1

[ "Archaea", "bioreactor metagenome" ]

[ 405, 1 ]

2

[]

0

true

Family

Coenzyme F420:L-glutamate ligase, archaeal

F420_ligase_CofE_arc

9

IPR023660

23,660

Protein arginine kinase

Arg_Kinase

Family

3,030

false

Bacterial arginine kinases catalyse the transfer of phosphate from ATP to arginine. Protein arginine phosphorylation is involved in the regulation of many critical cellular processes, such as protein degradation, competence and stress responses [ ]. Bacterial protein arginine kinase McsB main targets comprise central f...

[ "GO:0016775" ]

[ "phosphotransferase activity, nitrogenous group as acceptor" ]

[ "molecular_function" ]

1

[ "HAMAP", "CDD" ]

[ "MF_00602", "cd07930" ]

[ "Prot_Arg_kinase", "bacterial_phosphagen_kinase" ]

[ 2520, 3025 ]

2

[ "EC" ]

[ "2.7.14.1" ]

[ "EC:2.7.14.1" ]

1

[ "6fh1", "6fh2", "6fh3", "6tv6", "8gqd", "8wtb", "8wtc" ]

7

[ "PUB00052996", "PUB00081098", "PUB00081099", "PUB00081100", "PUB00081101" ]

[ "19498169", "22517742", "21622759", "19226326", "24263382" ]

[ "McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR.", "Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.", "Activity control of the ClpC adaptor McsB in Bacillus subtilis.", "McsA and B mediate the delocalization of compete...

[ 2009, 2012, 2011, 2009, 2014 ]

5

[ "IPR000749" ]

[]

1

0

1

[ "Bacteria", "Geodia barretti", "Thermococcus litoralis", "metagenomes" ]

[ 2985, 6, 1, 38 ]

4

[]

0

true

Family

Protein arginine kinase

Arg_Kinase

9

IPR023662

23,662

Rhomboid protease GlpG

Rhomboid_protease_GlpG

Family

2,155

false

This entry consists of rhomboid protease GlpG and its homologues without the conserved peptidase active sites. GlpG in E. coli is a rhomboid family intramembrane serine protease that has been extensively characterised as a proxy for rhomboid family proteases in animals. It efficiently cleaves eukaryote-derived model su...

[ "GO:0004252", "GO:0006508", "GO:0016020" ]

[ "serine-type endopeptidase activity", "proteolysis", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01594", "TIGR04239" ]

[ "Rhomboid_GlpG", "rhombo_GlpG" ]

[ 1279, 2155 ]

2

[ "EC" ]

[ "3.4.21.105" ]

[ "EC:3.4.21.105" ]

1

[ "2ic8", "2irv", "2nrf", "2o7l", "2xov", "2xow", "2xtu", "2xtv", "3b44", "3b45", "3txt", "3ubb", "3zeb", "3zmh", "3zmi", "3zmj", "3zot", "4h1d", "4njn", "4njp", "4qnz", "4qo0", "4qo2", "5f5b", "5f5d", "5f5g", "5f5j", "5f5k", "5mt6", "5mt7", "5mt8", "5mtf"...

47

[ "PUB00054935", "PUB00060488" ]

[ "21256137", "19919105" ]

[ "Structure of rhomboid protease in a lipid environment.", "Cleavage of a multispanning membrane protein by an intramembrane serine protease." ]

[ 2011, 2009 ]

2

[]

0

null

[ "Bacteria", "Beauveria bassiana D1-5", "marine sediment metagenome" ]

[ 2152, 1, 2 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Rhomboid protease GlpG

Rhomboid_protease_GlpG

8

IPR023664

23,664

Murein transglycosylase-C

Murein_transglycosylaseC

Family

1,355

false

Membrane-bound lytic murein transglycosylase C or murein hydrolase C is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division.

[ "GO:0016798", "GO:0016998", "GO:0009279" ]

[ "hydrolase activity, acting on glycosyl bonds", "cell wall macromolecule catabolic process", "cell outer membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_01616" ]

[ "MltC" ]

[ 1355 ]

1

[]

0

[ "4c5f", "4cfo", "4cfp", "4chx" ]

4

[]

0

[]

0

null

[ "Bacteria" ]

[ 1355 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Murein transglycosylase-C

Murein_transglycosylaseC

9

IPR023665

23,665

2,3-bisphosphoglycerate-independent phosphoglycerate mutase, prokaryotes

ApgAM_prokaryotes

Family

2,118

false

This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from baceria and archaea. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase is a metalloenzyme found particularly in archaea and some eubacteria. It is responsble for the interconversion of 2-phosphoglycerate and 3-phosphoglyce...

[]

0

[ "HAMAP", "HAMAP", "NCBIFAM" ]

[ "MF_01402_A", "MF_01402_B", "TIGR02535" ]

[ "ApgM_A", "ApgM_B", "hyp_Hser_kinase" ]

[ 540, 198, 1495 ]

3

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "5.4.2.12", "PWY-1042", "PWY-2221", "PWY-5484", "PWY-5723", "PWY-6142", "PWY-6886", "PWY-6901", "PWY-7003", "PWY-7124", "PWY-7218", "PWY-8362", "PWY-8404" ]

[ "EC:5.4.2.12", "METACYC:PWY-1042", "METACYC:PWY-2221", "METACYC:PWY-5484", "METACYC:PWY-5723", "METACYC:PWY-6142", "METACYC:PWY-6886", "METACYC:PWY-6901", "METACYC:PWY-7003", "METACYC:PWY-7124", "METACYC:PWY-7218", "METACYC:PWY-8362", "METACYC:PWY-8404" ]

13

[ "2zkt", "3idd", "3kd8" ]

3

[ "PUB00014397", "PUB00014447", "PUB00014464", "PUB00055097" ]

[ "12076796", "12062435", "12644480", "17576516" ]

[ "Molecular characterization of phosphoglycerate mutase in archaea.", "A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity.", "Phosphoprotein with phosphoglycerate mutase activity from the archaeon Sulfolobus solfataricus.", "Characte...

[ 2002, 2002, 2003, 2007 ]

4

[ "IPR004456" ]

[]

1

0

1

[ "Archaea", "Bacteria", "unclassified sequences" ]

[ 525, 1539, 54 ]

3

[]

0

true

Family

2,3-bisphosphoglycerate-independent phosphoglycerate mutase, prokaryotes

ApgAM_prokaryotes

5

IPR023666

23,666

Phosphoglucosamine mutase, archaeal

GlmM_arc

Family

164

false

The alpha-D-phosphohexomutase superfamily is composed of four related enzymes, each of which catalyses a phosphoryl transfer on their sugar substrates: phosphoglucomutase (PGM), phosphoglucomutase/phosphomannomutase (PGM/PMM), phosphoglucosamine mutase (PNGM), and phosphoacetylglucosamine mutase (PAGM) [ ]. PGM ( ) con...

[ "GO:0000287", "GO:0008966", "GO:0005975" ]

[ "magnesium ion binding", "phosphoglucosamine mutase activity", "carbohydrate metabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP" ]

[ "MF_01554_A" ]

[ "GlmM_A" ]

[ 164 ]

1

[ "EC", "METACYC" ]

[ "5.4.2.10", "PWY-6749" ]

[ "EC:5.4.2.10", "METACYC:PWY-6749" ]

2

[]

0

[ "PUB00022429", "PUB00037156", "PUB00040705", "PUB00042561", "PUB00042562", "PUB00042563", "PUB00042564", "PUB00054937" ]

[ "14725765", "15299905", "16595672", "10506283", "10913078", "11004509", "15238632", "18263721" ]

[ "Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.", "Structure of rabbit muscle phosphoglucomutase refined at 2.4 A resolution.", "The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme.", "Functional divers...

