LiteFold/InterPro · Datasets at Hugging Face

IPR023715

23,715

Trehalase, cytoplasmic

Cyt_trehalase

Family

868

false

O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...

[ "GO:0004555", "GO:0005993", "GO:0071474", "GO:0005737" ]

[ "alpha,alpha-trehalase activity", "trehalose catabolic process", "cellular hyperosmotic response", "cytoplasm" ]

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

4

[ "HAMAP" ]

[ "MF_01059" ]

[ "Cyt_trehalase" ]

[ 868 ]

1

[ "EC" ]

[ "3.2.1.28" ]

[ "EC:3.2.1.28" ]

1

[]

0

[ "PUB00002824", "PUB00004870", "PUB00005266", "PUB00054952", "PUB00054953" ]

[ "8444853", "7624375", "8535779", "8892826", "10816581" ]

[ "Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae.", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "Characterization of a cytoplasmic trehalase of Escherichia ...

[ 1993, 1995, 1995, 1996, 2000 ]

5

[ "IPR001661" ]

[]

1

0

1

[ "Pseudomonadota", "Trichuris trichiura" ]

[ 867, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Trehalase, cytoplasmic

Cyt_trehalase

2

IPR023716

23,716

Proline-tRNA ligase, class IIa, type 2

Prolyl-tRNA_ligase_IIa_type2

Family

2,642

false

Proline-tRNA ligase (also known as Prolyl-tRNA synthetase) belongs to class IIa. Proline-tRNA ligase( ) exists in two forms, which are loosely related. The first form is present in the majority of eubacteria species. The second one, present in some eubacteria, is essentially present in archaea and eukaryota. Proline-tR...

[ "GO:0004827", "GO:0005524", "GO:0006433", "GO:0005737" ]

[ "proline-tRNA ligase activity", "ATP binding", "prolyl-tRNA aminoacylation", "cytoplasm" ]

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

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_01570", "NF008979" ]

[ "Pro_tRNA_synth_type2", "PRK12325.1" ]

[ 2579, 2642 ]

2

[ "EC" ]

[ "6.1.1.15" ]

[ "EC:6.1.1.15" ]

1

[ "2i4l", "2i4m", "2i4n", "2i4o" ]

4

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00054954", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "12130657", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2002, 2000, 2002 ]

10

[ "IPR004500" ]

[]

1

0

1

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

[ 2604, 15, 23 ]

3

[]

0

true

Family

Proline-tRNA ligase, class IIa, type 2

Prolyl-tRNA_ligase_IIa_type2

5

IPR023717

23,717

Prolyl-tRNA synthetase, class IIa, type 1

Pro-tRNA-Synthase_IIa_type1

Family

17,509

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0004827", "GO:0005524", "GO:0006433", "GO:0005737" ]

[ "proline-tRNA ligase activity", "ATP binding", "prolyl-tRNA aminoacylation", "cytoplasm" ]

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

4

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

[ "MF_01569", "NF006625", "PIRSF001535" ]

[ "Pro_tRNA_synth_type1", "PRK09194.1", "ProRS_1" ]

[ 17263, 17481, 8017 ]

3

[ "EC" ]

[ "6.1.1.15" ]

[ "EC:6.1.1.15" ]

1

[ "2j3l", "2j3m", "5ucm", "5znj", "5znk", "8w8j", "8w8l", "8w9i" ]

8

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006366", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "9062123", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1997, 2000, 1990, 1999, 2000, 2002 ]

10

[ "IPR004500" ]

[]

1

0

1

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

[ 17178, 24, 307 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Prolyl-tRNA synthetase, class IIa, type 1

Pro-tRNA-Synthase_IIa_type1

7

IPR023719

23,719

Aliphatic amidase

Aliphatic_amidase

Family

698

false

These enzymes catalyzes the hydrolysis of short-chain aliphatic amides to their corresponding organic acids with release of ammonia [ ]. They also exhibit in vitro acyl transferase activity,transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates. Aliphatic amidases contain 1 CN hydrolas...

[ "GO:0004040" ]

[ "amidase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01242" ]

[ "Aliphatic_amidase" ]

[ 698 ]

1

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

[ "3.5.1.4", "PWY-3161", "PWY-5025", "PWY-581", "PWY-7308" ]

[ "EC:3.5.1.4", "METACYC:PWY-3161", "METACYC:PWY-5025", "METACYC:PWY-581", "METACYC:PWY-7308" ]

5

[ "2plq", "2uxy", "4gyl", "4gyn", "4kzf", "4lf0" ]

6

[ "PUB00055086" ]

[ "10978771" ]

[ "Cloning and expression of the nitrile hydratase and amidase genes from Bacillus sp. BR449 into Escherichia coli." ]

[ 2000 ]

1

[]

0

null

[ "Bacteria", "unclassified sequences" ]

[ 691, 7 ]

2

[]

0

true

Family

Aliphatic amidase

Aliphatic_amidase

2

IPR023720

23,720

Trehalase, periplasmic

Trehalase_periplasmic

Family

1,630

false

O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...

[ "GO:0004555", "GO:0005993", "GO:0071474", "GO:0042597" ]

[ "alpha,alpha-trehalase activity", "trehalose catabolic process", "cellular hyperosmotic response", "periplasmic space" ]

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

4

[ "HAMAP" ]

[ "MF_01060" ]

[ "Peripl_trehalase" ]

[ 1630 ]

1

[ "EC" ]

[ "3.2.1.28" ]

[ "EC:3.2.1.28" ]

1

[ "2jf4", "2jg0", "2jjb", "2wyn", "5z66", "5z6h" ]

6

[ "PUB00002824", "PUB00004870", "PUB00005266", "PUB00054952", "PUB00054953", "PUB00054955" ]

[ "8444853", "7624375", "8535779", "8892826", "10816581", "1710760" ]

[ "Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae.", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "Characterization of a cytoplasmic trehalase of Escherichia ...

[ 1993, 1995, 1995, 1996, 2000, 1991 ]

6

[ "IPR001661" ]

[]

1

0

1

[ "Pseudomonadota" ]

[ 1630 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Trehalase, periplasmic

Trehalase_periplasmic

8

IPR023721

23,721

Multidrug resistance protein MdtD

Multi-R_MdtD

Family

1,303

false

This putative multidrug resistance protein is transcriptionally regulated by the response regulator BaeR [ , ].

[]

0

[ "HAMAP" ]

[ "MF_01577" ]

[ "MFS_MdtD" ]

[ 1303 ]

1

[]

0

[]

0

[ "PUB00053900", "PUB00053915" ]

[ "12107133", "12107134" ]

[ "The putative response regulator BaeR stimulates multidrug resistance of Escherichia coli via a novel multidrug exporter system, MdtABC.", "The baeSR two-component regulatory system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobi...

[ 2002, 2002 ]

2

[ "IPR011701" ]

[]

1

0

1

[ "Opisthokonta", "Pseudomonadota" ]

[ 2, 1301 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Multidrug resistance protein MdtD

Multi-R_MdtD

8

IPR023722

23,722

Enterobactin exporter, EntS

Enterobactin_exp_EntS

Family

1,153

false

This group of proteins exports the siderophore enterobactin out of the cell and belongs to the major facilitator superfamily [ , ].

[ "GO:0042931", "GO:0042930", "GO:0005886" ]

[ "enterobactin transmembrane transporter activity", "enterobactin transport", "plasma membrane" ]

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

3

[ "HAMAP" ]

[ "MF_01436" ]

[ "MFS_EntS" ]

[ 1153 ]

1

[ "REACTOME" ]

[ "R-HSA-9638334" ]

[ "REACTOME:R-HSA-9638334" ]

1

[]

0

[ "PUB00053441", "PUB00060969" ]

[ "12068807", "16166532" ]

[ "Export of the siderophore enterobactin in Escherichia coli: involvement of a 43 kDa membrane exporter.", "TolC is involved in enterobactin efflux across the outer membrane of Escherichia coli." ]

[ 2002, 2005 ]

2

[ "IPR010290" ]

[]

1

0

1

[ "Bacteria" ]

[ 1153 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Enterobactin exporter, EntS

Enterobactin_exp_EntS

3

IPR023723

23,723

Glucan biosynthesis protein C

Glucans_biosynth_C

Family

1,245

false

This entry represents bacterial glucans biosynthesis proteins, which are responsible for the succinyl substitution of periplasmic glucans [ ].

[ "GO:0016741" ]

[ "transferase activity, transferring one-carbon groups" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01066", "NF003014" ]

[ "MdoC_OpgC", "PRK03854.1" ]

[ 1180, 1245 ]

2

[]

0

[]

0

[ "PUB00054956" ]

[ "10368134" ]

[ "The mdoC gene of Escherichia coli encodes a membrane protein that is required for succinylation of osmoregulated periplasmic glucans." ]

[ 1999 ]

1

[]

0

null

[ "Bacteria" ]

[ 1245 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glucan biosynthesis protein C

Glucans_biosynth_C

1

IPR023724

23,724

Glucan biosynthesis, MdoD

Glucan_biosyn_MdoD

Family

1,797

false

Membrane-derived oligosaccharides (MDO) are members of a family of glucans found in the periplasmic space of Gram-negative bacteria. MdoG has been shown to be necessary for the synthesis of MDO [ ], but its exact function is not known yet. MdoD, an MdoG paralog, is a twin-arginine-dependent periplasmic protein that con...

[]

0

[ "HAMAP" ]

[ "MF_01068" ]

[ "MdoD_OpgD" ]

[ 1797 ]

1

[]

0

[ "8iox", "8ip1", "8x18", "9e01", "9e08" ]

5

[ "PUB00027713", "PUB00027777", "PUB00027791" ]

[ "15175282", "7934824", "11325942" ]

[ "Identification of mdoD, an mdoG paralog which encodes a twin-arginine-dependent periplasmic protein that controls osmoregulated periplasmic glucan backbone structures.", "Homology between a genetic locus (mdoA) involved in the osmoregulated biosynthesis of periplasmic glucans in Escherichia coli and a genetic lo...

[ 2004, 1993, 2001 ]

3

[ "IPR014438" ]

[]

1

0

1

[ "Opisthokonta", "Pseudomonadati" ]

[ 3, 1794 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glucan biosynthesis, MdoD

Glucan_biosyn_MdoD

7

IPR023725

23,725

Glucan biosynthesis glucosyltransferase H

Glucans_biosynth_gluTrFase_H

Family

2,781

false

Proteins in this entry are thought to be glucan biosynthesis glucosyltransferases, which play a role in the synthesis of osmoregulated periplasmic glycoproteins.

[ "GO:0016758" ]

[ "hexosyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01072" ]

[ "MdoH_OpgH" ]

[ 2781 ]

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"...

[ "2.4.1.-", "PWY-1901", "PWY-1961", "PWY-1981", "PWY-2021", "PWY-2881", "PWY-2901", "PWY-2902", "PWY-4421", "PWY-4801", "PWY-5094", "PWY-5105", "PWY-5129", "PWY-5139", "PWY-5160", "PWY-5161", "PWY-5268", "PWY-5284", "PWY-5286", "PWY-5310", "PWY-5312", "PWY-5313", "PWY-5317...

[ "EC:2.4.1.-", "METACYC:PWY-1901", "METACYC:PWY-1961", "METACYC:PWY-1981", "METACYC:PWY-2021", "METACYC:PWY-2881", "METACYC:PWY-2901", "METACYC:PWY-2902", "METACYC:PWY-4421", "METACYC:PWY-4801", "METACYC:PWY-5094", "METACYC:PWY-5105", "METACYC:PWY-5129", "METACYC:PWY-5139", "METACYC:PWY-5...

200

[]

0

[]

0

[]

0

null

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

[ 2776, 4, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glucan biosynthesis glucosyltransferase H

Glucans_biosynth_gluTrFase_H

9

IPR023726

23,726

Threonine/serine transporter TdcC

Thr/Ser_transpt_TdcC

Family

784

false

This entry represents the threonine/serine transporter TdcC [ , ]. It is involved in the import of threonine and serine into the cell, with the concomitant import of a proton (symport system). TdcC is a multi-pass membrane protein [ ].

[ "GO:0015194", "GO:0015565", "GO:0015826", "GO:0032329", "GO:0016020" ]

[ "L-serine transmembrane transporter activity", "threonine efflux transmembrane transporter activity", "threonine transport", "serine transport", "membrane" ]

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

5

[ "HAMAP", "NCBIFAM" ]

[ "MF_01583", "NF010152" ]

[ "Thr_Ser_transp_TdcC", "PRK13629.1" ]

[ 761, 784 ]

2

[]

0

[]

0

[ "PUB00042652", "PUB00054957", "PUB00060294" ]

[ "15919996", "2115866", "9498571" ]

[ "Global topology analysis of the Escherichia coli inner membrane proteome.", "A novel membrane-associated threonine permease encoded by the tdcC gene of Escherichia coli.", "Isolation and characterization of an Escherichia coli mutant lacking the major serine transporter, and cloning of a serine transporter gen...

[ 2005, 1990, 1997 ]

3

[ "IPR004694" ]

[]

1

0

1

[ "Bacteria" ]

[ 784 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Threonine/serine transporter TdcC

Thr/Ser_transpt_TdcC

6

IPR023727

23,727

Lysophospholipid transporter LplT

LysoPLipid__transptr_LplT

Family

1,201

false

Lysophospholipid transporter LplT catalyzes the facilitated diffusion of 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) into the cell [ ].

[ "GO:0051978", "GO:0051977", "GO:0005886" ]

[ "lysophospholipid:sodium symporter activity", "lysophospholipid transport", "plasma membrane" ]

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

3

[ "HAMAP" ]

[ "MF_01585" ]

[ "MFS_LplT" ]

[ 1201 ]

1

[]

0

[]

0

[ "PUB00054958" ]

[ "15661733" ]

[ "Lysophospholipid flipping across the Escherichia coli inner membrane catalyzed by a transporter (LplT) belonging to the major facilitator superfamily." ]

[ 2005 ]

1

[ "IPR011701" ]

[]

1

0

1

[ "Gammaproteobacteria" ]

[ 1201 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Lysophospholipid transporter LplT

LysoPLipid__transptr_LplT

6

IPR023728

23,728

Small heat shock protein IbpA

HSP20_IbpA

Family

933

false

Small heat shock proteins IbpA associate with aggregated proteins, together with IbpB, to stabilise and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-de...

[]

0

[ "HAMAP", "NCBIFAM" ]

[ "MF_02000", "NF008013" ]

[ "HSP20_IbpA", "PRK10743.1" ]

[ 898, 933 ]

2

[]

0

[]

0

[ "PUB00054971", "PUB00054972", "PUB00159850", "PUB00159851" ]

[ "12055295", "12071954", "33839884", "34022209" ]

[ "The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock.", "Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants.", "Novel self-regulation strategy of a s...

