LiteFold/InterPro · Datasets at Hugging Face

IPR011127

11,127

D-alanine--D-alanine ligase, N-terminal domain

Dala_Dala_lig_N

Domain

31,972

false

This entry represents the N-terminal region of the D-alanine--D-alanine ligase enzyme ( ) which is thought to be involved in substrate binding [ , ]. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan b...

[]

0

[ "PFAM" ]

[ "PF01820" ]

[ "Dala_Dala_lig_N" ]

[ 31972 ]

1

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

[ "6.3.2.4", "PWY-6386", "PWY-6387", "PWY-7953" ]

[ "EC:6.3.2.4", "METACYC:PWY-6386", "METACYC:PWY-6387", "METACYC:PWY-7953" ]

4

[ "1e4e", "1ehi", "1iov", "1iow", "2dln", "2fb9", "2i80", "2i87", "2i8c", "2pvp", "2yzg", "2yzm", "2yzn", "2zdg", "2zdh", "2zdq", "3e5n", "3i12", "3k3p", "3lwb", "3n8d", "3q1k", "3r23", "3r5f", "3r5x", "3rfc", "3se7", "3tqt", "3v4z", "4c5a", "4c5b", "4c5c"...

64

[ "PUB00000444", "PUB00014326", "PUB00101159" ]

[ "9054558", "10908650", "20956591" ]

[ "D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant.", "The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA).", "Structure of the Mycobacterium tuberculosis D-alanine:D-alanin...

[ 1997, 2000, 2011 ]

3

[]

0

null

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

[ 30594, 807, 571 ]

3

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 22, 2, 1, 5, 5 ]

5

true

Domain

D-alanine--D-alanine ligase, N-terminal domain

Dala_Dala_lig_N

2

IPR011128

11,128

Glycerol-3-phosphate dehydrogenase, NAD-dependent, N-terminal

G3P_DH_NAD-dep_N

Domain

38,683

false

NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyses the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain [ ].

[ "GO:0016616", "GO:0051287", "GO:0046168" ]

[ "oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor", "NAD binding", "glycerol-3-phosphate catabolic process" ]

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

3

[ "PFAM" ]

[ "PF01210" ]

[ "NAD_Gly3P_dh_N" ]

[ 38683 ]

1

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

[ "1.1.1.94", "PWY-5667", "PWY-5981", "PWY-7902", "R-CEL-1483166", "R-DME-1483166", "R-DRE-1483166", "R-HSA-1483166", "R-MMU-1483166", "R-RNO-1483166", "R-SCE-1483166", "R-SPO-1483166", "R-XTR-1483166" ]

[ "EC:1.1.1.94", "METACYC:PWY-5667", "METACYC:PWY-5981", "METACYC:PWY-7902", "REACTOME:R-CEL-1483166", "REACTOME:R-DME-1483166", "REACTOME:R-DRE-1483166", "REACTOME:R-HSA-1483166", "REACTOME:R-MMU-1483166", "REACTOME:R-RNO-1483166", "REACTOME:R-SCE-1483166", "REACTOME:R-SPO-1483166", "REACTOME...

13

[ "1evy", "1evz", "1jdj", "1m66", "1m67", "1n1e", "1n1g", "1txg", "1wpq", "1x0v", "1x0x", "1yj8", "1z82", "2pla", "3k96", "4fgw", "6e8y", "6e8z", "6e90", "6iuy", "6pyp" ]

21

[ "PUB00014289" ]

[ "10801498" ]

[ "A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana." ]

[ 2000 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Megaviridae environmental sample", "unclassified sequences" ]

[ 74, 26943, 11071, 1, 594 ]

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",...

[ 15, 5, 6, 13, 1, 8, 4, 1, 9, 10, 2, 2, 24 ]

13

true

Domain

Glycerol-3-phosphate dehydrogenase, NAD-dependent, N-terminal

G3P_DH_NAD-dep_N

2

IPR011129

11,129

Cold-shock domain

CSD

Domain

132,376

false

A conserved domain of about 70 amino acids has been found in prokaryotic and eukaryotic single-strand nucleic-acid binding proteins [ , , , , ]. This domain, which is known as the 'cold-shock domain' (CSD) is present in the proteins listed below. Escherichia coli protein CS7.4 (gene cspA) which is induced in response t...

[ "GO:0003676" ]

[ "nucleic acid binding" ]

[ "molecular_function" ]

1

[ "SMART" ]

[ "SM00357" ]

[ "CSP" ]

[ 132376 ]

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-72163", "R-BTA-72165", "R-BTA-72203", "R-BTA-877300", "R-DRE-72163", "R-DRE-877300", "R-HSA-2173796", "R-HSA-452723", "R-HSA-72163", "R-HSA-72165", "R-HSA-72203", "R-HSA-877300", "R-HSA-9017802", "R-MMU-72163", "R-MMU-72165", "R-MMU-72203", "R-MMU-877300", "R-MMU-9017802", ...

[ "REACTOME:R-BTA-72163", "REACTOME:R-BTA-72165", "REACTOME:R-BTA-72203", "REACTOME:R-BTA-877300", "REACTOME:R-DRE-72163", "REACTOME:R-DRE-877300", "REACTOME:R-HSA-2173796", "REACTOME:R-HSA-452723", "REACTOME:R-HSA-72163", "REACTOME:R-HSA-72165", "REACTOME:R-HSA-72203", "REACTOME:R-HSA-877300", ...

23

[ "1a62", "1a63", "1a8v", "1c9o", "1csp", "1csq", "1g6p", "1h95", "1hz9", "1hza", "1hzb", "1hzc", "1i5f", "1mjc", "1nmf", "1nmg", "1pv4", "1pvo", "1wfq", "1x65", "1xpo", "1xpr", "1xpu", "2a8v", "2bh8", "2es2", "2f52", "2hax", "2ht1", "2i5l", "2i5m", "2id0"...

150

[ "PUB00003861", "PUB00004061", "PUB00004326", "PUB00021106", "PUB00028025" ]

[ "8022259", "2184368", "1622933", "9586995", "10446180" ]

[ "The cold-shock response--a hot topic.", "Cold shock and DNA binding.", "The product of unr, the highly conserved gene upstream of N-ras, contains multiple repeats similar to the cold-shock domain (CSD), a putative DNA-binding motif.", "Crystal structure of the RNA-binding domain from transcription terminatio...

[ 1994, 1990, 1992, 1998, 1999 ]

5

[]

[ "IPR002059", "IPR011113" ]

0

2

0

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

[ 1571, 112805, 16234, 25, 1741 ]

5

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

[ 17, 5, 48, 8, 12, 49, 37, 12, 35, 14 ]

10

true

Domain

Cold-shock domain

CSD

4

IPR011130

11,130

SecA, preprotein cross-linking domain

SecA_preprotein_X-link_dom

Domain

33,989

false

The SecA ATPase is involved in the insertion and retraction of preproteins through the plasma membrane. This domain has been found to cross-link to preproteins, thought to indicate a role in preprotein binding. The pre-protein cross-linking domain is comprised of two sub domains that are inserted within the ATPase doma...

[ "GO:0017038", "GO:0016020" ]

[ "protein import", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "SMART" ]

[ "PF01043", "SM00958" ]

[ "SecA_PP_bind", "SecA_PP_bind" ]

[ 33322, 33716 ]

2

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

[ "7.4.2.8", "R-HSA-1222387", "R-HSA-9636383", "R-HSA-9760173" ]

[ "EC:7.4.2.8", "REACTOME:R-HSA-1222387", "REACTOME:R-HSA-9636383", "REACTOME:R-HSA-9760173" ]

4

[ "1m6n", "1m74", "1nkt", "1nl3", "1tf2", "1tf5", "2fsf", "2fsg", "2fsh", "2fsi", "2ibm", "2ipc", "2vda", "3din", "3dl8", "3iqm", "3iqy", "3jux", "3jv2", "4uaq", "4ys0", "5eul", "5k94", "5k9t", "6gox", "6itc", "6s0k", "6sxh", "6t4h", "7xha", "7xhb", "8y9y"...