[ 2004, 1997, 2006, 1999, 2000, 2000, 2004, 2008 ]

8

[ "IPR005841" ]

[]

1

0

1

[ "Methanobacteriota", "bioreactor metagenome" ]

[ 163, 1 ]

2

[]

0

true

Family

Phosphoglucosamine mutase, archaeal

GlmM_arc

7

IPR023667

23,667

NAD-dependent malic enzyme, proteobacteria

NAD_malic_enz_proteobac

Family

2,276

false

Proteobacteria NAD-dependent malic enzymes use divalent metal cations as cofactor, with a preference for magnesium or manganese [ ]. They are non-competitively inhibited by high concentrations of NAD+ and L-malate, and activated by aspartate [ , ].

[ "GO:0004471" ]

[ "malate dehydrogenase (decarboxylating) (NAD+) activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01619" ]

[ "NAD_malic_enz" ]

[ 2276 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "1.1.1.38", "PWY-3641", "PWY-7115", "PWY-7118", "PWY-7384", "PWY-7686" ]

[ "EC:1.1.1.38", "METACYC:PWY-3641", "METACYC:PWY-7115", "METACYC:PWY-7118", "METACYC:PWY-7384", "METACYC:PWY-7686" ]

6

[ "6ags" ]

1

[ "PUB00054936", "PUB00054938" ]

[ "17557829", "17215140" ]

[ "Escherichia coli malic enzymes: two isoforms with substantial differences in kinetic properties, metabolic regulation, and structure.", "Over-expression, purification, and characterization of recombinant NAD-malic enzyme from Escherichia coli K12." ]

[ 2007, 2007 ]

2

[ "IPR001891" ]

[]

1

0

1

[ "Bacteria", "Eukaryota" ]

[ 2272, 4 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

NAD-dependent malic enzyme, proteobacteria

NAD_malic_enz_proteobac

2

IPR023668

23,668

Altronate oxidoreductase

Altronate_OxRdtase

Family

993

false

This entry represents a family of bacterial altronate (also known as tagaturonate) oxidoreductases. They are responsible for the NAD-dependent reduction of D-altronate.

[ "GO:0009026" ]

[ "tagaturonate reductase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00670" ]

[ "Altron_oxidoreduct" ]

[ 993 ]

1

[ "EC" ]

[ "1.1.1.58" ]

[ "EC:1.1.1.58" ]

1

[]

0

[]

0

[]

0

null

[ "Bacteria", "Siphoviridae sp. ctCCX1", "termite gut metagenome" ]

[ 989, 2, 2 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Altronate oxidoreductase

Altronate_OxRdtase

8

IPR023669

23,669

Large ribosomal subunit protein uL1, archaea

Ribosomal_uL1_arc

Family

898

false

This entry represents ribosomal uL1 from the archaea; it binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and it is involved in E site tRNA release [ , ]. Ribosomal protein uL1 (also known as L1) is the largest protein from the large ribosomal subunit. The uL1 protein contains two domains: 2-la...

[ "GO:0003723", "GO:0003735", "GO:0006412", "GO:0015934" ]

[ "RNA binding", "structural constituent of ribosome", "translation", "large ribosomal subunit" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_01318_A", "NF003244" ]

[ "Ribosomal_uL1_A", "PRK04203.1" ]

[ 879, 898 ]

2

[]

0

[ "1cjs", "1dwu", "1i2a", "1mzp", "1u63", "4d5y", "4d67", "4lq4", "4ujc", "4ujd", "4uje", "4v49", "4v4a", "4v4g", "4v4n", "4v5z", "4v65", "4v66", "4v6u", "8hku", "8hky", "8hkz", "8hl1", "8hl2", "8hl3", "8hl4", "8hl5" ]

27

[ "PUB00000254", "PUB00001280", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00029919", "PUB00031674", "PUB00039425", "PUB00153323", "PUB00153324" ]

[ "8607874", "8635468", "11297922", "11290319", "11114498", "12859903", "15659579", "16272117", "36817958", "29456023" ]

[ "The primary structure of rat ribosomal protein L10a.", "Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Locking and ...

[ 1996, 1996, 2001, 2001, 2000, 2003, 2005, 2005, 2023, 2018 ]

10

[ "IPR002143" ]

[]

1

0

1

[ "Archaea", "Candidatus Rhodobacter oscarellae", "Metazoa", "unclassified sequences" ]

[ 873, 1, 4, 20 ]

4

[]

0

true

Family

Large ribosomal subunit protein uL1, archaea

Ribosomal_uL1_arc

5

IPR023670

23,670

Tyrosine recombinase XerS

Recomb_XerS

Family

546

false

This entry represents the site-specific tyrosine recombinase XerS, which is part of the broader 'phage' integrase family. It acts by catalyzing the cutting and rejoining of recombining DNA molecules. It is essential for converting dimers of the bacterial chromosome into monomers to permit their segregation at cell divi...

[ "GO:0006310", "GO:0007059", "GO:0015074", "GO:0051301" ]

[ "DNA recombination", "chromosome segregation", "DNA integration", "cell division" ]

[ "biological_process", "biological_process", "biological_process", "biological_process" ]

4

[ "HAMAP" ]

[ "MF_01816" ]

[ "Recomb_XerS" ]

[ 546 ]

1

[]

0

[]

0

[ "PUB00054973" ]

[ "17630835" ]

[ "The unconventional Xer recombination machinery of Streptococci/Lactococci." ]

[ 2007 ]

1

[]

0

null

[ "Bacteria" ]

[ 546 ]

1

[]

0

true

Family

Tyrosine recombinase XerS

Recomb_XerS

3

IPR023671

23,671

ATPase RavA

ATPase_RavA

Family

637

false

ATPase RavA or regulatory ATPase variant A functions as an ATPase. It may play a role in metal insertion (metal-chelatase) or as a chaperone. RavA forms a complex with CadA, which represents a possible means of regulating RavA activity in response to acid stress conditions. This interaction results in an increase in Ra...

[ "GO:0016887", "GO:0005737" ]

[ "ATP hydrolysis activity", "cytoplasm" ]

[ "molecular_function", "cellular_component" ]

2

[ "HAMAP" ]

[ "MF_01625" ]

[ "ATPase_RavA" ]

[ 637 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "3.6.1.-", "PWY-5757", "PWY-6147", "PWY-6383", "PWY-6797", "PWY-7206", "PWY-7419", "PWY-7539", "PWY-7719", "PWY-7821", "PWY-8289" ]

[ "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" ]

11

[ "3nbx", "4upb", "6q7l", "6q7m", "6sza", "6szb" ]

6

[ "PUB00043412" ]

[ "16301313" ]

[ "Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase." ]

[ 2006 ]

1

[]

0

null

[ "Enterobacterales" ]

[ 637 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

ATPase RavA

ATPase_RavA

3

IPR023672

23,672

Large ribosomal subunit protein uL2, archaea/eukaryota

Ribosomal_uL2_arc_euk

Family

4,181

false

Ribosomal protein uL2 is one of the proteins from the large ribosomal subunit. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [ ], groups: Eubacterial uL2. Algal and plant chloroplast uL2. Cyanelle uL2. Archaebacterial uL2. Plant uL2. Slime mold uL2. Marchantia polymorpha mito...

[ "GO:0003723", "GO:0003735", "GO:0006412", "GO:0015934" ]

[ "RNA binding", "structural constituent of ribosome", "translation", "large ribosomal subunit" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_01320_A", "NF007180" ]

[ "Ribosomal_uL2_A", "PRK09612.1" ]

[ 2356, 4180 ]

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-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-9629569", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-9629569", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-7...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-9629569", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72...