[ 2002, 2002, 2021, 2021 ]

4

[]

0

null

[ "Opisthokonta", "Pseudomonadati" ]

[ 2, 931 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Small heat shock protein IbpA

HSP20_IbpA

7

IPR023729

23,729

K(+)/H(+) antiporter NhaP2

NhaP2

Family

1,998

false

This entry represents the NhaP2 family of bacterial K(+)/H(+) antiporters. They are thought to be involved in control of cell volumes under low osmotic conditions [ ]. Vc-NhaP2 from Vibrio cholerae functions as a specific K+/H+ antiporter while retaining the ability to exchange H+ for Na+ and bind (but not exchange wit...

[ "GO:0015386", "GO:0006812", "GO:0006813", "GO:0006884", "GO:0016020" ]

[ "potassium:proton antiporter activity", "monoatomic cation transport", "potassium ion transport", "cell volume homeostasis", "membrane" ]

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

5

[ "HAMAP" ]

[ "MF_01075" ]

[ "NhaP2" ]

[ 1998 ]

1

[]

0

[]

0

[ "PUB00044825", "PUB00071774" ]

[ "11700351", "20163190" ]

[ "Deletion of one of two Escherichia coli genes encoding putative Na+/H+ exchangers (ycgO) perturbs cytoplasmic alkali cation balance at low osmolarity.", "The putative Na+/H+ antiporter of Vibrio cholerae, Vc-NhaP2, mediates the specific K+/H+ exchange in vivo." ]

[ 2001, 2010 ]

2

[]

0

null

[ "Bacteria", "marine sediment metagenome" ]

[ 1997, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

K(+)/H(+) antiporter NhaP2

NhaP2

2

IPR023730

23,730

HTH-type transcriptional repressor NanR

Tscrpt_reg_NanR

Family

676

false

The nan operon encodes a group of proteins that are involved in sialic acid utilisation. Expression of the operon appears to be subject to negative control by the transcriptional repressor, NanR. Sialic acid may induce the nan operon by binding to this repressor [ ]. NanR possesses an N-terminal DNA binding domain, con...

[]

0

[ "HAMAP" ]

[ "MF_01236" ]

[ "HTH_NanR" ]

[ 676 ]

1

[]

0

[ "6on4", "6wfq", "6wg7" ]

3

[ "PUB00019912" ]

[ "9864311" ]

[ "Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli." ]

[ 1999 ]

1

[]

0

null

[ "Gammaproteobacteria" ]

[ 676 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

HTH-type transcriptional repressor NanR

Tscrpt_reg_NanR

6

IPR023732

23,732

Probable [Fe-S]-dependent transcriptional repressor

FeoC

Family

999

false

Bacteria commonly utilise a unique type of transporter, called Feo, to specifically acquire the ferrous (Fe2+) form of iron from their environment. Enterobacterial Feo systems are composed of three proteins: FeoA, a small, soluble SH3-domain protein probably located in the cytosol; FeoB, a large protein which likely fu...

[]

0

[ "HAMAP" ]

[ "MF_01586" ]

[ "FeoC" ]

[ 999 ]

1

[]

0

[ "1xn7", "2k02", "4awx", "7wqu" ]

4

[ "PUB00035969" ]

[ "16718600" ]

[ "Feo--transport of ferrous iron into bacteria." ]

[ 2006 ]

1

[]

0

null

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

[ 996, 1, 2 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Probable [Fe-S]-dependent transcriptional repressor

FeoC

2

IPR023733

23,733

Pyrophosphatase PpaX

Pyrophosphatase_Ppax

Family

795

false

Microorganisms that can utilise halogenated compounds as growth substrates produce enzymes that cleave carbon-halogen bonds and are commonly called dehalogenases. The hydrolytic dehalogenases catalyse a nucleophilic displacement reaction, with water as the sole co-substrate [ ]. They are divided into haloalkane dehalog...

[ "GO:0016462" ]

[ "pyrophosphatase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01250" ]

[ "Pyrophosphat_PpaX" ]

[ 795 ]

1

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

[ "3.6.1.1", "PWY-7805", "PWY-7807" ]

[ "EC:3.6.1.1", "METACYC:PWY-7805", "METACYC:PWY-7807" ]

3

[]

0

[ "PUB00000125", "PUB00003337", "PUB00054962" ]

[ "7826004", "7966317", "12359880" ]

[ "Genetics and biochemistry of dehalogenating enzymes.", "Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.", "Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphory...

[ 1994, 1994, 2002 ]

3

[ "IPR006439" ]

[]

1

0

1

[ "Bacillota" ]

[ 795 ]

1

[]

0

true

Family

Pyrophosphatase PpaX

Pyrophosphatase_Ppax

1

IPR023734

23,734

Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU

TagU

Family

868

false

This entry represents polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU. TagU was previously known as bacterial transcriptional regulator LytR, and was originally described a 35kDa protein which is responsible for attenuation of expression of both itself and the lytABC operon. LytABC form an N-a...

[]

0

[ "HAMAP" ]

[ "MF_01140" ]

[ "TagU_transferase" ]

[ 868 ]

1

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

[ "2.7.8.-", "PWY-6350", "PWY-6580", "PWY-6804", "PWY-7815", "PWY-7816", "PWY-7817", "PWY-7818", "PWY-7819", "PWY-7820", "PWY-7981", "PWY-8248" ]

[ "EC:2.7.8.-", "METACYC:PWY-6350", "METACYC:PWY-6580", "METACYC:PWY-6804", "METACYC:PWY-7815", "METACYC:PWY-7816", "METACYC:PWY-7817", "METACYC:PWY-7818", "METACYC:PWY-7819", "METACYC:PWY-7820", "METACYC:PWY-7981", "METACYC:PWY-8248" ]

12

[]

0

[ "PUB00021031", "PUB00057107" ]

[ "1357079", "21964069" ]

[ "Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier.", "A widespread family of bacterial cell wall assembly proteins." ]

[ 1992, 2011 ]

2

[]

0

null

[ "Bacilli" ]

[ 868 ]

1

[]

0

true

Family

Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU

TagU

7

IPR023735

23,735

Uncharacterised nudix hydrolase NudL

Nudix_NudL

Family

768

false

NudL probably mediates the hydrolysis of some nucleoside diphosphate derivatives, but the function of this protein is currently unknown.

[ "GO:0016818" ]

[ "hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01592" ]

[ "Nudix_NudL" ]

[ 768 ]

1

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

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

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

11

[]

0

[]

0

[ "IPR045121" ]

[]

1

0

1

[ "Enterobacterales", "marine sediment metagenome" ]

[ 767, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised nudix hydrolase NudL

Nudix_NudL

5

IPR023736

23,736

Antiholin-like protein LrgA

Antiholin-like_LrgA

Family

142

false

This entry contains bacterial antiholin-like LrgA proteins, which have been shown to modulate murein hydrolase activity [ ]. Together with holin-like CidA, LrgA function to control cell death and lysis during biofilm development [ ].

[]

0

[ "HAMAP" ]

[ "MF_01141" ]

[ "LrgA" ]

[ 142 ]

1

[]

0

[]

0

[ "PUB00009887", "PUB00067860" ]

[ "10714982", "21421752" ]

[ "The Staphylococcus aureus lrgAB operon modulates murein hydrolase activity and penicillin tolerance.", "Staphylococcus aureus CidA and LrgA proteins exhibit holin-like properties." ]

[ 2000, 2011 ]

2

[ "IPR005538" ]

[]

1

0

1

[ "Bacillales" ]

[ 142 ]

1

[]

0

true

Family

Antiholin-like protein LrgA

Antiholin-like_LrgA

4

IPR023737

23,737

Spermidine export protein MdtI

Spermidine_export_MdtI

Family

792

false

Spermidine export protein MdtI catalyzes the excretion of spermidine. It can also confer resistance to deoxycholate and SDS [ , ]. It is integral to membrane [ ].

[ "GO:0015606", "GO:0015848", "GO:0005886" ]

[ "spermidine transmembrane transporter activity", "spermidine transport", "plasma membrane" ]

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

3

[ "HAMAP" ]

[ "MF_01597" ]

[ "MdtI" ]

[ 792 ]

1

[]

0

[]

0

[ "PUB00045001", "PUB00053912", "PUB00054963" ]

[ "11867724", "11566977", "18039771" ]

[ "Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysis.", "Analysis of a complete library of putative drug transporter genes in Escherichia coli.", "Identification of a spermidine excretion protein complex (MdtJI) in Escherichia coli." ]

[ 2002, 2001, 2008 ]

3

[ "IPR045324" ]

[]

1

0

1

[ "Gammaproteobacteria" ]

[ 792 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Spermidine export protein MdtI

Spermidine_export_MdtI

9

IPR023738

23,738

Maltoporin

Family

1,419

false

Maltoporin (LamB) is involved in the transport of maltose and maltodextrins [ , ]. It forms homotrimers composing three 18-stranded antiparallel β-barrels, containing three independent channels [ ].

[ "GO:0015481", "GO:0042958", "GO:0015768", "GO:0042956", "GO:0009279" ]

[ "maltose transporting porin activity", "maltodextrin transmembrane transporter activity", "maltose transport", "maltodextrin transmembrane transport", "cell outer membrane" ]

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

5

[ "HAMAP" ]

[ "MF_01301" ]

[ "LamB" ]

[ 1419 ]

1

[]

0

[]

0

[ "PUB00054976", "PUB00061721", "PUB00061722" ]

[ "16079137", "12405347", "12700071" ]

[ "Protein complexes of the Escherichia coli cell envelope.", "Mechanism of maltodextrin transport through LamB.", "Maltodextrin transport through lamb." ]

[ 2005, 2002, 2003 ]

3

[ "IPR003192" ]

[]

1

0

1

[ "Bacteria", "Timema californicum" ]

[ 1418, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Maltoporin

3

IPR023739

23,739

3-phenylpropionate/cinnamic acid dioxygenase, ferredoxin subunit

HcaC

Family

69

false

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

[]

0

[ "HAMAP" ]

[ "MF_01650" ]

[ "HcaC" ]

[ 69 ]

1

[]

0

[]

0

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

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

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

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

7

[]

0

null

[ "Enterobacterales" ]

[ 69 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

3-phenylpropionate/cinnamic acid dioxygenase, ferredoxin subunit

HcaC

5

IPR023740

23,740

Spermidine export protein MdtJ

Spermidine_export_MdtJ

Family

818

false

Spermidine export protein MdtJ catalyzes the excretion of spermidine. It can also confer resistance to deoxycholate and SDS [ , ]. It is induced by spermidine.

[ "GO:0015606", "GO:0015848", "GO:0005886" ]

[ "spermidine transmembrane transporter activity", "spermidine transport", "plasma membrane" ]

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

3

[ "HAMAP" ]

[ "MF_01598" ]

[ "MdtJ" ]

[ 818 ]

1

[]

0

[]

0

[ "PUB00053912", "PUB00054963" ]

[ "11566977", "18039771" ]

[ "Analysis of a complete library of putative drug transporter genes in Escherichia coli.", "Identification of a spermidine excretion protein complex (MdtJI) in Escherichia coli." ]

[ 2001, 2008 ]

2

[ "IPR045324" ]

[]

1

0

1

[ "Bacteria" ]

[ 818 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Spermidine export protein MdtJ

Spermidine_export_MdtJ

3

IPR023741

23,741

Lipoate-protein ligase A

Lipoate_ligase_A

Family

1,495

false

Lipoate-protein ligase A catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes [ , ]. It is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carri...

[ "GO:0016979", "GO:0009249" ]

[ "lipoate-protein ligase activity", "protein lipoylation" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01602" ]

[ "LplA" ]

[ 1495 ]

1

[ "EC" ]

[ "6.3.1.20" ]

[ "EC:6.3.1.20" ]

1

[ "1x2g", "1x2h", "3a7a", "3a7r", "4tvw", "4tvy" ]

6

[ "PUB00007382", "PUB00043600" ]

[ "8206909", "7639702" ]

[ "Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product.", "Purification and properties of the lipoate protein ligase of Escherichia coli." ]

[ 1994, 1995 ]

2

[ "IPR004562" ]

[]

1

0

1

[ "Bacteria", "Oryza sativa subsp. indica" ]

[ 1494, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Lipoate-protein ligase A

Lipoate_ligase_A

2

IPR023742

23,742

Iron-sulfur cluster repair protein YftE

FeS-repair_YftE

Family

953

false

YtfE was is also known as regulator of cell morphogenesis and NO signaling because it is involved in anaerobic NO protection [ ]. It is part of a family of di-iron proteins involved in the repair of iron-sulphur clusters [ , ].

[ "GO:0030091" ]

[ "protein repair" ]

[ "biological_process" ]

1

[ "HAMAP" ]

[ "MF_01606" ]

[ "RIC_YtfE" ]

[ 953 ]

1

[]

0

[ "5fnn", "5fnp", "5fny", "7be8", "7bha", "7bhb", "7bhc", "7oyi" ]

8

[ "PUB00016665", "PUB00045447", "PUB00054964" ]

[ "15546870", "18203837", "17289666" ]

[ "New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide.", "Widespread distribution in pathogenic bacteria of di-iron proteins that repair oxidative and nitrosative damage to iron-sulfur centers.", "Escherichia coli di-iron YtfE protein is necessary for the repair of...

[ 2005, 2008, 2007 ]

3

[ "IPR019903" ]

[]

1

0

1

[ "Gammaproteobacteria" ]

[ 953 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Iron-sulfur cluster repair protein YftE

FeS-repair_YftE

9

IPR023743

23,743

Aquaporin Z

Aquaporin_Z

Family

3,580

false

Aquaporins are water channels, present in both higher and lower organisms, that belong to the major intrinsic protein family. Most aquaporins are highly selective for water, though some also facilitate the movement of small uncharged molecules such as glycerol [ ]. In higher eukaryotes these proteins play diverse roles...

[ "GO:0015250", "GO:0006833", "GO:0055085", "GO:0016020" ]

[ "water channel activity", "water transport", "transmembrane transport", "membrane" ]

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

4

[ "HAMAP" ]

[ "MF_01146" ]

[ "Aquaporin_Z" ]

[ 3580 ]

1

[]

0

[ "1rc2", "2abm", "2o9d", "2o9e", "2o9f", "2o9g", "3llq", "3nk5", "3nka", "3nkc", "8h1d", "8uy6" ]

12

[ "PUB00028718", "PUB00031522", "PUB00033222", "PUB00033223", "PUB00033224", "PUB00043535", "PUB00054966", "PUB00083165" ]

[ "11780053", "15377788", "15340377", "16406529", "14691544", "16650285", "10400575", "10872456" ]

[ "Structural basis of water-specific transport through the AQP1 water channel.", "The channel architecture of aquaporin 0 at a 2.2-A resolution.", "From structure to disease: the evolving tale of aquaporin biology.", "Why do microorganisms have aquaporins?", "Architecture and selectivity in aquaporins: 2.5 a...