36

[ "PUB00014329" ]

[ "12242434" ]

[ "Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA." ]

[ 2002 ]

1

[]

0

null

[ "Bacteria", "Candidatus Methanogaster sp.", "Eukaryota", "Siphoviridae sp. ctHip2", "unclassified sequences" ]

[ 31034, 1, 2389, 1, 564 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 11, 1, 8, 11 ]

4

true

Domain

SecA, preprotein cross-linking domain

SecA_preprotein_X-link_dom

5

IPR011134

11,134

Allophycocyanin linker protein

Allophyco_linker

Family

341

false

Members of this family are linker polypeptides that are associated with phycobilisomes. Phycobiliproteins (biliproteins) are accessory pigments that serve as receptors of light energy for photosystem II. Phycobilisomes are highly organised complex structures of biliproteins and linker polypeptides. The linker polypepti...

[ "GO:0015979", "GO:0030089" ]

[ "photosynthesis", "phycobilisome" ]

[ "biological_process", "cellular_component" ]

2

[ "PIRSF" ]

[ "PIRSF000083" ]

[ "Allophyco_linker" ]

[ 341 ]

1

[]

0

[ "1b33", "7ext", "7eyd", "7sc7", "7sc9", "7scb", "7scc", "7vea", "8to2", "8tpj", "8uhe", "8wql", "9i1r", "9v7j", "9v7k" ]

15

[ "PUB00014263", "PUB00014356", "PUB00014363" ]

[ "9990029", "6782105", "10049814" ]

[ "Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus.", "Molecular architecture of a light-harvesting antenna. In vitro assembly of the rod substructures of Synechococcus 6301 phycobilisomes.",...

[ 1999, 1981, 1998 ]

3

[]

0

null

[ "Cyanobacteriota", "Paulinella" ]

[ 337, 4 ]

2

[]

0

true

Family

Allophycocyanin linker protein

Allophyco_linker

3

IPR011138

11,138

Succinate dehydrogenase cytochrome b558 subunit

Cytochrome_b-558

Family

7,719

false

This family contains succinate dehydrogenase (also known as succinate:quinone oxidoreductase, SQR) subunit C of Bacillus subtilis, designated cytochrome b-558, and related sequences that include a fumarate reductase subunit C. This family is only weakly similar to the main group of succinate dehydrogenase cytochrome b ...

[]

0

[ "NCBIFAM" ]

[ "TIGR02046" ]

[ "sdhC_b558_fam" ]

[ 7719 ]

1

[ "GP" ]

[ "GenProp0033" ]

[ "GP:GenProp0033" ]

1

[ "9lay", "9laz", "9lb0", "9lb1" ]

4

[ "PUB00015564", "PUB00015643", "PUB00015715", "PUB00080558", "PUB00080947", "PUB00080948", "PUB00080949", "PUB00080952", "PUB00080953" ]

[ "3086287", "11004459", "15078221", "12788489", "2120540", "9799121", "2176107", "1324713", "11803013" ]

[ "Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex.", "Succinate: quinone oxidoreductases: new insights from X-ray crystal structures.", "Complex II from a structural perspective.", "Variation in proton donor/acceptor pathways in succinate:quinone oxi...

[ 1986, 2000, 2004, 2003, 1990, 1998, 1990, 1992, 2002 ]

9

[ "IPR000701" ]

[ "IPR016002" ]

1

0

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

[ 7605, 4, 110 ]

3

[]

0

true

Family

Succinate dehydrogenase cytochrome b558 subunit

Cytochrome_b-558

6

IPR011140

11,140

Autonomous glycyl radical cofactor GrcA

Glycyl_radical_cofactor_GrcA

Family

1,927

false

This group represents a glycyl radical cofactor protein, YfiD-type. YfiD of Escherichia coli, and the homologous Y06I of Bacteriophage T4, show striking sequence similarity with the C-terminal region of pyruvate formate-lyase (PFL). Expression of YfiD is known to be controlled by transcription regulator FNR, and in res...

[]

0

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

[ "MF_00806", "PIRSF000378", "TIGR04365" ]

[ "GrcA", "Gly_radicl_yfiD", "spare_glycyl" ]

[ 1402, 1904, 1532 ]

3

[ "GP" ]

[ "GenProp0943" ]

[ "GP:GenProp0943" ]

1

[ "6owr" ]

1

[ "PUB00014425", "PUB00014466" ]

[ "11444864", "11932447" ]

[ "YfiD of Escherichia coli and Y06I of bacteriophage T4 as autonomous glycyl radical cofactors reconstituting the catalytic center of oxygen-fragmented pyruvate formate-lyase.", "Expression of the Escherichia coli yfiD gene responds to intracellular pH and reduces the accumulation of acidic metabolic end products....

[ 2001, 2002 ]

2

[]

0

null

[ "Bacteria", "Opisthokonta", "Viruses", "bioreactor metagenome" ]

[ 1528, 4, 394, 1 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Autonomous glycyl radical cofactor GrcA

Glycyl_radical_cofactor_GrcA

1

IPR011141

11,141

Polyketide synthase, type III

Polyketide_synthase_type-III

Family

20,437

false

Type III polyketide synthases include plant naringenin-chalcone synthases (CHSs) [ , ] and stilbene synthases (STSs) (resveratrol synthases) [ , ]. This group also includes CHS-related enzymes such as bibenzyl synthase (BBS) [ ] and acridone synthase (ACS) [ ] that share a common chemical mechanism but differ from CHS ...

[ "GO:0016747", "GO:0009058" ]

[ "acyltransferase activity, transferring groups other than amino-acyl groups", "biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF", "PANTHER" ]

[ "PIRSF000451", "PTHR11877" ]

[ "PKS_III", "" ]

[ 15357, 20419 ]

2

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

[ "2.3.1", "2.3.1.74", "PWY-5135", "PWY-6316", "PWY-6515", "PWY-6787", "PWY-7397", "PWY-7897" ]

[ "EC:2.3.1", "EC:2.3.1.74", "METACYC:PWY-5135", "METACYC:PWY-6316", "METACYC:PWY-6515", "METACYC:PWY-6787", "METACYC:PWY-7397", "METACYC:PWY-7897" ]

8

[ "1bi5", "1bq6", "1cgk", "1cgz", "1chw", "1cml", "1d6f", "1d6h", "1d6i", "1ee0", "1i86", "1i88", "1i89", "1i8b", "1jwx", "1qlv", "1ted", "1tee", "1u0m", "1u0u", "1u0v", "1u0w", "1xes", "1xet", "1z1e", "1z1f", "2d3m", "2d51", "2d52", "2h84", "2p0u", "3a5q"...

133

[ "PUB00014368", "PUB00014374", "PUB00014376", "PUB00014381", "PUB00014399", "PUB00014406", "PUB00014424", "PUB00014451", "PUB00014454", "PUB00014465", "PUB00024511", "PUB00095622", "PUB00097923", "PUB00097924", "PUB00112203", "PUB00114049", "PUB00160371" ]

[ "9622493", "12502351", "10426957", "11732902", "7727746", "11828424", "10476972", "7872785", "1426272", "11752437", "11137815", "23615910", "15309535", "15170123", "12430724", "12636085", "31673313" ]

[ "Plant polyketide synthases: a chalcone synthase-type enzyme which performs a condensation reaction with methylmalonyl-CoA in the biosynthesis of C-methylated chalcones.", "Plant-like biosynthetic pathways in bacteria: from benzoic acid to chalcone.", "Structure of chalcone synthase and the molecular basis of p...