73

[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...

376

[ "PUB00004403", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "1579444", "11297922", "11290319", "11114498" ]

[ "cDNA nucleotide sequence and expression of a tobacco cytoplasmic ribosomal protein L2 gene.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 1992, 2001, 2001, 2000 ]

4

[ "IPR002171" ]

[]

1

0

1

[ "Archaea", "Eukaryota", "ecological metagenomes" ]

[ 908, 3249, 24 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 7, 1, 1, 1, 1, 3, 2, 3, 6 ]

9

true

Family

Large ribosomal subunit protein uL2, archaea/eukaryota

Ribosomal_uL2_arc_euk

1

IPR023673

23,673

Large ribosomal subunit protein uL1, conserved site

Ribosomal_uL1_CS

Conserved_site

30,435

false

Ribosomal protein uL1 is the largest protein from the large ribosomal subunit. In Escherichia coli, uL1 is known to bind to the 23S rRNA [ , ] This entry represents the best conserved region located in the central section of these proteins, at the end of an α-helix thought to be involved in RNA-binding. Ribosomes are t...

[]

0

[ "PROSITE" ]

[ "PS01199" ]

[ "RIBOSOMAL_L1" ]

[ 30435 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DRE-156827", "R-DRE-1799339", "R-DRE-72689", "R-DRE-975956", "R-DRE-9759...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-9759...

57

[ "1ad2", "1cjs", "1dwu", "1eg0", "1i2a", "1ml5", "1mzp", "1u63", "1zho", "2hw8", "2noq", "2om7", "2rdo", "3j0l", "3j0o", "3j0p", "3j0q", "3j3v", "3j3w", "3j46", "3j5s", "3j6x", "3j6y", "3j77", "3j78", "3j7r", "3j8g", "3j9z", "3ja1", "3jcd", "3jce", "3qoy"...

477

[ "PUB00000254", "PUB00001280", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "8607874", "8635468", "11297922", "11290319", "11114498" ]

[ "The primary structure of rat ribosomal protein L10a.", "Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 1996, 1996, 2001, 2001, 2000 ]

5

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 757, 22454, 6779, 445 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae ...

[ 10, 3, 3, 2, 2, 6, 1, 13, 7, 3, 2, 29 ]

12

true

Conserved_site

Large ribosomal subunit protein uL1, conserved site

Ribosomal_uL1_CS

8

IPR023676

23,676

Small ribosomal subunit protein uS14, archaea

Ribosomal_uS14_arc

Family

1,530

false

The entry includes the small ribosomal subunit protein uS14 from archaea, which belong to the zinc-binding subfamily of ribosomal protein uS14. They bind 1 zinc ion per subunit and bind to the 16S rRNA. uS14 is required for the assembly of 30S particles and may also be responsible for determining the conformation of th...

[ "GO:0003723", "GO:0003735", "GO:0006412", "GO:0015935" ]

[ "RNA binding", "structural constituent of ribosome", "translation", "small ribosomal subunit" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "HAMAP" ]

[ "MF_01364_A" ]

[ "Ribosomal_uS14_2_A" ]

[ 1530 ]

1

[]

0

[ "4v4n", "4v6u", "5jb3", "5jbh", "6skf", "6skg", "6sw9", "6swc", "6swe", "6th6", "6tmf", "7oyc", "7zag", "7zah", "7zai", "7zhg", "8hkx", "8hky", "8hkz", "8hl1", "8hl2", "8hl3", "8hl4", "8hl5", "8wkp", "8wq2", "8wq4", "9e71", "9e7f", "9fhl", "9fny", "9fnz"...

44

[ "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "11297922", "11290319", "11114498" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 2001, 2001, 2000 ]

3

[ "IPR039744" ]

[]

1

0

1

[ "Archaea", "Eukaryota", "ecological metagenomes" ]

[ 774, 750, 6 ]

3

[ "Arabidopsis thaliana", "Homo sapiens", "Oryza sativa subsp. japonica" ]

[ 3, 1, 2 ]

3

true

Family

Small ribosomal subunit protein uS14, archaea

Ribosomal_uS14_arc

7

IPR023677

23,677

UbiD decarboxylyase, bacteria

UbiD_bacteria

Family

4,642

false

3-octaprenyl-4-hydroxybenzoate carboxy-lyase (also known as UbiD) catalyses the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol. It is involved in ubiquinone biosynthesis [ ].

[ "GO:0008694", "GO:0006744", "GO:0005886" ]

[ "4-hydroxy-3-polyprenylbenzoate decarboxylase activity", "ubiquinone biosynthetic process", "plasma membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_01636" ]

[ "UbiD" ]

[ 4642 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "4.1.1.98", "PWY-5855", "PWY-5856", "PWY-5857", "PWY-6708", "PWY-6978" ]

[ "EC:4.1.1.98", "METACYC:PWY-5855", "METACYC:PWY-5856", "METACYC:PWY-5857", "METACYC:PWY-6708", "METACYC:PWY-6978" ]

6

[ "2idb", "5m1b", "5m1c", "5m1d", "5m1e" ]

5

[ "PUB00008052" ]

[ "11029449" ]

[ "Identification of the ubiD gene on the Escherichia coli chromosome." ]

[ 2000 ]

1

[ "IPR002830" ]

[]

1

0

1

[ "Bacteria", "Endopterygota", "metagenomes" ]

[ 4603, 2, 37 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

UbiD decarboxylyase, bacteria

UbiD_bacteria

1

IPR023678

23,678

Tyrosine-tRNA ligase, type 4

Tyr-tRNA-ligase_4

Family

215

false

The group of proteins in this entry are tyrosine-tRNA ligases from archaea, and they belong to tyrosine-tRNA ligases type 4. Tyrosine-tRNA ligases (TyrRS; also known as Tyrosyl-tRNA synthetases) ( ) are widely distributed, being found in archaea, bacteria and eukaryotes. TyrRS is a homodimer which attaches Tyr to the a...

[ "GO:0004831", "GO:0005524", "GO:0006437", "GO:0005737" ]

[ "tyrosine-tRNA ligase activity", "ATP binding", "tyrosyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "HAMAP" ]

[ "MF_02009" ]

[ "Tyr_tRNA_synth_type4" ]

[ 215 ]

1

[ "EC" ]

[ "6.1.1.1" ]

[ "EC:6.1.1.1" ]

1

[ "2cya", "2cyc", "7fg6" ]

3

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006465", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00055442", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10630994", "10673435", "2203971", "10447505", "11590011", "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, 2000, 1990, 1999, 2001, 2000, 2002 ]

11

[ "IPR023617" ]

[]

1

0

1

[ "Archaea", "Bacteria", "marine sediment metagenome" ]

[ 195, 19, 1 ]

3

[]

0

true

Family

Tyrosine-tRNA ligase, type 4

Tyr-tRNA-ligase_4

4

IPR023680

23,680

Purine ribonucleoside efflux pump, NepI

MFS_NepI

Family

943

false

Among the different families of transporter, only two occur ubiquitously in all classifications of organisms. These are the ATP-Binding Cassette (ABC) superfamily and the Major Facilitator Superfamily (MFS). The MFS transporters are single-polypeptide secondary carriers capable only of transporting small solutes in res...

[ "GO:0015211", "GO:0015860", "GO:0016020" ]

[ "purine nucleoside transmembrane transporter activity", "purine nucleoside transmembrane transport", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01189", "NF007578" ]

[ "MFS_NepI", "PRK10213.1" ]

[ 879, 943 ]

2

[]

0

[]

0

[ "PUB00007278", "PUB00007279", "PUB00054939", "PUB00054940", "PUB00097927" ]

[ "9529885", "9868370", "16040204", "20814730", "32205149" ]

[ "Major facilitator superfamily.", "Sugar transporters from bacteria, parasites and mammals: structure-activity relationships.", "The yicM (nepI) gene of Escherichia coli encodes a major facilitator superfamily protein involved in efflux of purine ribonucleosides.", "Enhancement of extracellular purine nucleos...

