LiteFold/InterPro · Datasets at Hugging Face

IPR023456

23,456

Crotonobetaine/carnitine-CoA ligase CaiC

CaiC

Family

775

false

Many enterobacteria are able to convert carnitine, via crotonobetaine, to gamma-butyrobetaine in the presence of carbon and nitrogen sources under anaerobic conditions [ ]. In Escherichia coli the enzymes involved in this pathway are encoded by the caiTABCDE operon [ ]. The adjacent but divergent fixABCD operon also ap...

[ "GO:0016878", "GO:0051108", "GO:0051109", "GO:0009437" ]

[ "acid-thiol ligase activity", "carnitine-CoA ligase activity", "crotonobetaine-CoA ligase activity", "carnitine metabolic process" ]

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

4

[ "HAMAP" ]

[ "MF_01524" ]

[ "CaiC" ]

[ 775 ]

1

[ "EC" ]

[ "6.2.1.48" ]

[ "EC:6.2.1.48" ]

1

[]

0

[ "PUB00003866", "PUB00019325", "PUB00032362", "PUB00053911", "PUB00054253", "PUB00060763" ]

[ "7815937", "11749953", "15518548", "9037756", "12081978", "18266698" ]

[ "Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli.", "A new family of CoA-transferases.", "Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism.", "Bacterial carnitine metabolism.", "The fixA and fixB genes are necessary for anaerob...

[ 1994, 2001, 2004, 1997, 2002, 2008 ]

6

[]

0

null

[ "Enterobacterales" ]

[ 775 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Crotonobetaine/carnitine-CoA ligase CaiC

CaiC

1

IPR023457

23,457

Methionine-tRNA synthetase, type 2

Met-tRNA_synth_2

Family

19,346

false

Methionine-tRNA ligase ( ) is an alpha 2 dimer. In some species (archaea, eubacteria and eukaryotes) a coding sequence, similar to the C-terminal end of MetRS, is present as an independent gene which is a tRNA binding domain as a dimer. In eubacteria, MetRS can also be split in two sub-classes corresponding to the pres...

[ "GO:0004825" ]

[ "methionine-tRNA ligase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "PANTHER" ]

[ "MF_01228", "PTHR43326" ]

[ "Met_tRNA_synth_type2", "" ]

[ 12356, 19345 ]

2

[ "EC", "REACTOME" ]

[ "6.1.1.10", "R-HSA-379726" ]

[ "EC:6.1.1.10", "REACTOME:R-HSA-379726" ]

2

[ "1a8h", "1woy", "2csx", "2ct8", "2d54", "2d5b", "2x1l", "2x1m", "3kfl", "3vu8", "4dlp", "4eg1", "4eg3", "4eg4", "4eg5", "4eg6", "4eg7", "4eg8", "4ega", "4mvw", "4mvx", "4mvy", "4mw0", "4mw1", "4mw2", "4mw4", "4mw5", "4mw6", "4mw7", "4mw9", "4mwb", "4mwc"...

69

[ "PUB00006254", "PUB00006477", "PUB00006518", "PUB00068784" ]

[ "2254937", "10673435", "10600385", "9607323" ]

[ "Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP.", "The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.", "Crystal structure of Escherichia coli methionyl-tRNA synthetase highlig...

[ 1990, 2000, 1999, 1998 ]

4

[ "IPR014758" ]

[]

1

0

1

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

[ 47, 13791, 5025, 6, 477 ]

5

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

[ 5, 4, 2, 1, 2, 2, 1, 4, 2, 1, 1, 12 ]

12

true

Family

Methionine-tRNA synthetase, type 2

Met-tRNA_synth_2

6

IPR023458

23,458

Methionine-tRNA ligase, type 1

Met-tRNA_ligase_1

Family

23,898

false

Methionine-tRNA ligase ( ) is an alpha 2 dimer. In some species (archaea, eubacteria and eukaryotes) a coding sequence, similar to the C-terminal end of MetRS, is present as an independent gene which is a tRNA binding domain as a dimer. In eubacteria, MetRS can also be split in two sub-classes corresponding to the pres...

[ "GO:0004825" ]

[ "methionine-tRNA ligase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "PANTHER" ]

[ "MF_00098", "PTHR45765" ]

[ "Met_tRNA_synth_type1", "" ]

[ 17605, 23897 ]

2

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

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

[ "EC:6.1.1.10", "REACTOME:R-DDI-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649" ]

6

[ "1f4l", "1p7p", "1pfu", "1pfv", "1pfw", "1pfy", "1pg0", "1pg2", "1qqt", "1rqg", "3h97", "3h99", "3h9b", "3h9c", "4bl7", "4bvx", "4bvy", "5gl7", "5goy", "5urb", "5y6l", "6spn", "6spo", "6spp", "6spq", "6spr", "6wq6", "6wqi", "6wqs", "6wqt", "7ulz", "8bru"...

35

[ "PUB00006254", "PUB00006477", "PUB00006518" ]

[ "2254937", "10673435", "10600385" ]

[ "Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP.", "The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.", "Crystal structure of Escherichia coli methionyl-tRNA synthetase highlig...

[ 1990, 2000, 1999 ]

3

[ "IPR014758" ]

[]

1

0

1

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

[ 927, 16642, 5905, 32, 392 ]

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",...

[ 7, 1, 3, 2, 1, 10, 3, 1, 8, 4, 1, 1, 30 ]

13

true

Family

Methionine-tRNA ligase, type 1

Met-tRNA_ligase_1

9

IPR023459

23,459

Transcription elongation factor GreA/GreB family

Tscrpt_elong_fac_GreA/B_fam

Family

43,377

false

Bacterial proteins GreA and GreB are necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. Arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked DNA/RNA/ polymerase ternary complexes. ...

[ "GO:0070063" ]

[ "RNA polymerase binding" ]

[ "molecular_function" ]

1

[ "PIRSF", "PANTHER" ]

[ "PIRSF006092", "PTHR30437" ]

[ "GreA_GreB", "" ]

[ 35390, 42474 ]

2

[]

0

[ "1grj", "2etn", "2eul", "2f23", "2p4v", "2pn0", "3aoh", "3aoi", "3bmb", "4wqt", "6ri7", "6rin" ]

12

[ "PUB00000884", "PUB00004205", "PUB00011909", "PUB00050693" ]

[ "8431948", "7854424", "12914698", "18760284" ]

[ "Transcript cleavage factors from E. coli.", "Crystal structure of the GreA transcript cleavage factor from Escherichia coli.", "Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase.", "Crystal structure of Escherichia coli Rnk, a new RNA polymerase-interacting ...

[ 1993, 1995, 2003, 2008 ]

4

[]

[ "IPR028624", "IPR028625" ]

0

2

0

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

[ 42605, 63, 2, 707 ]

4

[ "Escherichia coli (strain K12)" ]

[ 3 ]

1

true

Family

Transcription elongation factor GreA/GreB family

Tscrpt_elong_fac_GreA/B_fam

4

IPR023460

23,460

RNA-binding family, YbxF-like

RNA_bf_YbxF-like

Family

494

false

This entry represents the YbxF-like (also known as ribosomal eL8 or L7Ae-like) family found in selected Gram-positive bacteria [ , ]. 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 in...

[]

0

[ "HAMAP" ]

[ "MF_00574" ]

[ "Ribosomal_eL8_Bact" ]

[ 494 ]

1

[]

0

[ "3v7e", "4lck", "4tzp", "4tzv", "4tzw", "4tzz" ]

6

[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00058488", "PUB00151153" ]

[ "11297922", "11290319", "11114498", "22355167", "17468242" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "YbxF and YlxQ are bacterial homologs of L7Ae and bind K-turns but not K-loops.", "YbxF, a protein associated with exponential-phase ribosomes in Bacillus subt...

[ 2001, 2001, 2000, 2012, 2007 ]

5

[]

0

null

[ "Bacillota" ]

[ 494 ]

1

[]

0

true

Family

RNA-binding family, YbxF-like

RNA_bf_YbxF-like

1

IPR023463

23,463

Electron transfer flavoprotein, FixA subunit

FixA

Family

713

false

Electron transfer flavoproteins (ETFs) serve as specific electron acceptors for primary dehydrogenases, transferring the electrons to terminal respiratory systems. They can be functionally classified into constitutive, "housekeeping" ETFs, mainly involved in the oxidation of fatty acids (Group I), and ETFs produced by ...

[ "GO:0009055", "GO:0009437" ]

[ "electron transfer activity", "carnitine metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01055" ]

[ "FixA" ]

[ 713 ]

1

[]

0

[]

0

[ "PUB00003866", "PUB00004879", "PUB00004936", "PUB00005086", "PUB00024527", "PUB00033231", "PUB00033232", "PUB00053911", "PUB00054253" ]

[ "7815937", "8962055", "2326318", "8525056", "10026281", "8599534", "12567183", "9037756", "12081978" ]

[ "Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli.", "Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.", "Biosynthesis, molecular cloning and sequencing of electron transfer flavoprotein.", "Phylogenetic characterizatio...

[ 1994, 1996, 1990, 1995, 1999, 1996, 2003, 1997, 2002 ]

9

[ "IPR012255" ]

[]

1

0

1

[ "Enterobacterales" ]

[ 713 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Electron transfer flavoprotein, FixA subunit

FixA

3

IPR023464

23,464

DNA-directed RNA polymerase subunit Rpo12

Rpo12

Family

837

false

This entry represents the archaeal RNA polymerase subunit P, also known as Rpo12 following the eukaryotic nomenclature [ ]. Archaeal subunit P is the homologue of eukaryotic subunit Rbp12 [ ]. DNA-directed RNA polymerases, also known as DNA-dependent RNA polymerases, are responsible for the polymerisation of ribonucleo...

[ "GO:0003677", "GO:0003899", "GO:0006351" ]

[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]

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

3

[ "HAMAP" ]

[ "MF_00615" ]

[ "RNApol_arch_Rpo12" ]

[ 837 ]

1

[ "EC" ]

[ "2.7.7.6" ]

[ "EC:2.7.7.6" ]

1

[ "2pmz", "2waq", "2wb1", "2y0s", "3hkz", "4ayb", "4qiw", "4v8s", "6kf3", "6kf4", "6kf9", "7ok0", "7oq4", "7oqy", "8cro", "8oki", "8orq", "8p2i", "8rbo", "9bct", "9bcu" ]

21

[ "PUB00010736", "PUB00059148", "PUB00059149" ]

[ "11058130", "19419240", "19880312" ]

[ "Archaeal RNA polymerase subunits F and P are bona fide homologs of eukaryotic RPB4 and RPB12.", "Evolution of Complex RNA Polymerases: The Complete Archaeal RNA Polymerase Structure.", "Archaeal RNA polymerase." ]

[ 2000, 2009, 2009 ]

3

[ "IPR006591" ]

[]

1

0

1

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

[ 777, 44, 16 ]

3

[]

0

true

Family

DNA-directed RNA polymerase subunit Rpo12

Rpo12

6

IPR023465

23,465

Riboflavin kinase domain superfamily

Riboflavin_kinase_dom_sf

Homologous_superfamily

32,405

false

Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase ( ), which converts it into FMN, and FAD synthetase ( ), which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out b...

[ "GO:0008531", "GO:0009231" ]

[ "riboflavin kinase activity", "riboflavin biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:2.40.30.30", "SSF82114" ]

[ "", "" ]

[ 32375, 32305 ]

2

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

[ "2.7.1", "R-DME-196843", "R-HSA-196843", "R-MMU-196843", "R-SCE-196843", "R-SPO-196843" ]

[ "EC:2.7.1", "REACTOME:R-DME-196843", "REACTOME:R-HSA-196843", "REACTOME:R-MMU-196843", "REACTOME:R-SCE-196843", "REACTOME:R-SPO-196843" ]

6

[ "1mrz", "1n05", "1n06", "1n07", "1n08", "1nb0", "1nb9", "1p4m", "1q9s", "1s4m", "1t6x", "1t6y", "1t6z", "2i1l", "2oyn", "2p3m", "2vbs", "2vbt", "2vbu", "2vbv", "2x0k", "3bnw", "3cta", "3op1", "3zug", "4uze", "4uzf", "5a88", "5a89", "5a8a", "5fnz", "5fo0"...

34

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

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

[ "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 ]

3

[]

0

null

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

[ 916, 25150, 5702, 5, 632 ]

5

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

[ 4, 1, 1, 2, 1, 3, 1, 2, 5, 4, 1, 1, 17 ]

13

true

Homologous_superfamily

Riboflavin kinase domain superfamily

Riboflavin_kinase_dom_sf

3

IPR023467

23,467

Tetrahydromethanopterin S-methyltransferase, subunit H/Methyltransferase Mtx, subunit H

MeTrfase_MtrH/MtxH

Family

502

false

In archaea the enzyme tetrahydromethanopterin S-methyltransferase is composed of eight subunits, MtrA-H. The enzyme is a membrane- associated enzyme complex which catalyzes an energy-conserving, sodium-ion-translocating step in methanogenesis from hydrogen and carbon dioxide [ ]. Subunit MtrH catalyzes the methylation ...

[ "GO:0008168", "GO:0006730" ]

[ "methyltransferase activity", "one-carbon metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "PIRSF" ]

[ "PF02007", "PIRSF004960" ]

[ "MtrH", "MtrH_MtxH" ]

[ 502, 354 ]

2

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

[ "7.2.1.4", "GenProp0288", "GenProp0722" ]

[ "EC:7.2.1.4", "GP:GenProp0288", "GP:GenProp0722" ]

3

[ "6sj8", "6sjk", "6sjn", "6sjo", "6sjp", "6sjr", "6sjs", "6sk4", "8z9u" ]

9

[ "PUB00005738", "PUB00006446", "PUB00027982", "PUB00086416" ]

[ "7737157", "10338124", "9461302", "25313086" ]

[ "The energy conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits.", "The energy conserving methyltetrahydromethanopterin:coenzyme M methyltransferase complex from methanogenic archaea: function of the sub...

[ 1995, 1999, 1997, 2014 ]

4

[]

[ "IPR028342" ]

0

1

0

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

[ 368, 95, 1, 38 ]

4

[]

0

true

Family

Tetrahydromethanopterin S-methyltransferase, subunit H/Methyltransferase Mtx, subunit H

MeTrfase_MtrH/MtxH

4

IPR023468

23,468

Riboflavin kinase

Riboflavin_kinase

Family

31,753

false

This entry represents riboflavin kinase, which occurs as part of a bifunctional enzyme or a stand-alone enzyme. Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase ( ), which converts it into FMN, and FAD synthetase ( ), which adenylates FMN to FAD. Eukaryotes u...

[]

0

[ "PANTHER" ]

[ "PTHR22749" ]

[ "" ]

[ 31753 ]

1

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

[ "2.7.1.26", "PWY-5523", "PWY-6168", "PWY-7863", "R-DME-196843", "R-HSA-196843", "R-MMU-196843", "R-SCE-196843", "R-SPO-196843" ]

[ "EC:2.7.1.26", "METACYC:PWY-5523", "METACYC:PWY-6168", "METACYC:PWY-7863", "REACTOME:R-DME-196843", "REACTOME:R-HSA-196843", "REACTOME:R-MMU-196843", "REACTOME:R-SCE-196843", "REACTOME:R-SPO-196843" ]

9

[ "1mrz", "1n05", "1n06", "1n07", "1n08", "1nb0", "1nb9", "1p4m", "1q9s", "1s4m", "1t6x", "1t6y", "1t6z", "2i1l", "2x0k", "3bnw", "3op1", "3zug", "4uze", "4uzf", "5a88", "5a89", "5a8a", "5fnz", "5fo0", "5fo1" ]

26

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

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

[ "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 ]

3

[]

[ "IPR002606" ]

0

1

0

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

[ 25881, 5277, 3, 592 ]

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",...

[ 4, 1, 1, 2, 1, 3, 1, 2, 5, 4, 1, 1, 11 ]

13

true

Family

Riboflavin kinase

Riboflavin_kinase

8

IPR023470

23,470

Riboflavin kinase, archaeal

Riboflavin_kinase_archaeal

Family

631

false

Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase, which converts it into FMN, and FAD synthetase, which adenylates FMN to FAD. Bacteria utilize a single bifunctional enzyme containing the ATP-dependent riboflavin kinase and the FMN adenylyltransferase domains...