[ 1998, 2002, 1999, 2001, 1995, 2001, 1999, 1995, 1992, 2001, 2000, 2013, 2004, 2004, 2002, 2003, 2019 ]

17

[]

0

null

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

[ 8442, 11946, 2, 47 ]

4

[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 54, 1, 90, 78 ]

4

true

Family

Polyketide synthase, type III

Polyketide_synthase_type-III

9

IPR011142

11,142

Spider toxin CSTX, Knottin scaffold conserved site

Spider_toxin_CSTX_Knottin_CS

Conserved_site

350

false

Spider toxins of the CSTX family are ion channel toxins containing an inhibitor cystine knot structural motif or Knottin scaffold (https://www.dsimb.inserm.fr/KNOTTIN/). The four disulphide bonds present in the CSTX spider toxin family are arranged in the following pattern: 1-4, 2-5, 3-8 and 6-7. This family includes: ...

[]

0

[ "PROSITE" ]

[ "PS60029" ]

[ "SPIDER_CSTX" ]

[ 350 ]

1

[ "PROSITEDOC" ]

[ "PDOC60029" ]

[ "PROSITEDOC:PDOC60029" ]

1

[ "2mzf", "2mzg" ]

2

[ "PUB00033816", "PUB00033817", "PUB00033818" ]

[ "10897091", "11693532", "15272079" ]

[ "A lysine rich C-terminal tail is directly involved in the toxicity of CSTX-1, a neurotoxic peptide from the venom of the spider Cupiennius salei.", "CSTX-9, a toxic peptide from the spider Cupiennius salei: amino acid sequence, disulphide bridge pattern and comparison with other spider toxins containing the cyst...

[ 2000, 2001, 2004 ]

3

[]

0

null

[ "Eukaryota" ]

[ 350 ]

1

[]

0

true

Conserved_site

Spider toxin CSTX, Knottin scaffold conserved site

Spider_toxin_CSTX_Knottin_CS

6

IPR011143

11,143

Ganglioside GM2 synthase

GM2_synthase

Family

1,000

false

Ganglioside GM2 synthase (N-acetylgalactosaminyltransferase, GalNAcT) is one of the key enzymes in gangliosides biosynthesis, which involves a series of ER- or Golgi-based glycosyltransferases. GalNAcT is a type II integral membrane protein of the Golgi apparatus that catalyses the synthesis of the glycosphingolipids G...

[ "GO:0016758", "GO:0000139" ]

[ "hexosyltransferase activity", "Golgi membrane" ]

[ "molecular_function", "cellular_component" ]

2

[ "PIRSF" ]

[ "PIRSF000474" ]

[ "GM2_GD2_synthase" ]

[ 1000 ]

1

[ "EC", "EC", "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.-", "2.4.1.92", "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...

[ "EC:2.4.1.-", "EC:2.4.1.92", "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",...

209

[ "9h6j", "9h6k", "9h6l" ]

3

[ "PUB00014811", "PUB00014812", "PUB00014813" ]

[ "12234191", "11085888", "7515051" ]

[ "Regulation of ganglioside biosynthesis by enzyme complex formation of glycosyltransferases.", "A functional role for complex gangliosides: motor deficits in GM2/GD2 synthase knockout mice.", "Molecular cloning of a murine N-acetylgalactosamine transferase cDNA that determines expression of the T lymphocyte-spe...

[ 2002, 2000, 1994 ]

3

[]

0

null

[ "Chordata" ]

[ 1000 ]

1

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

[ 7, 3, 5, 9 ]

4

true

Family

Ganglioside GM2 synthase

GM2_synthase

5

IPR011145

11,145

Scavenger mRNA decapping enzyme, N-terminal

Scavenger_mRNA_decap_enz_N

Homologous_superfamily

3,313

false

This superfamily represents the N-terminal domain of scavenger mRNA decapping enzymes, such as Dcp2 and DcpS. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' mRNA degradation. DcpS uses cap dinucleotides or capped oligonucleotides as substrate to release m(7)GMP (N7-met...

[ "GO:0016787", "GO:0000290" ]

[ "hydrolase activity", "deadenylation-dependent decapping of nuclear-transcribed mRNA" ]

[ "molecular_function", "biological_process" ]

2

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.30.200.40", "SSF102860" ]

[ "", "" ]

[ 3254, 3308 ]

2

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

[ "3.6.1.59", "R-CEL-429958", "R-HSA-429958", "R-MMU-429958", "R-RNO-429958", "R-SCE-429958", "R-SPO-429958", "R-SSC-429958" ]

[ "EC:3.6.1.59", "REACTOME:R-CEL-429958", "REACTOME:R-HSA-429958", "REACTOME:R-MMU-429958", "REACTOME:R-RNO-429958", "REACTOME:R-SCE-429958", "REACTOME:R-SPO-429958", "REACTOME:R-SSC-429958" ]

8

[ "1st0", "1st4", "1vlr", "1xml", "1xmm", "3bl7", "3bl9", "3bla", "4qde", "4qdv", "4qeb", "5bv3", "5osy", "6gbs", "6trq" ]

15

[ "PUB00035577" ]

[ "16246173" ]

[ "Decapping the message: a beginning or an end." ]

[ 2006 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "seawater metagenome", "unclassified Klosneuvirinae" ]

[ 3, 3306, 1, 3 ]

4

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

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

9

true

Homologous_superfamily

Scavenger mRNA decapping enzyme, N-terminal

Scavenger_mRNA_decap_enz_N

9

IPR011146

11,146

HIT-like domain

HIT-like

Domain

71,413

false

The histidine triad motif (HIT) consists of the conserved sequence HXHXHXX (where X is a hydrophobic amino acid) at the enzymatic catalytic centre, in which the second histidine is strictly conserved and participates in catalysis with the third histidine [ , , ]. Proteins containing HIT domains form a superfamily of nu...

[ "GO:0003824" ]

[ "catalytic activity" ]

[ "molecular_function" ]

1

[ "PFAM", "PROFILE" ]

[ "PF01230", "PS51084" ]

[ "HIT", "HIT_2" ]

[ 62106, 69369 ]

2

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

[ "R-BTA-9013405", "R-CEL-9824594", "R-CEL-9825892", "R-CEL-9856649", "R-HSA-9013405", "R-HSA-9824594", "R-HSA-9825892", "R-HSA-9856649", "R-MMU-9013405", "R-MMU-9824594", "R-MMU-9825892", "R-MMU-9856649", "R-RNO-9824594", "R-RNO-9825892", "R-RNO-9856649" ]

[ "REACTOME:R-BTA-9013405", "REACTOME:R-CEL-9824594", "REACTOME:R-CEL-9825892", "REACTOME:R-CEL-9856649", "REACTOME:R-HSA-9013405", "REACTOME:R-HSA-9824594", "REACTOME:R-HSA-9825892", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9013405", "REACTOME:R-MMU-9824594", "REACTOME:R-MMU-9825892", "REACTOM...

15

[ "1av5", "1ems", "1fhi", "1fit", "1kpa", "1kpb", "1kpc", "1kpe", "1kpf", "1rzy", "1y23", "2eo4", "2f9i", "2fhi", "2fit", "2oik", "3ano", "3fit", "3i24", "3i4s", "3imi", "3ksv", "3l7x", "3lb5", "3n1s", "3n1t", "3nrd", "3o0m", "3o1c", "3o1x", "3o1z", "3ohe"...