[ 1998, 1998, 2005, 2011, 2020 ]

5

[ "IPR011701" ]

[]

1

0

1

[ "Gammaproteobacteria", "Opisthokonta" ]

[ 941, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Purine ribonucleoside efflux pump, NepI

MFS_NepI

5

IPR023684

23,684

Tyrosine-tRNA ligase, type 3

Tyr-tRNA-ligase_3

Family

544

false

The group of proteins in this entry are tyrosine-tRNA ligases from archaea, and they belong to tyrosine-tRNA ligases type 3. Tyrosine-tRNA ligases (TyrRS; also known as Tyrosyl-tRNA synthetases) ( ) are widely distributed, being found in archaea, bacteria and eukaryotes. TyrRS is a homodimer which attaches Tyr to the a...

[ "GO:0004831", "GO:0005524", "GO:0006437", "GO:0005737" ]

[ "tyrosine-tRNA ligase activity", "ATP binding", "tyrosyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "HAMAP" ]

[ "MF_02008" ]

[ "Tyr_tRNA_synth_type3" ]

[ 544 ]

1

[ "EC" ]

[ "6.1.1.1" ]

[ "EC:6.1.1.1" ]

1

[ "1j1u", "1u7d", "1u7x", "1zh0", "1zh6", "2ag6", "2cyb", "2hgz", "2pxh", "2zp1", "3d6u", "3d6v", "3n2y", "3qe4", "4hjr", "4hjx", "4hk4", "4hpw", "4nd6", "4nd7", "4nda", "4nx2", "4pbr", "4pbs", "4pbt", "5l7p", "5n5u", "5n5v", "5nsf", "5u36", "6wrk", "6wrn"...

38

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006465", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00055442", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10630994", "10673435", "2203971", "10447505", "11590011", "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, 2000, 1990, 1999, 2001, 2000, 2002 ]

11

[ "IPR023617" ]

[]

1

0

1

[ "Methanobacteriati", "ecological metagenomes" ]

[ 541, 3 ]

2

[]

0

true

Family

Tyrosine-tRNA ligase, type 3

Tyr-tRNA-ligase_3

8

IPR023685

23,685

Pyridoxal kinase PdxY

Pyridoxal_kinase_PdxY

Family

2,881

false

Pyridoxal phosphate is the active form of vitamin B6 (pyridoxine or pyridoxal). Pyridoxal 5'-phosphate (PLP) is a versatile catalyst, acting as a coenzyme in a multitude of reactions, including decarboxylation, deamination and transamination [ , , ]. PLP-dependent enzymes are primarily involved in the biosynthesis of a...

[ "GO:0008478", "GO:0009443" ]

[ "pyridoxal kinase activity", "pyridoxal 5'-phosphate salvage" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01639" ]

[ "PdxY" ]

[ 2881 ]

1

[ "EC", "METACYC", "METACYC" ]

[ "2.7.1.35", "PWY-7204", "PWY-7282" ]

[ "EC:2.7.1.35", "METACYC:PWY-7204", "METACYC:PWY-7282" ]

3

[ "1td2", "1vi9", "3pzs", "5b6a", "5tqi", "5trw" ]

6

[ "PUB00006322", "PUB00017544", "PUB00035504", "PUB00035505", "PUB00035506", "PUB00035507", "PUB00035508", "PUB00054941" ]

[ "7748903", "9537380", "15581583", "8690703", "15189147", "17109392", "16763894", "15249053" ]

[ "Pyridoxal phosphate-dependent enzymes.", "Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12.", "Reaction specificity in pyridoxal phosphate enzymes.", "Pyridoxal enzymes: mechani...

[ 1995, 1998, 2005, 1995, 2004, 2006, 2006, 2004 ]

8

[ "IPR004625" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "freshwater metagenome" ]

[ 2877, 3, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Pyridoxal kinase PdxY

Pyridoxal_kinase_PdxY

4

IPR023687

23,687

Oxaloacetate decarboxylase, bacterial

Oxaloacetate_deCOase_bac

Family

923

false

This entry describes a class of bacterial oxaloacetate decarboxylases from the PEP mutase/isocitrate lyase superfamily. The enzyme plays a role in the maintenance of cellular concentrations of bicarbonate and pyruvate [ ].

[ "GO:0008948" ]

[ "oxaloacetate decarboxylase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01299" ]

[ "OadC" ]

[ 923 ]

1

[ "EC", "METACYC" ]

[ "4.1.1.112", "PWY-6339" ]

[ "EC:4.1.1.112", "METACYC:PWY-6339" ]

2

[ "3b8i" ]

1

[ "PUB00050543" ]

[ "18081320" ]

[ "Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily." ]

[ 2008 ]

1

[]

0

null

[ "Pseudomonadota" ]

[ 923 ]

1

[]

0

true

Family

Oxaloacetate decarboxylase, bacterial

Oxaloacetate_deCOase_bac

8

IPR023689

23,689

2,3-diketo-L-gulonate reductase

Diketo_gul_Rdtase

Family

841

false

This entry represents a family of bacterial 2,3-diketo-L-gulonate reductases, which catalyse the reduction of 2,3-diketo-L-gulonate in the presence of NADH [ ]. The gene operon yiaK-S (of which yiaK encodes for the 2,3-diketo-L-gulonate reductase) is believed to encode proteins which are involved in the utilisation of ...

[ "GO:0016616", "GO:0047559", "GO:0070403" ]

[ "oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor", "3-dehydro-L-gulonate 2-dehydrogenase activity", "NAD+ binding" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "HAMAP" ]

[ "MF_00820" ]

[ "Diketo_gul_reduc" ]

[ 841 ]

1

[ "EC", "METACYC" ]

[ "1.1.1.130", "PWY-6961" ]

[ "EC:1.1.1.130", "METACYC:PWY-6961" ]

2

[ "1nxu", "1s20" ]

2

[ "PUB00009905", "PUB00029265" ]

[ "11741871", "14718529" ]

[ "Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons.", "A novel NAD-binding protein revealed by the crystal structure of 2,3-diketo-L-gulonate reductase (YiaK)." ]

[ 2002, 2004 ]

2

[ "IPR003767" ]

[]

1

0

1

[ "Pseudomonadota" ]

[ 841 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

2,3-diketo-L-gulonate reductase

Diketo_gul_Rdtase

2

IPR023690

23,690

Cytoskeleton protein RodZ

RodZ

Family

1,108

false

RodZ are cytoskeletal proteins that are involved in bacterial cell-shape control through regulation of the length of the long axis [ ]. They are transmembrane proteins, with a cytoplasmic N-terminal domain that includes a helix-turn-helix motif, and a large periplasmic C-terminal domain.

[ "GO:0008360", "GO:0016020" ]

[ "regulation of cell shape", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "HAMAP" ]

[ "MF_02017" ]

[ "RodZ" ]

[ 1108 ]

1

[]

0

[]

0

[ "PUB00054942" ]

[ "19008860" ]

[ "Determination of bacterial rod shape by a novel cytoskeletal membrane protein." ]

[ 2008 ]

1

[]

0

null

[ "Gammaproteobacteria", "Opisthokonta", "human gut metagenome" ]

[ 1104, 3, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Cytoskeleton protein RodZ

RodZ

2

IPR023691

23,691

ABC transporter, vitamin B12 import, permease protein BtuC

ABC_transptr_BtuC

Family

1,747

false

ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily, which uses the hydrolysis of ATP to energise diverse biological systems. ABC transporters minimally consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These can be found o...