[ 2001, 2004, 2004, 2006, 2003, 2006, 1999, 1999 ]

8

[ "IPR034294" ]

[]

1

0

1

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

[ 3556, 6, 18 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Aquaporin Z

Aquaporin_Z

6

IPR023744

23,744

3-phenylpropionate/cinnamic acid dioxygenase, ferredoxin--NAD(+) reductase subunit

HcaD

Family

119

false

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

[ "GO:0008860" ]

[ "ferredoxin-NAD+ reductase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01651" ]

[ "HcaD" ]

[ 119 ]

1

[ "EC" ]

[ "1.18.1.3" ]

[ "EC:1.18.1.3" ]

1

[]

0

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

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

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

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

7

[]

0

null

[ "Enterobacterales" ]

[ 119 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

3-phenylpropionate/cinnamic acid dioxygenase, ferredoxin--NAD(+) reductase subunit

HcaD

2

IPR023745

23,745

MSF-type transporter YcaD

MFS_YcaD

Family

1,339

false

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

[]

0

[ "HAMAP", "NCBIFAM" ]

[ "MF_01149", "NF002962" ]

[ "MFS_YcaD", "PRK03633.1" ]

[ 1246, 1338 ]

2

[]

0

[]

0

[ "PUB00007278", "PUB00007279", "PUB00097927" ]

[ "9529885", "9868370", "32205149" ]

[ "Major facilitator superfamily.", "Sugar transporters from bacteria, parasites and mammals: structure-activity relationships.", "Expansion of the Major Facilitator Superfamily (MFS) to include novel transporters as well as transmembrane-acting enzymes." ]

[ 1998, 1998, 2020 ]

3

[ "IPR047200" ]

[]

1

0

1

[ "Pseudomonadati" ]

[ 1339 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

MSF-type transporter YcaD

MFS_YcaD

3

IPR023746

23,746

Transcription regulator HTH, YidZ

Tscrpt_reg_YidZ

Family

760

false

YidZ is a HTH-type transcription regulator involved in anaerobic NO protection [ ].

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

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

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01607" ]

[ "HTH_type_YidZ" ]

[ 760 ]

1

[]

0

[]

0

[ "PUB00016665" ]

[ "15546870" ]

[ "New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide." ]

[ 2005 ]

1

[]

0

null

[ "Bacteria" ]

[ 760 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Transcription regulator HTH, YidZ

Tscrpt_reg_YidZ

8

IPR023747

23,747

Xanthine-guanine phosphoribosyltransferase

Xanthine_Guanine_PRibTrfase

Family

4,160

false

Xanthine-guanine phosphoribosyltransferases, part of the purine salvage pathway, catalyse the transfer of the phosphoribosyl group from 5-phospho-alpha-D-ribosyl 1-pyrophosphate to xanthine, guanine and (to a leser extent) hypoxanthine to form GMP, XMP, and IMP, respectively [ ]. This enzyme uses magnesium as a cofacto...

[ "GO:0000310" ]

[ "xanthine phosphoribosyltransferase activity" ]

[ "molecular_function" ]

1

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

[ "MF_01903", "NF006613", "PTHR39563" ]

[ "XGPRT", "PRK09177.1", "" ]

[ 3912, 4126, 4160 ]

3

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

[ "2.4.2.-", "2.4.2.22", "PWY-5381", "PWY-5800", "PWY-6148", "PWY-6720", "PWY-7018", "PWY-7025", "PWY-7450", "PWY-7817", "PWY-7981" ]

[ "EC:2.4.2.-", "EC:2.4.2.22", "METACYC:PWY-5381", "METACYC:PWY-5800", "METACYC:PWY-6148", "METACYC:PWY-6720", "METACYC:PWY-7018", "METACYC:PWY-7025", "METACYC:PWY-7450", "METACYC:PWY-7817", "METACYC:PWY-7981" ]

11

[ "1a95", "1a96", "1a97", "1a98", "1nul", "4jit", "4jls", "5xtk", "6kp5", "6kqc" ]

10

[ "PUB00037289" ]

[ "9100006" ]

[ "Crystal structure of Escherichia coli xanthine phosphoribosyltransferase." ]

[ 1997 ]

1

[]

0

null

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

[ 4113, 15, 5, 27 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Xanthine-guanine phosphoribosyltransferase

Xanthine_Guanine_PRibTrfase

1

IPR023750

23,750

RbsD-like superfamily

RbsD-like_sf

Homologous_superfamily

11,884

false

RbsD is a component of the ribose operon. It was originally thought to be a high affinity ribose transport protein, but further analysis [ ] shows that it is a D-ribose pyranase . It catalyses the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose ...

[ "GO:0016853", "GO:0048029", "GO:0005996" ]

[ "isomerase activity", "monosaccharide binding", "monosaccharide metabolic process" ]

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

3

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.40.1650.10", "SSF102546" ]

[ "", "" ]

[ 11852, 11865 ]

2

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

[ "5.4.99.62", "R-DRE-6787639", "R-HSA-6787639", "R-MMU-6787639" ]

[ "EC:5.4.99.62", "REACTOME:R-DRE-6787639", "REACTOME:R-HSA-6787639", "REACTOME:R-MMU-6787639" ]

4

[ "1ogc", "1ogd", "1oge", "1ogf", "2ob5", "2wcu", "2wcv", "3e7n", "3mvk", "3p12", "3p13", "4a34" ]

12

[ "PUB00029425", "PUB00053834" ]

[ "12738765", "16731978" ]

[ "Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture.", "Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein." ]

[ 2003, 2006 ]

2

[]

0

null

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

[ 8, 10934, 823, 119 ]

4

[ "Arabidopsis thaliana", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 1, 2, 4, 5, 10 ]

6

true

Homologous_superfamily

RbsD-like superfamily

RbsD-like_sf

7

IPR023753

23,753

FAD/NAD(P)-binding domain

FAD/NAD-binding_dom

Domain

441,652

false

This entry describes the FAD binding domain which has a nested NADH binding domain and is found in both class I and class II oxidoreductases. this domain seems to include contains the pair of redox-active cysteines involved in the transfer of reducing equivalents from the FAD cofactor to the substrate. FAD flavoprotein...

[ "GO:0016491" ]

[ "oxidoreductase activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF07992" ]

[ "Pyr_redox_2" ]

[ 441652 ]

1

[ "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...

[ "GenProp1273", "GenProp1353", "GenProp1371", "GenProp1373", "GenProp1380", "GenProp1426", "GenProp1474", "GenProp1554", "GenProp1641", "GenProp1677", "GenProp1746", "R-BTA-204174", "R-BTA-3299685", "R-BTA-499943", "R-BTA-5263617", "R-BTA-5362517", "R-BTA-5628897", "R-BTA-6783984", ...

[ "GP:GenProp1273", "GP:GenProp1353", "GP:GenProp1371", "GP:GenProp1373", "GP:GenProp1380", "GP:GenProp1426", "GP:GenProp1474", "GP:GenProp1554", "GP:GenProp1641", "GP:GenProp1677", "GP:GenProp1746", "REACTOME:R-BTA-204174", "REACTOME:R-BTA-3299685", "REACTOME:R-BTA-499943", "REACTOME:R-BT...

130

[ "1aog", "1bhy", "1bwc", "1bzl", "1cjc", "1cl0", "1d7y", "1dnc", "1dxl", "1e1k", "1e1l", "1e1m", "1e1n", "1e6e", "1ebd", "1f3p", "1f6m", "1f8w", "1fcd", "1fea", "1feb", "1fec", "1fl2", "1ger", "1ges", "1get", "1geu", "1gra", "1grb", "1gre", "1grf", "1grg"...

629

[ "PUB00001372", "PUB00002674", "PUB00003195", "PUB00003219", "PUB00003255", "PUB00003272", "PUB00003273", "PUB00003296", "PUB00004099", "PUB00004100", "PUB00004756" ]

[ "2924777", "1748631", "7411611", "3656429", "2319593", "1880807", "1942054", "1404382", "2067577", "2067578", "1924336" ]

[ "cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases.", "The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases.", "Gene duplication ...

[ 1989, 1991, 1980, 1987, 1990, 1991, 1991, 1992, 1991, 1991, 1991 ]

11

[]

0

null

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

[ 8241, 346901, 80808, 35, 5, 5662 ]

6

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

[ 109, 17, 47, 23, 16, 73, 42, 14, 64, 49, 10, 8, 219 ]

13

true

Domain

FAD/NAD(P)-binding domain

FAD/NAD-binding_dom

3

IPR023755

23,755

Heme A synthase, type 1, bacillales

HemeA_synthase_1_bacillales

Family

1,237

false

Heme A synthase catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group [ ]. The type 1 subfamily of this enzyme is found in Gram-positive bacteria. Bacillus subtilis CatA is involved in sporulation [ ].

[ "GO:0120547", "GO:0006784", "GO:0016020" ]

[ "heme A synthase activity", "heme A biosynthetic process", "membrane" ]

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

3

[ "HAMAP" ]

[ "MF_01664" ]

[ "HemeA_synth_type1" ]

[ 1237 ]

1

[ "EC" ]

[ "1.17.99.9" ]

[ "EC:1.17.99.9" ]

1

[ "6a2j", "6ied" ]

2

[ "PUB00054974", "PUB00054975" ]

[ "15491161", "12206660" ]

[ "Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli.", "Identification of novel hemes generated by heme A synthase: evidence for two successive monooxygenase reactions." ]

[ 2004, 2002 ]

2

[ "IPR050450" ]

[]

1

0

1

[ "Bacillota", "Rhizophagus irregularis" ]

[ 1236, 1 ]

2

[]

0

true

Family

Heme A synthase, type 1, bacillales

HemeA_synthase_1_bacillales

5

IPR023756

23,756

Glyoxylate/hydroxypyruvate reductase B

Glyo/OHPyrv_Rdtase_B

Family

1,372

false

Glyoxylate/hydroxypyruvate reductase B catalyzes the 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", "NCBIFAM" ]

[ "MF_01667", "NF011938" ]

[ "2_Hacid_dh_C_GhrB", "PRK15409.1" ]

[ 1240, 1368 ]

2

[ "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

[]

0

[ "PUB00054979" ]

[ "11237876" ]

[ "Biochemical characterization of the 2-ketoacid reductases encoded by ycdW and yiaE genes in Escherichia coli." ]

[ 2001 ]

1

[]

0

null

[ "Bacteria", "Beauveria bassiana D1-5", "human gut metagenome" ]

[ 1370, 1, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glyoxylate/hydroxypyruvate reductase B

Glyo/OHPyrv_Rdtase_B

1

IPR023758

23,758

tRNA-modifying protein YgfZ

tRNA-modifying_YgfZ

Family

1,845

false

YgfZ is a folate-binding protein [ ] involved in regulating the level of ATP-dnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication [ ].

[ "GO:0005542", "GO:0009451" ]

[ "folic acid binding", "RNA modification" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01175" ]

[ "tRNA_modifying_YgfZ" ]

[ 1845 ]

1

[]

0

[ "1nrk", "1vly" ]

2

[ "PUB00022265", "PUB00043084" ]

[ "15489424", "16359333" ]

[ "Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolism.", "Involvement of the Escherichia coli folate-binding protein YgfZ in RNA modification and regulation of chromosomal replication initiation." ]

[ 2004, 2006 ]

2

[ "IPR045179" ]

[]

1

0

1

[ "Bacteria", "Ecdysozoa", "human gut metagenome" ]

[ 1841, 3, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

tRNA-modifying protein YgfZ

tRNA-modifying_YgfZ

3

IPR023760

23,760

Holin-like protein CidA

Holin-like_CidA

Family

312

false

This entry represents CidA, which increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. It is inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed ...

[ "GO:0016020" ]

[ "membrane" ]

[ "cellular_component" ]

1

[ "HAMAP" ]

[ "MF_01143" ]

[ "CidA" ]

[ 312 ]

1

[]

0

[]

0

[ "PUB00055101" ]

[ "12670989" ]

[ "The Staphylococcus aureus cidAB operon: evaluation of its role in regulation of murein hydrolase activity and penicillin tolerance." ]

[ 2003 ]

1

[ "IPR005538" ]

[]

1

0

1

[ "Bacteria" ]

[ 312 ]

1

[]

0

true

Family

Holin-like protein CidA

Holin-like_CidA

1

IPR023761

23,761

Transcriptional repressor HTH, NsrR

Tscrpt_rep_HTH_NsrR

Family

948

false

The HTH-type transcriptional repressor NsrR is a nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress, such as ytfE, hmpA and ygbA. It may require iron for activity. NsrR does not regulate its own transcription [ ].

[ "GO:0045892" ]

[ "negative regulation of DNA-templated transcription" ]

[ "biological_process" ]

1

[ "HAMAP" ]

[ "MF_01177" ]

[ "HTH_type_NsrR" ]

[ 948 ]

1

[]

0

[]

0

[ "PUB00033788" ]

[ "16428390" ]

[ "The yjeB (nsrR) gene of Escherichia coli encodes a nitric oxide-sensitive transcriptional regulator." ]

[ 2006 ]

1

[ "IPR000944" ]

[]

1

0

1

[ "Bacteria", "uncultured organism" ]

[ 947, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Transcriptional repressor HTH, NsrR

Tscrpt_rep_HTH_NsrR

5

IPR023762

23,762

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, bacterial

PGP_synthase_bac

Family

911

false

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase ( ), also known as phosphatidylglycerophosphate synthase, glycerophosphate phosphatidyltransferase and PGP synthase, catalyses the conversion of CDP-diacylglycerol and glycerol-3-phosphate to CMP and 3-(3-phosphatidyl)-glycerol 1-phosphate in the commit...

[ "GO:0008444", "GO:0008654", "GO:0016020" ]

[ "CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity", "phospholipid biosynthetic process", "membrane" ]

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

3

[ "HAMAP" ]

[ "MF_01437" ]

[ "PgsA" ]

[ 911 ]

1

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

[ "2.7.8.5", "PWY-5269", "PWY-5668", "PWY-7817" ]

[ "EC:2.7.8.5", "METACYC:PWY-5269", "METACYC:PWY-5668", "METACYC:PWY-7817" ]

4

[]

0

[ "PUB00054981" ]

[ "3003065" ]

[ "Structure and expression of the gene locus encoding the phosphatidylglycerophosphate synthase of Escherichia coli." ]

[ 1986 ]

1

[ "IPR004570" ]

[]

1

0

1

[ "Opisthokonta", "Pseudomonadota" ]

[ 3, 908 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, bacterial

PGP_synthase_bac

2

IPR023764

23,764

Transcriptional repressor HTH, FabR

Tscrpt_reg_HTH_FabR

Family

1,077

false

This entry is represented by the transcriptional repressor FabR found in Gammaproteobacteria. Members of this family contain one HTH TetR-type DNA-binding domain. FabR represses the transcription of FabB, which is involved in unsaturated fatty acid (UFA) biosynthesis. By controlling UFA production, FabR directly influe...