164

[ "PUB00008005", "PUB00035586", "PUB00035587", "PUB00097343", "PUB00097344", "PUB00097345", "PUB00097346", "PUB00097347", "PUB00097349" ]

[ "12119013", "15904496", "15273322", "27005423", "23373416", "19112177", "32723815", "23659632", "30622225" ]

[ "Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases.", "HinT proteins and their putative interaction partners in Mollicutes and Chlamydiaceae.", "Functional analysis of mRNA scavenger decapping enzyme...

[ 2002, 2005, 2004, 2016, 2012, 2009, 2020, 2013, 2019 ]

9

[]

0

null

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

[ 1664, 48628, 19862, 63, 1196 ]

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",...

[ 29, 4, 17, 9, 1, 23, 14, 4, 26, 21, 3, 3, 22 ]

13

true

Domain

HIT-like domain

HIT-like

5

IPR011147

11,147

Bifunctional aspartokinase/homoserine dehydrogenase, homoserine dehydrogenase domain

Bifunc_Aspkin/hSer_DH

Domain

14,008

false

This entry represents the homoserine dehydrogenase domain from the bifunctional enzyme aspartokinase/homoserine dehydrogenase (AK-HSDH) found in bacteria and plant chloroplasts, which catalyses the first and third steps of the aspartate pathway. Homoserine dehydrogenase ( ) catalyses the conversion of L-homoserine to L...

[ "GO:0004412" ]

[ "homoserine dehydrogenase activity" ]

[ "molecular_function" ]

1

[ "PANTHER" ]

[ "PTHR43070" ]

[ "" ]

[ 14008 ]

1

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

[ "1.1.1.3", "2.7.2.4", "PWY-2941", "PWY-2942", "PWY-5097", "PWY-6160", "PWY-6559", "PWY-6562", "PWY-7153", "PWY-7977", "PWY-8088", "PWY-8179", "PWY-8296" ]

[ "EC:1.1.1.3", "EC:2.7.2.4", "METACYC:PWY-2941", "METACYC:PWY-2942", "METACYC:PWY-5097", "METACYC:PWY-6160", "METACYC:PWY-6559", "METACYC:PWY-6562", "METACYC:PWY-7153", "METACYC:PWY-7977", "METACYC:PWY-8088", "METACYC:PWY-8179", "METACYC:PWY-8296" ]

13

[ "1ebf", "1ebu", "1q7g", "1tve", "6mx1", "7m92" ]

6

[ "PUB00014809", "PUB00014810", "PUB00021481", "PUB00034672", "PUB00091752" ]

[ "12435751", "11888290", "10700284", "11352712", "16216875" ]

[ "Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine.", "Production and characterization of bifunctional enzymes. Substrate channeling in the aspartate pathway.", "Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductas...

[ 2003, 2002, 2000, 2001, 2005 ]

5

[]

0

null

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

[ 8, 9570, 4311, 119 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 21, 2, 1, 17, 1, 1, 31 ]

7

true

Domain

Bifunctional aspartokinase/homoserine dehydrogenase, homoserine dehydrogenase domain

Bifunc_Aspkin/hSer_DH

4

IPR011149

11,149

DNA polymerase II small subunit, archaeal

Pol2_small_arc

Family

798

false

Archaeal DNA polymerase II (Pol II, or Pol D) is heterodimeric, containing a DP1 small subunit, and a DP2 large subunit, the latter acting as the catalytic subunit. This entry represents the DP1 small subunit, which shows sequence similarity with the small subunit of eukaryotic DNA polymerase delta; a homologue of this...

[ "GO:0003676", "GO:0003887", "GO:0008408", "GO:0006260" ]

[ "nucleic acid binding", "DNA-directed DNA polymerase activity", "3'-5' exonuclease activity", "DNA replication" ]

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

4

[ "HAMAP", "PIRSF" ]

[ "MF_00325", "PIRSF000803" ]

[ "DNApol_II_A_arch", "Arc_Pol2_small" ]

[ 794, 732 ]

2

[ "EC", "EC" ]

[ "2.7.7.7", "3.1.11.1" ]

[ "EC:2.7.7.7", "EC:3.1.11.1" ]

2

[ "5ihe", "6hmf", "6hms", "6knb", "6knc", "6t8h", "8ppt", "8ppu", "8ppv", "9f29", "9f2a" ]

11

[ "PUB00014808" ]

[ "10430556" ]

[ "Archaeal DNA replication: identifying the pieces to solve a puzzle." ]

[ 1999 ]

1

[ "IPR024826" ]

[]

1

0

1

[ "Archaea", "ecological metagenomes" ]

[ 778, 20 ]

2

[]

0

true

Family

DNA polymerase II small subunit, archaeal

Pol2_small_arc

3

IPR011150

11,150

Cutinase, monofunctional

Cutinase_monf

Family

4,220

false

Aerial plant organs are protected by a cuticle composed of an insoluble polymeric structural compound, cutin, which is a polyester composed of hydroxy and hydroxyepoxy fatty acids. Plant pathogenic fungi produce extracellular degradative enzymes [ ] that play an important role in pathogenesis. They include cutinase, wh...

[ "GO:0050525", "GO:0005576" ]

[ "cutinase activity", "extracellular region" ]

[ "molecular_function", "cellular_component" ]

2

[ "PRINTS", "PANTHER" ]

[ "PR00129", "PTHR48250" ]

[ "CUTINASE", "" ]

[ 3305, 4150 ]

2

[ "EC", "PROSITEDOC" ]

[ "3.1.1.74", "PDOC00140" ]

[ "EC:3.1.1.74", "PROSITEDOC:PDOC00140" ]

2

[ "1agy", "1cex", "1cua", "1cub", "1cuc", "1cud", "1cue", "1cuf", "1cug", "1cuh", "1cui", "1cuj", "1cus", "1cuu", "1cuv", "1cuw", "1cux", "1cuy", "1cuz", "1ffa", "1ffb", "1ffc", "1ffd", "1ffe", "1oxm", "1xza", "1xzb", "1xzc", "1xzd", "1xze", "1xzf", "1xzg"...

61

[ "PUB00003749", "PUB00004118" ]

[ "1557023", "1560844" ]

[ "Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea.", "Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent." ]

[ 1992, 1992 ]

2

[ "IPR000675" ]

[]

1

0

1

[ "Actinomycetes", "Eukaryota" ]

[ 48, 4172 ]

2

[]

0

true

Family

Cutinase, monofunctional

Cutinase_monf

3

IPR011152

11,152

Phosphoesterase MJ0912

Pesterase_MJ0912

Family

9,450

false

This group of conserved proteins from bacteria and archaea contain one copy of the calcineurin-like phosphoesterase domain. Many members possess motifs characteristic of a variety of enzymatically active phosphoesterases [ ], including acid and alkaline phosphatases, phosphoprotein phosphatases, 5'-nucleotidase, bis(5'...

[]

0

[ "PIRSF" ]

[ "PIRSF000883" ]

[ "Pesterase_MJ0912" ]

[ 9450 ]

1

[]

0

[ "1nnw", "2gju", "3qfm", "3qfn", "3qfo", "3rqz" ]

6

[ "PUB00014394" ]

[ "8683579" ]

[ "Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures." ]

[ 1996 ]

1

[]

0

null

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

[ 589, 8738, 3, 4, 116 ]

5

[]

0

true

Family

Phosphoesterase MJ0912

Pesterase_MJ0912

5

IPR011159

11,159

Phosphoprotein phosphatase PPZ/Ppq1

PPPtase_PPZ/Ppq1

Family

1,444

false

This group represents the yeast phosphoprotein phosphatase, Ppz-type. Ppz proteins function in the regulation of K+ transport. Ppz proteins and the Hal3p inhibitory subunit of Ppz1 are important determinants of salt tolerance, cell wall integrity and cell cycle progression, each of which is dependent upon the Trk K+ tr...