[ "GO:0015889", "GO:0016020" ]

[ "cobalamin transport", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01004", "NF003001" ]

[ "BtuC", "PRK03784.1" ]

[ 1577, 1747 ]

2

[ "GP", "GP" ]

[ "GenProp1150", "GenProp1156" ]

[ "GP:GenProp1150", "GP:GenProp1156" ]

2

[ "1l7v", "2qi9", "4dbl", "4fi3", "4r9u" ]

5

[ "PUB00006343", "PUB00015401", "PUB00015423", "PUB00026953", "PUB00062318" ]

[ "8596459", "15475351", "12475936", "12004122", "3528128" ]

[ "Differential expression of two siderophore-dependent iron-acquisition pathways in Erwinia chrysanthemi 3937: characterization of a novel ferrisiderophore permease of the ABC transporter family.", "FhuD1, a ferric hydroxamate-binding lipoprotein in Staphylococcus aureus: a case of gene duplication and lateral tra...

[ 1995, 2004, 2002, 2002, 1986 ]

5

[ "IPR000522" ]

[]

1

0

1

[ "Bacteria" ]

[ 1747 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

ABC transporter, vitamin B12 import, permease protein BtuC

ABC_transptr_BtuC

2

IPR023692

23,692

Multidrug resistance protein MdtG

Mutidrug-R_MdtG

Family

1,150

false

MdtG is found in enterobacteria and confers resistance to fosfomycin and deoxycholate [ ]. It belongs to the major facilitator superfamily.

[ "GO:0005886" ]

[ "plasma membrane" ]

[ "cellular_component" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01528", "NF007372" ]

[ "MFS_MdtG", "PRK09874.1" ]

[ 1055, 1150 ]

2

[]

0

[]

0

[ "PUB00053912" ]

[ "11566977" ]

[ "Analysis of a complete library of putative drug transporter genes in Escherichia coli." ]

[ 2001 ]

1

[ "IPR001958" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta" ]

[ 1148, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Multidrug resistance protein MdtG

Mutidrug-R_MdtG

5

IPR023693

23,693

ABC transporter, vitamin B12, BtuD

ABC_transptr_BtuD

Family

1,586

false

This entry represents bacterial BtuD, which is the ATP-binding cassette component of the vitamin B12 ABC transport system, involved in vitamin B12 import. It is responsible for energy coupling to the transport system [ ]. Most bacterial importers employ a periplasmic substrate-binding protein (PBP) that delivers the li...

[ "GO:0005524", "GO:0016887", "GO:0015889" ]

[ "ATP binding", "ATP hydrolysis activity", "cobalamin transport" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01005", "NF002981" ]

[ "BtuD", "PRK03695.1" ]

[ 1540, 1585 ]

2

[ "EC", "GP", "GP" ]

[ "7.6.2.8", "GenProp1150", "GenProp1156" ]

[ "EC:7.6.2.8", "GP:GenProp1150", "GP:GenProp1156" ]

3

[ "1l7v", "2qi9", "4dbl", "4fi3", "4r9u" ]

5

[ "PUB00004290", "PUB00006343", "PUB00014769", "PUB00015401", "PUB00015402", "PUB00015423", "PUB00017894", "PUB00017895", "PUB00017896", "PUB00017897", "PUB00017898", "PUB00017899", "PUB00025109", "PUB00026406", "PUB00026953", "PUB00043654" ]

[ "9872322", "8596459", "9873074", "15475351", "12468528", "12475936", "11421269", "1282354", "9640644", "11988180", "11470432", "11402022", "11080142", "11532960", "12004122", "11421270" ]

[ "Crystal structure of the ATP-binding subunit of an ABC transporter.", "Differential expression of two siderophore-dependent iron-acquisition pathways in Erwinia chrysanthemi 3937: characterization of a novel ferrisiderophore permease of the ABC transporter family.", "Getting in or out: early segregation betwee...

[ 1998, 1995, 1999, 2004, 2003, 2002, 2001, 1992, 1998, 2002, 2001, 2001, 2000, 2001, 2002, 2001 ]

16

[]

0

null

[ "Bacteria" ]

[ 1586 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

ABC transporter, vitamin B12, BtuD

ABC_transptr_BtuD

9

IPR023694

23,694

Agmatinase

Family

1,044

false

This enzyme belongs to the arginase family and more specifically the agmatinase (agmatine ureohydrolase ) subfamily. Agmatinase catalyses the hydrolysis of agmatine to putrescine and urea. Manganese is required as a cofactor in this reaction [ ]. Agmatinase may play important regulatory roles by modulating the cellular...

[ "GO:0008783", "GO:0030145", "GO:0009446" ]

[ "agmatinase activity", "manganese ion binding", "putrescine biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP" ]

[ "MF_01418" ]

[ "SpeB" ]

[ 1044 ]

1

[ "EC", "METACYC" ]

[ "3.5.3.11", "PWY-40" ]

[ "EC:3.5.3.11", "METACYC:PWY-40" ]

2

[ "7lba", "7lol", "7lox" ]

3

[ "PUB00054978", "PUB00055103" ]

[ "10329468", "3081491" ]

[ "Manganese is essential for catalytic activity of Escherichia coli agmatinase.", "Purification and properties of agmatine ureohydrolyase, a putrescine biosynthetic enzyme in Escherichia coli." ]

[ 1999, 1986 ]

2

[ "IPR005925" ]

[]

1

0

1

[ "Bacteria" ]

[ 1044 ]

1

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Agmatinase

6

IPR023695

23,695

Thiosulfate sulfurtransferase, bacterial

Thiosulf_sulfurTrfase

Family

4,406

false

This entry represents the GlpE cytoplasmic bacterial family of rhodanese thiosulphate sulphurtransferases [ ]. They are responsible for the transfer of sulphur from thiosulphate to thiophilic acceptors. The related periplasmic thiosulphate sulphurtransferases, PspE, are responsible for a much greater proportion of rhod...

[ "GO:0004792", "GO:0005737" ]

[ "thiosulfate-cyanide sulfurtransferase activity", "cytoplasm" ]

[ "molecular_function", "cellular_component" ]

2

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_01009", "NF001195", "cd01444" ]

[ "Thiosulf_sulfurtr", "PRK00162.1", "GlpE_ST" ]

[ 3048, 3241, 4392 ]

3

[ "EC", "METACYC", "METACYC" ]

[ "2.8.1.1", "PWY-5350", "PWY-7927" ]

[ "EC:2.8.1.1", "METACYC:PWY-5350", "METACYC:PWY-7927" ]

3

[ "1gmx", "1gn0" ]

2

[ "PUB00017928", "PUB00054943", "PUB00055085", "PUB00104064" ]

[ "11709175", "19088907", "10735872", "11092948" ]

[ "Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily.", "Biochemical and Genetic Characterization of PspE and GlpE, Two Single-domain Sulfurtransferases of Escherichia coli.", "Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia co...

[ 2001, 2008, 2000, 2000 ]

4

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 4378, 2, 26 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Thiosulfate sulfurtransferase, bacterial

Thiosulf_sulfurTrfase

2

IPR023696

23,696

Ureohydrolase domain superfamily

Ureohydrolase_dom_sf

Homologous_superfamily

121,103

false

This entry represents hydrolases that cleave carbon-nitrogen bonds other than peptide bonds ([ec:3.5.-.-]). It includes mainly members of the ureohydrolase superfamily. It also represents the histone deacetylase family ( ) and other related hydrolases. The ureohydrolase superfamily includes arginase ( ), agmatinase ( )...