[ "GO:0003700", "GO:0006631" ]

[ "DNA-binding transcription factor activity", "fatty acid metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01190" ]

[ "HTH_type_FabR" ]

[ 1077 ]

1

[]

0

[]

0

[ "PUB00099702", "PUB00099703", "PUB00099704" ]

[ "27004424", "21276098", "19854834" ]

[ "FabR regulates Salmonella biofilm formation via its direct target FabB.", "Complex binding of the FabR repressor of bacterial unsaturated fatty acid biosynthesis to its cognate promoters.", "Transcriptional regulation of membrane lipid homeostasis in Escherichia coli." ]

[ 2016, 2011, 2009 ]

3

[]

0

null

[ "Bacteria", "Opisthokonta" ]

[ 1075, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Transcriptional repressor HTH, FabR

Tscrpt_reg_HTH_FabR

3

IPR023765

23,765

Solute-binding protein family 5, conserved site

SBP_5_CS

Conserved_site

30,418

false

This entry represents a conserved site located near the N-terminal end of bacterial solute-binding proteins from family 5. Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one...

[]

0

[ "PROSITE" ]

[ "PS01040" ]

[ "SBP_BACTERIAL_5" ]

[ 30418 ]

1

[ "REACTOME" ]

[ "R-HSA-9927020" ]

[ "REACTOME:R-HSA-9927020" ]

1

[ "1b05", "1b0h", "1b1h", "1b2h", "1b32", "1b3f", "1b3g", "1b3h", "1b3l", "1b40", "1b46", "1b4h", "1b4z", "1b51", "1b52", "1b58", "1b5h", "1b5i", "1b5j", "1b6h", "1b7h", "1b9j", "1dpe", "1dpp", "1jet", "1jeu", "1jev", "1ola", "1olc", "1qka", "1qkb", "1rkm"...

146

[ "PUB00003610", "PUB00071925", "PUB00071938" ]

[ "8336670", "18310026", "8003968" ]

[ "Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria.", "Characterization of a Pseudomonas putida ABC transporter (AatJMQP) required for acidic amino acid uptake: biochemical properties and regulation by the Aau two-component system.", "Sequence relati...

[ 1993, 2008, 1994 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "Plasmid pAD1", "unclassified sequences" ]

[ 236, 29976, 2, 35, 1, 168 ]

6

[ "Escherichia coli (strain K12)" ]

[ 8 ]

1

true

Conserved_site

Solute-binding protein family 5, conserved site

SBP_5_CS

9

IPR023766

23,766

D-phenylhydantoinase

D_phenylhydantoinase

Family

240

false

D-phenylhydantoinase catalyses the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'-position. It has no activity on dihydropyrimidines. The physiological function of this enzyme is unknown [ ].

[ "GO:0016812", "GO:0006208", "GO:0005737" ]

[ "hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides", "pyrimidine nucleobase catabolic process", "cytoplasm" ]

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

3

[ "HAMAP" ]

[ "MF_01644" ]

[ "D_hydantoinase" ]

[ 240 ]

1

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

[ "3.5.2.-", "PWY-5497", "PWY-6633", "PWY-7823", "PWY-7978" ]

[ "EC:3.5.2.-", "METACYC:PWY-5497", "METACYC:PWY-6633", "METACYC:PWY-7823", "METACYC:PWY-7978" ]

5

[]

0

[ "PUB00054984" ]

[ "11092864" ]

[ "Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli." ]

[ 2000 ]

1

[ "IPR011778" ]

[]

1

0

1

[ "Bacteria" ]

[ 240 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-phenylhydantoinase

D_phenylhydantoinase

4

IPR023769

23,769

Nucleoid occlusion factor SlmA

NO_SlmA

Family

2,551

false

This entry represents SlmA, which is a cell-division inhibitor required for nucleoid occlusion (NO) that contains 1 HTH TetR-type DNA-binding domain [ ], and similar sequences from gammaproteobacteria. It participates in the proper positioning of the FtsZ/septal ring at midcell during cell division, functioning as a DN...

[ "GO:0010974" ]

[ "negative regulation of division septum assembly" ]

[ "biological_process" ]

1

[ "HAMAP" ]

[ "MF_01839" ]

[ "NO_factor_SlmA" ]

[ 2551 ]

1

[]

0

[ "3nxc", "4gck", "4gcl", "4gct", "4gfk", "4gfl", "5haw", "5hbu", "5hsz", "5k58" ]

10

[ "PUB00054986", "PUB00060569" ]

[ "15916962", "21321206" ]

[ "SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli.", "Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist." ]

[ 2005, 2011 ]

2

[]

0

null

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

[ 2534, 1, 16 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Nucleoid occlusion factor SlmA

NO_SlmA

2

IPR023770

23,770

5-deoxy-glucuronate isomerase, Bacilli

IolB_Bacilli

Family

294

false

Members of this family include several bacterial myo-inositol catabolism (IolB) proteins. The Bacillus subtilis inositol operon (iolABCDEFGHIJ) is involved in myo-inositol catabolism. Glucose repression of the iol operon induced by inositol is exerted through catabolite repression mediated by CcpA and the iol induction...

[ "GO:0008880", "GO:0019310" ]

[ "glucuronate isomerase activity", "inositol catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01673" ]

[ "IolB" ]

[ 294 ]

1

[ "EC" ]

[ "5.3.1.30" ]

[ "EC:5.3.1.30" ]

1

[]

0

[ "PUB00012857", "PUB00053908" ]

[ "11566986", "18310071" ]

[ "Involvement of two distinct catabolite-responsive elements in catabolite repression of the Bacillus subtilis myo-inositol (iol) operon.", "myo-Inositol catabolism in Bacillus subtilis." ]

[ 2001, 2008 ]

2

[ "IPR024203" ]

[]

1

0

1

[ "Bacillota" ]

[ 294 ]

1

[]

0

true

Family

5-deoxy-glucuronate isomerase, Bacilli

IolB_Bacilli

9

IPR023774

23,774

Putative metal-dependent hydrolase YfiT

Put_metal_dep_hydrolase_YfiT

Family

1,497

false

This entry is represented by YfiT, which is a 19kDa polypeptide from Bacillus subtilis, belonging to a small sequence family with members predominantly from Gram-positive bacteria. The crystal structure of YfiT in complex with Ni(2+) has been determined to a resolution of 1.7 A [ ]. YfiT exists as a dimer and binds Ni(...

[]

0

[ "HAMAP" ]

[ "MF_01256" ]

[ "YfiT_hydrol" ]

[ 1497 ]

1

[]

0

[ "1rxq" ]

1

[ "PUB00030833" ]

[ "15581359" ]

[ "YfiT from Bacillus subtilis is a probable metal-dependent hydrolase with an unusual four-helix bundle topology." ]

[ 2004 ]

1

[]

0

null

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

[ 1493, 1, 3 ]

3

[]

0

true

Family

Putative metal-dependent hydrolase YfiT

Put_metal_dep_hydrolase_YfiT

1

IPR023775

23,775

Bifunctional protein Aas

Aas

Family

1,331

false

This entry represents a bifunctional enzyme which possesses 2-acylglycerophosphoethanolamine acyltransferase and acyl synthetase activity. It is responsible for regeneration of phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholip...

[ "GO:0008779", "GO:0008922", "GO:0006631", "GO:0008654" ]

[ "acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity", "long-chain fatty acid [acyl-carrier-protein] ligase activity", "fatty acid metabolic process", "phospholipid biosynthetic process" ]

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

4

[ "HAMAP" ]

[ "MF_01162" ]

[ "Aas" ]

[ 1331 ]

1

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

[ "2.3.1.40", "6.2.1.20", "PWY-6622", "PWY-7032" ]

[ "EC:2.3.1.40", "EC:6.2.1.20", "METACYC:PWY-6622", "METACYC:PWY-7032" ]

4

[]

0

[ "PUB00054987", "PUB00054988" ]

[ "1649829", "378999" ]

[ "Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity.", "Solubilization, purification, and salt activation of acyl-acyl carrier protein synthetase from Escherichia coli." ]

[ 1991, 1979 ]

2

[]

0

null

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

[ 1, 1330 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Bifunctional protein Aas

Aas

5

IPR023776

23,776

Anti-adapter protein, IraD

Anti-adapt_IraD

Family

527

false

This entry represents the bacterial anti-adapter protein IraD (inhibitor of RssB after DNA damage) family. It inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS during oxidative stress. Its effect on RpoS stability is due to its interaction with RssB,...

[ "GO:0043856", "GO:0006974" ]

[ "anti-sigma factor antagonist activity", "DNA damage response" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_02010" ]

[ "IraD" ]

[ 527 ]

1

[]

0

[]

0

[ "PUB00044149" ]

[ "18383615" ]

[ "Multiple pathways for regulation of sigmaS (RpoS) stability in Escherichia coli via the action of multiple anti-adaptors." ]

[ 2008 ]

1

[]

0

null

[ "Bacteria" ]

[ 527 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Anti-adapter protein, IraD

Anti-adapt_IraD

3

IPR023777

23,777

Amino acid/peptide transporter family, dipeptide permease D

AA/pep_transptr_DtpD

Family

732

false

The transport of peptides into cells is a well-documented biological phenomenon which is accomplished by specific, energy-dependent transporters found in a number of organisms as diverse as bacteria and humans. The amino acid/peptide transporter family of proteins is distinct from the ABC-type peptide transporters and ...

[ "GO:0042938", "GO:0005886" ]

[ "dipeptide transport", "plasma membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "HAMAP" ]

[ "MF_01880" ]

[ "PTR2_DtpD_subfam" ]

[ 732 ]

1

[]

0

[ "4q65" ]

1

[ "PUB00003872", "PUB00094229" ]

[ "7476181", "26246134" ]

[ "The PTR family: a new group of peptide transporters.", "Role of electrostatic interactions for ligand recognition and specificity of peptide transporters." ]

[ 1995, 2015 ]

2

[ "IPR005279" ]

[]

1

0

1

[ "Enterobacteriaceae" ]

[ 732 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Amino acid/peptide transporter family, dipeptide permease D

AA/pep_transptr_DtpD

5

IPR023778

23,778

Amino acid/peptide transporter family, dipeptide/tripeptide permease B

AA/pep_transptr_DtpB

Family

879

false

The transport of peptides into cells is a well-documented biological phenomenon which is accomplished by specific, energy-dependent transporters found in a number of organisms as diverse as bacteria and humans. The amino acid/peptide transporter family of proteins is distinct from the ABC-type peptide transporters and ...

[]

0

[ "HAMAP" ]

[ "MF_01879" ]

[ "PTR2_DtpB_subfam" ]

[ 879 ]

1

[]

0

[ "8b17", "8b18", "8b19", "8b1a", "8b1b", "8b1c", "8b1d", "8b1e", "8b1f", "8b1g", "8b1h", "8b1i", "8b1j", "8b1k" ]

14

[ "PUB00003872", "PUB00094229" ]

[ "7476181", "26246134" ]

[ "The PTR family: a new group of peptide transporters.", "Role of electrostatic interactions for ligand recognition and specificity of peptide transporters." ]

[ 1995, 2015 ]

2

[ "IPR005279" ]

[]

1

0

1

[ "Bacteria", "Trichuris trichiura" ]

[ 878, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Amino acid/peptide transporter family, dipeptide/tripeptide permease B

AA/pep_transptr_DtpB

9

IPR023780

23,780

Chromo domain

Chromo_domain

Domain

77,946

false

The CHROMO (CHRromatin Organization MOdifier) domain [ , , , ] is a conserved region of around 60 amino acids, originally identified in Drosophila modifiers of variegation. These are proteins that alter the structure of chromatin to the condensed morphology of heterochromatin, a cytologically visible condition where ge...

[]

0

[ "PFAM" ]

[ "PF00385" ]

[ "Chromo" ]

[ 77946 ]

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-4551638", "R-CEL-6804758", "R-CEL-73772", "R-CEL-9031628", "R-CEL-983231", "R-DME-2559580", "R-DME-3108214", "R-DME-3214815", "R-DME-3899300", "R-DME-427359", "R-DME-4570464", "R-DME-6804758", "R-DME-8939243", "R-DME-8943724", "R-DME-9031628", "R-DRE-3769402", "R-HSA-1368108",...

[ "REACTOME:R-CEL-4551638", "REACTOME:R-CEL-6804758", "REACTOME:R-CEL-73772", "REACTOME:R-CEL-9031628", "REACTOME:R-CEL-983231", "REACTOME:R-DME-2559580", "REACTOME:R-DME-3108214", "REACTOME:R-DME-3214815", "REACTOME:R-DME-3899300", "REACTOME:R-DME-427359", "REACTOME:R-DME-4570464", "REACTOME:R-...

78

[ "1ap0", "1g6z", "1guw", "1kna", "1kne", "1pdq", "1pfb", "1q3l", "1x3p", "2b2t", "2b2u", "2b2v", "2b2w", "2b2y", "2d9u", "2dnt", "2dnv", "2dy7", "2dy8", "2ee1", "2epb", "2h1e", "2k1b", "2k28", "2kvm", "2l11", "2l12", "2l1b", "2m2l", "2mj8", "2n88", "2rsn"...

125

[ "PUB00004399", "PUB00004460", "PUB00004461", "PUB00005519", "PUB00017969" ]

[ "1708124", "7667093", "7501439", "1982376", "11574148" ]

[ "A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants.", "The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1.", "The chromo superfamily: new members, duplication of the chromo domain and possible role in delivering transcriptio...

[ 1991, 1995, 1995, 1990, 2001 ]

5

[ "IPR000953" ]

[ "IPR017984", "IPR030300", "IPR038033", "IPR049558", "IPR049937" ]

1

5

0

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

[ 15, 77920, 4, 7 ]

4

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

[ 58, 15, 106, 69, 105, 78, 9, 49, 98, 2, 7, 186 ]

12

true

Domain

Chromo domain

Chromo_domain

1

IPR023781

23,781

Nucleoside triphosphatase NudI

Nucleoside_triphosphatase_NudI

Family

728

false

This entry represents a family of Nudix hydrolases that catalyse the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP) [ , ].

[ "GO:0016818" ]

[ "hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01846" ]

[ "Nudix_NudI" ]

[ 728 ]

1

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

[ "3.6.1.-", "3.6.1.12", "3.6.1.23", "3.6.1.9", "PWY-5757", "PWY-6147", "PWY-6383", "PWY-6545", "PWY-6797", "PWY-7184", "PWY-7187", "PWY-7206", "PWY-7419", "PWY-7539", "PWY-7719", "PWY-7821", "PWY-8289" ]

[ "EC:3.6.1.-", "EC:3.6.1.12", "EC:3.6.1.23", "EC:3.6.1.9", "METACYC:PWY-5757", "METACYC:PWY-6147", "METACYC:PWY-6383", "METACYC:PWY-6545", "METACYC:PWY-6797", "METACYC:PWY-7184", "METACYC:PWY-7187", "METACYC:PWY-7206", "METACYC:PWY-7419", "METACYC:PWY-7539", "METACYC:PWY-7719", "METACYC...