[ "GO:0008531", "GO:0009231" ]

[ "riboflavin kinase activity", "riboflavin biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01285" ]

[ "Riboflavin_kinase" ]

[ 631 ]

1

[ "EC", "METACYC" ]

[ "2.7.1.161", "PWY-6167" ]

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

2

[ "2oyn", "2p3m", "2vbs", "2vbt", "2vbu", "2vbv" ]

6

[ "PUB00042719", "PUB00088845" ]

[ "18073108", "18245297" ]

[ "A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels.", "Identification and characterization of an archaeon-specific riboflavin kinase." ]

[ 2007, 2008 ]

2

[ "IPR039063" ]

[]

1

0

1

[ "Archaea", "ecological metagenomes" ]

[ 626, 5 ]

2

[]

0

true

Family

Riboflavin kinase, archaeal

Riboflavin_kinase_archaeal

7

IPR023471

23,471

Cytochrome c oxidase assembly protein CtaG/Cox11, domain superfamily

CtaG/Cox11_dom_sf

Homologous_superfamily

10,954

false

Cytochrome c oxidase assembly protein is essential for the assembly of functional cytochrome oxidase protein. In eukaryotes it is an integral protein of the mitochondrial inner membrane. Cox11 is essential for the insertion of Cu(I) ions to form the CuB site. This is essential for the stability of other structures in s...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:2.60.370.10", "SSF110111" ]

[ "", "" ]

[ 10908, 10951 ]

2

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

[ "R-BTA-9864848", "R-HSA-9864848", "R-MMU-9864848" ]

[ "REACTOME:R-BTA-9864848", "REACTOME:R-HSA-9864848", "REACTOME:R-MMU-9864848" ]

3

[ "1so9", "1sp0" ]

2

[ "PUB00010096", "PUB00010118", "PUB00031140" ]

[ "10617659", "12063264", "15181013" ]

[ "Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase.", "Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein.", "Solution structure of Cox11, a novel type of beta-immunoglobulin-like fold involved in CuB site formation of ...

[ 2000, 2002, 2004 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 6302, 4574, 78 ]

3

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

[ 3, 2, 1, 1, 4, 2, 1, 5, 2, 1, 2, 4 ]

12

true

Homologous_superfamily

Cytochrome c oxidase assembly protein CtaG/Cox11, domain superfamily

CtaG/Cox11_dom_sf

1

IPR023472

23,472

Uncharacterised protein family MJ0810

Uncharacterised_MJ0810

Family

725

false

This entry contains a group of prokaryotic proteins that share protein sequence similarity to eukaryotic Nuclear protein AMMECR1, including Protein PH0010 from Pyrococcus horikoshii. PH0010 consists of two distinct domains of different sizes: the large domain, which contains both the N- and C-terminal regions, consists...

[]

0

[ "HAMAP" ]

[ "MF_00645" ]

[ "AMMECR1" ]

[ 725 ]

1

[]

0

[ "1vaj", "1wsc", "1zq7" ]

3

[ "PUB00017067" ]

[ "15558565" ]

[ "Crystal structure of PH0010 from Pyrococcus horikoshii, which is highly homologous to human AMMECR 1C-terminal region." ]

[ 2005 ]

1

[ "IPR023473" ]

[]

1

0

1

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

[ 512, 188, 3, 22 ]

4

[]

0

true

Family

Uncharacterised protein family MJ0810

Uncharacterised_MJ0810

4

IPR023473

23,473

AMMECR1

Family

8,954

false

Nuclear protein AMMECR1, presently a protein of unknown function, is encoded by one of the genes affected by an X-linked deletion that causes the association of Alport syndrome, midface hypoplasia, intellectual disability and elliptocytosis in humans [ ]. Homologues appear in species ranging from bacteria and archaea t...

[]

0

[ "PANTHER", "NCBIFAM" ]

[ "PTHR13016", "TIGR00296" ]

[ "", "" ]

[ 8510, 6913 ]

2

[]

0

[ "1vaj", "1wsc", "1zq7" ]

3

[ "PUB00006433", "PUB00015590", "PUB00017067", "PUB00101144" ]

[ "10049589", "10828604", "15558565", "27811305" ]

[ "Identification and characterization of a highly conserved protein absent in the Alport syndrome (A), mental retardation (M), midface hypoplasia (M), and elliptocytosis (E) contiguous gene deletion syndrome (AMME).", "Identification and characterization of mouse orthologs of the AMMECR1 and FACL4 genes deleted in...

[ 1999, 2000, 2005, 2017 ]

4

[]

[ "IPR023472", "IPR027623" ]

0

2

0

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

[ 781, 2510, 5491, 172 ]

4

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

[ 3, 1, 1, 2, 14, 5, 1, 3, 7, 1, 1, 5 ]

12

true

Family

AMMECR1

8

IPR023474

23,474

Exosome complex component Rrp4

Rrp4

Family

458

false

The archaeal exosome is a protein complex involved in the degradation and the posttranscriptional tailing of RNA [ ]. Rrp4 is a structural component of the exosome that confers poly(A) specificity [ ].

[ "GO:0008143", "GO:0000178" ]

[ "poly(A) binding", "exosome (RNase complex)" ]

[ "molecular_function", "cellular_component" ]

2

[ "HAMAP" ]

[ "MF_00623" ]

[ "Exosome_Rrp4" ]

[ 458 ]

1

[]

0

[ "2ba0", "2je6", "2jea", "2jeb", "2z0s", "3l7z", "4ba1", "4ba2", "8xie" ]

9

[ "PUB00074087", "PUB00074089" ]

[ "22503705", "24789718" ]

[ "Heterogeneous complexes of the RNA exosome in Sulfolobus solfataricus.", "Structure and function of the archaeal exosome." ]

[ 2012, 2014 ]

2

[ "IPR026699" ]

[]

1

0

1

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

[ 445, 2, 11 ]

3

[]

0

true

Family

Exosome complex component Rrp4

Rrp4

1

IPR023475

23,475

Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) CbiT

CbiT

Family

356

false

CbiT is a bifunctional enzyme that catalyses two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. It participates in the biosynthesis of vitamin B12 [ ]. In the anaerobic pathway, two enzymes are required to pr...

[ "GO:0008168" ]

[ "methyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00786" ]

[ "CbiT" ]

[ 356 ]

1

[ "EC", "METACYC" ]

[ "2.1.1.196", "PWY-7377" ]

[ "EC:2.1.1.196", "METACYC:PWY-7377" ]

2

[ "1f38", "1kxz", "1l3b", "1l3c", "1l3i", "2yxd" ]

6

[ "PUB00009744", "PUB00014672", "PUB00014680", "PUB00014681", "PUB00015657", "PUB00035308", "PUB00035309", "PUB00035310", "PUB00070131", "PUB00074099" ]

[ "11215515", "11153269", "12429089", "1732195", "12869542", "17163662", "16042605", "12055304", "23922391", "16198574" ]

[ "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Multiple biosynthetic pathways for vitamin B12: variations on a central theme.", "The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.", "Biosynthesis of vitamin B12 in Pseudomonas...

[ 2000, 2001, 2002, 1992, 2003, 2006, 2005, 2002, 2013, 2006 ]

10

[ "IPR014008" ]

[]

1

0

1

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

[ 302, 49, 1, 4 ]

4

[]

0

true

Family

Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) CbiT

CbiT

8

IPR023476

23,476

Peptidyl-tRNA hydrolase II domain superfamily

Pep_tRNA_hydro_II_dom_sf

Homologous_superfamily

16,471

false

Peptidyl-tRNA hydrolases are enzymes that release tRNAs from peptidyl-tRNA during translation [ ]. This superfamily represents the structural domain found in these t-RNA hydrolases and which form dimers [ ].

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.40.1490.10", "SSF102462" ]

[ "", "" ]

[ 16193, 16424 ]

2

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

[ "3.1.1.29", "R-BTA-5689880", "R-CEL-5689880", "R-HSA-5689880", "R-MMU-5689880", "R-SPO-5689880" ]

[ "EC:3.1.1.29", "REACTOME:R-BTA-5689880", "REACTOME:R-CEL-5689880", "REACTOME:R-HSA-5689880", "REACTOME:R-MMU-5689880", "REACTOME:R-SPO-5689880" ]

6

[ "1q7s", "1rlk", "1rzw", "1wn2", "1xty", "2d3k", "2gax", "2zv3", "3erj" ]

9

[ "PUB00020200", "PUB00032523" ]

[ "12475929", "15766258" ]

[ "Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA hydrolase are nonessential in yeast.", "Crystal structure at 1.8 A resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase." ]

[ 2002, 2005 ]

2

[]

0

null

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

[ 930, 6673, 8604, 171, 93 ]

5

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

[ 22, 3, 7, 6, 4, 2, 1, 9, 5, 1, 1, 15 ]

12

true

Homologous_superfamily

Peptidyl-tRNA hydrolase II domain superfamily

Pep_tRNA_hydro_II_dom_sf

7

IPR023477

23,477

Adenylate kinase AdkA

Adenylate_kinase_AdkA

Family

419

false

AdkA belongs to the archaeal adenylate kinase family [ ]. It catalyses the interconversion of adenine nucleotides.

[ "GO:0004017" ]

[ "AMP kinase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00234" ]

[ "Adenylate_kinase_AdkA" ]

[ 419 ]

1

[ "EC", "METACYC" ]

[ "2.7.4.3", "PWY-7219" ]

[ "EC:2.7.4.3", "METACYC:PWY-7219" ]

2

[ "1kht", "1ki9", "1nks", "3h86", "6hf7", "6ln3", "6pjw", "6pk5", "6psp", "9cm0" ]

10

[ "PUB00074109" ]

[ "9055821" ]

[ "The adenylate kinase genes of M. voltae, M. thermolithotrophicus, M. jannaschii, and M. igneus define a new family of adenylate kinases." ]

[ 1997 ]

1

[]

0

null

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

[ 399, 2, 1, 17 ]

4

[]

0

true

Family

Adenylate kinase AdkA

Adenylate_kinase_AdkA

4

IPR023479

23,479

Pyridoxine/pyridoxal/pyridoxamine kinase

PdxK

Family

610

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_01638" ]

[ "PdxK" ]

[ 610 ]

1

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

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

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

3

[ "2ddm", "2ddo", "2ddw", "5zw9", "5zwa", "5zwb" ]

6

[ "PUB00006322", "PUB00017545", "PUB00035504", "PUB00035505", "PUB00035506", "PUB00035507", "PUB00035508", "PUB00040223" ]

[ "7748903", "8764513", "15581583", "8690703", "15189147", "17109392", "16763894", "16740960" ]

[ "Pyridoxal phosphate-dependent enzymes.", "Identification of the pdxK gene that encodes pyridoxine (vitamin B6) kinase in Escherichia coli K-12.", "Reaction specificity in pyridoxal phosphate enzymes.", "Pyridoxal enzymes: mechanistic diversity and uniformity.", "Pyridoxal phosphate enzymes: mechanistic, st...

[ 1995, 1996, 2005, 1995, 2004, 2006, 2006, 2006 ]

8

[ "IPR004625" ]

[]

1

0

1

[ "Pseudomonadota" ]

[ 610 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Pyridoxine/pyridoxal/pyridoxamine kinase

PdxK

4

IPR023480

23,480

Uncharacterised protein family UPF0312/YceI

UPF0312/YceI

Family

1,674

false

This entry represents the uncharacterised protein family UPF0312 and the lipid-binding protein YceI from Escherichia coli [ ] and its homologues.

[]

0

[ "HAMAP" ]

[ "MF_00780" ]

[ "UPF0312" ]

[ 1674 ]

1

[]

0

[ "1y0g", "7bwl" ]

2

[ "PUB00009923" ]

[ "12107143" ]

[ "pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli." ]

[ 2002 ]

1

[]

0

null

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

[ 1671, 2, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family UPF0312/YceI

UPF0312/YceI

9

IPR023481

23,481

Regulatory protein ViaA

ViaA

Family

1,405

false

This entry contains ViaA (VWA domain protein interacting with AAA ATPase) proteins. They are a component of the RavA-ViaA chaperone complex, which may act on the membrane to optimise the function of some of the respiratory chains. ViaA stimulates the ATPase activity of RavA.

[]

0

[ "HAMAP" ]

[ "MF_01626" ]

[ "ViaA" ]

[ 1405 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Trichuris trichiura" ]

[ 1404, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Regulatory protein ViaA

ViaA

1

IPR023482

23,482

Uncharacterised protein family Ves

Uncharacterised_Ves

Family

168

false

Proteins of the Ves family have no known function. Ves is induced by various environmental stresses, including low temperature, osmotic shock and oxygen. Expression is induced more than 10 fold by reducing temperature from 37 to 25 degrees Celsius [ ].

[]

0

[ "HAMAP" ]

[ "MF_01591" ]

[ "Ves" ]

[ 168 ]

1

[]

0

[]

0

[ "PUB00054602" ]

[ "11873911" ]

[ "Characterization of the ves gene, which is expressed at a low temperature in Escherichia coli." ]

[ 2002 ]

1

[ "IPR010282" ]

[]

1

0

1

[ "Enterobacteriaceae" ]

[ 168 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family Ves

Uncharacterised_Ves

5

IPR023484

23,484

Transcription initiation factor TFIIB, archaea

TFIIB_arc

Family

3,176

false

Transcription initiation factor IIB stabilises the TBP (TATA-binding protein) binding to an archaeal box-A promoter. It is also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB).

[]

0

[ "HAMAP" ]

[ "MF_00383" ]

[ "TF2B_arch" ]

[ 3176 ]

1

[]

0

[]

0

[]

0

[ "IPR000812" ]

[]

1

0

1

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

[ 3138, 5, 2, 31 ]

4

[]

0

true

Family

Transcription initiation factor TFIIB, archaea

TFIIB_arc

2

IPR023485

23,485

Phosphotyrosine protein phosphatase I

Ptyr_pPase

Domain

59,774

false

Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is ...

[]

0

[ "PFAM", "SMART" ]

[ "PF01451", "SM00226" ]

[ "LMWPc", "LMWPc" ]

[ 58816, 58615 ]

2

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

[ "GenProp0474", "R-HSA-9635465", "R-HSA-9636383", "R-HSA-9636467", "R-HSA-9637628" ]

[ "GP:GenProp0474", "REACTOME:R-HSA-9635465", "REACTOME:R-HSA-9636383", "REACTOME:R-HSA-9636467", "REACTOME:R-HSA-9637628" ]

5

[ "1bvh", "1c0e", "1d1p", "1d1q", "1d2a", "1dg9", "1jf8", "1jfv", "1jl3", "1ljl", "1lju", "1lk0", "1p8a", "1phr", "1pnt", "1rxe", "1rxi", "1u2p", "1u2q", "1xww", "1y1l", "1z12", "1z13", "1z2d", "1z2e", "1zgg", "2cd7", "2cwd", "2fek", "2fxi", "2gi4", "2ipa"...

93

[ "PUB00002706", "PUB00004186", "PUB00005003", "PUB00035793", "PUB00035794", "PUB00035795", "PUB00035796", "PUB00035797", "PUB00035798" ]

[ "1587862", "8052313", "1304913", "9818190", "14625689", "12678841", "16672235", "8948575", "9646865" ]

[ "Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase.", "The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase.", "Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase.", ...

[ 1992, 1994, 1992, 1998, 2003, 2003, 2006, 1996, 1998 ]

9

[]

0

null

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

[ 862, 52612, 5399, 6, 895 ]

5

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

[ 16, 1, 2, 8, 2, 7, 4, 1, 3, 12, 1, 1, 14 ]

13

true

Domain

Phosphotyrosine protein phosphatase I

Ptyr_pPase

6

IPR023486

23,486

Transcription factor TFIIB, conserved site

TFIIB_CS

Conserved_site

8,328

false

In eukaryotes, transcription initiation by polymerase II is modulated by both general and specific transcription factors. The general factors (which include TFIIA, TFIIB, TFIID, TFIIE, TFIIF, TFIIG and TFIIH) operate through common promoter elements, such as the TATA box. Transcription factor IIB (TFIIB) is of central ...

[]

0

[ "PROSITE" ]

[ "PS00782" ]

[ "TFIIB" ]

[ 8328 ]

1

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

[ "R-CEL-674695", "R-CEL-6807505", "R-CEL-73776", "R-CEL-73779", "R-CEL-75953", "R-CEL-76042", "R-DDI-674695", "R-DDI-6807505", "R-DDI-73776", "R-DDI-73779", "R-DDI-75953", "R-DDI-76042", "R-DME-674695", "R-DME-6807505", "R-DME-73776", "R-DME-73779", "R-DME-75953", "R-DME-76042", "...

[ "REACTOME:R-CEL-674695", "REACTOME:R-CEL-6807505", "REACTOME:R-CEL-73776", "REACTOME:R-CEL-73779", "REACTOME:R-CEL-75953", "REACTOME:R-CEL-76042", "REACTOME:R-DDI-674695", "REACTOME:R-DDI-6807505", "REACTOME:R-DDI-73776", "REACTOME:R-DDI-73779", "REACTOME:R-DDI-75953", "REACTOME:R-DDI-76042", ...