[ "GO:0004722" ]

[ "protein serine/threonine phosphatase activity" ]

[ "molecular_function" ]

1

[ "PIRSF" ]

[ "PIRSF000909" ]

[ "PPPtase_PPZ" ]

[ 1444 ]

1

[ "EC" ]

[ "3.1.3.16" ]

[ "EC:3.1.3.16" ]

1

[ "5jpe", "5jpf" ]

2

[ "PUB00014802", "PUB00074962", "PUB00074963", "PUB00075005", "PUB00075006" ]

[ "11867520", "16166647", "22232558", "8269960", "24309106" ]

[ "The Ppz protein phosphatases are key regulators of K+ and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression.", "pH-Responsive, posttranslational regulation of the Trk1 potassium transporter by the type 1-related Ppz1 phosphatase.", "Conserved Ser/Arg-rich motif in ...

[ 2002, 2005, 2012, 1993, 2014 ]

5

[]

0

null

[ "Eukaryota" ]

[ 1444 ]

1

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

[ 1, 3, 1 ]

3

true

Family

Phosphoprotein phosphatase PPZ/Ppq1

PPPtase_PPZ/Ppq1

8

IPR011160

11,160

Sphingomyelin phosphodiesterase

Sphingomy_PDE

Family

3,376

false

Sphingomyelin phosphodiesterase, or sphingomyelinase (SMase), enzymes catalyse the hydrolysis of sphingomyelin into ceramide (N-acylsphingosine) and phosphorylcholine. There are six types of SMases: acid SMase, secretory SMase, neutral magnesium-dependent SMase, neutral magnesium-independent SMase, alkaline SMase, and ...

[ "GO:0004767", "GO:0006685" ]

[ "sphingomyelin phosphodiesterase activity", "sphingomyelin catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF" ]

[ "PIRSF000948" ]

[ "Sphingomy_PDE" ]

[ 3376 ]

1

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

[ "3.1.4.12", "PWY-7277", "R-BTA-9840310", "R-CEL-9840310", "R-DDI-9840310", "R-HSA-9840310", "R-MMU-9840310" ]

[ "EC:3.1.4.12", "METACYC:PWY-7277", "REACTOME:R-BTA-9840310", "REACTOME:R-CEL-9840310", "REACTOME:R-DDI-9840310", "REACTOME:R-HSA-9840310", "REACTOME:R-MMU-9840310" ]

7

[ "5fi9", "5fib", "5fic", "5hqn", "5i81", "5i85", "5i8r", "5jg8" ]

8

[ "PUB00014800", "PUB00014801" ]

[ "12401200", "12531545" ]

[ "Sphingomyelinases: enzymology and membrane activity.", "Sphingomyelin hydrolysis during apoptosis." ]

[ 2002, 2002 ]

2

[]

0

null

[ "Eukaryota" ]

[ 3376 ]

1

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

[ 4, 1, 9, 5, 4, 1, 2 ]

7

true

Family

Sphingomyelin phosphodiesterase

Sphingomy_PDE

1

IPR011161

11,161

MHC class I-like antigen recognition-like

MHC_I-like_Ag-recog

Domain

80,123

false

Class I MHC glycoproteins are expressed on the surface of all somatic nucleated cells, with the exception of neurons. MHC class I receptors present peptide antigens that are synthesised in the cytoplasm, which includes self-peptides (presented for self-tolerance) as well as foreign peptides (such as viral proteins). Th...

[]

0

[ "PFAM", "PFAM" ]

[ "PF00129", "PF16497" ]

[ "MHC_I", "MHC_I_3" ]

[ 77037, 3090 ]

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-140875", "R-BTA-202733", "R-HSA-1236974", "R-HSA-1236977", "R-HSA-140875", "R-HSA-163125", "R-HSA-164940", "R-HSA-198933", "R-HSA-202733", "R-HSA-2172127", "R-HSA-2424491", "R-HSA-5223345", "R-HSA-6798695", "R-HSA-877300", "R-HSA-8866654", "R-HSA-909733", "R-HSA-917977", "R-...

[ "REACTOME:R-BTA-140875", "REACTOME:R-BTA-202733", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-1236977", "REACTOME:R-HSA-140875", "REACTOME:R-HSA-163125", "REACTOME:R-HSA-164940", "REACTOME:R-HSA-198933", "REACTOME:R-HSA-202733", "REACTOME:R-HSA-2172127", "REACTOME:R-HSA-2424491", "REACTOME:R-HSA...

35

[ "1a1m", "1a1n", "1a1o", "1a6z", "1a9b", "1a9e", "1agb", "1agc", "1agd", "1age", "1agf", "1akj", "1ao7", "1b0g", "1b0r", "1b3j", "1bd2", "1bii", "1bqh", "1bz9", "1c16", "1cd1", "1ce6", "1cg9", "1ddh", "1de4", "1duy", "1duz", "1e27", "1e28", "1ed3", "1eey"...

1,750

[ "PUB00007109", "PUB00016272", "PUB00025007", "PUB00026524", "PUB00035588", "PUB00035589", "PUB00035590", "PUB00035591", "PUB00035592", "PUB00035593", "PUB00035594", "PUB00035595", "PUB00035596" ]

[ "9485452", "15526153", "7969498", "11825567", "15454423", "17291278", "12857997", "11677624", "16475792", "16500675", "12667138", "12594837", "17327234" ]

[ "Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding.", "Evolutionary and functional perspectives of the major histocompatibility complex class I antigen-processing machinery.", "Crystal structure of the complex of rat neonatal Fc receptor with Fc.", "...

[ 1998, 2004, 1994, 2002, 2004, 2007, 2003, 2001, 2006, 2006, 2003, 2003, 2007 ]

13

[]

[ "IPR001039" ]

0

1

0

[ "Bacteria", "Bilateria", "Viruses" ]

[ 8, 79971, 144 ]

3

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

[ 28, 29160, 506, 309 ]

4

true

Domain

MHC class I-like antigen recognition-like

MHC_I-like_Ag-recog

2

IPR011162

11,162

MHC classes I/II-like antigen recognition protein

MHC_I/II-like_Ag-recog

Homologous_superfamily

145,449

false

Major Histocompatibility Complex (MHC) glycoproteins are heterodimeric cell surface receptors that function to present antigen peptide fragments to T cells responsible for cell-mediated immune responses. MHC molecules can be subdivided into two groups on the basis of structure and function: class I molecules present in...

[]

0

[ "SSF" ]

[ "SSF54452" ]

[ "" ]

[ 145449 ]

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-140875", "R-BTA-202733", "R-HSA-1236974", "R-HSA-1236977", "R-HSA-140875", "R-HSA-163125", "R-HSA-164940", "R-HSA-198933", "R-HSA-202424", "R-HSA-202427", "R-HSA-202430", "R-HSA-202433", "R-HSA-202733", "R-HSA-2132295", "R-HSA-2172127", "R-HSA-2424491", "R-HSA-389948", "R-HS...

[ "REACTOME:R-BTA-140875", "REACTOME:R-BTA-202733", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-1236977", "REACTOME:R-HSA-140875", "REACTOME:R-HSA-163125", "REACTOME:R-HSA-164940", "REACTOME:R-HSA-198933", "REACTOME:R-HSA-202424", "REACTOME:R-HSA-202427", "REACTOME:R-HSA-202430", "REACTOME:R-HSA-2...

59

[ "1a1m", "1a1n", "1a1o", "1a6a", "1a6z", "1a9b", "1a9e", "1agb", "1agc", "1agd", "1age", "1agf", "1akj", "1ao7", "1aqd", "1b0g", "1b0r", "1b3j", "1bd2", "1bii", "1bqh", "1bx2", "1bz9", "1c16", "1cd1", "1ce6", "1cg9", "1d5m", "1d5x", "1d5z", "1d6e", "1d9k"...