[]

0

[ "SSF" ]

[ "SSF52768" ]

[ "" ]

[ 121103 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "3.5.3", "R-BTA-1538133", "R-BTA-201722", "R-BTA-2173795", "R-BTA-3214815", "R-BTA-350054", "R-BTA-3769402", "R-BTA-4551638", "R-BTA-6798695", "R-BTA-6804758", "R-BTA-70635", "R-BTA-73762", "R-BTA-8936459", "R-BTA-8943724", "R-BTA-9018519", "R-BTA-9022692", "R-BTA-9701898", "R-BTA-...

[ "EC:3.5.3", "REACTOME:R-BTA-1538133", "REACTOME:R-BTA-201722", "REACTOME:R-BTA-2173795", "REACTOME:R-BTA-3214815", "REACTOME:R-BTA-350054", "REACTOME:R-BTA-3769402", "REACTOME:R-BTA-4551638", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6804758", "REACTOME:R-BTA-70635", "REACTOME:R-BTA-73762", ...

233

[ "1c3p", "1c3r", "1c3s", "1cev", "1d3v", "1gq6", "1gq7", "1hq5", "1hqf", "1hqg", "1hqh", "1hqx", "1p8m", "1p8n", "1p8o", "1p8p", "1p8q", "1p8r", "1p8s", "1pq3", "1r1o", "1rla", "1t4p", "1t4r", "1t4s", "1t4t", "1t5f", "1t5g", "1t64", "1t67", "1t69", "1ta1"...

584

[ "PUB00001437", "PUB00025337", "PUB00028086", "PUB00028087" ]

[ "7916684", "12020346", "15355972", "16141327" ]

[ "Developmental and hormonal regulation of the Xenopus liver-type arginase gene.", "Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis.", "Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ur...

[ 1993, 2002, 2004, 2005 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 2745, 62875, 54032, 45, 1406 ]

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",...

[ 65, 11, 54, 54, 2, 137, 61, 9, 49, 89, 6, 8, 102 ]

13

true

Homologous_superfamily

Ureohydrolase domain superfamily

Ureohydrolase_dom_sf

4

IPR023697

23,697

Multidrug resistance protein MdtL

Multidrug-R_MdtL

Family

937

false

MdtL confers resistance to chloramphenicol [ ].

[ "GO:0005886" ]

[ "plasma membrane" ]

[ "cellular_component" ]

1

[ "HAMAP" ]

[ "MF_01530" ]

[ "MFS_MdtL" ]

[ 937 ]

1

[]

0

[]

0

[ "PUB00053912" ]

[ "11566977" ]

[ "Analysis of a complete library of putative drug transporter genes in Escherichia coli." ]

[ 2001 ]

1

[ "IPR011701" ]

[]

1

0

1

[ "Bacteria", "Trichuris trichiura" ]

[ 936, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Multidrug resistance protein MdtL

Multidrug-R_MdtL

6

IPR023698

23,698

3-isopropylmalate dehydrogenase, actinobacteria

LeuB_actb

Family

3,562

false

This entry represents 3-isopropylmalate dehydrogenases found in actinobacteria. This enzyme is responsible for the catalysis of 3-isopropylmalate to 3-carboxy-4-methyl-2-oxopentanoate [ ].

[ "GO:0003862", "GO:0009098" ]

[ "3-isopropylmalate dehydrogenase activity", "L-leucine biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01035" ]

[ "LeuB_type2" ]

[ 3562 ]

1

[ "EC", "METACYC" ]

[ "1.1.1.85", "PWY-7396" ]

[ "EC:1.1.1.85", "METACYC:PWY-7396" ]

2

[ "1w0d", "2g4o" ]

2

[ "PUB00032144" ]

[ "15663922" ]

[ "The high-resolution Structure of LeuB (Rv2995c) from Mycobacterium tuberculosis." ]

[ 2005 ]

1

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 3545, 17 ]

2

[]

0

true

Family

3-isopropylmalate dehydrogenase, actinobacteria

LeuB_actb

1

IPR023699

23,699

Transcription activator HTH, RhaR

Tscrpt_act_RhaR

Family

1,048

false

RhaR activates expression of the rhaSR operon in response to L-rhamnose [ , ]. It is one of numerous bacterial transcription regulatory proteins that bind DNA via a helix-turn-helix (HTH) motif.

[ "GO:0003700", "GO:0045893", "GO:0005737" ]

[ "DNA-binding transcription factor activity", "positive regulation of DNA-templated transcription", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_01533" ]

[ "HTH_type_RhaR" ]

[ 1048 ]

1

[]

0

[]

0

[ "PUB00013420", "PUB00054944" ]

[ "8757746", "8230210" ]

[ "Transcriptional regulation of the Escherichia coli rhaT gene.", "A regulatory cascade in the induction of rhaBAD." ]

[ 1996, 1993 ]

2

[]

0

null

[ "Pseudomonadati", "human gut metagenome" ]

[ 1047, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Transcription activator HTH, RhaR

Tscrpt_act_RhaR

7

IPR023700

23,700

Divalent cation tolerance protein CutA, Enterobacteria

CutA_Enterobact

Family

899

false

This entry represents CutA, which is involved in resistance toward heavy metals [ ]. It binds 1 copper ion per subunit. Similar sequences to CutA are found in several genomes. The metal binding sites are not conserved in many of the family members and their is currently unknown.

[ "GO:0005507", "GO:0005737" ]

[ "copper ion binding", "cytoplasm" ]

[ "molecular_function", "cellular_component" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01160", "NF007930" ]

[ "CutA", "PRK10645.1" ]

[ 860, 899 ]

2

[]

0

[ "1naq", "3aa8", "3aa9", "3ah6", "3gsd", "3opk", "3x3u", "4y65", "4y6i" ]

9

[ "PUB00007506", "PUB00014093" ]

[ "7623666", "12949080" ]

[ "Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12.", "The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction." ]

[ 1995, 2003 ]

2

[ "IPR004323" ]

[]

1

0

1

[ "Bacteria" ]

[ 899 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Divalent cation tolerance protein CutA, Enterobacteria

CutA_Enterobact

1

IPR023701

23,701

4-hydroxy-2-oxo-heptane-1,7-dioate aldolase, Enterobacteriales

HKHD_aldolase_ent

Family

727

false

This entry represents the aldolase which performs the final step unique to the 4-hydroxyphenylacetic acid catabolism pathway in which 2,4-dihydroxyhept-2-ene-1,7-dioic acid is split into pyruvate and succinate-semialdehyde [ ]. The gene for this enzyme is generally found adjacent to other genes for this pathway [ ]. Th...

[ "GO:0016832", "GO:0010124" ]

[ "aldehyde-lyase activity", "phenylacetate catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01292" ]

[ "HKHD_aldolase" ]

[ 727 ]

1

[ "EC" ]

[ "4.1.2.52" ]

[ "EC:4.1.2.52" ]

1

[ "2v5j", "2v5k" ]

2

[ "PUB00055089", "PUB00055090" ]

[ "15996099", "20364820" ]

[ "Purification and biochemical characterization of a pyruvate-specific class II aldolase, HpaI.", "Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling." ]

[ 2005, 2010 ]

2

[ "IPR012689" ]

[]

1

0

1

[ "Enterobacteriaceae" ]

[ 727 ]

1

[]

0

true

Family

4-hydroxy-2-oxo-heptane-1,7-dioate aldolase, Enterobacteriales

HKHD_aldolase_ent

9

IPR023702

23,702

D-cysteine desulphhydrase, bacterial

D_Cys_desulphydr_bac

Family

1,088

false

This entry represents a family of bacterial D-cysteine desulphydrases, which are responsible for the decomposition of D-cysteine, which is a powerful inhibitor of E. coli growth. D-cysteine is decomposed into pyruvate, H 2 S and NH 3 [ ], and restricts growth through inhibition of key amino acid biosynthethis.