52

[ "1ais", "1c9b", "1d3u", "1tfb", "1vol", "2phg", "3k7a", "4bbr", "4bbs", "4v1n", "4v1o", "5fmf", "5fyw", "5fz5", "5iy6", "5iy7", "5iy8", "5iy9", "5iya", "5iyb", "5iyc", "5iyd", "5oqj", "5oqm", "5sva", "5wh1", "6cnb", "6cnc", "6cnd", "6cnf", "6eu0", "6f40"...

100

[ "PUB00004101", "PUB00005378" ]

[ "1876184", "1949150" ]

[ "Cloning of a human gene encoding the general transcription initiation factor IIB.", "Transcriptional activation: enter TFIIB." ]

[ 1991, 1991 ]

2

[]

0

null

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

[ 3125, 103, 4980, 120 ]

4

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

[ 5, 1, 1, 2, 3, 4, 1, 6, 5, 2, 1, 12 ]

12

true

Conserved_site

Transcription factor TFIIB, conserved site

TFIIB_CS

9

IPR023488

23,488

HTH-type transcriptional regulator Hpr

HTH_tscrpt_reg_Hpr

Family

472

false

The MarR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 135 amino acids present in transcription regulators of the MarR/SlyA family, involved in the development of antibiotic resistance. The MarR family of transcription regulators is named after Escherichia coli MarR, a repressor of ge...

[]

0

[ "HAMAP" ]

[ "MF_01911" ]

[ "HTH_type_Hpr" ]

[ 472 ]

1

[]

0

[ "2fxa", "9fa0", "9ff3", "9ff4", "9ff5" ]

5

[ "PUB00015407", "PUB00015408", "PUB00015409", "PUB00015410" ]

[ "10498949", "10094687", "11473263", "12649270" ]

[ "The mar regulon: multiple resistance to antibiotics and other toxic chemicals.", "BadR, a new MarR family member, regulates anaerobic benzoate degradation by Rhodopseudomonas palustris in concert with AadR, an Fnr family member.", "The crystal structure of MarR, a regulator of multiple antibiotic resistance, a...

[ 1999, 1999, 2001, 2003 ]

4

[ "IPR039422" ]

[]

1

0

1

[ "Bacillales" ]

[ 472 ]

1

[]

0

true

Family

HTH-type transcriptional regulator Hpr

HTH_tscrpt_reg_Hpr

5

IPR023489

23,489

Haloalkane dehalogenase, subfamily 1

Haloalkane_dehalogenase_1

Family

297

false

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 subfamilies which differ in the amino acids and the topology of their c...

[ "GO:0018786" ]

[ "haloalkane dehalogenase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01230" ]

[ "Haloalk_dehal_type1" ]

[ 297 ]

1

[ "EC" ]

[ "3.8.1.5" ]

[ "EC:3.8.1.5" ]

1

[ "1b6g", "1be0", "1bee", "1bez", "1cij", "1edb", "1edd", "1ede", "1hde", "2dhc", "2dhd", "2dhe", "2eda", "2edc", "2had", "2pky", "2yxp", "5esr", "6f9o" ]

19

[ "PUB00054255" ]

[ "4019411" ]

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

[ 1985 ]

1

[ "IPR000639" ]

[]

1

0

1

[ "Bacteria", "ecological metagenomes" ]

[ 295, 2 ]

2

[]

0

true

Family

Haloalkane dehalogenase, subfamily 1

Haloalkane_dehalogenase_1

3

IPR023490

23,490

HTH-type transcriptional regulator ArgP, gammaproteobacteria

ArgP_gammaproteobact

Family

1,798

false

This entry represents HTH-type transcriptional regulator ArgP from Gammaproteobacteria. ArgP (formally known as IciA) is a positive regulator of argK. It is a negative autoregulator in presence of arginine. It competes with DnaA for oriC iteron (13-mer) binding. It activates dnaA and nrd transcription. It has been demo...

[]

0

[ "HAMAP" ]

[ "MF_00513" ]

[ "HTH_type_ArgP" ]

[ 1798 ]

1

[]

0

[]

0

[ "PUB00042857", "PUB00042858", "PUB00067927" ]

[ "10589831", "15150242", "18502871" ]

[ "PhoB-dependent transcriptional activation of the iciA gene during starvation for phosphate in Escherichia coli.", "Evidence for an arginine exporter encoded by yggA (argO) that is regulated by the LysR-type transcriptional regulator ArgP in Escherichia coli.", "Lysine represses transcription of the Escherichia...

[ 1999, 2004, 2008 ]

3

[ "IPR017685" ]

[]

1

0

1

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

[ 1795, 2, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

HTH-type transcriptional regulator ArgP, gammaproteobacteria

ArgP_gammaproteobact

4

IPR023491

23,491

Acyl carrier protein phosphodiesterase, gammaproteobacteria

ACP_phosphodiesterase_gpbac

Family

895

false

This entry contains the Acyl carrier protein phosphodiesterase (AcpH, also called ACP hydrolyase) from Escherichia coli. Proteins in this entry are restricted to the gammaproteobacteria. AcpH converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP [ , ]. A mutant E. coli ...

[ "GO:0008770", "GO:0006633" ]

[ "[acyl-carrier-protein] phosphodiesterase activity", "fatty acid biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01950" ]

[ "AcpH" ]

[ 895 ]

1

[ "EC", "METACYC" ]

[ "3.1.4.14", "PWY-6012" ]

[ "EC:3.1.4.14", "METACYC:PWY-6012" ]

2

[]

0

[ "PUB00044655", "PUB00062378" ]

[ "16107329", "17198382" ]

[ "The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization.", "Acyl carrier protein phosphodiesterase (AcpH) of Escherichia coli is a non-canonical member of the HD phosphatase/phosphodiesterase family." ]

[ 2005, 2007 ]

2

[ "IPR007431" ]

[]

1

0

1

[ "Opisthokonta", "Pseudomonadati" ]

[ 2, 893 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Acyl carrier protein phosphodiesterase, gammaproteobacteria

ACP_phosphodiesterase_gpbac

9

IPR023492

23,492

L-ribulose-5-phosphate 3-epimerase, Enterobacteriaceae

L-Ru-5P_3-Epase_Enterobacteria

Family

540

false

Proteins in this entry are L-ribulose-5-phosphate 3-epimerases (UlaE) from Enterobacteriaceae. They are supsected to be involved in isomerisation of L-xylulose-5-phosphate to L-ribulose-5-phosphate. UlaE in E. coli contains a TIM barrel and forms dimers [ ]. The ulaABCDEF operon encodes an L-ascorbate phosphotransferas...

[ "GO:0034015" ]

[ "L-ribulose-5-phosphate 3-epimerase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01951" ]

[ "UlaE" ]

[ 540 ]

1

[ "EC", "METACYC" ]

[ "5.1.3.22", "PWY-6961" ]

[ "EC:5.1.3.22", "METACYC:PWY-6961" ]

2

[ "3cqh", "3cqi", "3cqj", "3cqk" ]

4

[ "PUB00051092" ]

[ "18849419" ]

[ "Structure of L-xylulose-5-Phosphate 3-epimerase (UlaE) from the anaerobic L-ascorbate utilization pathway of Escherichia coli: identification of a novel phosphate binding motif within a TIM barrel fold." ]

[ 2008 ]

1

[ "IPR004560" ]

[]

1

0

1

[ "Enterobacteriaceae" ]

[ 540 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

L-ribulose-5-phosphate 3-epimerase, Enterobacteriaceae

L-Ru-5P_3-Epase_Enterobacteria

9

IPR023493

23,493

N-methyl-L-tryptophan oxidase MTOX

Me_Trp_Oxase_MTOX

Family

1,324

false

N-methyl-L-tryptophan oxidase catalyzes the oxidative demethylation of N-methyl-L-tryptophan [ ].

[ "GO:0050131", "GO:0050660" ]

[ "N-methyl-L-amino-acid oxidase activity", "flavin adenine dinucleotide binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP" ]

[ "MF_00515" ]

[ "MTOX" ]

[ 1324 ]

1

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

[ "1.5.3.-", "PWY-7542", "PWY-7638" ]

[ "EC:1.5.3.-", "METACYC:PWY-7542", "METACYC:PWY-7638" ]

3

[ "2uzz" ]

1

[ "PUB00049520" ]

[ "18186483" ]

[ "The X-ray structure of N-methyltryptophan oxidase reveals the structural determinants of substrate specificity." ]

[ 2008 ]

1

[ "IPR045170" ]

[]

1

0

1

[ "Gammaproteobacteria", "Opisthokonta" ]

[ 1321, 3 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

N-methyl-L-tryptophan oxidase MTOX

Me_Trp_Oxase_MTOX

3

IPR023494

23,494

Cytochrome c biogenesis protein Ccs1/CcsB/ResB

Cyt_c_bgen_Ccs1/CcsB/ResB

Family

10,746

false

The Css1/CcsB/ResB family of proteins are found in bacteria and chloroplasts. They are essential for the biogenesis of c-type cytochromes, apparently being required at the step of heme attachment [ , , ].

[]

0

[ "HAMAP", "PANTHER" ]

[ "MF_01392", "PTHR31566" ]

[ "CytC_Ccs1", "" ]

[ 1304, 10746 ]

2

[]

0

[]

0

[ "PUB00010215", "PUB00054256", "PUB00054257" ]

[ "10844653", "10542282", "12427747" ]

[ "Genes required for cytochrome c synthesis in Bacillus subtilis.", "Accumulation of pre-apocytochrome f in a Synechocystis sp. PCC 6803 mutant impaired in cytochrome c maturation.", "Functional analysis of a divergent system II protein, Ccs1, involved in c-type cytochrome biogenesis." ]

[ 2000, 1999, 2003 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 9278, 1232, 236 ]

3

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

[ 5, 1, 5 ]

3

true

Family

Cytochrome c biogenesis protein Ccs1/CcsB/ResB

Cyt_c_bgen_Ccs1/CcsB/ResB

1

IPR023495

23,495

Sugar efflux transporter, putative

Sugar_effux_transptr_put

Family

1,742

false

This family is involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites.

[]

0

[ "HAMAP" ]

[ "MF_00517" ]

[ "MFS_SotB" ]

[ 1742 ]

1

[]

0

[ "6kki", "6kkj", "6kkk", "6kkl" ]

4

[]

0

[ "IPR011701" ]

[]

1

0

1

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

[ 1741, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Sugar efflux transporter, putative

Sugar_effux_transptr_put

4

IPR023496

23,496

Deoxyhypusine synthase-like

Deoxyhypusine_synthase-like

Family

699

false

The entry represents a number of deoxyhypusine synthase-like proteins found in bacteria. The function of these proteins is not known. Eukaryotic initiation factor 5A (eIF-5A), now considered to be an elongation factor (see ), contains an unusual amino acid, hypusine [N epsilon-(4-aminobutyl-2-hydroxy)lysine]. The first...

[ "GO:0016765" ]

[ "transferase activity, transferring alkyl or aryl (other than methyl) groups" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00640" ]

[ "DHS_like" ]

[ 699 ]

1

[]

0

[]

0

[ "PUB00005808" ]

[ "9493264" ]

[ "Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site." ]

[ 1998 ]

1

[ "IPR002773" ]

[]

1

0

1

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

[ 11, 679, 9 ]

3

[]

0

true

Family

Deoxyhypusine synthase-like

Deoxyhypusine_synthase-like

5

IPR023497

23,497

Acid shock protein

Acid_shock

Family

1,357

false

Acid shock protein is required for growth and/or survival in acidic conditions. It is needed for the adaptation process at pH 4.5 that enables cells to survive at extremely low pH (pH 2.0) [ ]. The proteins generally consist of a conserved N terminus followed by three disordered repeats.

[]

0

[ "HAMAP", "PFAM" ]

[ "MF_00546", "PF06392" ]

[ "Asr", "Asr" ]

[ 925, 1356 ]

2

[]

0

[]

0

[ "PUB00012360" ]

[ "12670971" ]

[ "Molecular characterization of the acid-inducible asr gene of Escherichia coli and its role in acid stress response." ]

[ 2003 ]

1

[]

0

null

[ "Beauveria bassiana D1-5", "Pseudomonadota" ]

[ 1, 1356 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Acid shock protein

Acid_shock

9

IPR023499

23,499

L-ribulose-5-phosphate 4-epimerase UlaF

UlaF

Family

812

false

The ulaABCDEF operon encodes an L-ascorbate phosphotransferase transport system (UlaABC, formerly designated SgaTBA)responsible for the uptake and phosphorylation of L-ascorbate. The ulaDEF genes encode three enzymes that catalyze the anaerobic conversion of the phosphorylated, hydrolytic product of L-ascorbate, 3-keto...

[ "GO:0008742" ]

[ "L-ribulose-phosphate 4-epimerase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01952" ]

[ "UlaF" ]

[ 812 ]

1

[ "EC", "METACYC" ]

[ "5.1.3.4", "PWY-6961" ]

[ "EC:5.1.3.4", "METACYC:PWY-6961" ]

2

[]

0

[]

0

[]

0

null

[ "Enterobacterales" ]

[ 812 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

L-ribulose-5-phosphate 4-epimerase UlaF

UlaF

5

IPR023501

23,501

Proteasome-activating nucleotidase PAN

Nucleotidase_PAN

Family

1,209

false

Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Proteasome-activating nucleotidase PAN1 from Haloferax volcanii has been shown to associate to sampylated proteins in proteasome-mediated proteolysis [ ]. AAA-ATPase PAN is responsible for recognizi...

[]

0

[ "HAMAP", "NCBIFAM" ]

[ "MF_00553", "NF003069" ]

[ "PAN", "PRK03992.1" ]

[ 1036, 1206 ]

2

[ "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

[ "3h4m", "6he4", "6he5", "6he8", "6he9", "6hea", "6hec", "6hed" ]

8

[ "PUB00054260", "PUB00054261", "PUB00054262", "PUB00054263", "PUB00054264", "PUB00070171" ]

[ "10692374", "10473546", "16337593", "17803938", "19481528", "24343376" ]

[ "Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome.", "An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes.", "ATP bindi...

[ 2000, 1999, 2005, 2007, 2009, 2014 ]

6

[]

0

null

[ "Archaea", "ecological metagenomes" ]

[ 1191, 18 ]

2

[]

0

true

Family

Proteasome-activating nucleotidase PAN

Nucleotidase_PAN

9

IPR023502

23,502

G/U mismatch-specific DNA glycosylase MUG, bacterial

MUG_bact

Family

803

false

This family represents the bacterial G/U mismatch-specific DNA glycosylase MUG. G:U mismatches resulting from deamination of cytosine are the most common pro-mutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- an...

[ "GO:0000700", "GO:0006285" ]

[ "mismatch base pair DNA N-glycosylase activity", "base-excision repair, AP site formation" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01956" ]

[ "MUG" ]

[ 803 ]

1

[ "EC" ]

[ "3.2.2.28" ]

[ "EC:3.2.2.28" ]

1

[ "1mtl", "1mug", "1mwi", "1mwj" ]

4

[ "PUB00008091", "PUB00080609", "PUB00095804" ]

[ "9489705", "19909758", "18789404" ]

[ "Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions.", "Uracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognition.", "Repair of deaminated base damage by Schizosaccharomyces pombe thymine DNA glyc...

[ 1998, 2010, 2008 ]

3

[ "IPR015637" ]

[]

1

0

1

[ "Gammaproteobacteria", "Peduoviridae" ]

[ 801, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

G/U mismatch-specific DNA glycosylase MUG, bacterial

MUG_bact

7

IPR023505

23,505

N-acetyl-D-glucosamine kinase

N-acetyl-D-glucosamine_kinase

Family

1,597

false

This entry represents N-acetyl-D-glucosamine kinases which catalyse the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P [ , ]. This group of proteins belong to the NagK subfamily of the ROK (nagC/xylR) family.

[ "GO:0045127" ]

[ "N-acetylglucosamine kinase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01271" ]

[ "GlcNAc_kinase" ]

[ 1597 ]

1

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

[ "2.7.1.59", "PWY-6517", "PWY-6906" ]

[ "EC:2.7.1.59", "METACYC:PWY-6517", "METACYC:PWY-6906" ]

3

[ "2ap1", "4db3", "7p7i", "7p7w", "7p9l", "7p9p", "7p9y", "7pa1" ]

8

[ "PUB00054266", "PUB00054267" ]

[ "15489439", "15157072" ]

[ "The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling.", "Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases." ]

[ 2004, 2004 ]

2

[ "IPR000600" ]

[]

1

0

1

[ "Bacteria" ]

[ 1597 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

N-acetyl-D-glucosamine kinase

N-acetyl-D-glucosamine_kinase

7

IPR023507

23,507

Serine/threonine protein kinase PknD

Ser/Thr_kinase_PknD

Family

45

false

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra...