17

[ "3n77", "3oga", "6dt3" ]

3

[ "PUB00043005", "PUB00054989" ]

[ "16766526", "17768363" ]

[ "Three new Nudix hydrolases from Escherichia coli.", "Overexpression, crystallization and preliminary X-ray crystallographic analysis of Nudix hydrolase Orf141 from Escherichia coli K-1." ]

[ 2006, 2007 ]

2

[]

0

null

[ "Eukaryota", "Pseudomonadota" ]

[ 2, 726 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Nucleoside triphosphatase NudI

Nucleoside_triphosphatase_NudI

3

IPR023783

23,783

Cation efflux pump FieF

Cation_efflux_FieF

Family

1,066

false

The ferrous iron efflux (FieF) proteins are members of the cation diffusion facilitator (CDF) family of membrane-bound transporters. These are divalent metal cation transporters that, in addition to their involvement in iron detoxification in Escherichia coli, FieF proteins are also able to transport Zn2 and Cd2 in a p...

[ "GO:0046873", "GO:0006826", "GO:0006829", "GO:0016020" ]

[ "metal ion transmembrane transporter activity", "iron ion transport", "zinc ion transport", "membrane" ]

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

4

[ "HAMAP" ]

[ "MF_01425" ]

[ "Cation_efflux_FieF" ]

[ 1066 ]

1

[]

0

[ "2qfi", "3h90" ]

2

[ "PUB00054990" ]

[ "15549269" ]

[ "FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress." ]

[ 2005 ]

1

[ "IPR050291" ]

[]

1

0

1

[ "Beauveria bassiana D1-5", "Gammaproteobacteria", "human gut metagenome" ]

[ 1, 1064, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Cation efflux pump FieF

Cation_efflux_FieF

4

IPR023784

23,784

2-oxoglutarate dehydrogenase E1 component, bacterial

2oxoglutarate_DH_E1_bac

Family

1,568

false

2-oxoglutarate dehydrogenase is a key enzyme in the TCA cycle, converting 2-oxoglutarate, coenzyme A and NAD(+) to succinyl-CoA, NADH and carbon dioxide [ ]. This activity of this enzyme is tightly regulated and it is a major determinant of the metabolic flux through the TCA cycle. This enzyme is composed of multiple c...

[]

0

[ "HAMAP" ]

[ "MF_01169" ]

[ "SucA_OdhA" ]

[ 1568 ]

1

[ "EC", "METACYC" ]

[ "1.2.4.2", "PWY-5084" ]

[ "EC:1.2.4.2", "METACYC:PWY-5084" ]

2

[]

0

[ "PUB00033922", "PUB00033923" ]

[ "16321804", "9278141" ]

[ "Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress.", "2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain." ]

[ 2005, 1997 ]

2

[ "IPR011603" ]

[]

1

0

1

[ "Bacteria" ]

[ 1568 ]

1

[]

0

true

Family

2-oxoglutarate dehydrogenase E1 component, bacterial

2oxoglutarate_DH_E1_bac

7

IPR023785

23,785

Regulator of RNA polymerase sigma(70) subunit, Rsd

Sigma70_reg_Rsd

Family

995

false

This family includes bacterial transcriptional regulators that are thought to act through an interaction with the conserved region 4 of the sigma 70 subunit of RNA polymerase. They are responsible for switching between sigma 70 to sigma S during the transition from exponential growth to stationary phase [ ].

[]

0

[ "HAMAP" ]

[ "MF_01181" ]

[ "Rsd" ]

[ 995 ]

1

[]

0

[ "2p7v", "4xwj" ]

2

[ "PUB00054998" ]

[ "10368152" ]

[ "Transcriptional organization and in vivo role of the Escherichia coli rsd gene, encoding the regulator of RNA polymerase sigma D." ]

[ 1999 ]

1

[]

0

null

[ "Pseudomonadota" ]

[ 995 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Regulator of RNA polymerase sigma(70) subunit, Rsd

Sigma70_reg_Rsd

4

IPR023787

23,787

Type III secretion system flagellar brake protein YcgR

T3SS_YcgR

Family

2,420

false

This entry represents YcgR a member of the T3SS. It acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. Increasing levels of c-di-GMP lead to decreased motility. YcgR binds 1 c-di-GMP dimer per subunit. YcgR is composed of two domains: an N-te...

[ "GO:0035438", "GO:0071945" ]

[ "cyclic-di-GMP binding", "regulation of bacterial-type flagellum-dependent cell motility by regulation of motor speed" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01457" ]

[ "YcgR" ]

[ 2420 ]

1

[]

0

[ "2gjg", "5y6f" ]

2

[ "PUB00049330" ]

[ "18034161" ]

[ "The structural basis of cyclic diguanylate signal transduction by PilZ domains." ]

[ 2007 ]

1

[]

0

null

[ "Opisthokonta", "Pseudomonadota", "ecological metagenomes" ]

[ 3, 2400, 17 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Type III secretion system flagellar brake protein YcgR

T3SS_YcgR

7

IPR023788

23,788

D-tagatose-bisphosphate aldolase, class II, subunit KbaY

TagBP_ald_KbaY

Family

243

false

Escherichia coli and other enteric bacteria contain two closely related D-tagatose 1,6-bisphosphate (TagBP)-specific aldolases - KbaYZ (also known as AgaYZ) and GatYZ. Unlike other class II aldolases, which are homodimeric enzymes, KbaYZ and GatYZ are heterodimers, and are comprised of subunits KbaY/GatY and GatY/GatZ....

[ "GO:0008270", "GO:0009025", "GO:0005975", "GO:2001059" ]

[ "zinc ion binding", "tagatose-bisphosphate aldolase activity", "carbohydrate metabolic process", "D-tagatose 6-phosphate catabolic process" ]

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

4

[ "HAMAP" ]

[ "MF_01293" ]

[ "TagBP_aldolase_KbaY" ]

[ 243 ]

1

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

[ "4.1.2.40", "PWY-7077", "PWY-7395", "PWY-8324" ]

[ "EC:4.1.2.40", "METACYC:PWY-7077", "METACYC:PWY-7395", "METACYC:PWY-8324" ]

4

[ "1gvf" ]

1

[ "PUB00014683", "PUB00014684" ]

[ "11976750", "8955298" ]

[ "Two class II D-tagatose-bisphosphate aldolases from enteric bacteria.", "Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism." ]

[ 2002, 1996 ]

2

[ "IPR011288" ]

[]

1

0

1

[ "Enterobacterales" ]

[ 243 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-tagatose-bisphosphate aldolase, class II, subunit KbaY

TagBP_ald_KbaY

7

IPR023789

23,789

2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase

DHPP/DHXA_dioxygenase

Family

1,200

false

This entry represents 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase. This enzyme catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respecti...

[ "GO:0005506", "GO:0047070" ]

[ "iron ion binding", "3-carboxyethylcatechol 2,3-dioxygenase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP", "CDD" ]

[ "MF_01653", "cd07365" ]

[ "MhpB", "MhpB_like" ]

[ 1104, 911 ]

2

[ "EC", "METACYC" ]

[ "1.13.11.16", "PWY-6690" ]

[ "EC:1.13.11.16", "METACYC:PWY-6690" ]

2

[ "8k04", "9kti" ]

2

[ "PUB00053149" ]

[ "8399388" ]

[ "Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli." ]

[ 1993 ]

1

[]

0

null

[ "Bacteria", "freshwater metagenome", "leotiomyceta" ]

[ 1190, 2, 8 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase

DHPP/DHXA_dioxygenase

5

IPR023790

23,790

Chloride channel, voltage-gated, ClcB

Cl-channel_volt-gated_ClcB

Family

773

false

Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t...

[ "GO:0006821", "GO:0010447" ]

[ "chloride transport", "response to acidic pH" ]

[ "biological_process", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01203" ]

[ "CLC_ClcB" ]

[ 773 ]

1

[]

0

[]

0

[ "PUB00000734", "PUB00004085", "PUB00004913", "PUB00055002" ]

[ "9046241", "2174129", "9207144", "12384697" ]

[ "Chloride channels: an emerging molecular picture.", "Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes.", "Transmembrane topology of a CLC chloride channel.", "A biological role for prokaryotic ClC chloride channels." ]

[ 1997, 1990, 1997, 2002 ]

4

[ "IPR001807" ]

[]

1

0

1

[ "Pseudomonadota" ]

[ 773 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Chloride channel, voltage-gated, ClcB

Cl-channel_volt-gated_ClcB

1

IPR023791

23,791

2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase

MhpC_alpha/beta_hydrolase

Family

444

false

2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6-oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring fission product of the bacterial meta-cleavage pathway for degradation of phenylpropionic acid [ ]. The purified enzyme i...

[ "GO:0016787", "GO:0018771", "GO:0042803", "GO:0005737" ]

[ "hydrolase activity", "2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity", "protein homodimerization activity", "cytoplasm" ]

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

4

[ "HAMAP" ]

[ "MF_01654" ]

[ "MhpC" ]

[ 444 ]

1

[ "EC", "METACYC" ]

[ "3.7.1.14", "PWY-6690" ]

[ "EC:3.7.1.14", "METACYC:PWY-6690" ]

2

[ "1u2e", "9ijk" ]

2

[ "PUB00016015", "PUB00055003" ]

[ "9098055", "9315862" ]

[ "Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12.", "Purification, characterization, and stereochemical analysis of a C-C hydrolase: 2-hydroxy-6-keto-nona-2,4-diene-1,9-dioic acid 5,6-hydrolase." ]

[ 1997, 1997 ]

2

[ "IPR000639" ]

[]

1

0

1

[ "Pseudomonadota" ]

[ 444 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase

MhpC_alpha/beta_hydrolase

1

IPR023792

23,792

Protein-disulfide oxidoreductase DsbI

DiS_OxRdtase_Dsbl

Family

423

false

This group of proteins belongs to the DsbI subfamily of the DsbB family. DsbI is required for disulfide bond formation in some proteins. It is part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in arylsulfate sulfotransferase AssT [ ].

[]

0

[ "HAMAP" ]

[ "MF_01311" ]

[ "DsbI" ]

[ 423 ]

1

[]

0

[]

0

[ "PUB00050921" ]

[ "18565543" ]

[ "DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli." ]

[ 2008 ]

1

[ "IPR003752" ]

[]

1

0

1

[ "Enterobacterales" ]

[ 423 ]

1

[]

0

true

Family

Protein-disulfide oxidoreductase DsbI

DiS_OxRdtase_Dsbl

5

IPR023793

23,793

2-keto-4-pentenoate hydratase

Keto_pentenoate-hydratase

Family

336

false

2-keto-4-pentenoate hydratase catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid. It uses divalent metal ions as cofactor, with optimum activity obtained with Mn2+ [ ].

[ "GO:0008684", "GO:0030145" ]

[ "2-oxopent-4-enoate hydratase activity", "manganese ion binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP" ]

[ "MF_01655" ]

[ "MhpD" ]

[ 336 ]

1

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

[ "4.2.1.80", "PWY-5162", "PWY-5645" ]

[ "EC:4.2.1.80", "METACYC:PWY-5162", "METACYC:PWY-5645" ]

3

[ "1sv6", "2wqt" ]

2

[ "PUB00001474" ]

[ "9492273" ]

[ "Purification, characterisation and reaction mechanism of monofunctional 2-hydroxypentadienoic acid hydratase from Escherichia coli." ]

[ 1998 ]

1

[]

0

null

[ "Pseudomonadota" ]

[ 336 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

2-keto-4-pentenoate hydratase

Keto_pentenoate-hydratase

9

IPR023794

23,794

Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase

MI/DCI_dehydrogenase

Family

3,244

false

Inositol 2-dehydrogenase catalyses the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose). In firmicutes (Gram-positive bacteria), the enzyme also shows D-chiro-inositol 3-dehydrogenase activity and is involved in the oxidation of D-chiro-inositol (DCI) to 1-keto-D-chiro-inositol (1KDCI) [ , ].

[ "GO:0050112", "GO:0019310" ]

[ "inositol 2-dehydrogenase (NAD+) activity", "inositol catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01671" ]

[ "IolG" ]

[ 3244 ]

1

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

[ "1.1.1.18", "PWY-5940", "PWY-7237", "PWY-7241" ]

[ "EC:1.1.1.18", "METACYC:PWY-5940", "METACYC:PWY-7237", "METACYC:PWY-7241" ]

4

[ "3ec7", "3mz0", "3nt2", "3nt4", "3nt5", "3nto", "3ntq", "3ntr", "4l8v", "4l9r", "4mie", "4min", "4mio", "4miy", "4mjl" ]

15

[ "PUB00055004", "PUB00055005" ]

[ "112095", "16461681" ]

[ "Purification and properties of Bacillus subtilis inositol dehydrogenase.", "Genetic modification of Bacillus subtilis for production of D-chiro-inositol, an investigational drug candidate for treatment of type 2 diabetes and polycystic ovary syndrome." ]

[ 1979, 2006 ]

2

[]

0

null

[ "Bacteria", "Mycosphaerellaceae", "metagenomes" ]

[ 3238, 2, 4 ]

3

[]

0

true

Family

Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase

MI/DCI_dehydrogenase

1

IPR023795

23,795

Serpin, conserved site

Serpin_CS

Conserved_site

37,771

false

This entry represents a conserved site for the Serpin family of proteins, centred on a well conserved Pro-Phe sequence which is found ten to fifteen residues on the C-terminal side of the reactive bond. Serpins (SERine Proteinase INhibitors) belong to MEROPS inhibitor family I4, clan ID. Most serpin family members are ...

[]

0

[ "PROSITE" ]

[ "PS00284" ]

[ "SERPIN" ]

[ 37771 ]

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-1650814", "R-BTA-194002", "R-BTA-2022377", "R-BTA-204005", "R-BTA-375276", "R-BTA-381426", "R-BTA-416476", "R-BTA-418594", "R-BTA-5694530", "R-BTA-6798695", "R-BTA-75205", "R-BTA-8957275", "R-BTA-9757110", "R-DME-114608", "R-DME-140837", "R-DME-140875", "R-DM...

[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-1650814", "REACTOME:R-BTA-194002", "REACTOME:R-BTA-2022377", "REACTOME:R-BTA-204005", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-416476", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-5694530", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA...

94

[ "1a7c", "1ant", "1as4", "1ath", "1att", "1atu", "1azx", "1b3k", "1br8", "1by7", "1c5g", "1c8o", "1d5s", "1db2", "1dvm", "1dvn", "1dzg", "1dzh", "1e03", "1e04", "1e05", "1ezx", "1f0c", "1hle", "1hp7", "1imv", "1jjo", "1jmj", "1jmo", "1jrr", "1jti", "1jvq"...