[ "GO:0019148" ]

[ "D-cysteine desulfhydrase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01045" ]

[ "D_Cys_desulfhydr" ]

[ 1088 ]

1

[ "EC" ]

[ "4.4.1.15" ]

[ "EC:4.4.1.15" ]

1

[ "4d8t", "4d8u", "4d8w", "4d92", "4d96", "4d97", "4d99", "4d9b", "4d9c", "4d9e", "4d9f" ]

11

[ "PUB00017658" ]

[ "11527960" ]

[ "Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to D-cysteine." ]

[ 2001 ]

1

[ "IPR005966" ]

[]

1

0

1

[ "Gammaproteobacteria", "Opisthokonta" ]

[ 1086, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-cysteine desulphhydrase, bacterial

D_Cys_desulphydr_bac

5

IPR023703

23,703

Membrane-bound lytic murein transglycosylase F

MltF

Family

4,446

false

This entry represents membrane-bound lytic murein transglycosylase F (MltF). In Escherichia coli, MltF function as an lytic transglycosylases; it degrades peptidoglycan producing 1,6-anhydromuramoyl residues in the process [ ].

[ "GO:0016837" ]

[ "carbon-oxygen lyase activity, acting on polysaccharides" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_02016", "NF008112" ]

[ "MltF", "PRK10859.1" ]

[ 4109, 4445 ]

2

[]

0

[ "4owd", "4oxv", "4oyv", "4oz9", "4p0g", "4p11", "5a5x", "5aa1", "5aa2", "5aa3", "5aa4" ]

11

[ "PUB00054945" ]

[ "18234673" ]

[ "The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase." ]

[ 2008 ]

1

[]

0

null

[ "Bacteria", "Opisthokonta", "unclassified sequences" ]

[ 4390, 2, 54 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Membrane-bound lytic murein transglycosylase F

MltF

8

IPR023704

23,704

Glucan biosynthesis protein G

MdoG_OpgG

Family

2,446

false

Membrane-derived oligosaccharides (MDO) are members of a family of glucans found in the periplasmic space of Gram-negative bacteria. MdoG has been shown to be necessary for the synthesis of MDO [ ], but its exact function is not known yet. This entry contains proteins that are involved in the biosynthesis of osmoregula...

[]

0

[ "HAMAP" ]

[ "MF_01069" ]

[ "MdoG_OpgG" ]

[ 2446 ]

1

[]

0

[ "1txk", "8ip2" ]

2

[ "PUB00027777" ]

[ "7934824" ]

[ "Homology between a genetic locus (mdoA) involved in the osmoregulated biosynthesis of periplasmic glucans in Escherichia coli and a genetic locus (hrpM) controlling pathogenicity of Pseudomonas syringae." ]

[ 1993 ]

1

[ "IPR014438" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta" ]

[ 2443, 3 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glucan biosynthesis protein G

MdoG_OpgG

8

IPR023705

23,705

Nucleoid occlusion protein

Nucleoid_occlusion_protein

Family

2,404

false

This entry represents nucleoid occlusion proteins belonging to the parB family. Nucleoid occlusion protein effects nucleoid occlusion by binding relatively nonspecifically to DNA and preventing the assembly of the division machinery in the vicinity of the nucleoid, especially under conditions that disturb the cell cycl...

[]

0

[ "HAMAP", "NCBIFAM" ]

[ "MF_02015", "TIGR04285" ]

[ "ParB_Noc", "nucleoid_noc" ]

[ 756, 2404 ]

2

[]

0

[ "7nfu", "7ng0", "7ol9" ]

3

[ "PUB00054946" ]

[ "15210112" ]

[ "Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis." ]

[ 2004 ]

1

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 2396, 8 ]

2

[]

0

true

Family

Nucleoid occlusion protein

Nucleoid_occlusion_protein

9

IPR023706

23,706

Para-hydroxybenzoic acid efflux pump, subunit AaeB

PHBA_efflux_pump_AaeB

Family

1,180

false

The para-hydroxybenzoic acid efflux pump's substrates are p-hydroxybenzoic acid (pHBA), 6-hydroxy-2-naphthoic and 2-hydroxycinnamate. It could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell [ ]. Both AaeB and AaeA subunits are required for t...

[ "GO:0046942", "GO:0005886" ]

[ "carboxylic acid transport", "plasma membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01545", "NF007916" ]

[ "AaeB", "PRK10631.1" ]

[ 1142, 1180 ]

2

[]

0

[]

0

[ "PUB00054183" ]

[ "15489430" ]

[ "Characterization of the Escherichia coli AaeAB efflux pump: a metabolic relief valve?" ]

[ 2004 ]

1

[ "IPR006726" ]

[]

1

0

1

[ "Pseudomonadota" ]

[ 1180 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Para-hydroxybenzoic acid efflux pump, subunit AaeB

PHBA_efflux_pump_AaeB

7

IPR023707

23,707

Outer membrane protein assembly factor BamA

OM_assembly_BamA

Family

14,924

false

This entry represents the BamA (also known as YaeT) family of proteins. BamA forms part of the outer membrane protein assembly complex, which is involved in assembly and insertion of β-barrel proteins into the outer membrane in Gram-negative bacteria [ ].

[ "GO:0071709" ]

[ "membrane assembly" ]

[ "biological_process" ]

1

[ "HAMAP", "PIRSF", "NCBIFAM" ]

[ "MF_01430", "PIRSF006076", "TIGR03303" ]

[ "OM_assembly_BamA", "OM_assembly_OMP85", "OM_YaeT" ]

[ 10628, 14401, 13683 ]

3

[ "GP", "GP", "REACTOME" ]

[ "GenProp0725", "GenProp1116", "R-HSA-9760173" ]

[ "GP:GenProp0725", "GP:GenProp1116", "REACTOME:R-HSA-9760173" ]

3

[ "2qcz", "2qdf", "3efc", "4c4v", "4k3b", "4k3c", "4n75", "4pk1", "4xga", "5ayw", "5d0o", "5d0q", "5ekq", "5ljo", "5or1", "6fsu", "6lyq", "6lyr", "6lys", "6lyu", "6qgw", "6qgx", "6qgy", "6smx", "6sn0", "6sn2", "6sn3", "6sn4", "6sn5", "6sn7", "6sn8", "6sn9"...

120

[ "PUB00060770", "PUB00077091" ]

[ "21823654", "23882017" ]

[ "The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of β-barrel assembly.", "Receptor polymorphism restricts contact-dependent growth inhibition to members of the same species." ]

[ 2011, 2013 ]

2

[ "IPR039910" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 14690, 29, 205 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Outer membrane protein assembly factor BamA

OM_assembly_BamA

3

IPR023709

23,709

Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase

Guo-5TP_3DP_PyrP

Family

1,936

false

Guanosine pentaphosphate (pppGpp) is a cytoplasmic signalling molecule which together with ppGpp controls the "stringent response", an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. Guanosine-5'-triphosphate,3'-diphosph...

[ "GO:0008894", "GO:0015974" ]

[ "guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity", "guanosine pentaphosphate catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01550" ]

[ "GppA" ]

[ 1936 ]

1

[ "EC" ]

[ "3.6.1.40" ]

[ "EC:3.6.1.40" ]

1

[ "6pbz" ]

1

[]

0

[ "IPR030673" ]

[]

1

0

1

[ "Bacteria", "metagenomes" ]

[ 1933, 3 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase

Guo-5TP_3DP_PyrP

6

IPR023710

23,710

Probable phosphatase YcdX

Phosphatase_YcdX_put

Family

1,815

false

This phosphatase is a homotrimer. Each subunit binds 3 zinc ions [ ].