[ "GO:0004674" ]

[ "protein serine/threonine kinase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01957", "NF009651" ]

[ "PknD_kinase", "PRK13184.1" ]

[ 45, 40 ]

2

[ "EC" ]

[ "2.7.11.1" ]

[ "EC:2.7.11.1" ]

1

[]

0

[ "PUB00005115", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899", "PUB00054265" ]

[ "3291115", "12368087", "12471243", "15078142", "15320712", "14500499" ]

[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "Evolution of protein kinase signaling from yeast to man.", "The protein kinase complement of the human genome.", "High-throughput structural biology in drug discovery: protein kinases.", "Creating chemical dive...

[ 1988, 2002, 2002, 2004, 2004, 2003 ]

6

[]

0

null

[ "Bacteria" ]

[ 45 ]

1

[]

0

true

Family

Serine/threonine protein kinase PknD

Ser/Thr_kinase_PknD

3

IPR023508

23,508

Acetyl esterase

Acetyl_esterase

Family

988

false

Proteins in this entry belong to the 'GDXG' family of lypolytic enzymes and are also known as Aes proteins. They have esterase activity against short chain (up to 8 carbon atoms) fatty esters and are able to hydrolyse triacetin and tributyrin but not triolein or cholesterol oleate. These proteins are involved in the do...

[ "GO:0052689", "GO:0005737" ]

[ "carboxylic ester hydrolase activity", "cytoplasm" ]

[ "molecular_function", "cellular_component" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01958", "NF007547" ]

[ "Acetyl_esterase", "PRK10162.1" ]

[ 854, 987 ]

2

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...

[ "3.1.1.-", "PWY-1921", "PWY-5835", "PWY-6190", "PWY-6308", "PWY-6322", "PWY-6339", "PWY-6415", "PWY-6558", "PWY-6848", "PWY-7002", "PWY-7352", "PWY-7367", "PWY-7521", "PWY-7599", "PWY-7660", "PWY-7712", "PWY-7713", "PWY-7730", "PWY-7769", "PWY-7982", "PWY-8058", "PWY-8143...

[ "EC:3.1.1.-", "METACYC:PWY-1921", "METACYC:PWY-5835", "METACYC:PWY-6190", "METACYC:PWY-6308", "METACYC:PWY-6322", "METACYC:PWY-6339", "METACYC:PWY-6415", "METACYC:PWY-6558", "METACYC:PWY-6848", "METACYC:PWY-7002", "METACYC:PWY-7352", "METACYC:PWY-7367", "METACYC:PWY-7521", "METACYC:PWY-7...

28

[ "3ga7", "4krx", "4kry" ]

3

[ "PUB00054268", "PUB00054269" ]

[ "11867639", "12374803" ]

[ "The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon.", "The Aes protein and the monomeric alpha-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism." ]

[ 2002, 2002 ]

2

[]

0

null

[ "Bacteria", "Trichuris trichiura" ]

[ 987, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Acetyl esterase

Acetyl_esterase

4

IPR023509

23,509

D-aminoacyl-tRNA deacylase-like superfamily

DTD-like_sf

Homologous_superfamily

26,493

false

D-tyrosyl-tRNA(Tyr) deacylase (DTD), also known as D-aminoacyl-tRNA deacylase, is an editing enzyme that removes D-amino acids from mischarged tRNAs. Structural studies have shown various different modes of D-amino acid recognition by DTDs, suggesting an inherent plasticity that can accommodate all d-amino acids. DTDs ...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.50.80.10", "SSF69500" ]

[ "", "" ]

[ 26456, 25666 ]

2

[ "EC" ]

[ "3.1.1.96" ]

[ "EC:3.1.1.96" ]

1

[ "1j7g", "1jke", "1tc5", "1y2q", "2dbo", "2hkz", "2hl0", "2hl1", "2hl2", "2okv", "3knf", "3knp", "3ko3", "3ko4", "3ko5", "3ko7", "3ko9", "3kob", "3koc", "3kod", "3lmt", "3lmu", "3lmv", "3pd2", "3pd3", "3pd4", "3pd5", "4nbi", "4nbj", "4rr6", "4rr7", "4rr8"...

55

[ "PUB00017393", "PUB00058619", "PUB00088138", "PUB00097389" ]

[ "11568181", "20007323", "26113036", "20445234" ]

[ "Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases.", "Ligand-bound structures provide atomic snapshots for the catalytic mechanism of D-amino acid deacylase.", "Specificity and catalysis hardwired at the RNA-protein interface in a translational pro...

[ 2001, 2010, 2015, 2010 ]

4

[]

0

null

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

[ 621, 19643, 5819, 1, 409 ]

5

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

[ 6, 1, 3, 3, 1, 7, 2, 1, 2, 7, 1, 1, 8 ]

13

true

Homologous_superfamily

D-aminoacyl-tRNA deacylase-like superfamily

DTD-like_sf

5

IPR023510

23,510

Methylmalonate-semialdehyde dehydrogenase, Gram-positive bacteria

MSDH_GmP_bac

Family

1,611

false

Methylmalonate-semialdehyde dehydrogenase (MMSDH, ) catalyses the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterised in both prokaryotes [ , ] and eukaryotes [ ], functioning as a mammalian tetr...

[ "GO:0004491" ]

[ "methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01670" ]

[ "IolA" ]

[ 1611 ]

1

[ "EC", "METACYC" ]

[ "1.2.1.27", "PWY-5642" ]

[ "EC:1.2.1.27", "METACYC:PWY-5642" ]

2

[ "1t90" ]

1

[ "PUB00002721", "PUB00013470", "PUB00013471", "PUB00013472", "PUB00087086" ]

[ "1339433", "8550471", "1527093", "9226270", "21515690" ]

[ "Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase.", "Cloning and characterization of a gene (msdA) encoding methylmalonic acid semialdehyde dehydrogenase from Streptomyces coelicolor.", "CoA-dependent me...

[ 1992, 1996, 1992, 1997, 2011 ]

5

[ "IPR010061" ]

[]

1

0

1

[ "Bacillota" ]

[ 1611 ]

1

[]

0

true

Family

Methylmalonate-semialdehyde dehydrogenase, Gram-positive bacteria

MSDH_GmP_bac

3

IPR023511

23,511

Plastocyanin, cyanobacteria

Plastocyanin_cyanobac

Family

221

false

Blue or 'type-1' copper proteins are small proteins which bind a single copper atom and which are characterised by an intense electronic absorption band near 600 nm [ , ]. The most well known members of this class of proteins are the plant chloroplastic plastocyanins, and the distantly related bacterial azurins, which ...

[]

0

[ "HAMAP" ]

[ "MF_00566" ]

[ "Cytb6_f_plastocyanin" ]

[ 221 ]

1

[]

0

[ "1baw", "1bxu", "1bxv", "1fa4", "1j5c", "1j5d", "1jxd", "1jxf", "1m9w", "1nin", "1pcs", "1tu2", "2cj3", "2gim", "2q5b", "2w88", "2w8c", "3bqv", "3cvb", "3cvc", "3cvd", "4r0o" ]

22

[ "PUB00003327", "PUB00003425", "PUB00014468", "PUB00081028" ]

[ "8035459", "8433378", "14567714", "8027022" ]

[ "Solution structure of the type 1 blue copper protein amicyanin from Thiobacillus versutus.", "Evolution of protein complexity: the blue copper-containing oxidases and related proteins.", "Electron transfer between membrane complexes and soluble proteins in photosynthesis.", "Plastocyanin: structural and func...

[ 1994, 1993, 2003, 1994 ]

4

[ "IPR002387" ]

[]

1

0

1

[ "Cyanobacteriota" ]

[ 221 ]

1

[]

0

true

Family

Plastocyanin, cyanobacteria

Plastocyanin_cyanobac

4

IPR023513

23,513

Quinolinate synthase A, type 1

Quinolinate_synth_A_type1

Family

4,034

false

This entry represents a group of bacterial type 1 quinolinate synthetases (NadA). Quinolinate synthetase catalyses the second step of the de novo biosynthetic pathway of pyridine nucleotide formation. In particular, quinolinate synthetase is involved in the condensation of dihydroxyacetone phosphate and iminoaspartate ...

[ "GO:0016765" ]

[ "transferase activity, transferring alkyl or aryl (other than methyl) groups" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00567" ]

[ "NadA_type1" ]

[ 4034 ]

1

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

[ "2.5.1.72", "PWY-5316", "PWY-7342", "PWY-8277", "PWY-8352" ]

[ "EC:2.5.1.72", "METACYC:PWY-5316", "METACYC:PWY-7342", "METACYC:PWY-8277", "METACYC:PWY-8352" ]

5

[]

0

[ "PUB00009471" ]

[ "10648170" ]

[ "Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase." ]

[ 2000 ]

1

[ "IPR003473" ]

[]

1

0

1

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

[ 4028, 3, 3 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Quinolinate synthase A, type 1

Quinolinate_synth_A_type1

7

IPR023514

23,514

Glyoxylate/hydroxypyruvate reductase A, Enterobacterales

GhrA_Enterobacterales

Family

1,077

false

This entry represents glyoxylate/hydroxypyruvate reductase A (GrhA) from Enterobacterales. They are implicated in NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively.

[ "GO:0016618", "GO:0030267" ]

[ "hydroxypyruvate reductase [NAD(P)H] activity", "glyoxylate reductase (NADPH) activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP" ]

[ "MF_01666" ]

[ "2_Hacid_dh_C_GhrA" ]

[ 1077 ]

1

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

[ "1.1.1.79", "1.1.1.81", "PWY-1622", "PWY-8011" ]

[ "EC:1.1.1.79", "EC:1.1.1.81", "METACYC:PWY-1622", "METACYC:PWY-8011" ]

4

[ "3kbo", "3pp8", "6ovl", "6oxn", "6p35", "7jqh", "7jqi", "7jqj" ]

8

[]

0

[]

0

null

[ "Acrobeloides nanus", "Enterobacterales" ]

[ 1, 1076 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glyoxylate/hydroxypyruvate reductase A, Enterobacterales

GhrA_Enterobacterales

8

IPR023515

23,515

Quinolinate synthase A, type 3

Quinolinate_synth_A_type3

Family

4,673

false

This entry represents a group of bacterial type 3 quinolinate synthetases (NadA). Quinolinate synthetase catalyses the second step of the de novo biosynthetic pathway of pyridine nucleotide formation. In particular, quinolinate synthetase is involved in the condensation of dihydroxyacetone phosphate and iminoaspartate ...

[ "GO:0016765" ]

[ "transferase activity, transferring alkyl or aryl (other than methyl) groups" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00569" ]

[ "NadA_type3" ]

[ 4673 ]

1

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

[ "2.5.1.72", "PWY-5316", "PWY-7342", "PWY-8277", "PWY-8352" ]

[ "EC:2.5.1.72", "METACYC:PWY-5316", "METACYC:PWY-7342", "METACYC:PWY-8277", "METACYC:PWY-8352" ]

5

[]

0

[ "PUB00009471" ]

[ "10648170" ]

[ "Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase." ]

[ 2000 ]

1

[ "IPR003473" ]

[]

1

0

1

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

[ 4277, 4, 246, 146 ]

4

[]

0

true

Family

Quinolinate synthase A, type 3

Quinolinate_synth_A_type3

6

IPR023516

23,516

tRNA-splicing endonuclease, archaeal long subfamily

tRNA_splic_arch_long

Family

426

false

tRNA-splicing endonucleases ( ) catalyse the endonucleolytic cleavage of pre tRNA at the 5' and 3' splice sites to release the intron and produces two half tRNA molecules bearing 5' hydroxyl and 2', 3'-cyclic phosphate termini [ , ]. The genes encoding these proteins are homologous in eukaryotes and archea. The eukaryo...

[ "GO:0000213" ]

[ "tRNA-intron lyase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01834" ]

[ "EndA_long" ]

[ 426 ]

1

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

[ "4.6.1.16", "PWY-6689", "PWY-7803" ]

[ "EC:4.6.1.16", "METACYC:PWY-6689", "METACYC:PWY-7803" ]

3

[ "1r0v", "1r11", "1rlv", "2gjw", "2ohc", "2ohe", "3p1y" ]

7

[ "PUB00054270", "PUB00055529" ]

[ "9321408", "9200603" ]

[ "RNA-protein interactions of an archaeal homotetrameric splicing endoribonuclease with an exceptional evolutionary history.", "The yeast tRNA splicing endonuclease: a tetrameric enzyme with two active site subunits homologous to the archaeal tRNA endonucleases." ]

[ 1997, 1997 ]

2

[ "IPR006676" ]

[]

1

0

1

[ "Methanobacteriati", "hydrocarbon metagenome" ]

[ 425, 1 ]

2

[]

0

true

Family

tRNA-splicing endonuclease, archaeal long subfamily

tRNA_splic_arch_long

5

IPR023519

23,519

Glyoxylate reductase GyaR

Glyoxylate_reductase_GyaR

Family

44

false

The GyaR family of glyoxylate reductases catalyses the NADH-linked reduction of glyoxylate to glycolate. This family is found in hyperthermophilic archaea, where it is thought to play an important role in the glyoxylate and 3-hydroxypropionic acid cycles [ ]. Structurally, GyaR is similar to other NADH-linked dehydroge...

[ "GO:0047964" ]

[ "glyoxylate reductase (NADH) activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00776" ]

[ "GyaR" ]

[ 44 ]

1

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

[ "1.1.1.26", "PWY-7294", "PWY-7295" ]

[ "EC:1.1.1.26", "METACYC:PWY-7294", "METACYC:PWY-7295" ]

3

[ "2dbq", "2dbr", "2dbz", "5aov", "6bii" ]

5

[ "PUB00047236", "PUB00054275" ]

[ "17327673", "11532010" ]

[ "Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate.", "A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litoralis. Characterization, gene cloning, nucleotide sequence and expression in Escherichia coli." ]

[ 2007, 2001 ]

2

[]

0

null

[ "Archaea" ]

[ 44 ]

1

[]

0

true

Family

Glyoxylate reductase GyaR

Glyoxylate_reductase_GyaR

9

IPR023520

23,520

UV-endonuclease UvdE, bacterial

UvdE_bac

Family

468

false

Proteins in this entry are bacterial UV DNA damage endonucleases. They help the removal of UV-light damaged nucleotides. They can recognise pyrimidine dimers and cleave a phosphodiester bond immediately 5' to the lesion [ ].

[ "GO:0004519", "GO:0009411" ]

[ "endonuclease activity", "response to UV" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_00606" ]

[ "UV_endonuclease" ]

[ 468 ]

1

[]

0

[]

0

[ "PUB00014887" ]

[ "11807060" ]

[ "Genetic evidence that the uvsE gene product of Deinococcus radiodurans R1 is a UV damage endonuclease." ]

[ 2002 ]

1

[ "IPR004601" ]

[]

1

0

1

[ "Bacteria" ]

[ 468 ]

1

[]

0

true

Family

UV-endonuclease UvdE, bacterial

UvdE_bac

7

IPR023521

23,521

Pelota, archaea

Pelota_arc

Family

853

false

Proteins in this entry are archaeal homologues of the eukaryotic gene pelota (DOM34 in yeast), which functions in recognising stalled ribosomes [ ]. Pelota (known as DOM34 in yeast) is a conserved protein in eukaryotes and archaea [ ] that binds Hbs1, a GTPase related to the EF1-alpha subfamily, and plays a central rol...

[ "GO:0070481", "GO:0070966", "GO:0071025" ]

[ "nuclear-transcribed mRNA catabolic process, non-stop decay", "nuclear-transcribed mRNA catabolic process, no-go decay", "RNA surveillance" ]

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

3

[ "HAMAP" ]

[ "MF_01853" ]

[ "PelO" ]

[ 853 ]

1

[]

0

[ "2qi2", "3j15", "3obw", "3oby", "3wxm", "6ji2" ]

6

[ "PUB00049007", "PUB00058728", "PUB00070080", "PUB00070081", "PUB00070083", "PUB00161397", "PUB00161398", "PUB00161399" ]

[ "17889667", "20682285", "21448132", "18022361", "20974926", "22358840", "20890290", "31611569" ]

[ "Structural and functional insights into Dom34, a key component of no-go mRNA decay.", "Crystal structures of two archaeal Pelotas reveal inter-domain structural plasticity.", "Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes.", "RNA quality control in ...

[ 2007, 2010, 2011, 2007, 2010, 2012, 2010, 2019 ]

8

[ "IPR004405" ]

[]

1

0

1

[ "Archaea", "Desulfofervidus auxilii", "Halorubrum virus BJ1", "ecological metagenomes" ]

[ 835, 1, 1, 16 ]

4

[]

0

true

Family

Pelota, archaea

Pelota_arc

4

IPR023522

23,522

Chromosome-anchoring protein RacA

Chrosome_anchoring_RacA

Family

532

false

Spore formation in Bacillus subtilis involves a highly asymmetric cell division where the chromosome destined to enter the spore needs to move to the extreme pole of the cell in order to be captured in the prespore cell. This is accomplished by a specialised that moves the oriC region of the chromosome close to the cel...