246

[ "PUB00001649", "PUB00002863", "PUB00067349", "PUB00067350" ]

[ "8417965", "8034697", "7851535", "21781239" ]

[ "The ovalbumin family of serpin proteins.", "Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition.", "Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L.", "Serpin structure, function and dysfunction." ]

[ 1993, 1994, 1995, 2011 ]

4

[]

0

null

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

[ 224, 2271, 34877, 325, 74 ]

5

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

[ 58, 7, 47, 30, 126, 104, 15, 113, 15 ]

9

true

Conserved_site

Serpin, conserved site

Serpin_CS

8

IPR023796

23,796

Serpin domain

Serpin_dom

Domain

56,803

false

This entry represents the structural domain of serpins. Serpins (SERine Proteinase INhibitors) belong to MEROPS inhibitor family I4, clan ID. Most serpin family members are indeed serine protease inhibitors, but several have additional cross-class inhibition functions and inhibit cysteine protease family members such a...

[]

0

[ "PFAM", "SMART" ]

[ "PF00079", "SM00093" ]

[ "Serpin", "SERPIN" ]

[ 56796, 49792 ]

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-114608", "R-BTA-1650814", "R-BTA-194002", "R-BTA-2022377", "R-BTA-204005", "R-BTA-375276", "R-BTA-381426", "R-BTA-416476", "R-BTA-418594", "R-BTA-5694530", "R-BTA-6798695", "R-BTA-75205", "R-BTA-8957275", "R-BTA-9757110", "R-DME-114608", "R-DME-140837", "R-DME-140875", "R-DM...

[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-1650814", "REACTOME:R-BTA-194002", "REACTOME:R-BTA-2022377", "REACTOME:R-BTA-204005", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-416476", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-5694530", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA...

104

[ "1a7c", "1ant", "1as4", "1ath", "1att", "1atu", "1azx", "1b3k", "1br8", "1by7", "1c5g", "1c8o", "1d5s", "1db2", "1dvm", "1dvn", "1dzg", "1dzh", "1e03", "1e04", "1e05", "1ezx", "1f0c", "1hle", "1hp7", "1imv", "1iz2", "1jjo", "1jmj", "1jmo", "1jrr", "1jti"...

281

[ "PUB00001649", "PUB00002863", "PUB00067349", "PUB00067350" ]

[ "8417965", "8034697", "7851535", "21781239" ]

[ "The ovalbumin family of serpin proteins.", "Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition.", "Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L.", "Serpin structure, function and dysfunction." ]

[ 1993, 1994, 1995, 2011 ]

4

[]

[ "IPR033829", "IPR033830", "IPR033831", "IPR033832", "IPR033833", "IPR033834", "IPR033835", "IPR033836" ]

0

8

0

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

[ 253, 3934, 51956, 528, 132 ]

5

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

[ 78, 13, 62, 82, 233, 182, 60, 160, 17 ]

9

true

Domain

Serpin domain

Serpin_dom

3

IPR023797

23,797

RNA 3'-terminal phosphate cyclase domain

RNA3'_phos_cyclase_dom

Domain

10,473

false

RNA cyclases are a family of RNA-modifying enzymes that are conserved in eukaryotes, bacteria and archaea. Type 1 RNA 3'-terminal phosphate cyclases ( ) [ , ] catalyse the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA: ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2'...

[]

0

[ "PFAM" ]

[ "PF01137" ]

[ "RTC" ]

[ 10473 ]

1

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

[ "6.5.1.4", "R-BTA-6791226", "R-CEL-6791226", "R-DDI-6791226", "R-DME-6791226", "R-HSA-6790901", "R-HSA-6791226", "R-MMU-6791226", "R-SCE-6791226", "R-SPO-6791226" ]

[ "EC:6.5.1.4", "REACTOME:R-BTA-6791226", "REACTOME:R-CEL-6791226", "REACTOME:R-DDI-6791226", "REACTOME:R-DME-6791226", "REACTOME:R-HSA-6790901", "REACTOME:R-HSA-6791226", "REACTOME:R-MMU-6791226", "REACTOME:R-SCE-6791226", "REACTOME:R-SPO-6791226" ]

10

[ "1qmh", "1qmi", "3kgd", "3pqv", "3tut", "3tux", "3tv1", "3tw3", "4clq", "4o89", "4o8j", "5jpq", "5oql", "5tzs", "5wlc", "5wyj", "5wyk", "6ke6", "6lqp", "6lqq", "6lqr", "6lqs", "6lqt", "6lqu", "6lqv", "6rxt", "6rxu", "6rxv", "6rxx", "6rxy", "6rxz", "6zqa"...

65

[ "PUB00001300", "PUB00003565", "PUB00006476", "PUB00042947" ]

[ "9184239", "2199762", "10673421", "10790377" ]

[ "The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea.", "RNA 3'-terminal phosphate cyclase from HeLa cells.", "Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology.", "Rcl1p, the yeast prote...

[ 1997, 1990, 2000, 2000 ]

4

[]

0

null

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

[ 650, 1851, 7911, 61 ]

4

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

[ 5, 1, 2, 3, 1, 7, 12, 3, 3, 10, 1, 1, 5 ]

13

true

Domain

RNA 3'-terminal phosphate cyclase domain

RNA3'_phos_cyclase_dom

2

IPR023798

23,798

Small ribosomal subunit protein uS7 domain

Ribosomal_uS7_dom

Domain

58,132

false

This entry represents the uS7 structural domain, which consists of a bundle of six helices and an extended β hairpin between helices 3 and 4, with two or more RNA-binding sites on its surface [ ]. This entry includes the small ribosomal subunit protein uS7, formerly referred to as 30S ribosomal proteins S7 (bacterial, ...

[]

0

[ "PFAM" ]

[ "PF00177" ]

[ "Ribosomal_S7" ]

[ 58132 ]

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-72649", "R-BTA-72689", "R-BTA-72695", "R-BTA-72702", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-BTA-9937383", "R-CEL-156827", "R-CEL-1799339", "R-CEL-5389840", "R-CEL-5419276", "R-CEL-...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-5389840", "REACTOME:R-BTA-5419276", "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-9759...

116

[ "1dv4", "1eg0", "1fjg", "1fka", "1hnw", "1hnx", "1hnz", "1hr0", "1hus", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1iqv", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1qd7", "1rss", "1vvj", "1vy4", "1vy5", "1vy6"...

1,895

[ "PUB00000754", "PUB00004462", "PUB00005285", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00059258", "PUB00110894", "PUB00151110" ]

[ "8338632", "8524651", "9331418", "11297922", "11290319", "11114498", "11160889", "23636399", "34516797" ]

[ "N-terminal modification and amino-acid sequence of the ribosomal protein HmaS7 from Haloarcula marismortui and homology studies to other ribosomal proteins.", "Cloning and characterisation of the gene encoding the ribosomal protein S5 (also known as rp14, S2, YS8) of Saccharomyces cerevisiae.", "The structure ...

[ 1993, 1995, 1997, 2001, 2001, 2000, 2001, 2013, 2021 ]

9

[]

[ "IPR047988" ]

0

1

0

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

[ 914, 23546, 33181, 491 ]

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",...

[ 14, 2, 4, 6, 1, 11, 4, 2, 18, 8, 2, 3, 17 ]

13

true

Domain

Small ribosomal subunit protein uS7 domain

Ribosomal_uS7_dom

6

IPR023801

23,801

Histone deacetylase domain

His_deacetylse_dom

Domain

67,006

false

This entry represents the structural domain found in histone deacetylases. It consists of a 3-layer(α-β-α) sandwich. Histone deacetylases (HDACs) are a class of enzymes that remove acetyl groups from N(6)-acetyl-lysine residues on histones. This process plays a critical role in transcription regulation, as HDACs facili...

[]

0

[ "PFAM" ]

[ "PF00850" ]

[ "Hist_deacetyl" ]

[ 67006 ]

1

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

[ "3.5.1", "3.5.1.98", "R-BTA-1538133", "R-BTA-201722", "R-BTA-2173795", "R-BTA-3214815", "R-BTA-350054", "R-BTA-3769402", "R-BTA-4551638", "R-BTA-6804758", "R-BTA-73762", "R-BTA-8936459", "R-BTA-8943724", "R-BTA-9018519", "R-BTA-9022692", "R-BTA-9701898", "R-BTA-9764725", "R-BTA-982...

[ "EC:3.5.1", "EC:3.5.1.98", "REACTOME:R-BTA-1538133", "REACTOME:R-BTA-201722", "REACTOME:R-BTA-2173795", "REACTOME:R-BTA-3214815", "REACTOME:R-BTA-350054", "REACTOME:R-BTA-3769402", "REACTOME:R-BTA-4551638", "REACTOME:R-BTA-6804758", "REACTOME:R-BTA-73762", "REACTOME:R-BTA-8936459", "REACTOME...

210

[ "1c3p", "1c3r", "1c3s", "1t64", "1t67", "1t69", "1vkg", "1w22", "1zz0", "1zz1", "1zz3", "2gh6", "2v5w", "2v5x", "2vcg", "2vqj", "2vqm", "2vqo", "2vqq", "2vqv", "2vqw", "3c0y", "3c0z", "3c10", "3ew8", "3ewf", "3ezp", "3ezt", "3f06", "3f07", "3f0r", "3max"...

384

[ "PUB00004480", "PUB00006434", "PUB00006504", "PUB00006562", "PUB00160366" ]

[ "9278492", "10072350", "10322454", "10322142", "38822399" ]

[ "Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily.", "Histone acetylases and deacetylases in cell proliferation.", "Histone deacetylases: transcriptional repression with SINers and NuRDs.", "Histone acetylation and cancer.", ...

[ 1997, 1999, 1999, 1999, 2024 ]

5

[]

[ "IPR044150" ]

0

1

0

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

[ 967, 23910, 41509, 32, 588 ]

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...

[ 50, 10, 51, 50, 115, 50, 4, 44, 70, 5, 3, 94 ]

12

true

Domain

Histone deacetylase domain

His_deacetylse_dom

1

IPR023803

23,803

Small ribosomal subunit protein bS16 domain superfamily

Ribosomal_bS16_dom_sf

Homologous_superfamily

43,202

false

This superfamily represents the structural domain of ribosomal bS16 proteins, consisting of an α-β 2 layer sandwich. Ribosomal protein S16 (also known as bS16) is one of the proteins from the small ribosomal subunit. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities, groups: Euba...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.30.1320.10", "SSF54565" ]

[ "", "" ]

[ 43117, 43185 ]

2

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

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

[ "REACTOME:R-BTA-5389840", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-9937383", "REACTOME:R-CEL-5389840", "REACTOME:R-CEL-5419276", "REACTOME:R-CEL-9937383", "REACTOME:R-DME-5389840", "REACTOME:R-DME-5419276", "REACTOME:R-DME-9937383", "REACTOME:R-HSA-5368286", "REACTOME:R-HSA-5389840", "REACTOM...

16

[ "1emw", "1fjg", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xmo", "1xmq", "1xnq", "1xnr", "2e5l"...

1,274

[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00082325" ]

[ "11297922", "11290319", "11114498", "18453549" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Substitution of the gene for chloroplast RPS16 was assisted by generation of a dual targeting signal." ]

[ 2001, 2001, 2000, 2008 ]

4

[]

0

null

[ "Bacteria", "Escherichia phage vB_EcoM-613R3", "Eukaryota", "candidate division MSBL1 archaeon SCGC-AAA382M17", "unclassified sequences" ]

[ 23508, 1, 19191, 1, 501 ]

5

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

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

13

true

Homologous_superfamily

Small ribosomal subunit protein bS16 domain superfamily

Ribosomal_bS16_dom_sf

8

IPR023804

23,804

Protein of unknown function DUF3792, transmembrane

DUF3792_TM

Family

2,510

false

Members of this family of strongly hydrophobic putative transmembrane protein average about 125 amino acids in length and occur mostly, but not exclusively, in the Firmicutes. Members are quite diverse in sequence. Their function is unknown.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF12670", "TIGR04086" ]

[ "DUF3792", "TIGR04086_membr" ]

[ 2457, 2499 ]

2

[]

0

[]

0

[]

0

[]

0

null

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

[ 2, 2489, 19 ]

3

[]

0

true

Family

Protein of unknown function DUF3792, transmembrane

DUF3792_TM

5

IPR023806

23,806

Conserved hypothetical protein CHP03905

CHP03905

Family

1,752

false

This entry describes a family of conserved hypothetical proteins of small size with four invariant Cys residues. This small protein is distantly homologous to a C-terminal domain found in proteins identified by N-terminal homology as ribonucleotide reductases.

[]

0

[ "NCBIFAM" ]

[ "TIGR03905" ]

[ "TIGR03905_4_Cys" ]

[ 1752 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Aduncisulcus paluster", "Bacteria", "Myoviridae sp. ctVCj30", "metagenomes" ]

[ 1, 1706, 1, 44 ]

4

[]

0

true

Family

Conserved hypothetical protein CHP03905

CHP03905

1

IPR023807

23,807

Peptide modification radical SAM enzyme, putative

Peptide_mod_rSAM

Family

38

false

Members of this protein family are predicted radical SAM (rSAM) enzymes similar in sequence to others with known or postulated roles in peptide modification [ , ]. They are found in Thermodesulfobacteriota bacteria.

[]

0

[ "NCBIFAM" ]

[ "TIGR04082" ]

[ "rSAM_for_selen" ]

[ 38 ]

1

[ "GP" ]

[ "GenProp0956" ]

[ "GP:GenProp0956" ]

1

[]

0

[ "PUB00055953", "PUB00106225" ]

[ "21478363", "34730336" ]

[ "Biological systems discovery in silico: radical S-adenosylmethionine protein families and their target peptides for posttranslational modification.", "New Role for Radical SAM Enzymes in the Biosynthesis of Thio(seleno)oxazole RiPP Natural Products." ]

[ 2011, 2021 ]

2

[ "IPR050377" ]

[]

1

0

1

[ "Bacteria" ]

[ 38 ]

1

[]

0

true

Family

Peptide modification radical SAM enzyme, putative

Peptide_mod_rSAM

7

IPR023808

23,808

Nitrile hydratase accessory protein, putative

Nitrile_Hydratase_acc_put

Family

1,727

false

Members of this protein family are found in operons with the alpha and beta subunits of nitrile hydratase and appear to be accessory proteins for maturation or activation of the enzyme.