[ "GO:0008270" ]

[ "zinc ion binding" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01561" ]

[ "YcdX_phosphat" ]

[ 1815 ]

1

[ "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"...

[ "3.1.3.-", "PWY-4702", "PWY-5491", "PWY-6148", "PWY-6352", "PWY-6365", "PWY-6366", "PWY-6368", "PWY-6456", "PWY-6575", "PWY-6627", "PWY-6664", "PWY-6686", "PWY-6720", "PWY-6724", "PWY-6955", "PWY-6990", "PWY-6991", "PWY-7018", "PWY-7119", "PWY-7321", "PWY-7531", "PWY-7771...

[ "EC:3.1.3.-", "METACYC:PWY-4702", "METACYC:PWY-5491", "METACYC:PWY-6148", "METACYC:PWY-6352", "METACYC:PWY-6365", "METACYC:PWY-6366", "METACYC:PWY-6368", "METACYC:PWY-6456", "METACYC:PWY-6575", "METACYC:PWY-6627", "METACYC:PWY-6664", "METACYC:PWY-6686", "METACYC:PWY-6720", "METACYC:PWY-6...

36

[ "1m65", "1m68", "1pb0" ]

3

[ "PUB00027226" ]

[ "12661000" ]

[ "Crystal structure of the Escherichia coli YcdX protein reveals a trinuclear zinc active site." ]

[ 2003 ]

1

[]

0

null

[ "Bacteria", "Opisthokonta", "termite gut metagenome" ]

[ 1812, 2, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Probable phosphatase YcdX

Phosphatase_YcdX_put

9

IPR023711

23,711

Transcription regulator HTH, UlaR

Tscrpt_reg_HTH_UlaR

Family

351

false

The HTH-type transcription regulator UlaR represses ulaG and the ulaABCDEF operon. Two UlaR binding sites have been identified in each promoter. Full activity requires simultaneous interaction of UlaR with both divergent promoters and seems to be dependent on repressor-mediated DNA loop formation, which is helped by th...

[ "GO:0045892", "GO:0005737" ]

[ "negative regulation of DNA-templated transcription", "cytoplasm" ]

[ "biological_process", "cellular_component" ]

2

[ "HAMAP" ]

[ "MF_01563" ]

[ "HTH_type_UlaR" ]

[ 351 ]

1

[]

0

[]

0

[ "PUB00054947", "PUB00054948", "PUB00054949" ]

[ "12374842", "12644495", "14996803" ]

[ "The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is involved in L-ascorbate metabolism in Escherichia coli.", "The ascorbate transporter of Escherichia coli.", "Regulation of expression of the divergent ulaG and ulaABCDEF operons involved in LaAscorbate dissimilation in Escherichia coli."...

[ 2002, 2003, 2004 ]

3

[]

0

null

[ "Enterobacteriaceae" ]

[ 351 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Transcription regulator HTH, UlaR

Tscrpt_reg_HTH_UlaR

3

IPR023712

23,712

3-phenylpropionate/cinnamic acid dioxygenase, beta subunit

HcaF

Family

94

false

Phenylpropanoid compounds are widely available in natural environments, and they can originate from putrefaction of proteins in soil or as breakdown products of several constituents of plants, such as lignin, various oils, and resins. Microbial catabolism of phenylpropanoid compounds plays an important role not only in...

[ "GO:0019380" ]

[ "3-phenylpropionate catabolic process" ]

[ "biological_process" ]

1

[ "HAMAP" ]

[ "MF_01649" ]

[ "HcaF" ]

[ 94 ]

1

[ "EC", "METACYC" ]

[ "1.14.12.19", "PWY-6690" ]

[ "EC:1.14.12.19", "METACYC:PWY-6690" ]

2

[ "8k0a" ]

1

[ "PUB00053145", "PUB00053146", "PUB00053147", "PUB00053148", "PUB00053149", "PUB00054929", "PUB00054961" ]

[ "4348920", "6345502", "9324265", "3531186", "8399388", "9603882", "11729263" ]

[ "The purification and properties of the flavoprotein melilotate hydroxylase.", "Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli.", "A 3-(3-hydroxyphenyl)propionic acid catabolic pathway in Rhodococcus globerulus PWD1: cloning and characterization of the hpp operon.", "Isola...

[ 1973, 1983, 1997, 1986, 1993, 1998, 2001 ]

7

[ "IPR000391" ]

[]

1

0

1

[ "Enterobacterales" ]

[ 94 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

3-phenylpropionate/cinnamic acid dioxygenase, beta subunit

HcaF

5

IPR023713

23,713

Endonuclease VIII

Endonuclease-VIII

Family

1,215

false

This entry represents the endonuclease 8 (also known as Nei) enzyme involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Endonuclease 8 acts as DNA glycosylase [ ] that recognises and removes damaged bases [ ]. The enzyme has a preference for oxidized pyrimidines, such as thymine glycol,...

[ "GO:0000703", "GO:0008270", "GO:0140078", "GO:0006284" ]

[ "oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity", "zinc ion binding", "class I DNA-(apurinic or apyrimidinic site) endonuclease activity", "base-excision repair" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "HAMAP" ]

[ "MF_01253" ]

[ "Endonuclease_8" ]

[ 1215 ]

1

[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "3.2.2.-", "4.2.99.18", "PWY-2681", "PWY-5316", "PWY-5381", "PWY-7342", "PWY-7564", "PWY-8106" ]

[ "EC:3.2.2.-", "EC:4.2.99.18", "METACYC:PWY-2681", "METACYC:PWY-5316", "METACYC:PWY-5381", "METACYC:PWY-7342", "METACYC:PWY-7564", "METACYC:PWY-8106" ]

8

[ "1k3w", "1k3x", "1q39", "1q3b", "1q3c", "2ea0", "2opf", "2oq4", "6fbu" ]

9

[ "PUB00037432", "PUB00055087", "PUB00055088" ]

[ "16145054", "17002303", "10862773" ]

[ "Structure of the uncomplexed DNA repair enzyme endonuclease VIII indicates significant interdomain flexibility.", "Catalytic mechanism of Escherichia coli endonuclease VIII: roles of the intercalation loop and the zinc finger.", "Characterization of a novel 8-oxoguanine-DNA glycosylase activity in Escherichia ...

[ 2005, 2006, 2000 ]

3

[]

0

null

[ "Gammaproteobacteria" ]

[ 1215 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Endonuclease VIII

Endonuclease-VIII

7

IPR023714

23,714

Zinc transport protein ZntB

Zn_transp_ZntB

Family

1,174

false

ZntB is integral membrane protein consisting largely of two independent domains. The first 266 amino acids form a large, highly charged domain within the cytoplasm, while the remaining 61 residues form a small membrane domain containing two membrane-spanning segments [ ]. ZntB mediates efflux of zinc ions [ ].

[ "GO:0005385", "GO:0071577", "GO:0005886" ]

[ "zinc ion transmembrane transporter activity", "zinc ion transmembrane transport", "plasma membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP" ]

[ "MF_01565" ]

[ "ZntB" ]

[ 1174 ]

1

[]

0

[ "5n9y" ]

1

[ "PUB00054950", "PUB00054951" ]

[ "12142406", "12486076" ]

[ "ZntB is a novel Zn2+ transporter in Salmonella enterica serovar Typhimurium.", "Membrane topology of the ZntB efflux system of Salmonella enterica serovar Typhimurium." ]

[ 2002, 2003 ]

2

[ "IPR002523" ]

[]

1

0

1

[ "Bacteria" ]

[ 1174 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Zinc transport protein ZntB

Zn_transp_ZntB

7