[]

0

[ "HAMAP" ]

[ "MF_01170" ]

[ "RacA" ]

[ 532 ]

1

[]

0

[]

0

[ "PUB00054276", "PUB00054277" ]

[ "12493822", "12950914" ]

[ "RacA, a bacterial protein that anchors chromosomes to the cell poles.", "RacA and the Soj-Spo0J system combine to effect polar chromosome segregation in sporulating Bacillus subtilis." ]

[ 2003, 2003 ]

2

[]

0

null

[ "Bacillales" ]

[ 532 ]

1

[]

0

true

Family

Chromosome-anchoring protein RacA

Chrosome_anchoring_RacA

2

IPR023523

23,523

Histidine decarboxylase, bacteria

Hist_deCOase_bac

Family

188

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:0004398", "GO:0030170" ]

[ "histidine decarboxylase activity", "pyridoxal phosphate binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP" ]

[ "MF_00609" ]

[ "Pyridoxal_decarbox" ]

[ 188 ]

1

[ "EC", "METACYC" ]

[ "4.1.1.22", "PWY-6173" ]

[ "EC:4.1.1.22", "METACYC:PWY-6173" ]

2

[ "7eru", "7erv" ]

2

[ "PUB00001452", "PUB00002358", "PUB00003414", "PUB00004715", "PUB00006322", "PUB00035504", "PUB00035505", "PUB00035506", "PUB00035507", "PUB00035508", "PUB00076906", "PUB00094543" ]

[ "8181483", "8889823", "2124279", "2300558", "7748903", "15581583", "8690703", "15189147", "17109392", "16763894", "24415726", "16766535" ]

[ "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.", "Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.", "Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous.", ...

[ 1994, 1996, 1990, 1990, 1995, 2005, 1995, 2004, 2006, 2006, 2014, 2006 ]

12

[]

0

null

[ "Bacteria" ]

[ 188 ]

1

[]

0

true

Family

Histidine decarboxylase, bacteria

Hist_deCOase_bac

6

IPR023524

23,524

Uncharacterised protein family SprT-like

Uncharacterised_SprT-like

Family

2,057

false

The proteins in this entry have no known function.

[]

0

[ "HAMAP" ]

[ "MF_00745" ]

[ "SprT_like" ]

[ 2057 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacilli", "Phytophthora kernoviae 00238/432", "bioreactor metagenome" ]

[ 2054, 1, 2 ]

3

[]

0

true

Family

Uncharacterised protein family SprT-like

Uncharacterised_SprT-like

7

IPR023525

23,525

Ureidoglycolate lyase, bacterial

Ureidogly_lyase_bac

Family

2,789

false

Ureidoglycolate lyase ( ) is involved in the degradation of ureidoglycolate, an intermediate of purine degradation. It breaks down (S)-ureidoglycolate to produce glyoxylate and urea [ ]. This family of ureidoglycolate lyases were initially annotated as ureidoglycolate hydrolases, but this has since been corrected [ ]. ...

[ "GO:0050385", "GO:0000256" ]

[ "ureidoglycolate lyase activity", "allantoin catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_00616" ]

[ "Ureidogly_lyase" ]

[ 2789 ]

1

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

[ "4.3.2.3", "PWY-5694", "PWY-5705" ]

[ "EC:4.3.2.3", "METACYC:PWY-5694", "METACYC:PWY-5705" ]

3

[ "1xsq", "1xsr", "1yqc", "2bdr" ]

4

[ "PUB00074208", "PUB00078751" ]

[ "24107613", "19935661" ]

[ "Ureidoglycolate hydrolase, amidohydrolase, lyase: how errors in biological databases are incorporated in scientific papers and vice versa.", "Ureide catabolism in Arabidopsis thaliana and Escherichia coli." ]

[ 2013, 2010 ]

2

[ "IPR007247" ]

[]

1

0

1

[ "Protostomia", "Pseudomonadota", "unclassified sequences" ]

[ 17, 2768, 4 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ureidoglycolate lyase, bacterial

Ureidogly_lyase_bac

6

IPR023526

23,526

Sulphur relay, TusB

Sulphur_relay_TusB

Family

1,239

false

This entry represents TusB, which is a part of a sulphur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions [ ]. TusB is part of a heterohexamer, formed by a dimer of trimers; the hexameric TusBCD complex contains 2 copies each of TusB, TusC and TusD. The ...

[ "GO:0002143", "GO:0005737" ]

[ "tRNA wobble position uridine thiolation", "cytoplasm" ]

[ "biological_process", "cellular_component" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01564", "NF010035" ]

[ "Thiourid_synth_B", "PRK13510.1" ]

[ 1130, 1239 ]

2

[ "GP" ]

[ "GenProp1134" ]

[ "GP:GenProp1134" ]

1

[ "2d1p" ]

1

[ "PUB00040153", "PUB00043028" ]

[ "16472754", "16387657" ]

[ "Structural basis for sulfur relay to RNA mediated by heterohexameric TusBCD complex.", "Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions." ]

[ 2006, 2006 ]

2

[ "IPR007215" ]

[]

1

0

1

[ "Dendroctonus ponderosae", "Pseudomonadota", "human gut metagenome" ]

[ 1, 1237, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Sulphur relay, TusB

Sulphur_relay_TusB

9

IPR023527

23,527

Adaptive-response sensory-kinase SasA

Kinase_SasA

Family

364

false

This entry represents the adaptive-response sensory-kinase SasA family, a member of the two-component regulatory system SasA/RpaA involved in genome-wide circadian gene expression [ ]. This family of proteins participate in the kaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteri...

[ "GO:0016772" ]

[ "transferase activity, transferring phosphorus-containing groups" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01837", "NF006800" ]

[ "Kinase_SasA", "PRK09303.1" ]

[ 329, 364 ]

2

[ "EC" ]

[ "2.7.13.3" ]

[ "EC:2.7.13.3" ]

1

[]

0

[ "PUB00054600", "PUB00103555", "PUB00103628", "PUB00103629" ]

[ "10786837", "20133618", "16882723", "34618577" ]

[ "A kaiC-interacting sensory histidine kinase, SasA, necessary to sustain robust circadian oscillation in cyanobacteria.", "Three major output pathways from the KaiABC-based oscillator cooperate to generate robust circadian kaiBC expression in cyanobacteria.", "A KaiC-associating SasA-RpaA two-component regulato...

[ 2000, 2010, 2006, 2021 ]

4

[]

0

null

[ "Cyanobacteriota" ]

[ 364 ]

1

[]

0

true

Family

Adaptive-response sensory-kinase SasA

Kinase_SasA

6

IPR023528

23,528

Major facilitator superfamily transporter, TsgA

MFS_TsgA

Family

1,186

false

The proteins in this entry have no known function but are multi-pass membrane proteins that are putative transporters, which are induced by tellurite and selenite.

[]

0

[ "HAMAP" ]

[ "MF_01044" ]

[ "MFS_TsgA" ]

[ 1186 ]

1

[]

0

[]

0

[]

0

[ "IPR011701" ]

[]

1

0

1

[ "Bacteria", "human gut metagenome" ]

[ 1185, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Major facilitator superfamily transporter, TsgA

MFS_TsgA

8

IPR023529

23,529

RNA chaperone ProQ

ProQ

Family

4,197

false

ProQ is a RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. It may regulate ProP activity through an RNA-based, post-transcriptional mechanism. It contains a FinO-like domain that serves as a high-affinity RNA-binding domain and a Hfq-like domain that is largely responsible f...

[ "GO:0003723", "GO:0033592", "GO:0034057", "GO:0010608" ]

[ "RNA binding", "RNA strand annealing activity", "RNA strand-exchange activity", "post-transcriptional regulation of gene expression" ]

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

4

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

[ "MF_00749", "NF003434", "PTHR38106" ]

[ "ProQ", "PRK04950.1", "" ]

[ 2132, 2195, 4197 ]

3

[]

0

[ "5nb9", "5nbb", "6s10", "7rgs", "7rgt", "7rgu" ]

6

[ "PUB00020191", "PUB00074100" ]

[ "10049386", "21381725" ]

[ "Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12.", "ProQ is an RNA chaperone that controls ProP levels in Escherichia coli." ]

[ 1999, 2011 ]

2

[]

0

null

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

[ 4183, 6, 2, 6 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

RNA chaperone ProQ

ProQ

6

IPR023530

23,530

Cytochrome b6, PetB

Cyt_B6_PetB

Family

13,957

false

In the mitochondrion of eukaryotes and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III ( ) - also known as the bc1 complex or ubiquinol-cytochrome c reductase. In plant chloroplasts and cyanobacteria, there is a analogous protein, cytochrome b6, a component of the plastoquinone-plas...

[]

0

[ "HAMAP" ]

[ "MF_00633" ]

[ "Cytb6_f_cytb6" ]

[ 13957 ]

1

[]

0

[ "1q90", "1vf5", "2d2c", "2e74", "2e75", "2e76", "2zt9", "4h0l", "4h13", "4h44", "4i7z", "4ogq", "4pv1", "6rqf", "7qrm", "7r0w", "7zxy", "7zyv", "9es7", "9es8", "9es9" ]

21

[ "PUB00000640", "PUB00003404" ]

[ "8329437", "2509716" ]

[ "Mitochondrial cytochrome b: evolution and structure of the protein.", "Evolutionary conservation of protein regions in the protonmotive cytochrome b and their possible roles in redox catalysis." ]

[ 1993, 1989 ]

2

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 391, 13566 ]

2

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

[ 5, 2, 1 ]

3

true

Family

Cytochrome b6, PetB

Cyt_B6_PetB

7

IPR023531

23,531

Preprotein translocase subunit SecG

Preprot_translocase_SecG

Family

726

false

SecG is an homologue of Sec61 subunit beta, a component of the Sec61/SecYEG protein secretory system. It is involved in protein export. The function of this subunit is unknown, but it may be involved in stabilisation of the trimeric complex.

[]

0

[ "HAMAP" ]

[ "MF_00751" ]

[ "SecG" ]

[ 726 ]

1

[]

0

[ "1rh5", "1rhz", "2yxq", "2yxr", "4v4n", "4v7i" ]

6

[]

0

[ "IPR016482" ]

[]

1

0

1

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

[ 705, 3, 18 ]

3

[]

0

true

Family

Preprotein translocase subunit SecG

Preprot_translocase_SecG

9

IPR023532

23,532

H/ACA ribonucleoprotein complex subunit Nop10 , archaeal-type

Nop10_arc-typ

Family

797

false

Nop10 is a component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs). H/ACA snoRNPs are primarily responsible for catalysing the isomerisation of uridine to pseudouridine (Psi) in ribosomal and other cellular RNAs. The protein component of the H/ACA snoRNP consists of Cb...

[ "GO:0030515", "GO:0001522", "GO:0042254" ]

[ "snoRNA binding", "pseudouridine synthesis", "ribosome biogenesis" ]

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

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00803", "NF009623" ]

[ "Nop10", "PRK13130.1" ]

[ 763, 760 ]

2

[]

0

[ "2apo", "2aqc", "2aus", "2ey4", "2hvy", "2rfk", "3hax", "3hay", "3hjw", "3hjy", "3lwo", "3lwp", "3lwq", "3lwr", "3lwv", "3mqk" ]

16

[ "PUB00039361", "PUB00040471", "PUB00066234" ]

[ "16286935", "16427014", "18473479" ]

[ "The Cbf5-Nop10 complex is a molecular bracket that organizes box H/ACA RNPs.", "Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita.", "Nop10 is a conserved H/ACA snoRNP molecular adaptor." ]

[ 2005, 2006, 2008 ]

3

[ "IPR007264" ]

[]

1

0

1

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

[ 761, 20, 1, 15 ]

4

[]

0

true

Family

H/ACA ribonucleoprotein complex subunit Nop10 , archaeal-type

Nop10_arc-typ

7

IPR023533

23,533

Ribosomal protein bS6-L-glutamate ligase

RimK

Family

4,397

false

Escherichia coli RimK (also known as Ribosomal protein bS6-L-glutamate ligase) adds additional Glu residues to the native Glu-Glu C terminus of ribosomal protein bS6. Mutation of the Glu-Glu terminus to Lys-Glu blocked addition. Ribosomal protein bS6 has the C-terminal sequence Glu-Glu in few species, suggesting the ho...

[]

0

[ "HAMAP" ]

[ "MF_01552" ]

[ "RimK" ]

[ 4397 ]

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"...

[ "6.3.2.-", "PWY-6289", "PWY-6374", "PWY-6378", "PWY-6379", "PWY-6409", "PWY-6574", "PWY-7510", "PWY-7533", "PWY-7542", "PWY-7543", "PWY-7549", "PWY-7555", "PWY-7556", "PWY-7561", "PWY-7563", "PWY-7565", "PWY-7569", "PWY-7570", "PWY-7571", "PWY-7577", "PWY-7600", "PWY-7605...

[ "EC:6.3.2.-", "METACYC:PWY-6289", "METACYC:PWY-6374", "METACYC:PWY-6378", "METACYC:PWY-6379", "METACYC:PWY-6409", "METACYC:PWY-6574", "METACYC:PWY-7510", "METACYC:PWY-7533", "METACYC:PWY-7542", "METACYC:PWY-7543", "METACYC:PWY-7549", "METACYC:PWY-7555", "METACYC:PWY-7556", "METACYC:PWY-7...

42

[ "4iwx", "4iwy", "5zct", "5zk6", "7qyr", "7qys" ]

6

[ "PUB00015491", "PUB00151159" ]

[ "2570347", "36134899" ]

[ "Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12.", "Structural insights into the mechanism of adaptive ribosomal modification by Pseudomonas RimK." ]

[ 1989, 2023 ]

2

[ "IPR004666" ]

[]

1

0

1

[ "Bacteria", "Knufia peltigerae", "Methanosarcinaceae", "unclassified sequences" ]

[ 4357, 1, 22, 17 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ribosomal protein bS6-L-glutamate ligase

RimK

8

IPR023534

23,534

Rof/RNase P-like

Rof/RNase_P-like

Homologous_superfamily

7,780

false

This superfamily represents a domain with a core β barrel found in the inhibitor of Rho (Rof) [ ] and in ribonuclease P [ ].

[]

0

[ "SSF" ]

[ "SSF101744" ]

[ "" ]

[ 7780 ]

1

[ "EC", "REACTOME" ]

[ "3.1.26.5", "R-HSA-6784531" ]

[ "EC:3.1.26.5", "REACTOME:R-HSA-6784531" ]

2

[ "1oqk", "1pc0", "1sg5", "1ts9", "1tsf", "1v76", "2ki7", "2zae", "6agb", "6ah3", "6ahr", "6ahu", "6jie", "6k0a", "6k0b", "6w6v", "7c79", "7c7a", "8ptm", "8ptn", "8pto", "8ptp", "8w8d" ]

23

[ "PUB00031561", "PUB00043330" ]

[ "15518563", "17565995" ]

[ "Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus.", "Solution structure of YaeO, a Rho-specific inhibitor of transcription termination." ]

[ 2004, 2007 ]

2

[]

0

null

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

[ 901, 2404, 4440, 35 ]

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",...

[ 6, 1, 2, 3, 1, 4, 1, 1, 4, 2, 1, 1, 10 ]

13

true

Homologous_superfamily

Rof/RNase P-like

Rof/RNase_P-like

8

IPR023535

23,535

Threonylcarbamoyl-AMP synthase

TC-AMP_synthase

Family

4,980

false

This entry represents the threonylcarbamoyl-AMP synthase, includding RimN or YrdC (also known as TsaC) [ ], which is involved in the biosynthesis of N6-threonyl-carbamoyl-adenosine (t6A) modified tRNA. This is a universal modification, found at position 37 of ANN decoding tRNAs. Analysis shows that YrdC binds ATP and p...

[ "GO:0005524", "GO:0002949" ]

[ "ATP binding", "tRNA threonylcarbamoyladenosine modification" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01852" ]

[ "TsaC" ]

[ 4980 ]

1

[ "EC" ]

[ "2.7.7.87" ]

[ "EC:2.7.7.87" ]

1

[ "1hru", "2mx1" ]

2

[ "PUB00054278", "PUB00063355" ]

[ "19287007", "22378793" ]

[ "The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA.", "Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside." ]

[ 2009, 2012 ]

2

[]

0

null

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

[ 4931, 4, 45 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Threonylcarbamoyl-AMP synthase

TC-AMP_synthase

8

IPR023536

23,536

Coenzyme A disulphide reductase, staphyolococci

CoA_disulphide_reductase_staph

Family

130

false

Coenzyme A disulphide reductase ( ) has been characterised in Staphylococcus aureus, Pyrococcus horikoshii, and Borrelia burgdorferi (Lyme disease spirochete), and inferred in several other species on the basis of high levels of CoA and an absence of glutathione as a protective thiol. Coenzyme A disulphide reductase sp...