[]

0

[ "NCBIFAM" ]

[ "TIGR03889" ]

[ "nitrile_acc" ]

[ 1727 ]

1

[ "GP" ]

[ "GenProp0899" ]

[ "GP:GenProp0899" ]

1

[]

0

[]

0

[]

0

null

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

[ 1676, 3, 18, 30 ]

4

[]

0

true

Family

Nitrile hydratase accessory protein, putative

Nitrile_Hydratase_acc_put

9

IPR023810

23,810

Conserved hypothetical protein CHP03894

CHP03894

Family

20

false

This protein family is restricted to cyanobacteria, and is sporadic in those lineages. Members average 100 amino acids in length, including a 30-residue, highly polar, low complexity region sandwiched between an N-terminal region of about 60 residues and a C-terminal [KR]VVR[KR]RS motif, both well-conserved. Their func...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF27796", "TIGR03894" ]

[ "CHP03894", "chp_P_marinus_1" ]

[ 20, 20 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Prochlorococcaceae" ]

[ 20 ]

1

[]

0

true

Family

Conserved hypothetical protein CHP03894

CHP03894

2

IPR023812

23,812

Conserved hypothetical protein CHP04002

CHP04002

Family

151

false

This family of proteins occur strictly as part of a tandem gene pair where one of the two represents an uncharacterised radical SAM protein.

[]

0

[ "NCBIFAM" ]

[ "TIGR04002" ]

[ "" ]

[ 151 ]

1

[ "GP" ]

[ "GenProp1094" ]

[ "GP:GenProp1094" ]

1

[]

0

[]

0

[ "IPR009825" ]

[]

1

0

1

[ "Bacillota", "metagenomes" ]

[ 147, 4 ]

2

[]

0

true

Family

Conserved hypothetical protein CHP04002

CHP04002

6

IPR023813

23,813

Heme sensing membrane protein HsmA-like

HsmA-like

Family

625

false

This entry represents a group of bacterial proteins, including Heme sensing membrane protein HsmA from Clostridioides difficile, part of a heme-sensing membrane protein system (HsmRA) that induces a protective response that repurposes heme to counteract antimicrobial oxidative stress responses [ ].

[]

0

[ "NCBIFAM" ]

[ "TIGR03987" ]

[ "" ]

[ 625 ]

1

[]

0

[]

0

[ "PUB00106804" ]

[ "32526159" ]

[ "Clostridioides difficile Senses and Hijacks Host Heme for Incorporation into an Oxidative Stress Defense System." ]

[ 2020 ]

1

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 618, 7 ]

2

[]

0

true

Family

Heme sensing membrane protein HsmA-like

HsmA-like

9

IPR023814

23,814

His-Xaa-Ser system protein

His-Xaa-Ser_sys

Family

56

false

Members of this rare protein family occur in the presence of and , which in turn occur only in the context of radical SAM protein families and . Their function is unknown [ ].

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF27798", "TIGR03982" ]

[ "His-Xaa-Ser_sys", "" ]

[ 56, 49 ]

2

[ "GP" ]

[ "GenProp0921" ]

[ "GP:GenProp0921" ]

1

[]

0

[ "PUB00055953" ]

[ "21478363" ]

[ "Biological systems discovery in silico: radical S-adenosylmethionine protein families and their target peptides for posttranslational modification." ]

[ 2011 ]

1

[]

0

null

[ "Pseudomonadota", "marine metagenome" ]

[ 54, 2 ]

2

[]

0

true

Family

His-Xaa-Ser system protein

His-Xaa-Ser_sys

9

IPR023815

23,815

CRISPR-associated protein Csx19

CRISPR-assoc_Csx19

Family

283

false

Members of this protein family are found exclusively in CRISPR-containing organisms, in operon contexts with RAMP (repeat-associated mystery protein) proteins also linked to CRISPR. The Csx19 family previously was known as the TIGR03984 family CRISPR-associated protein [ ].

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF27799", "TIGR03984" ]

[ "CRISPR-assoc_Csx19", "" ]

[ 280, 252 ]

2

[ "GP" ]

[ "GenProp0021" ]

[ "GP:GenProp0021" ]

1

[ "8s9t", "8s9u", "8s9v", "8s9x" ]

4

[ "PUB00106803" ]

[ "28698278" ]

[ "On the Origin of Reverse Transcriptase-Using CRISPR-Cas Systems and Their Hyperdiverse, Enigmatic Spacer Repertoires." ]

[ 2017 ]

1

[]

0

null

[ "Bacteria", "Methanosarcinales", "ecological metagenomes" ]

[ 270, 10, 3 ]

3

[]

0

true

Family

CRISPR-associated protein Csx19

CRISPR-assoc_Csx19

5

IPR023816

23,816

CRISPR-associated protein CYA0889

CRISPR-assoc_CYA0889

Family

161

false

Members of this protein family belong to CRISPR-associated (Cas) gene clusters. The majority of members are Cyanobacterial.

[]

0

[ "NCBIFAM" ]

[ "TIGR03985" ]

[ "" ]

[ 161 ]

1

[ "GP" ]

[ "GenProp0021" ]

[ "GP:GenProp0021" ]

1

[]

0

[]

0

[]

0

null

[ "Cyanobacteriota" ]

[ 161 ]

1

[]

0

true

Family

CRISPR-associated protein CYA0889

CRISPR-assoc_CYA0889

2

IPR023818

23,818

Conserved hypothetical protein CHP03890, nif11/cupin domain-containing

Nif11_cupin

Family

8

false

Members of this protein family occur exclusively in the Cyanobacteria and contain both a nif11 and a cupin domain. The function is unknown.

[]

0

[ "NCBIFAM" ]

[ "TIGR03890" ]

[ "nif11_cupin" ]

[ 8 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Cyanophyceae" ]

[ 8 ]

1

[]

0

true

Family

Conserved hypothetical protein CHP03890, nif11/cupin domain-containing

Nif11_cupin

7

IPR023819

23,819

Peptide-modifying radical SAM enzyme putative, AF0577

Pep-mod_rSAM_AF0577

Family

282

false

This radical SAM family contains a C-terminal region motif CXXCX5CX3C that is found in PqqE and other radical SAM enzymes that act on peptide substrates. Members of this family are found primarily in the Archaea, but also several eukaryotes (Trichomonas vaginalis G3, Entamoeba dispar SAW760, Giardia intestinalis ATCC 5...

[]

0

[ "SFLD", "NCBIFAM" ]

[ "SFLDG01104", "TIGR04084" ]

[ "Uncharacterised_Radical_SAM_Su", "rSAM_AF0577" ]

[ 275, 240 ]

2

[]

0

[]

0

[ "PUB00055418" ]

[ "20218986" ]

[ "Anaerobic sulfatase-maturating enzyme--a mechanistic link with glycyl radical-activating enzymes?" ]

[ 2010 ]

1

[ "IPR023867" ]

[]

1

0

1

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

[ 178, 59, 40, 5 ]

4

[]

0

true

Family

Peptide-modifying radical SAM enzyme putative, AF0577

Pep-mod_rSAM_AF0577

3

IPR023820

23,820

Radical SAM GDL-associated

rSAM_GDL-assoc

Family

158

false

This narrowly distributed protein family contains an N-terminal radical SAM domain. It occurs in Pseudomonas fluorescens Pf0-1, Ralstonia solanacearum, and numerous species and strains of Burkholderia. Members always occur next to a trio of three mutually homologous genes, all of which contain the domain as the whole o...

[]

0

[ "NCBIFAM" ]

[ "TIGR03913" ]

[ "rad_SAM_trio" ]

[ 158 ]

1

[ "GP" ]

[ "GenProp0920" ]

[ "GP:GenProp0920" ]

1

[]

0

[]

0

[]

0

null

[ "Bacteria" ]

[ 158 ]

1

[]

0

true

Family

Radical SAM GDL-associated

rSAM_GDL-assoc

6

IPR023821

23,821

Radical SAM, TatD-associated

rSAM_TatD-assoc

Family

968

false

Members of this family are radical SAM proteins found in about 5 percent of microbial genomes. A portion occur as gene fusions with, or adjacent to, members of the TatD family of hydrolases ( ). The TatD family may have several paralogs per genome, including TatD itself from E. coli (a soluble protein not actually part...

[]

0

[ "SFLD", "NCBIFAM" ]

[ "SFLDG01111", "TIGR04038" ]

[ "Uncharacterised_Radical_SAM_Su", "tatD_link_rSAM" ]

[ 905, 968 ]

2

[]

0

[]

0

[]

0

[]

[ "IPR023822" ]

0

1

0

[ "Bacteria", "Eutreptiella gymnastica", "Methanosarcinales", "unclassified sequences" ]

[ 869, 1, 62, 36 ]

4

[]

0

true

Family

Radical SAM, TatD-associated

rSAM_TatD-assoc

6

IPR023822

23,822

Radical SAM, TatD-associated, bacteria

rSAM_TatD-assoc_bac

Family

225

false

Members of this protein family are radical SAM enzymes that appear paired with members of , a family of small (~170 residue), mostly hydrophobic proteins. This family of radical SAM enzymes belongs to a larger family , in which some members show regularly in contexts with TatD.

[]

0

[ "NCBIFAM" ]

[ "TIGR04100" ]

[ "rSAM_pair_X" ]

[ 225 ]

1

[]

0

[]

0

[]

0

[ "IPR023821" ]

[]

1

0

1

[ "Bacillota", "bioreactor metagenome" ]

[ 223, 2 ]

2

[]

0

true

Family

Radical SAM, TatD-associated, bacteria

rSAM_TatD-assoc_bac

3

IPR023823

23,823

Conserved hypothetical protein CHP04066, peptide maturation system

CHP04066_peptide_maturation

Family

171

false

Members of this protein family occur in various Clostridial genomes, always in the context of a short peptide, which is likely to be a bacteriocin, and a radical SAM protein that is predicted to modify the short peptide. Sequence analysis suggests a relationship between family members and archaeal proteins designated a...

[]

0

[ "NCBIFAM" ]

[ "TIGR04066" ]

[ "nat_prod_clost" ]

[ 171 ]

1

[ "GP" ]

[ "GenProp0945" ]

[ "GP:GenProp0945" ]

1

[]

0

[]

0

[]

0

null

[ "Bacteria" ]

[ 171 ]

1

[]

0

true

Family

Conserved hypothetical protein CHP04066, peptide maturation system

CHP04066_peptide_maturation

7

IPR023824

23,824

Conserved hypothetical protein CHP04073, exosortase-affiliated

CHP04073_exosortase-affil

Family

336

false

Members of this protein family are found in beta, gamma, and delta proteobacteria, and in the verrucomicrobia. Twenty-two of twenty-four species encountered contain the PEP-CTERM/exosortase system for modulating extracellular polysaccharide biosynthesis production, suggesting a role in protein sorting. There is a dista...

[]

0

[ "NCBIFAM" ]

[ "TIGR04073" ]

[ "exo_TIGR04073" ]

[ 336 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 330, 6 ]

2

[]

0

true

Family

Conserved hypothetical protein CHP04073, exosortase-affiliated

CHP04073_exosortase-affil

1

IPR023825

23,825

CRISPR-associated RAMP BGP1436

CRISPR-assoc_RAMP_BGP1436

Family

535

false

Members of this protein family, part of the larger Repeat-Associated Mystery Protein (RAMP) family, are found in local contexts containing other RAMPs. They occur exclusively in species with type III CRISPR systems.

[]

0

[ "NCBIFAM" ]

[ "TIGR03986" ]

[ "" ]

[ 535 ]

1

[ "GP" ]

[ "GenProp0021" ]

[ "GP:GenProp0021" ]

1

[ "8s9t", "8s9u", "8s9v", "8s9x" ]

4

[]

0

[]

0

null

[ "Bacteria", "Methanosarcinales", "metagenomes" ]

[ 518, 10, 7 ]

3

[]

0

true

Family

CRISPR-associated RAMP BGP1436

CRISPR-assoc_RAMP_BGP1436

4

IPR023826

23,826

Rhomboid-like serine protease, proteobacteria

Rhom-like_SP_proteobac

Family

1,626

false

This entry describes a rhomboid-like intramembrane serine protease. Its species distribution closely matches that of GlyGly-CTERM ( ), a protein targeting domain analogous to LPXTG and PEP-CTERM. In a number of species (Ralstonia eutropha, R. metallidurans, R. solanacearum, Marinobacter aquaeolei, etc) with just one Gl...

[]

0

[ "NCBIFAM" ]

[ "TIGR03902" ]

[ "rhom_GG_sort" ]

[ 1626 ]

1

[ "GP" ]

[ "GenProp0778" ]

[ "GP:GenProp0778" ]

1

[]

0

[ "PUB00060404" ]

[ "22194940" ]

[ "GlyGly-CTERM and rhombosortase: a C-terminal protein processing signal in a many-to-one pairing with a rhomboid family intramembrane serine protease." ]

[ 2011 ]

1

[]

0

null

[ "Bacteria", "Cladocopium goreaui", "ecological metagenomes" ]

[ 1602, 1, 23 ]

3

[]

0

true

Family

Rhomboid-like serine protease, proteobacteria

Rhom-like_SP_proteobac

3

IPR023827

23,827

Peptidase S8, subtilisin, Asp-active site

Peptidase_S8_Asp-AS

Active_site

85,378

false

Subtilases [ ] are an extensive family of serine proteases belonging to the MEROPS peptidase family S8 (subtilisin, clan SB). Members of this family have a catalytic triad in the order Asp, His and Ser in the sequence, which is a different order to that of families S1, S9 and S10. The catalytic activity is provided by ...

[]

0

[ "PROSITE" ]

[ "PS00136" ]

[ "SUBTILASE_ASP" ]

[ 85378 ]

1

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

[ "3.4.21", "3.4.21.-", "PWY-7884", "R-CEL-1592389", "R-CEL-186797", "R-CEL-2173789", "R-CEL-2173796", "R-DME-1592389", "R-DME-186797", "R-DME-2173789", "R-DME-2173796", "R-DME-8963889", "R-DME-9768727", "R-HSA-1181150", "R-HSA-1442490", "R-HSA-1566948", "R-HSA-1592389", "R-HSA-15978...

[ "EC:3.4.21", "EC:3.4.21.-", "METACYC:PWY-7884", "REACTOME:R-CEL-1592389", "REACTOME:R-CEL-186797", "REACTOME:R-CEL-2173789", "REACTOME:R-CEL-2173796", "REACTOME:R-DME-1592389", "REACTOME:R-DME-186797", "REACTOME:R-DME-2173789", "REACTOME:R-DME-2173796", "REACTOME:R-DME-8963889", "REACTOME:R-...

72

[ "1a2q", "1af4", "1ah2", "1ak9", "1aqn", "1au9", "1av7", "1avt", "1be6", "1be8", "1bfk", "1bfu", "1bh6", "1bjr", "1c3l", "1c9j", "1c9m", "1c9n", "1cnm", "1cse", "1dbi", "1dui", "1ea7", "1egq", "1gci", "1gns", "1gnv", "1ht3", "1iav", "1ic6", "1jea", "1lw6"...