2,032

[ "PUB00025007", "PUB00025626", "PUB00035588", "PUB00035589", "PUB00035590", "PUB00035591", "PUB00035592", "PUB00035593", "PUB00035594", "PUB00035595", "PUB00035596" ]

[ "7969498", "9768757", "15454423", "17291278", "12857997", "11677624", "16475792", "16500675", "12667138", "12594837", "17327234" ]

[ "Crystal structure of the complex of rat neonatal Fc receptor with Fc.", "The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation.", "Conformational flexibility of the MHC class I alpha1-alpha2 domain in peptide bound and free states: a m...

[ 1994, 1998, 2004, 2007, 2003, 2001, 2006, 2006, 2003, 2003, 2007 ]

11

[]

0

null

[ "Bacteria", "Eukaryota", "Viruses", "bird metagenome" ]

[ 26, 145089, 333, 1 ]

4

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

[ 76, 44694, 897, 448 ]

4

true

Homologous_superfamily

MHC classes I/II-like antigen recognition protein

MHC_I/II-like_Ag-recog

3

IPR011163

11,163

Peptidase S1A, enteropeptidase

Pept_S1A_enterop

Family

56

false

Enteropeptidase ( ) originally called enterokinase, belongs to MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)), subfamily S1A. It is the protease in mammalian intestinal brush border that is responsible for generation of active trypsin from trypsinogen; trypsin, in turn, activates other digestive enzymes. ...

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

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

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

3

[ "PIRSF" ]

[ "PIRSF001138" ]

[ "Enteropeptidase" ]

[ 56 ]

1

[ "EC" ]

[ "3.4.21.9" ]

[ "EC:3.4.21.9" ]

1

[]

0

[ "PUB00004849" ]

[ "8052624" ]

[ "Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains." ]

[ 1994 ]

1

[ "IPR001314" ]

[]

1

0

1

[ "Boreoeutheria" ]

[ 56 ]

1

[ "Homo sapiens", "Mus musculus" ]

[ 1, 2 ]

2

true

Family

Peptidase S1A, enteropeptidase

Pept_S1A_enterop

5

IPR011166

11,166

Beta-eliminating lyase family

Beta-eliminating_lyase

Family

3,696

false

Tryptophanase (tryptophan indole-lyase, TNase) ( ) and tyrosine phenol-lyase (TPL) ( ) are related pyridoxal-phosphate dependent homotetrameric enzymes that catalyse the reversible hydrolytic cleavage of L-tryptophan or L-tyrosine to indole or phenol, respectively, and ammonium pyruvate. These two enzymes are very simi...

[ "GO:0016830", "GO:0009072" ]

[ "carbon-carbon lyase activity", "aromatic amino acid metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM", "PIRSF" ]

[ "NF009709", "PIRSF001386" ]

[ "PRK13238.1", "Trpase" ]

[ 3694, 3092 ]

2

[ "EC", "PROSITEDOC" ]

[ "4.1.99.1", "PDOC00667" ]

[ "EC:4.1.99.1", "PROSITEDOC:PDOC00667" ]

2

[ "1ax4", "1c7g", "1tpl", "2c44", "2ez1", "2ez2", "2oqx", "2tpl", "2v0y", "2v1p", "2vlf", "2vlh", "2ycn", "2ycp", "2yct", "2yhk", "4up2", "4w1y", "4w4h", "5d8g", "5w19", "5w1b", "6dur", "6dvx", "6dxv", "6dyt", "6dz5", "6ecg", "6mls", "6mme", "6mo3", "6mpd"...

48

[ "PUB00014799" ]

[ "12686128" ]

[ "Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase." ]

[ 2003 ]

1

[]

[ "IPR013440", "IPR013441" ]

0

2

0

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

[ 183, 3184, 246, 83 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Beta-eliminating lyase family

Beta-eliminating_lyase

6

IPR011167

11,167

Iron-dependent fumarate hydratase

Fe_dep_fumarate_hydratase

Family

13,576

false

Iron-dependent fumarate hydratase, or fumarase, is a bacterial enzyme that converts malate to fumarate. There are three fumarase proteins in Escherichia coli, FumA, FumB, and FumC, which fall into two biochemically distinct classes: class I (FumA, FumB) are dimeric enzymes and class II (FumC) are tetrameric enzymes, th...

[ "GO:0004333", "GO:0006091" ]

[ "fumarate hydratase activity", "generation of precursor metabolites and energy" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF" ]

[ "PIRSF001394" ]

[ "Fe_dep_fumar_hy" ]

[ 13576 ]

1

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

[ "4.2.1.2", "PWY-5392", "PWY-561", "PWY-5690", "PWY-5913", "PWY-6728", "PWY-6969", "PWY-7254", "PWY-7384", "PWY-8086" ]

[ "EC:4.2.1.2", "METACYC:PWY-5392", "METACYC:PWY-561", "METACYC:PWY-5690", "METACYC:PWY-5913", "METACYC:PWY-6728", "METACYC:PWY-6969", "METACYC:PWY-7254", "METACYC:PWY-7384", "METACYC:PWY-8086" ]

10

[ "5l2r", "6msn", "6mso", "6unz", "6uo0", "6uoi", "6uoj", "6up9", "6upm", "6upo", "6uq8", "6uq9", "6uqb", "6uql", "6uqm", "6uqn" ]

16

[ "PUB00000586" ]

[ "3282546" ]

[ "Two biochemically distinct classes of fumarase in Escherichia coli." ]

[ 1988 ]

1

[]

0

null

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

[ 12966, 382, 1, 227 ]

4

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Iron-dependent fumarate hydratase

Fe_dep_fumarate_hydratase

2

IPR011170

11,170

Growth factor, vaccinia C11R type

GF_C11R

Family

95

false

Virus-encoded growth factors (GF) are important for the virulence of poxviruses. They act to promote the growth of their host cell through their binding to host ErbB receptor tyrosine kinases, which in turn activate the MAPK pathway. These growth factors are related to mammalian epidermal growth factor (EGF), one of se...

[ "GO:0005154" ]

[ "epidermal growth factor receptor binding" ]

[ "molecular_function" ]

1

[ "PIRSF" ]

[ "PIRSF001779" ]

[ "GF_C11R" ]

[ 95 ]

1

[]

0

[]

0

[ "PUB00014750" ]

[ "9774339" ]

[ "Pathogenic poxviruses reveal viral strategies to exploit the ErbB signaling network." ]

[ 1998 ]

1

[]

0

null

[ "Orthopoxvirus" ]

[ 95 ]

1

[]

0

true

Family

Growth factor, vaccinia C11R type

GF_C11R

5

IPR011171

11,171

Glia maturation factor

GMF

Family

3,736

false

This entry represents glia maturation factor beta and gamma (GMFB/GMFG), Aim7 from budding yeasts and Gmf1 from fission yeasts. GMF family proteins do not interact with actin, but instead bind to Arp2/3 complex. They sever actin-Arp2/3 complex branch junctions by a cofilin-like mechanism [ , , ]. Human GMFB was initial...