[ "GO:0050451" ]

[ "CoA-disulfide reductase (NADPH) activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01608" ]

[ "CoA_diS_reduct" ]

[ 130 ]

1

[ "EC" ]

[ "1.8.1.14" ]

[ "EC:1.8.1.14" ]

1

[ "1yqz", "4em3", "4em4", "4emw", "4eqr", "4eqs", "4eqw", "4eqx" ]

8

[ "PUB00038606", "PUB00044719", "PUB00096676", "PUB00096677" ]

[ "16981688", "18399646", "23530771", "24723088" ]

[ "Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution.", "Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity.", "Structure and substrate specificity of the pyrococcal coenzyme A disulfide ...

[ 2006, 2008, 2013, 2014 ]

4

[ "IPR017758" ]

[]

1

0

1

[ "Staphylococcaceae" ]

[ 130 ]

1

[]

0

true

Family

Coenzyme A disulphide reductase, staphyolococci

CoA_disulphide_reductase_staph

7

IPR023537

23,537

Deoxyuridine triphosphate nucleotidohydrolase, archaeal

dUTPase_archaeal

Family

82

false

The essential enzyme deoxyuridine triphosphate nucleotidohydrolase (dUTPase) ( ) is specific for dUTP and is critical for the fidelity of DNA replication and repair. dUTPase hydrolyzes dUTP to dUMP and pyrophosphate, simultaneously reducing dUTP levels and providing the dUMP for dTTP biosynthesis. dUTPase decreases the...

[ "GO:0004170" ]

[ "dUTP diphosphatase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00635" ]

[ "dUTPase_arch" ]

[ 82 ]

1

[ "EC" ]

[ "3.6.1.23" ]

[ "EC:3.6.1.23" ]

1

[]

0

[ "PUB00005269" ]

[ "8805593" ]

[ "Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits." ]

[ 1996 ]

1

[ "IPR011962" ]

[]

1

0

1

[ "Archaea", "Nitrolancea hollandica Lb", "bioreactor metagenome" ]

[ 80, 1, 1 ]

3

[]

0

true

Family

Deoxyuridine triphosphate nucleotidohydrolase, archaeal

dUTPase_archaeal

1

IPR023538

23,538

Ribonuclease P protein subunit RNP1

RNP1

Family

2,045

false

This entry represents RNP1 from archaea and its homologues from eukaryotes [ ]. Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life [ ]. In bacteria, the catalytic RNA (typically ~120kDa) is a...

[ "GO:0001682", "GO:0030677" ]

[ "tRNA 5'-leader removal", "ribonuclease P complex" ]

[ "biological_process", "cellular_component" ]

2

[ "HAMAP" ]

[ "MF_00754" ]

[ "RNase_P_1" ]

[ 2045 ]

1

[ "EC" ]

[ "3.1.26.5" ]

[ "EC:3.1.26.5" ]

1

[ "1oqk", "1ts9", "1tsf", "1v76", "2ki7", "2zae", "6k0a", "6k0b" ]

8

[ "PUB00006321", "PUB00007201", "PUB00042695", "PUB00088366" ]

[ "7731988", "10024167", "16650980", "28971852" ]

[ "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.", "Rpp14 and Rpp29, two protein subunits of human ribonuclease P.", "Structure of ribonuclease P--a universal ribozyme.", "Chance and necessity in the evolution of RNase P." ]

[ 1995, 1999, 2006, 2018 ]

4

[ "IPR002730" ]

[]

1

0

1

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

[ 851, 1172, 22 ]

3

[ "Caenorhabditis elegans" ]

[ 1 ]

1

true

Family

Ribonuclease P protein subunit RNP1

RNP1

2

IPR023539

23,539

Ribonuclease P, protein component 3, archaeal

RNase_P_comp-3_arc

Family

641

false

This entry represents the protein component 3 of ribonuclease P. RNase P is a protein complex that functions in the processing of pre-tRNA, generating mature tRNA molecules by cleaving their 5'-ends. It consists of a RNA moiety and at least 4 protein subunits. Unlike most other natural ribozymes, it recognises and clea...

[ "GO:0004526", "GO:0001682" ]

[ "ribonuclease P activity", "tRNA 5'-leader removal" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_00756" ]

[ "RNase_P_3" ]

[ 641 ]

1

[ "EC" ]

[ "3.1.26.5" ]

[ "EC:3.1.26.5" ]

1

[ "1v77", "2czv", "3wyz", "3wz0", "6k0a", "6k0b" ]

6

[ "PUB00042695" ]

[ "16650980" ]

[ "Structure of ribonuclease P--a universal ribozyme." ]

[ 2006 ]

1

[ "IPR002738" ]

[]

1

0

1

[ "Archaea", "ecological metagenomes" ]

[ 636, 5 ]

2

[]

0

true

Family

Ribonuclease P, protein component 3, archaeal

RNase_P_comp-3_arc

3

IPR023540

23,540

Phosphopantetheine adenylyltransferase, archaea

PPAT_arch

Family

776

false

This entry contains phosphopantetheine adenyltransferases, primarily of the archaeal type. They are responsible for the ATP-dependent conversion of pantetheine 4'-phosphate to 3'-dephospho-CoA [ ].

[ "GO:0004595" ]

[ "pantetheine-phosphate adenylyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00647" ]

[ "PPAT_arch" ]

[ 776 ]

1

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

[ "2.7.7.3", "PWY-7851", "PWY-8342" ]

[ "EC:2.7.7.3", "METACYC:PWY-7851", "METACYC:PWY-8342" ]

3

[ "3do8" ]

1

[ "PUB00054279" ]

[ "12756245" ]

[ "Identification, purification, and characterization of an eukaryotic-like phosphopantetheine adenylyltransferase (coenzyme A biosynthetic pathway) in the hyperthermophilic archaeon Pyrococcus abyssi." ]

[ 2003 ]

1

[]

0

null

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

[ 756, 9, 11 ]

3

[]

0

true

Family

Phosphopantetheine adenylyltransferase, archaea

PPAT_arch

6

IPR023541

23,541

rRNA small subunit methyltransferase B, enterobacteriaceae

rRNA_ssu_MeTfrase_B_ent

Family

1,434

false

RNA (C5-cytosine) methyltransferases (RCMTs) catalyse the transfer of a methyl group to the 5th carbon of a cytosine base in RNA sequences to produce C5-methylcytosine. RCMTs use the cofactor S-adenosyl-L-methionine (SAM) as a methyl donor [ ]. The catalytic mechanism of RCMTs involves an attack by the thiolate of a Cy...

[ "GO:0008649" ]

[ "rRNA methyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01856" ]

[ "16SrRNA_methyltr_B" ]

[ 1434 ]

1

[ "EC" ]

[ "2.1.1.176" ]

[ "EC:2.1.1.176" ]

1

[ "1sqf", "1sqg" ]

2

[ "PUB00014203", "PUB00014204", "PUB00014205", "PUB00054125", "PUB00054126", "PUB00054127", "PUB00054128", "PUB00054129", "PUB00054130" ]

[ "10026269", "14656444", "10454610", "12826405", "12220187", "19135144", "20007150", "10194318", "15121902" ]

[ "Purification, cloning, and characterization of the 16S RNA m5C967 methyltransferase from Escherichia coli.", "The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate.", "Exposition of a family of RNA m(5)C methyltransferases from...

[ 1999, 2003, 1999, 2003, 2002, 2009, 2010, 1999, 2004 ]

9

[ "IPR004573" ]

[]

1

0

1

[ "Gammaproteobacteria", "Timema douglasi", "human gut metagenome" ]

[ 1432, 1, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

rRNA small subunit methyltransferase B, enterobacteriaceae

rRNA_ssu_MeTfrase_B_ent

8

IPR023542

23,542

Ribosomal RNA large subunit methyltransferase I

RLMI

Family

1,655

false

Members of this entry specifically methylate the cytosine at position 1962(m5C1962) of 23S rRNA [ ].

[ "GO:0008649" ]

[ "rRNA methyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01857" ]

[ "23SrRNA_methyltr_I" ]

[ 1655 ]

1

[ "EC" ]

[ "2.1.1.191" ]

[ "EC:2.1.1.191" ]

1

[ "3c0k" ]

1

[ "PUB00050847" ]

[ "18789337" ]

[ "Crystal structure of the Escherichia coli 23S rRNA:m5C methyltransferase RlmI (YccW) reveals evolutionary links between RNA modification enzymes." ]

[ 2008 ]

1

[]

0

null

[ "Bacteria", "marine sediment metagenome" ]

[ 1654, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ribosomal RNA large subunit methyltransferase I

RLMI

1

IPR023543

23,543

rRNA small subunit methyltransferase C

rRNA_ssu_MeTfrase_C

Family

3,939

false

Members of this entry specifically methylate the guanosine at position 1207 of 16S rRNA [ ].

[ "GO:0008649" ]

[ "rRNA methyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01862" ]

[ "16SrRNA_methyltr_C" ]

[ 3939 ]

1

[ "EC" ]

[ "2.1.1.172" ]

[ "EC:2.1.1.172" ]

1

[ "2pjd" ]

1

[ "PUB00020947" ]

[ "9873033" ]

[ "Purification, cloning, and characterization of the 16 S RNA m2G1207 methyltransferase from Escherichia coli." ]

[ 1999 ]

1

[ "IPR046977" ]

[]

1

0

1

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

[ 3934, 2, 3 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

rRNA small subunit methyltransferase C

rRNA_ssu_MeTfrase_C

2

IPR023544

23,544

ABC transporter, vitamin B12-binding protein

ABC_transptr_vit_B12-bd

Family

1,749

false

This entry represents Vitamin B12-binding protein Escherichia coli (BtuF) and similar found in gammaproteobacteria. The vitamin B12-binding protein BtuF is part of the ABC transporter complex BtuCDF involved in vitamin B12 import. This protein binds vitamin B12 and delivers it to the periplasmic surface of BtuC [ ]. Th...

[ "GO:0031419", "GO:0015889", "GO:0042597" ]

[ "cobalamin binding", "cobalamin transport", "periplasmic space" ]

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

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01000", "NF002894" ]

[ "BtuF", "PRK03379.1" ]

[ 1681, 1745 ]

2

[ "GP" ]

[ "GenProp1150" ]

[ "GP:GenProp1150" ]

1

[ "1n2z", "1n4a", "1n4d", "2qi9", "4dbl", "4fi3", "5m29", "5m2q", "5m34", "5m3b", "5ovw", "5ysc" ]

12

[ "PUB00014769", "PUB00017894", "PUB00043654", "PUB00054280" ]

[ "9873074", "11421269", "11421270", "11790740" ]

[ "Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.", "ABC transporters: physiology, structure and mechanism--an overview.", "The ABC of ABCS: a phylogenetic and functional classification of ABC systems in living organisms.", "Iden...

[ 1999, 2001, 2001, 2002 ]

4

[]

0

null

[ "Acyrthosiphon pisum", "Bacteria" ]

[ 1, 1748 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

ABC transporter, vitamin B12-binding protein

ABC_transptr_vit_B12-bd

4

IPR023545

23,545

rRNA small subunit methyltransferase F

rRNA_ssu_MeTfrase_F

Family

2,169

false

Members of this entry specifically methylate the cytosine at position 1407(m5C1407) of 16S rRNA [ ].

[ "GO:0008649" ]

[ "rRNA methyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01579", "NF008898" ]

[ "16SrRNA_methyltr_F", "PRK11933.1" ]

[ 2104, 2167 ]

2

[ "EC" ]

[ "2.1.1.178" ]

[ "EC:2.1.1.178" ]

1

[ "2frx" ]

1

[ "PUB00054601" ]

[ "16678201" ]

[ "YebU is a m5C methyltransferase specific for 16 S rRNA nucleotide 1407." ]

[ 2006 ]

1

[ "IPR023267" ]

[]

1

0

1

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

[ 2166, 1, 2 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

rRNA small subunit methyltransferase F

rRNA_ssu_MeTfrase_F

7

IPR023546

23,546

Methylated-DNA--protein-cysteine methyltransferase

MGMT

Family

19,678

false

The repair of DNA containing O6-alkylated guanine is carried out by DNA-[protein]-cysteine S-methyltransferase ( ), also known as 6-O-methylguanine-DNA methyltransferase. The major mutagenic and carcinogenic effect of methylating agents in DNA is the formation of O6-alkylguanine. The alkyl group at the O-6 position is ...

[ "GO:0003824", "GO:0006281" ]

[ "catalytic activity", "DNA repair" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_00772" ]

[ "OGT" ]

[ 19678 ]

1

[ "EC" ]

[ "2.1.1.63" ]

[ "EC:2.1.1.63" ]

1

[ "1mgt", "1wrj", "2g7h", "4bhb", "4bhc", "4wx9", "4wxc", "4wxd", "4zye", "4zyg", "7dkn", "7dqr" ]

12

[ "PUB00000053", "PUB00060566" ]

[ "3052269", "3100503" ]

[ "Regulation and expression of the adaptive response to alkylating agents.", "Multiple species of Bacillus subtilis DNA alkyltransferase involved in the adaptive response to simple alkylating agents." ]

[ 1988, 1987 ]

2

[]

0

null

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

[ 145, 19318, 20, 195 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Methylated-DNA--protein-cysteine methyltransferase

MGMT

4

IPR023547

23,547

Digeranylgeranylglyceryl phosphate synthase

DGGGP_synth

Family

607

false

Digeranylgeranylglyceryl phosphate (DGGGP) synthase is a prenyltransferase involved in the synthesis of archaeal membrane ether-linked lipids [ ]. This enzyme catalyses the transfer of a geranylgeranyl group from geranylgeranyl diphosphate to (geranylgeranylglyceryl phosphate. DGGGP synthase has been found in almost al...

[ "GO:0000287", "GO:0047295", "GO:0008654", "GO:0005886" ]

[ "magnesium ion binding", "geranylgeranylglycerol-phosphate geranylgeranyltransferase activity", "phospholipid biosynthetic process", "plasma membrane" ]

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

4

[ "HAMAP" ]

[ "MF_01286" ]

[ "DGGGP_synth" ]

[ 607 ]

1

[ "EC", "METACYC" ]

[ "2.5.1.42", "PWY-6349" ]

[ "EC:2.5.1.42", "METACYC:PWY-6349" ]

2

[ "6m31", "6m34", "7bpu" ]

3

[ "PUB00054281" ]

[ "15356000" ]

[ "(S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids." ]

[ 2004 ]

1

[ "IPR050475" ]

[]

1

0

1

[ "Archaea", "Candidatus Kryptoniota", "ecological metagenomes" ]

[ 598, 3, 6 ]

3

[]

0

true

Family

Digeranylgeranylglyceryl phosphate synthase

DGGGP_synth

5

IPR023548

23,548

Probable Brix domain-containing ribosomal biogenesis protein

Brix_dom_Rbsml_bgen_prot

Family

268

false

This entry represents archaeal sequences containing a single Brix domain. The sequences have two unique characteristics: (1) the Brix domain charged regions are totally absent at the N-terminal and are reduced in number to about 10 residues at the C-terminal; and (2) the C-terminal part of the Brix domain itself is min...

[]

0

[ "HAMAP" ]

[ "MF_00699" ]

[ "BriX" ]

[ 268 ]

1

[]

0

[ "1w94", "2cxh" ]

2

[ "PUB00018304", "PUB00018305" ]

[ "11406393", "11246005" ]

[ "The Brix domain protein family -- a key to the ribosomal biogenesis pathway?", "The archaeal homolog of the Imp4 protein, a eukaryotic U3 snoRNP component." ]

[ 2001, 2001 ]

2

[]

0

null

[ "Archaea", "bioreactor metagenome" ]

[ 266, 2 ]

2

[]

0

true

Family

Probable Brix domain-containing ribosomal biogenesis protein

Brix_dom_Rbsml_bgen_prot

5

IPR023549

23,549

Subtilisin inhibitor

Subtilisin_inhibitor

Domain

3,606

false

The Streptomyces family of bacteria produce a number of proteinase inhibitors, which belong to MEROPS inhibitor family I16, clan IY. They are characterised by their strong activity towards subtilisin (MEROPS peptidase family S8, ) and are collectively known as Streptomyces subtilisin inhibitors (SSI). Some SSI also inh...