533

[ "PUB00004957" ]

[ "1798697" ]

[ "Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases." ]

[ 1991 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Plasmid pAD1", "Viruses", "unclassified sequences" ]

[ 1312, 49423, 34123, 1, 33, 486 ]

6

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

[ 41, 4, 20, 8, 25, 19, 4, 41, 26, 4, 3, 75 ]

12

true

Active_site

Peptidase S8, subtilisin, Asp-active site

Peptidase_S8_Asp-AS

1

IPR023828

23,828

Peptidase S8, subtilisin, Ser-active site

Peptidase_S8_Ser-AS

Active_site

141,408

false

This entry represents the conserved sequence around the Ser active site. Subtilases [ ] are an extensive family of serine proteases belonging to the MEROPS peptidase family S8 (subtilisin, clan SB). Members of this family have a catalytic triad in the order Asp, His and Ser in the sequence, which is a different order t...

[]

0

[ "PROSITE" ]

[ "PS00138" ]

[ "SUBTILASE_SER" ]

[ 141408 ]

1

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

[ "3.4.21", "3.4.21.-", "PWY-7884", "R-CEL-1592389", "R-CEL-186797", "R-CEL-2173789", "R-CEL-2173796", "R-CEL-983168", "R-DDI-1369007", "R-DDI-159418", "R-DDI-193368", "R-DDI-382556", "R-DDI-9754706", "R-DDI-9757110", "R-DME-1592389", "R-DME-186797", "R-DME-2173789", "R-DME-2173796",...

[ "EC:3.4.21", "EC:3.4.21.-", "METACYC:PWY-7884", "REACTOME:R-CEL-1592389", "REACTOME:R-CEL-186797", "REACTOME:R-CEL-2173789", "REACTOME:R-CEL-2173796", "REACTOME:R-CEL-983168", "REACTOME:R-DDI-1369007", "REACTOME:R-DDI-159418", "REACTOME:R-DDI-193368", "REACTOME:R-DDI-382556", "REACTOME:R-DDI...

102

[ "1a2q", "1af4", "1ah2", "1ak9", "1aqn", "1au9", "1av7", "1be6", "1be8", "1bfk", "1bfu", "1bh6", "1bjr", "1c3l", "1c9j", "1c9m", "1c9n", "1cnm", "1cse", "1dbi", "1dui", "1ea7", "1egq", "1ga1", "1ga4", "1ga6", "1gci", "1gnv", "1ht3", "1iav", "1ic6", "1jea"...

504

[ "PUB00004957" ]

[ "1798697" ]

[ "Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases." ]

[ 1991 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Plasmid pAD1", "Viruses", "unclassified sequences" ]

[ 2135, 68547, 69884, 1, 76, 765 ]

6

[ "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...

[ 245, 4, 25, 12, 35, 29, 9, 148, 35, 4, 4, 232 ]

12

true

Active_site

Peptidase S8, subtilisin, Ser-active site

Peptidase_S8_Ser-AS

6

IPR023830

23,830

Peptidase S8A, PatG

Peptidase_S8A_PatG

Family

338

false

Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...

[]

0

[ "NCBIFAM" ]

[ "TIGR03895" ]

[ "protease_PatA" ]

[ 338 ]

1

[ "GP" ]

[ "GenProp1083" ]

[ "GP:GenProp1083" ]

1

[ "4uvq" ]

1

[ "PUB00000522", "PUB00003576", "PUB00035098", "PUB00035099" ]

[ "8439290", "7845208", "10656993", "9572109" ]

[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "Subtilase-like pro-protein convertases: from molecular specificity to therapeutic applications.", "Subtilisin-related serine proteases in the mammalian constitutive secretory pathway." ]

[ 1993, 1994, 2000, 1998 ]

4

[ "IPR015500" ]

[]

1

0

1

[ "Bacteria", "Methanosarcina barkeri", "freshwater metagenome" ]

[ 327, 4, 7 ]

3

[]

0

true

Family

Peptidase S8A, PatG

Peptidase_S8A_PatG

6

IPR023831

23,831

Serine peptidase MXAN_5808-like

MXAN_5808-like

Family

116

false

This entry represents a group of protein sequences mainly found in the order Myxococcales in the Deltaproteobacteria, including MXAN_5808 from Myxococcus xanthus ( ). Members are multidomain proteins of about 1070 residues that contain a PDZ domain, an S41 family peptidase domain belonging to MEROPS peptidase family S4...

[]

0

[ "NCBIFAM" ]

[ "TIGR03900" ]

[ "prc_long_Delta" ]

[ 116 ]

1

[]

0

[]

0

[]

0

[ "IPR004447" ]

[]

1

0

1

[ "Bacteria" ]

[ 116 ]

1

[]

0

true

Family

Serine peptidase MXAN_5808-like

MXAN_5808-like

3

IPR023832

23,832

Histidine triad protein

His_triad_protein

Family

1,223

false

This entry represents a family of Streptococcal proteins that contain a number of repeated His-X-X-His-X-His (histidine triad) motifs. Members of the family are suggested to cleave human complement component 3, and family member PhpA has been shown in vaccine studies to be a protective antigen in mice [ ].

[]

0

[ "NCBIFAM" ]

[ "TIGR01363" ]

[ "strep_his_triad" ]

[ 1223 ]

1

[]

0

[ "2cs7", "3zfj", "6csl" ]

3

[ "PUB00009544" ]

[ "11349048" ]

[ "Recombinant PhpA protein, a unique histidine motif-containing protein from Streptococcus pneumoniae, protects mice against intranasal pneumococcal challenge." ]

[ 2001 ]

1

[]

0

null

[ "Bacteria" ]

[ 1223 ]

1

[]

0

true

Family

Histidine triad protein

His_triad_protein

7

IPR023833

23,833

SipW-dependent-type signal peptide

Signal_pept_SipW-depend-type

Domain

4,421

false

This entry describes an N-terminal domain found regularly in proteins encoded near a variant form of signal peptidase I such as the SipW protein of Bacillus subtilis. Many though not all members are homologues of camelysin (a casein-cleaving metalloprotease) and TasA (CotN), a metalloprotease that is secreted, along wi...

[]

0

[ "NCBIFAM" ]

[ "TIGR04088" ]

[ "cognate_SipW" ]

[ 4421 ]

1

[ "GP" ]

[ "GenProp0957" ]

[ "GP:GenProp0957" ]

1

[ "5l8r", "6yac", "6yez", "6zoo", "6zxs", "7dkz" ]

6

[]

0

[]

0

null

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

[ 586, 3679, 127, 29 ]

4

[]

0

true

Domain

SipW-dependent-type signal peptide

Signal_pept_SipW-depend-type

6

IPR023834

23,834

Type VII secretion system peptidase S8A, mycosin

T7SS_pept_S8A_mycosin

Family

5,324

false

Members of this family are subtilisin-related serine proteases belonging to MEROPS peptidase family S8A, mycosin-1 clan SB. They are found strictly in the Actinobacteria and associated with type VII secretion operons [ ]. The designation mycosin is used for members from Mycobacterium [ ].

[]

0

[ "NCBIFAM" ]

[ "TIGR03921" ]

[ "T7SS_mycosin" ]

[ 5324 ]

1

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

[ "3.4.21.-", "GenProp0904", "PWY-7884" ]

[ "EC:3.4.21.-", "GP:GenProp0904", "METACYC:PWY-7884" ]

3

[ "4hvl", "4j94", "4kb5", "4kg7", "4kpg", "4m1z", "7np7", "7npr", "7nps" ]

9

[ "PUB00053896", "PUB00082312" ]

[ "19876390", "10974545" ]

[ "Systematic genetic nomenclature for type VII secretion systems.", "The mycosins of Mycobacterium tuberculosis H37Rv: a family of subtilisin-like serine proteases." ]

[ 2009, 2000 ]

2

[ "IPR015500" ]

[]

1

0

1

[ "Actinomycetes", "freshwater metagenome" ]

[ 5323, 1 ]

2

[]

0

true

Family

Type VII secretion system peptidase S8A, mycosin

T7SS_pept_S8A_mycosin

1

IPR023835

23,835

Type VII secretion system AAA-ATPase, EccA

T7SS_EccA

Family

1,327

false

This entry represents the AAA family ATPase, EccA, of the type VII secretion system from the actinobacteria. Species such as Mycobacterium tuberculosis have multicopies of this secretion system with genes designated: EccA1, EccA2, etc.

[]

0

[ "NCBIFAM" ]

[ "TIGR03922" ]

[ "T7SS_EccA" ]

[ 1327 ]

1

[ "GP" ]

[ "GenProp0904" ]

[ "GP:GenProp0904" ]

1

[]

0

[]

0

[ "IPR000641" ]

[]

1

0

1

[ "Mycobacteriales" ]

[ 1327 ]

1

[]

0

true

Family

Type VII secretion system AAA-ATPase, EccA

T7SS_EccA

7

IPR023836

23,836

EccCa-like, Actinobacteria

EccCa-like_Actinobacteria

Family

5,738

false

This entry represents the EccCa subunit of the type VII secretion system from Actinobacteria. In many proteins it forms the N-terminal domain being fused to EccCb as the C-terminal domain. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in ...

[]

0

[ "NCBIFAM" ]

[ "TIGR03924" ]

[ "T7SS_EccC_a" ]

[ 5738 ]

1

[ "GP" ]

[ "GenProp0904" ]

[ "GP:GenProp0904" ]

1

[ "4nh0", "7b9f", "7b9s", "7np7", "7npr", "7npt", "7npu", "7npv" ]

8

[ "PUB00053896" ]

[ "19876390" ]

[ "Systematic genetic nomenclature for type VII secretion systems." ]

[ 2009 ]

1

[]

0

null

[ "Acrobeloides nanus", "Bacillati", "metagenomes" ]

[ 1, 5732, 5 ]

3

[]

0

true

Family

EccCa-like, Actinobacteria

EccCa-like_Actinobacteria

7

IPR023837

23,837

EccCb-like, Actinobacteria

EccCb-like_Actinobacteria

Family

6,122

false

This entry represents the EccCb subunit of the type VII secretion system from Actinobacteria. In many proteins it forms the C-terminal domain being fused to EccCa as the N-terminal domain. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in ...

[]

0

[ "NCBIFAM" ]

[ "TIGR03925" ]

[ "T7SS_EccC_b" ]

[ 6122 ]

1

[ "GP" ]

[ "GenProp0904" ]

[ "GP:GenProp0904" ]

1

[ "4n1a", "4nh0", "7b9f", "7b9s", "7np7", "7npr", "7npt", "7npu", "7npv", "9jv8" ]

10

[ "PUB00053896" ]

[ "19876390" ]

[ "Systematic genetic nomenclature for type VII secretion systems." ]

[ 2009 ]

1

[]

0

null

[ "Acrobeloides nanus", "Bacillati", "metagenomes" ]

[ 1, 6115, 6 ]

3

[]

0

true

Family

EccCb-like, Actinobacteria

EccCb-like_Actinobacteria

3

IPR023838

23,838

Type VII secretion system EsaA

T7SS_EsaA

Domain

972

false

Members of this family are associated with type VII secretion systems. EsaA from Staphylococcus aureus is encoded within a cluster comprised of eight predicted ORFs (esxA, esaA, essA, esaB, essB, essC, esxY, and esxB) [ ]. Its function is unknown, though it is probably involved, with EsxA and EsxB, in the establishment...

[ "GO:0016020" ]

[ "membrane" ]

[ "cellular_component" ]

1

[ "NCBIFAM" ]

[ "TIGR03929" ]

[ "T7_esaA_Nterm" ]

[ 972 ]

1

[ "GP" ]

[ "GenProp0905" ]

[ "GP:GenProp0905" ]

1

[]

0

[ "PUB00044259", "PUB00055111", "PUB00067874" ]

[ "15657139", "18554323", "21705600" ]

[ "EsxA and EsxB are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections.", "EsaC substrate for the ESAT-6 secretion pathway and its role in persistent infections of Staphylococcus aureus.", "Bacteriophage infection in rod-shaped gram-positive bacteria: evid...

[ 2005, 2008, 2011 ]

3

[]

0

null

[ "Bacteria" ]

[ 972 ]

1

[]

0

true

Domain

Type VII secretion system EsaA

T7SS_EsaA

6

IPR023839

23,839

Firmicutes EssC, C-terminal

Firmicutes_EssC_C

Domain

1,536

false

This entry describes the C-terminal domain of the type VII secretion protein EssC from Firmicutes. EssC contains the FtsK domains and is typically between 107 and 121 amino acids in length. It is required for secretion of EsxA and EsxB. It is related to the FtsK/SpoIIIE proteins ( ), which are DNA transporters responsi...

[]

0

[ "NCBIFAM" ]

[ "TIGR03928" ]

[ "T7_EssCb_Firm" ]

[ 1536 ]

1

[ "GP" ]

[ "GenProp0905" ]

[ "GP:GenProp0905" ]

1

[]

0

[ "PUB00005183" ]

[ "8160014" ]

[ "Bacillus subtilis SpoIIIE protein required for DNA segregation during asymmetric cell division." ]

[ 1994 ]

1

[]

0

null

[ "Bacillati", "human gut metagenome" ]

[ 1535, 1 ]

2

[]

0

true

Domain

Firmicutes EssC, C-terminal

Firmicutes_EssC_C

7

IPR023841

23,841

Bacillithiol biosynthesis deacetylase BshB2

BshB2

Family

1,571

false

Bacillithiol (BSH) is a low-molecular-weight thiol, an analog of glutathione and mycothiol, that is found largely in the Firmicutes. BSH biosynthesis requires the presence of deacetylase BshB1 or BshB2 (also termed YpjG and YojG, respectively) [ ]. This entry represents BshB2.

[]

0

[ "NCBIFAM" ]

[ "TIGR04000" ]

[ "thiol_BshB2" ]

[ 1571 ]

1

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

[ "3.5.1.-", "GenProp0927", "GenProp1505", "PWY-1822", "PWY-5497", "PWY-5784", "PWY-5846", "PWY-6409", "PWY-6899", "PWY-7018", "PWY-7403", "PWY-7430", "PWY-7496", "PWY-7571", "PWY-7652", "PWY-7771", "PWY-7821", "PWY-7850", "PWY-8229", "PWY-8293", "PWY-8402", "PWY-8418", "PW...

[ "EC:3.5.1.-", "GP:GenProp0927", "GP:GenProp1505", "METACYC:PWY-1822", "METACYC:PWY-5497", "METACYC:PWY-5784", "METACYC:PWY-5846", "METACYC:PWY-6409", "METACYC:PWY-6899", "METACYC:PWY-7018", "METACYC:PWY-7403", "METACYC:PWY-7430", "METACYC:PWY-7496", "METACYC:PWY-7571", "METACYC:PWY-7652"...

25

[]

0

[ "PUB00055031" ]

[ "20308541" ]

[ "Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli." ]

[ 2010 ]

1

[ "IPR003737" ]

[]

1

0

1

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

[ 1570, 1 ]

2

[]

0

true

Family

Bacillithiol biosynthesis deacetylase BshB2

BshB2

1