[ "GO:0071933", "GO:0071846" ]

[ "Arp2/3 complex binding", "actin filament debranching" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF", "PANTHER", "CDD" ]

[ "PIRSF001788", "PTHR11249", "cd11283" ]

[ "GMF-beta", "", "ADF_GMF-beta_like" ]

[ 2959, 3699, 2920 ]

3

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

[ "R-BTA-6798695", "R-DME-6798695", "R-HSA-6798695", "R-MMU-6798695", "R-RNO-6798695", "R-SCE-6798695", "R-SPO-6798695" ]

[ "REACTOME:R-BTA-6798695", "REACTOME:R-DME-6798695", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-6798695", "REACTOME:R-SCE-6798695", "REACTOME:R-SPO-6798695" ]

7

[ "1v6f", "1vkk", "1wfs", "3l50", "4jd2", "5ynr" ]

6

[ "PUB00014553", "PUB00071594", "PUB00071598", "PUB00071599", "PUB00101791" ]

[ "12697657", "20517925", "23727094", "23897816", "25308079" ]

[ "Glia maturation factor produced by thymic epithelial cells plays a role in T cell differentiation in the thymic microenvironment.", "GMF is an evolutionarily developed Adf/cofilin-super family protein involved in the Arp2/3 complex-mediated organization of the actin cytoskeleton.", "GMF severs actin-Arp2/3 com...

[ 2003, 2010, 2013, 2013, 2014 ]

5

[]

0

null

[ "Eukaryota" ]

[ 3736 ]

1

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

[ 1, 2, 1, 12, 10, 1, 15, 1, 1 ]

9

true

Family

Glia maturation factor

GMF

2

IPR011172

11,172

Poxvirus, TNF-alpha receptor-II

Poxvirus_TNF_rcpt-II

Family

137

false

Cytokines can be grouped into a family on the basis of sequence, functional and structural similarities [ , , ]. Tumor necrosis factor (TNF) (also known as TNF-alpha or cachectin) is a monocyte-derived cytotoxin that has been implicated in tumour regression, septic shock and cachexia [ , ]. The protein is synthesised a...

[ "GO:0005031", "GO:0033209", "GO:0052031" ]

[ "tumor necrosis factor receptor activity", "tumor necrosis factor-mediated signaling pathway", "symbiont-mediated perturbation of host defense response" ]

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

3

[ "PIRSF" ]

[ "PIRSF001790" ]

[ "TNF_C22L" ]

[ 137 ]

1

[]

0

[]

0

[ "PUB00002042", "PUB00004130", "PUB00006091", "PUB00006095", "PUB00006098", "PUB00006101", "PUB00014444", "PUB00014549", "PUB00014550", "PUB00014551", "PUB00015257" ]

[ "8095800", "1377364", "2989794", "3349526", "2777790", "2268312", "10211965", "11878931", "10989308", "14532286", "15335677" ]

[ "A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.", "Emerging cytokine family.", "Molecular cloning of mouse tumour necrosis factor cDNA and its eukaryotic expression.", "A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein:...

[ 1993, 1992, 1985, 1988, 1989, 1990, 1999, 2002, 2000, 2003, 1993 ]

11

[]

0

null

[ "Chordopoxvirinae" ]

[ 137 ]

1

[]

0

true

Family

Poxvirus, TNF-alpha receptor-II

Poxvirus_TNF_rcpt-II

9

IPR011174

11,174

Ezrin/radixin/moesin

ERM

Family

11,116

false

This entry represents ERM family of proteins. The ERM family consists of three closely-related proteins, ezrin, radixin and moesin [ ]. Ezrin was first identified as a constituent of microvilli [ ], radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions [ ], and moesin as a heparin...

[ "GO:0003779" ]

[ "actin binding" ]

[ "molecular_function" ]

1

[ "PIRSF", "PANTHER" ]

[ "PIRSF002305", "PTHR23281" ]

[ "ERM", "" ]

[ 8164, 11116 ]

2

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

[ "R-BTA-373752", "R-DME-2029482", "R-DME-373752", "R-DME-5627123", "R-HSA-2029482", "R-HSA-373752", "R-HSA-437239", "R-HSA-5627123", "R-HSA-8950505", "R-HSA-9662360", "R-HSA-9662361", "R-HSA-9725370", "R-MMU-2029482", "R-MMU-373752", "R-MMU-437239", "R-MMU-5627123", "R-RNO-2029482", ...

[ "REACTOME:R-BTA-373752", "REACTOME:R-DME-2029482", "REACTOME:R-DME-373752", "REACTOME:R-DME-5627123", "REACTOME:R-HSA-2029482", "REACTOME:R-HSA-373752", "REACTOME:R-HSA-437239", "REACTOME:R-HSA-5627123", "REACTOME:R-HSA-8950505", "REACTOME:R-HSA-9662360", "REACTOME:R-HSA-9662361", "REACTOME:R-...

20

[ "1e5w", "1ef1", "1gc6", "1gc7", "1h4r", "1isn", "1j19", "1ni2", "1sgh", "2d10", "2d11", "2d2q", "2ems", "2emt", "2i1j", "2i1k", "2yvc", "2zpy", "3u8z", "3wa0", "3x23", "4p7i", "4rm8", "4rm9", "4rma", "4yl8", "4zri", "4zrj", "4zrk", "6cds", "6txq", "6txs"...

42

[ "PUB00000467", "PUB00003053", "PUB00003059", "PUB00005477", "PUB00041575", "PUB00095065", "PUB00095066", "PUB00098656", "PUB00098657", "PUB00098658" ]

[ "3046603", "6885906", "2500445", "9048483", "17134719", "27405666", "21167305", "9298994", "9616160", "17061246" ]

[ "A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation.", "Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells.", "A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-c...

[ 1988, 1983, 1989, 1997, 2007, 2016, 2011, 1997, 1998, 2007 ]

10

[ "IPR000798" ]

[]

1

0

1

[ "Eukaryota" ]

[ 11116 ]

1

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

[ 6, 19, 8, 39, 28, 29 ]

6

true

Family

Ezrin/radixin/moesin

ERM

6

IPR011175

11,175

Alpha-s2 casein

Alpha-s2_casein

Family

151

false

Caseins are the major protein component of milk, functioning as nutritive carriers of both amino acids and minerals in milk. They are phosphoproteins that can be classified into two families, the kappa-casein family and the alpha-s1, alpha-s2 and beta-casein family, the later displaying considerable species variation [...

[ "GO:0005576" ]

[ "extracellular region" ]

[ "cellular_component" ]

1

[ "PIRSF", "PANTHER" ]

[ "PIRSF002371", "PTHR16656" ]

[ "Alpha-s2-casein", "" ]

[ 113, 151 ]

2

[]

0

[ "6fs5" ]

1

[ "PUB00014749" ]

[ "10584297" ]

[ "Comparative aspects of milk caseins." ]

[ 1999 ]

1

[ "IPR001588" ]

[]

1

0

1

[ "Eutheria" ]

[ 151 ]

1

[ "Mus musculus", "Rattus norvegicus" ]

[ 10, 11 ]

2

true

Family

Alpha-s2 casein

Alpha-s2_casein

1

IPR011177

11,177

Transcription initiation factor TFIID subunit 1, animal

TAF1_animal

Family

1,819

false

Transcription initiation factor TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. The complex includes TATA binding protein (TBP) and various TBP-associated factors (TAFS). TFIID is a RNA polymerase II-specific TATA-binding protein-asso...

[ "GO:0003677", "GO:0006352", "GO:0005669" ]

[ "DNA binding", "DNA-templated transcription initiation", "transcription factor TFIID complex" ]

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

3

[ "PIRSF" ]

[ "PIRSF003047" ]

[ "TAF1_animal" ]

[ 1819 ]

1

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

[ "2.7.11.1", "GenProp2054", "R-CEL-674695", "R-CEL-73776", "R-CEL-73779", "R-CEL-75953", "R-CEL-76042", "R-DME-674695", "R-DME-6804756", "R-DME-73776", "R-DME-73779", "R-DME-75953", "R-DME-76042", "R-HSA-167161", "R-HSA-167162", "R-HSA-167172", "R-HSA-674695", "R-HSA-6804756", "R-...