[ "GO:0004867" ]

[ "serine-type endopeptidase inhibitor activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF00720" ]

[ "SSI" ]

[ 3606 ]

1

[]

0

[ "2sic", "2tld", "3sic", "3ssi", "4hwx", "4hx2", "4hx3", "5sic", "6i0i" ]

9

[ "PUB00002322", "PUB00002348", "PUB00003205", "PUB00014133" ]

[ "6993452", "1908859", "6387152", "14705960" ]

[ "Importance of the carboxyl-terminal four amino acid residues in the inhibitory activity of Streptomyces subtilisin inhibitor (with a revision of its carboxyl-terminal sequence).", "Inhibition of subtilisin BPN' by reaction site P1 mutants of Streptomyces subtilisin inhibitor.", "Crystal structure at 2.6 A reso...

[ 1980, 1991, 1984, 2004 ]

4

[]

0

null

[ "Bacteria", "Fungi incertae sedis", "freshwater metagenome" ]

[ 3566, 30, 10 ]

3

[]

0

true

Domain

Subtilisin inhibitor

Subtilisin_inhibitor

9

IPR023550

23,550

PKHD-type hydroxylase

PKHD_hydroxylase

Family

5,275

false

This entry contains bacterial PKHD-type hydroxylases.

[ "GO:0016706" ]

[ "2-oxoglutarate-dependent dioxygenase activity" ]

[ "molecular_function" ]

1

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

[ "MF_00657", "NF003974", "PTHR41536" ]

[ "Hydroxyl_YbiX", "PRK05467.1-3", "" ]

[ 5070, 5130, 5275 ]

3

[ "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"...

[ "1.14.11.-", "PWY-102", "PWY-1187", "PWY-5035", "PWY-5036", "PWY-5047", "PWY-5070", "PWY-5349", "PWY-6085", "PWY-6086", "PWY-6495", "PWY-6682", "PWY-6915", "PWY-6919", "PWY-7150", "PWY-7151", "PWY-7232", "PWY-7274", "PWY-7298", "PWY-7398", "PWY-7419", "PWY-7517", "PWY-764...

[ "EC:1.14.11.-", "METACYC:PWY-102", "METACYC:PWY-1187", "METACYC:PWY-5035", "METACYC:PWY-5036", "METACYC:PWY-5047", "METACYC:PWY-5070", "METACYC:PWY-5349", "METACYC:PWY-6085", "METACYC:PWY-6086", "METACYC:PWY-6495", "METACYC:PWY-6682", "METACYC:PWY-6915", "METACYC:PWY-6919", "METACYC:PWY-...

35

[ "3dkq", "9ghl" ]

2

[]

0

[]

0

null

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

[ 5172, 7, 46, 50 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

PKHD-type hydroxylase

PKHD_hydroxylase

9

IPR023551

23,551

Iron-sulfur cluster repair protein ScdA

ScdA

Family

52

false

The ScdA protein was originally identified as a cell wall biosynthesis protein since mutations in the scdA gene produce cell walls with highly aberrant morphology [ ]. Subsequent studies have shown that ScdA belongs to the wider Repairs of iron centres (RIC) family and is a di-iron protein that, amongst other functions...

[ "GO:0006979" ]

[ "response to oxidative stress" ]

[ "biological_process" ]

1

[ "HAMAP" ]

[ "MF_01156" ]

[ "RIC_ScdA" ]

[ 52 ]

1

[]

0

[ "9j47", "9r7j", "9w8g" ]

3

[ "PUB00016649", "PUB00045447", "PUB00056780" ]

[ "9308171", "18203837", "16452450" ]

[ "The Staphylococcus aureus scdA gene: a novel locus that affects cell division and morphogenesis.", "Widespread distribution in pathogenic bacteria of di-iron proteins that repair oxidative and nitrosative damage to iron-sulfur centers.", "Global transcriptome analysis of Staphylococcus aureus response to hydro...

[ 1997, 2008, 2006 ]

3

[ "IPR019903" ]

[]

1

0

1

[ "Bacillales" ]

[ 52 ]

1

[]

0

true

Family

Iron-sulfur cluster repair protein ScdA

ScdA

9

IPR023552

23,552

Hut operon regulatory protein HutP, bacillales

Regulatory_HutP_bacillales

Family

301

false

The HutP protein regulates the expression of Bacillus 'hut' structural genes by an anti-termination complex, which recognises three UAG triplet units, separated by four non-conserved nucleotides on the RNA terminator region. L-Histidine and Mg2+ ions are also required. These proteins exhibit the structural elements of ...

[]

0

[ "HAMAP" ]

[ "MF_00779" ]

[ "HutP" ]

[ 301 ]

1

[]

0

[ "1vea", "1wmq", "1wps", "1wpt", "1wpu", "1wpv", "1wrn", "1wro", "1wrq", "3boy", "4h4l", "4ok9", "4okq" ]

13

[ "PUB00032271" ]

[ "15758992" ]

[ "Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand." ]

[ 2005 ]

1

[ "IPR015111" ]

[]

1

0

1

[ "Bacillales" ]

[ 301 ]

1

[]

0

true

Family

Hut operon regulatory protein HutP, bacillales

Regulatory_HutP_bacillales

2

IPR023553

23,553

Uncharacterised methyltransferase, YrrT

Uncharacterised_MeTfrase_YrrT

Family

816

false

This entry represent uncharacterised methyltransferases that belong to the YrrT family. It has been suggested that they are S-adenosyl-L-methionine-dependent.

[ "GO:0008168" ]

[ "methyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_02100" ]

[ "Methyltr_YrrT" ]

[ 816 ]

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"...

[ "2.1.1.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-5987", "PWY-601", "PWY-6045"...

[ "EC:2.1.1.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", "METACYC:PWY-5729", "METACYC:PWY-5...

146

[ "3hnr" ]

1

[]

0

[]

0

null

[ "Bacillota" ]

[ 816 ]

1

[]

0

true

Family

Uncharacterised methyltransferase, YrrT

Uncharacterised_MeTfrase_YrrT

2

IPR023554

23,554

ATP-dependent RNA helicase RhlB type

RNA_helicase_ATP-dep_RhlB

Family

4,628

false

This entry represents the RhiB type of ATP-dependent RNA helicases. They contain a DEAD box domain. They are responsible for ATP-dependent unwinding of double-stranded RNA as part of the RNA degradosome [ ].

[ "GO:0003724" ]

[ "RNA helicase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00661" ]

[ "DEAD_helicase_RhlB" ]

[ 4628 ]

1

[ "EC", "GP" ]

[ "3.6.4.13", "GenProp1166" ]

[ "EC:3.6.4.13", "GP:GenProp1166" ]

2

[]

0

[ "PUB00033639" ]

[ "8610017" ]

[ "A DEAD-box RNA helicase in the Escherichia coli RNA degradosome." ]

[ 1996 ]

1

[]

0

null

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

[ 4577, 6, 45 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

ATP-dependent RNA helicase RhlB type

RNA_helicase_ATP-dep_RhlB

9

IPR023555

23,555

Thiol-disulphide oxidoreductase ResA

Thiol-dS_OxRdtase_ResA

Family

230

false

The thiol-disulphide oxidoreductase protein ResA acts in cytochrome c maturation by reducing the disulphide bond present in apocytochromes prior to covalent attachment of heme [ ].

[ "GO:0015036", "GO:0017004", "GO:0005886" ]

[ "disulfide oxidoreductase activity", "cytochrome complex assembly", "plasma membrane" ]

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

3

[ "HAMAP" ]

[ "MF_01319" ]

[ "ResA" ]

[ 230 ]

1

[]

0

[]

0

[ "PUB00054282" ]

[ "12637552" ]

[ "Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis." ]

[ 2003 ]

1

[]

0

null

[ "Bacillales" ]

[ 230 ]

1

[]

0

true

Family

Thiol-disulphide oxidoreductase ResA

Thiol-dS_OxRdtase_ResA

2

IPR023558

23,558

Tryptophan RNA-binding attenuator protein domain

Trp_RNA-bd_attenuator_dom

Domain

1,385

false

The tryptophan RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes in Bacillus sp. by binding to the leader region of the nascent trp operon mRNA [ ]. The crystal structure of the Trp RNA-binding attenuation protein of Bacillus subtilis (mtrB, ) has been solved [ ]. TRAP for...

[]

0

[ "PFAM" ]

[ "PF02081" ]

[ "TrpBP" ]

[ 1385 ]

1

[]

0

[ "1c9s", "1gtf", "1gtn", "1qaw", "1utd", "1wap", "2exs", "2ext", "2zcz", "2zd0", "2zp8", "2zp9", "3aqd", "3zte", "3zzl", "3zzq", "3zzs", "4b27", "4v4f", "5eeu", "5eev", "5eew", "5eex", "5eey", "5eez", "5ef0", "5ef1", "5ef2", "5ef3", "6rvv", "6rvw", "8r59"...

36

[ "PUB00004208", "PUB00022801", "PUB00025371" ]

[ "7715723", "15050822", "11914485" ]

[ "The structure of trp RNA-binding attenuation protein.", "The interaction of RNA with TRAP: the role of triplet repeats and separating spacer nucleotides.", "Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences." ]

[ 1995, 2004, 2002 ]

3

[]

0

null

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

[ 1377, 1, 1, 6 ]

4

[]

0

true

Domain

Tryptophan RNA-binding attenuator protein domain

Trp_RNA-bd_attenuator_dom

3

IPR023559

23,559

Flagellar transcriptional activator FlhD

Flagellar_FlhD

Family

3,415

false

This family consists of several bacterial flagellar transcriptional activator (FlhD) proteins. FlhD combines with FlhC to form a regulatory complex in Escherichia coli [ ]. This complex has been shown to be a global transcriptional regulator involved in many cellular processes as well as a flagellar transcriptional act...

[ "GO:0044780", "GO:0045893" ]

[ "bacterial-type flagellum assembly", "positive regulation of DNA-templated transcription" ]

[ "biological_process", "biological_process" ]

2

[ "HAMAP", "PFAM" ]

[ "MF_00725", "PF05247" ]

[ "FlhD", "FlhD" ]

[ 2707, 3415 ]

2

[]

0

[ "1g8e", "2avu", "4es4", "5hxg", "8j56" ]

5

[ "PUB00010441", "PUB00025171", "PUB00056774", "PUB00056775", "PUB00056776" ]

[ "11287152", "11169099", "7961507", "11169100", "15941987" ]

[ "FlhD/FlhC-regulated promoters analyzed by gene array and lacZ gene fusions.", "Crystal structure of the global regulator FlhD from Escherichia coli at 1.8 A resolution.", "The FlhD/FlhC complex, a transcriptional activator of the Escherichia coli flagellar class II operons.", "Extensive alanine scanning reve...

[ 2001, 2001, 1994, 2001, 2005 ]

5

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 3390, 8, 17 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Flagellar transcriptional activator FlhD

Flagellar_FlhD

9

IPR023562

23,562

Clp protease proteolytic subunit /Translocation-enhancing protein TepA

ClpP/TepA

Family

77,459

false

This entry includes peptidases from the MEROPS peptidase family S14, including ClpP endopeptidase and translocation-enhancing protein TepA. ClpP is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin [ ]. It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits...

[]

0

[ "PFAM", "PANTHER" ]

[ "PF00574", "PTHR10381" ]

[ "CLP_protease", "" ]

[ 77451, 70622 ]

2

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

[ "3.4.21.92", "R-BTA-9837999", "R-CEL-9837999", "R-HSA-9837999", "R-MMU-9837999" ]

[ "EC:3.4.21.92", "REACTOME:R-BTA-9837999", "REACTOME:R-CEL-9837999", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-9837999" ]

5

[ "1tg6", "1tyf", "1y7o", "1yg6", "1yg8", "2c8t", "2cby", "2ce3", "2f6i", "2fzs", "2zl0", "2zl2", "2zl3", "2zl4", "3hln", "3ktg", "3kth", "3kti", "3ktj", "3ktk", "3mt6", "3p2l", "3q7h", "3qwd", "3st9", "3sta", "3tt6", "3tt7", "3v5e", "3v5i", "4emm", "4emp"...

190

[ "PUB00002564", "PUB00007689" ]

[ "2197275", "10455123" ]

[ "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.", "Signal peptide peptidase- and ClpP-like proteins of Bacillus subtilis required for efficient translocation and processing of secretory proteins." ]

[ 1990, 1999 ]

2

[]

[ "IPR001907" ]

0

1

0

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

[ 21, 49406, 25555, 1303, 1174 ]

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",...

[ 36, 1, 1, 3, 1, 5, 3, 1, 37, 2, 73 ]

11

true

Family

Clp protease proteolytic subunit /Translocation-enhancing protein TepA

ClpP/TepA

9

IPR023563

23,563

Large ribosomal subunit protein uL13, conserved site

Ribosomal_uL13_CS

Conserved_site

21,312

false

This entry represents a conserved region located in the C-terminal section of uL13 proteins. Ribosomal protein uL13 is one of the proteins from the large ribosomal subunit [ ]. In Escherichia coli, uL13 is known to be one of the early assembly proteins of the 50S ribosomal subunit. uL13 proteins were previously known a...

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

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

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

3

[ "PROSITE" ]

[ "PS00783" ]

[ "RIBOSOMAL_L13" ]

[ 21312 ]

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-5389840", "R-BTA-5419276", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-BTA-9937383", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-5389840", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-BTA-9937383", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-...

74

[ "1ffk", "1j3a", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1ml5", "1n8r", "1nji", "1nkw", "1nwx", "1nwy", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1sm1", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk"...

1,838

[ "PUB00002889", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "8119894", "11297922", "11290319", "11114498" ]

[ "A leucine zipper-like motif and a basic region-leucine zipper-like element in rat ribosomal protein L13a. Identification of the tum- transplantation antigen P198.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal protein...

[ 1994, 2001, 2001, 2000 ]

4

[]

0

null

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

[ 692, 14454, 5833, 333 ]

4

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

[ 15, 1, 3, 1, 1, 12, 9, 2, 7, 6, 3, 3, 6 ]

13

true

Conserved_site

Large ribosomal subunit protein uL13, conserved site

Ribosomal_uL13_CS

1

IPR023566

23,566

Peptidyl-prolyl cis-trans isomerase Fpr3/Fpr4-like

PPIase_Fpr3/Fpr4-like

Family

2,470

false

FK506-binding proteins (FKBPs) are a particular class of peptidyl-prolyl cis-trans isomerases (PPIases) ( ) [ ]. This entry represents a group of nuclear FK506-binding proteins that act as histone chaperones. They each containing an extended acidic domain in addition to the conserved FK506-binding/peptidylprolyl isomer...

[ "GO:0003755" ]

[ "peptidyl-prolyl cis-trans isomerase activity" ]

[ "molecular_function" ]

1

[ "PIRSF" ]

[ "PIRSF001473" ]

[ "FK506-bp_FPR3" ]

[ 2470 ]

1

[ "EC" ]

[ "5.2.1.8" ]

[ "EC:5.2.1.8" ]

1

[]

0

[ "PUB00083172", "PUB00094164", "PUB00094165", "PUB00094166" ]

[ "15353370", "24297734", "20142844", "14981505" ]

[ "Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases.", "Nuclear FKBPs, Fpr3 and Fpr4 affect genome-wide genes transcription.", "AtFKBP53 is a histone chaperone required for repression of ribosomal RNA gene expression in Arabidopsis.", "A nuclear FK506-binding protein is a histone ch...

[ 2004, 2014, 2010, 2004 ]

4

[]

0

null

[ "Eukaryota" ]

[ 2470 ]

1

[ "Arabidopsis thaliana", "Drosophila melanogaster", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

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

6

true

Family

Peptidyl-prolyl cis-trans isomerase Fpr3/Fpr4-like

PPIase_Fpr3/Fpr4-like

1

IPR023569

23,569

Prokineticin domain

Prokineticin_domain

Domain

2,275

false

The prokineticin family includes prokinectin itself and related proteins such as BM8 and the AVIToxins. The suprachiasmatic nucleus (SCN) controls the circadian rhythm of physiological and behavioural processes in mammals. It has been shown that prokineticin 2 (PK2), a cysteine-rich secreted protein, functions as an ou...

[]

0

[ "PFAM" ]

[ "PF06607" ]

[ "Prokineticin" ]

[ 2275 ]

1

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

[ "R-HSA-375276", "R-HSA-416476", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476" ]

[ "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476" ]

6

[ "1imt", "2kra" ]

2

[ "PUB00012756" ]

[ "12024206" ]

[ "Prokineticin 2 transmits the behavioural circadian rhythm of the suprachiasmatic nucleus." ]

[ 2002 ]

1

[]

[ "IPR047299" ]

0

1

0

[ "Bacteria", "Opisthokonta" ]

[ 3, 2272 ]

2

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

[ 5, 4, 4, 12 ]

4

true

Domain

Prokineticin domain

Prokineticin_domain

5

IPR023572

23,572

Archease domain

Archease_dom

Domain

5,395

false

The archease superfamily of proteins are represented in all three domains of life. Archease genes are generally located adjacent to genes encoding proteins involved in DNA or RNA processing and therefore have been predicted to be modulators or chaperones involved in DNA or RNA metabolism. Many of the roles of archeases...

[]

0

[ "PFAM" ]

[ "PF01951" ]

[ "Archease" ]

[ 5395 ]

1

[ "REACTOME" ]

[ "R-HSA-6784531" ]

[ "REACTOME:R-HSA-6784531" ]

1

[ "1j5u", "1jw3", "4n2p", "5yz1", "5yzj", "5yzl", "8btx", "8odo", "8odp" ]

9

[ "PUB00020987", "PUB00045441" ]

[ "11854485", "17470432" ]

[ "An NMR approach to structural proteomics.", "Archease from Pyrococcus abyssi improves substrate specificity and solubility of a tRNA m5C methyltransferase." ]

[ 2002, 2007 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Halorubrum virus BJ1", "unclassified sequences" ]

[ 876, 1511, 2897, 1, 110 ]

5

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

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

6

true

Domain

Archease domain

Archease_dom

4

IPR023573

23,573

Large ribosomal subunit protein eL20 domain

Ribosomal_eL20_dom

Domain

6,867

false

This entry includes the large ribosomal subunit protein eL20 from archaea (previously known as 50S ribosomal protein L18A) and eukaryotes (also known as L20 and 60S ribosomal protein L18a) [ , ].

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

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

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

3

[ "PFAM" ]

[ "PF01775" ]

[ "Ribosomal_L18A" ]

[ 6867 ]

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-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72706", "R-DDI-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...

69

[ "2jxt", "3j6x", "3j6y", "3j77", "3j78", "3j79", "3j7o", "3j7p", "3j7q", "3j7r", "3j92", "3jag", "3jah", "3jai", "3jaj", "3jan", "3jbn", "3jbo", "3jbp", "3jcs", "3jct", "4adx", "4d5y", "4d67", "4u3m", "4u3n", "4u3u", "4u4n", "4u4o", "4u4q", "4u4r", "4u4u"...

609

[ "PUB00000194", "PUB00006236" ]

[ "1840484", "3371159" ]

[ "The primary structure of rat ribosomal protein L38.", "The primary structure of rat ribosomal protein L18." ]

[ 1991, 1988 ]

2

[]

0

null

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

[ 737, 2, 6107, 21 ]

4

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

[ 12, 1, 1, 1, 11, 7, 2, 6, 8, 2, 2, 23 ]

12

true

Domain

Large ribosomal subunit protein eL20 domain

Ribosomal_eL20_dom

2

IPR023574

23,574

Large ribosomal subunit protein uL4 domain superfamily

Ribosomal_uL4_dom_sf

Homologous_superfamily

38,043

false

This superfamily represents a domain found in the large ribosomal subunit protein uL4 (also known as L4/L1). Its structure consists of three layers (α/β/α) with parallel β-sheet of four strands. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are expose...

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

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

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

3

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.40.1370.10", "SSF52166" ]

[ "", "" ]

[ 38019, 37929 ]

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-5389840", "R-BTA-5419276", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-BTA-9937383", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-5389840", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-BTA-9937383", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-...

76

[ "1dmg", "1ffk", "1j5a", "1jj2", "1jzx", "1jzy", "1jzz", "1k01", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1ml5", "1n8r", "1nji", "1nkw", "1nwx", "1nwy", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1sm1", "1vq4", "1vq5"...

1,989

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

[ 955, 24158, 12382, 548 ]

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",...

[ 28, 2, 3, 3, 1, 17, 9, 2, 15, 10, 3, 3, 27 ]

13

true

Homologous_superfamily

Large ribosomal subunit protein uL4 domain superfamily

Ribosomal_uL4_dom_sf

2

IPR023575

23,575

Small ribosomal subunit protein uS19, superfamily

Ribosomal_uS19_SF

Homologous_superfamily

50,720

false

The signatures in this entry match the structural unit of the ribosomal S19 family. The small subunit ribosomal proteins can be categorised as: primary binding proteins, which bind directly and independently to 16S rRNA; secondary binding proteins, which display no specific affinity for 16S rRNA, but its assembly is co...

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

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

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

3

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.30.860.10", "SSF54570" ]

[ "", "" ]

[ 50672, 50395 ]

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-72649", "R-BTA-72689", "R-BTA-72695", "R-BTA-72702", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72649", "R-CEL-72689", "R-CEL-72695", "R-CEL-72702", "R-CEL-72706", "R-CEL-975956", ...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72695", "REACTOME:R-BTA-72702", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-179933...

100

[ "1fjg", "1fka", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1qkf", "1qkh", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xmo", "1xmq", "1xnq"...

1,756

[ "PUB00001612", "PUB00004907", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "2044758", "9371771", "11297922", "11290319", "11114498" ]

[ "rig encodes ribosomal protein S15. The primary structure of mammalian ribosomal protein S15.", "Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: str...

[ 1991, 1997, 2001, 2001, 2000 ]

5

[]

0

null

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

[ 916, 23220, 26132, 452 ]

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",...

[ 35, 1, 1, 2, 1, 8, 4, 2, 10, 4, 2, 3, 42 ]

13

true

Homologous_superfamily

Small ribosomal subunit protein uS19, superfamily

Ribosomal_uS19_SF

6

IPR023576

23,576

UbiE/COQ5 methyltransferase, conserved site

UbiE/COQ5_MeTrFase_CS

Conserved_site

28,099

false

A number of methyltransferases have been shown to share regions of similarities [ ]. Apart from the ubiquinone/menaquinone biosynthesis methyltransferases (for example, the C-methyltransferase from the ubiE gene of Escherichia coli), the ubiquinone biosynthesis methyltransferases (for example, the C-methyltransferase f...

[ "GO:0008168" ]

[ "methyltransferase activity" ]

[ "molecular_function" ]

1

[ "PROSITE", "PROSITE" ]

[ "PS01183", "PS01184" ]

[ "UBIE_1", "UBIE_2" ]

[ 22239, 22545 ]

2

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

[ "2.1.1.163", "2.1.1.201", "PWY-5839", "PWY-5844", "PWY-5849", "PWY-5855", "PWY-5856", "PWY-5857", "PWY-5870", "PWY-5871", "PWY-5872", "PWY-5873", "PWY-5890", "PWY-5891", "PWY-5892", "PWY-5895", "PWY-6708", "PWY-7230", "PWY-7996", "R-BTA-2142789", "R-CEL-2142789", "R-DDI-214...

[ "EC:2.1.1.163", "EC:2.1.1.201", "METACYC:PWY-5839", "METACYC:PWY-5844", "METACYC:PWY-5849", "METACYC:PWY-5855", "METACYC:PWY-5856", "METACYC:PWY-5857", "METACYC:PWY-5870", "METACYC:PWY-5871", "METACYC:PWY-5872", "METACYC:PWY-5873", "METACYC:PWY-5890", "METACYC:PWY-5891", "METACYC:PWY-589...

31

[ "1vl5", "2zfu", "3sm3", "4obw", "4obx" ]

5

[ "PUB00002307" ]

[ "9045837" ]

[ "A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene." ]

[ 1997 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctRlz6", "unclassified sequences" ]

[ 272, 21545, 5869, 1, 412 ]

5

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

[ 6, 1, 1, 2, 1, 6, 2, 1, 2, 9, 1, 1, 17 ]

13

true

Conserved_site

UbiE/COQ5 methyltransferase, conserved site

UbiE/COQ5_MeTrFase_CS

4

IPR023577

23,577

CYTH domain

CYTH_domain

Domain

26,992

false

The entry represents the CYTH domain. The bacterial CyaB like adenylyl cyclase and the mammalian thiamine triphosphatases (ThTPases) define a superfamily of catalytic domains called the CYTH (CyaB, thiamine triphosphatase) domain that is present in all three superkingdoms of life [ ]. Proteins containing this domain ac...

[]

0

[ "PFAM", "PROFILE", "SMART" ]

[ "PF01928", "PS51707", "SM01118" ]

[ "CYTH", "CYTH", "CYTH" ]

[ 25795, 24878, 22832 ]

3

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

[ "3.6.1", "R-BTA-196819", "R-DDI-196807", "R-DDI-73614", "R-HSA-196819", "R-MMU-196819", "R-RNO-196819" ]

[ "EC:3.6.1", "REACTOME:R-BTA-196819", "REACTOME:R-DDI-196807", "REACTOME:R-DDI-73614", "REACTOME:R-HSA-196819", "REACTOME:R-MMU-196819", "REACTOME:R-RNO-196819" ]

7

[ "1yem", "2aca", "2dc4", "2een", "2fbl", "2fjt", "2gfg", "2jmu", "3bhd", "3n0y", "3n0z", "3n10", "3sy3", "3tj7", "3tvl", "3typ", "3v85", "5a5y", "5a60", "5a61", "5a64", "5a65", "5a66", "5a67", "5a68", "6yp4", "7ns8", "7ns9", "7nsa", "7nsd", "7nsf", "7oa2"...

35

[ "PUB00010433", "PUB00076458", "PUB00076464" ]

[ "12456267", "22984449", "24021036" ]

[ "The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates.", "High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved.", "Thiamine triphosphatase and the CYTH superf...

[ 2002, 2012, 2013 ]

3

[]

0

null

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

[ 870, 21326, 4489, 44, 263 ]

5

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

[ 13, 1, 8, 3, 1, 3, 1, 8, 5, 8 ]

10

true

Domain

CYTH domain

CYTH_domain

6

IPR023578

23,578

Ras guanine nucleotide exchange factor domain superfamily

Ras_GEF_dom_sf

Homologous_superfamily

68,439

false

Small GTPases of the Ras family alternate between 2 conformations induced by the binding of either GTP or GDP. Guanine nucleotide exchange factors (GEFs) induce the dissociation of GDP to allow association of the more abundant GTP. The Ras-like family of small GTPases includes, among others, Ras, Rap1, R-ras, and Ral. ...

[]

0

[ "SSF" ]

[ "SSF48366" ]

[ "" ]

[ 68439 ]

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-354192", "R-BTA-392517", "R-BTA-5673001", "R-CEL-1433557", "R-CEL-1433559", "R-CEL-179812", "R-CEL-180336", "R-CEL-1855204", "R-CEL-186763", "R-CEL-193648", "R-CEL-1963640", "R-CEL-2179392", "R-CEL-354192", "R-CEL-354194", "R-CEL-375165", "R-CEL-381676", "R-CEL-392517", "R-C...

[ "REACTOME:R-BTA-354192", "REACTOME:R-BTA-392517", "REACTOME:R-BTA-5673001", "REACTOME:R-CEL-1433557", "REACTOME:R-CEL-1433559", "REACTOME:R-CEL-179812", "REACTOME:R-CEL-180336", "REACTOME:R-CEL-1855204", "REACTOME:R-CEL-186763", "REACTOME:R-CEL-193648", "REACTOME:R-CEL-1963640", "REACTOME:R-CE...

231

[ "1bkd", "1nvu", "1nvv", "1nvw", "1nvx", "1xd2", "1xd4", "1xdv", "2byv", "2ii0", "2ije", "3cf6", "3ksy", "3qxl", "3t6a", "3t6g", "4f7z", "4jgw", "4l9m", "4mgi", "4mgk", "4mgy", "4mgz", "4mh0", "4nyi", "4nyj", "4nym", "4uru", "4urv", "4urw", "4urx", "4ury"...

116

[ "PUB00010624", "PUB00032394" ]

[ "10579920", "15507210" ]

[ "Ras and Rap1: two highly related small GTPases with distinct function.", "Structural analysis of autoinhibition in the Ras activator Son of sevenless." ]

[ 1999, 2004 ]

2

[]

0

null

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

[ 155, 68257, 25, 2 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...

[ 26, 326, 38, 211, 149, 4, 176, 5, 2 ]

9

true

Homologous_superfamily

Ras guanine nucleotide exchange factor domain superfamily

Ras_GEF_dom_sf

8

IPR023580

23,580

RNA polymerase subunit RPB10

RNA_pol_su_RPB10

Homologous_superfamily

4,988

false

The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukaryota. Structure determination of this subunit reveals a zinc-bundle topology, consisting of three α-helices stabilised by a zinc ion [ ].

[]

0

[ "SSF" ]

[ "SSF46924" ]

[ "" ]

[ 4988 ]

1

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

[ "2.7.7.6", "R-BTA-112382", "R-BTA-113418", "R-BTA-5250924", "R-BTA-5578749", "R-BTA-674695", "R-BTA-6781823", "R-BTA-6782135", "R-BTA-6782210", "R-BTA-6796648", "R-BTA-6803529", "R-BTA-6807505", "R-BTA-72086", "R-BTA-72163", "R-BTA-72165", "R-BTA-72203", "R-BTA-73762", "R-BTA-73772...

[ "EC:2.7.7.6", "REACTOME:R-BTA-112382", "REACTOME:R-BTA-113418", "REACTOME:R-BTA-5250924", "REACTOME:R-BTA-5578749", "REACTOME:R-BTA-674695", "REACTOME:R-BTA-6781823", "REACTOME:R-BTA-6782135", "REACTOME:R-BTA-6782210", "REACTOME:R-BTA-6796648", "REACTOME:R-BTA-6803529", "REACTOME:R-BTA-6807505...

216

[ "1ef4", "1i3q", "1i50", "1i6h", "1k83", "1nik", "1nt9", "1pqv", "1r5u", "1r9s", "1r9t", "1sfo", "1twa", "1twc", "1twf", "1twg", "1twh", "1wcm", "1y1v", "1y1w", "1y1y", "1y77", "2b63", "2b8k", "2e2h", "2e2i", "2e2j", "2ja5", "2ja6", "2ja7", "2ja8", "2nvq"...

546

[ "PUB00015096" ]

[ "10841539" ]

[ "Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum." ]

[ 2000 ]

1

[]

0

null

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

[ 879, 7, 3740, 84, 278 ]

5

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

[ 6, 1, 1, 2, 1, 1, 1, 7, 4, 1, 1, 10 ]

12

true

Homologous_superfamily

RNA polymerase subunit RPB10

RNA_pol_su_RPB10

5

IPR023581

23,581

Platelet-derived growth factor, conserved site

PD_growth_factor_CS

Conserved_site

7,990

false

This entry represents a conserved site found in PDGF and VEGF families, amongst others, that includes four of the eight cysteines conserved in the sequences of these proteins. In PDGF, these cysteines are known to be involved in intra and inter-chain disulphide bonds [ ]. Platelet-derived growth factor (PDGF) [ , , ] i...

[]

0

[ "PROSITE" ]

[ "PS00249" ]

[ "PDGF_1" ]

[ 7990 ]

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-114608", "R-BTA-1257604", "R-BTA-186763", "R-BTA-186797", "R-BTA-194313", "R-BTA-195399", "R-BTA-4420097", "R-BTA-5218921", "R-BTA-5673001", "R-BTA-6811558", "R-CFA-114608", "R-CFA-1257604", "R-CFA-186763", "R-CFA-186797", "R-CFA-5673001", "R-CFA-6811558", "R-DRE-114608", "R...

[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-1257604", "REACTOME:R-BTA-186763", "REACTOME:R-BTA-186797", "REACTOME:R-BTA-194313", "REACTOME:R-BTA-195399", "REACTOME:R-BTA-4420097", "REACTOME:R-BTA-5218921", "REACTOME:R-BTA-5673001", "REACTOME:R-BTA-6811558", "REACTOME:R-CFA-114608", "REACTOME:R-CF...

59

[ "1bj1", "1cz8", "1flt", "1fzv", "1kat", "1pdg", "1qty", "1rv6", "1tzh", "1tzi", "1vpf", "1vpp", "1wq8", "1wq9", "2c7w", "2fjg", "2fjh", "2gnn", "2qr0", "2vpf", "2vwe", "2x1w", "2x1x", "2xac", "2xv7", "3bdy", "3mjg", "3mjk", "3p9w", "3qtk", "3s1b", "3s1k"...

69

[ "PUB00000590", "PUB00001226", "PUB00001228", "PUB00001288", "PUB00004494", "PUB00004886", "PUB00014075", "PUB00032112", "PUB00081653", "PUB00081654", "PUB00081655" ]

[ "2546599", "1396586", "1425569", "8617204", "7681160", "8637916", "12952899", "9207067", "7640655", "8323751", "11345501" ]

[ "Structure and function of platelet-derived growth factor (PDGF) and related proteins.", "Crystal structure of human platelet-derived growth factor BB.", "Structural and functional studies on platelet-derived growth factor.", "A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR...

[ 1989, 1992, 1992, 1996, 1993, 1996, 2003, 1997, 1995, 1993, 2001 ]

11

[]

0

null

[ "Eumetazoa", "Viruses" ]

[ 7926, 64 ]

2

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

[ 28, 36, 24, 50 ]

4

true

Conserved_site

Platelet-derived growth factor, conserved site

PD_growth_factor_CS

3