[ "EC:2.7.11.1", "GP:GenProp2054", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-73776", "REACTOME:R-CEL-73779", "REACTOME:R-CEL-75953", "REACTOME:R-CEL-76042", "REACTOME:R-DME-674695", "REACTOME:R-DME-6804756", "REACTOME:R-DME-73776", "REACTOME:R-DME-73779", "REACTOME:R-DME-75953", "REACTOME:R-DME...

28

[ "5fur", "6mzd", "6mzl", "7edx", "7eg7", "7eg8", "7eg9", "7ega", "7egb", "7egc", "7egd", "7ege", "7egh", "7egi", "7egj", "7ena", "7enc", "8gxq", "8gxs", "8wak", "8wal", "8wan", "8wao", "8wap", "8waq", "8war", "8was" ]

27

[ "PUB00014354", "PUB00014373", "PUB00014430" ]

[ "11963920", "845088", "7680771" ]

[ "A unified nomenclature for TATA box binding protein (TBP)-associated factors (TAFs) involved in RNA polymerase II transcription.", "Estrus, ovulation and conception following synchronization with progesterone, prostaglandin F2alpha and human chorionic gonadotropin in pony mares.", "Cloning and expression of hu...

[ 2002, 1977, 1993 ]

3

[ "IPR040240" ]

[]

1

0

1

[ "Bilateria" ]

[ 1819 ]

1

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

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

6

true

Family

Transcription initiation factor TFIID subunit 1, animal

TAF1_animal

8

IPR011178

11,178

Amyloidogenic glycoprotein, copper-binding

Amyloid_glyco_Cu-bd

Domain

6,650

false

Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [ , , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with D...

[ "GO:0046914" ]

[ "transition metal ion binding" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF12924" ]

[ "APP_Cu_bd" ]

[ 6650 ]

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-114608", "R-CEL-3000178", "R-CEL-381426", "R-CEL-416476", "R-CEL-8957275", "R-CEL-9609523", "R-DME-114608", "R-DME-3000178", "R-DME-381426", "R-DME-416476", "R-DME-8957275", "R-DME-9609523", "R-DME-9837999", "R-HSA-114608", "R-HSA-3000178", "R-HSA-381426", "R-HSA-416476", "R...

[ "REACTOME:R-CEL-114608", "REACTOME:R-CEL-3000178", "REACTOME:R-CEL-381426", "REACTOME:R-CEL-416476", "REACTOME:R-CEL-8957275", "REACTOME:R-CEL-9609523", "REACTOME:R-DME-114608", "REACTOME:R-DME-3000178", "REACTOME:R-DME-381426", "REACTOME:R-DME-416476", "REACTOME:R-DME-8957275", "REACTOME:R-DM...

67

[ "1owt", "2fjz", "2fk1", "2fk2", "2fk3", "2fkl", "2fma", "2m05", "3ktm", "4jfn", "4pwq", "7mqy", "7mrk", "7mrm", "7mrn", "7mrs", "8kew", "8kf1", "8kf3", "8kf4", "8kf5", "8kf6", "8otf" ]

23

[ "PUB00029624", "PUB00033916", "PUB00033917", "PUB00033918", "PUB00099232", "PUB00099233" ]

[ "12611883", "16301322", "16406235", "16364896", "28713158", "33302541" ]

[ "Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis.", "Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging.", "The amyloid precursor protein and postnatal neurogenesis/...

[ 2003, 2006, 2006, 2005, 2017, 2020 ]

6

[]

0

null

[ "Eumetazoa" ]

[ 6650 ]

1

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

[ 1, 16, 6, 20, 22, 16 ]

6

true

Domain

Amyloidogenic glycoprotein, copper-binding

Amyloid_glyco_Cu-bd

4

IPR011179

11,179

Isopentenyl-diphosphate delta-isomerase, FMN-dependent

IPdP_isomerase

Family

6,348

false

This entry represents the bacterial and archaeal isopentenyl-diphosphate delta-isomerase (IPP isomerase). IPP isomerase catalyses the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), and is a key enzyme in the biosynthesis of isoprenoids via the mevalonate pathway. The bacterial a...

[ "GO:0004452", "GO:0010181", "GO:0008299" ]

[ "isopentenyl-diphosphate delta-isomerase activity", "FMN binding", "isoprenoid biosynthetic process" ]

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

3

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

[ "MF_00354", "PIRSF003314", "PTHR43665", "TIGR02151", "cd02811" ]

[ "Idi_2", "IPP_isomerase", "", "IPP_isom_2", "IDI-2_FMN" ]

[ 6047, 5961, 6348, 6064, 5825 ]

5

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

[ "5.3.3.2", "GenProp0758", "PWY-6174", "PWY-6383", "PWY-6859", "PWY-7102", "PWY-7391", "PWY-7524", "PWY-7560", "PWY-8125", "PWY-922" ]

[ "EC:5.3.3.2", "GP:GenProp0758", "METACYC:PWY-6174", "METACYC:PWY-6383", "METACYC:PWY-6859", "METACYC:PWY-7102", "METACYC:PWY-7391", "METACYC:PWY-7524", "METACYC:PWY-7560", "METACYC:PWY-8125", "METACYC:PWY-922" ]

11

[ "1p0k", "1p0n", "1vcf", "1vcg", "2zru", "2zrv", "2zrw", "2zrx", "2zry", "2zrz", "3b03", "3b04", "3b05", "3b06", "3dh7", "3sr7", "3vkj", "4n02" ]

18

[ "PUB00014546", "PUB00014547" ]

[ "15009187", "12798687" ]

[ "Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.", "Crystal structure of the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Bacillus subtilis." ]

[ 2004, 2003 ]

2

[]

0

null

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

[ 612, 5596, 80, 60 ]

4

[]

0

true

Family

Isopentenyl-diphosphate delta-isomerase, FMN-dependent

IPdP_isomerase

9

IPR011181

11,181

Protein VP3, rotavirus

VP3_Rotav

Family

3,776

false

Viral protein 3 (VP3) specifically binds to GTP and contains mRNA guanylyltransferase and mRNA (guanine-N(7)-)-methyltransferase activities. It is a multifunctional enzyme involved in mRNA capping. It catalyses the formation of the 5' cap structure on the viral plus-strand transcripts [ , ]. Structure analyses revealed...

[ "GO:0004482", "GO:0005525", "GO:0016032", "GO:0019013" ]

[ "mRNA 5'-cap (guanine-N7-)-methyltransferase activity", "GTP binding", "viral process", "viral nucleocapsid" ]

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

4

[ "HAMAP", "HAMAP", "PFAM", "PIRSF", "PROFILE", "CDD" ]

[ "MF_04124", "MF_04128", "PF06929", "PIRSF004015", "PS51589", "cd20757" ]

[ "Rota_VP3", "Rota_VP3_A", "Rotavirus_VP3", "LigT_rotavirus", "SAM_MT56_VP3", "capping_2-OMTase_Rotavirus" ]

[ 3163, 2714, 3776, 3140, 3174, 3181 ]

6

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

[ "2.1.1.56", "2.7.7.50", "3.1.4.-", "PWY-5978", "PWY-6129", "PWY-6689", "PWY-7119", "PWY-7366", "PWY-7375", "R-HSA-8983711" ]

[ "EC:2.1.1.56", "EC:2.7.7.50", "EC:3.1.4.-", "METACYC:PWY-5978", "METACYC:PWY-6129", "METACYC:PWY-6689", "METACYC:PWY-7119", "METACYC:PWY-7366", "METACYC:PWY-7375", "REACTOME:R-HSA-8983711" ]

10

[ "6o3v", "6o6b" ]

2

[ "PUB00012924", "PUB00095808", "PUB00095809" ]

[ "10603323", "24899176", "25724417" ]

[ "Rotavirus open cores catalyze 5'-capping and methylation of exogenous RNA: evidence that VP3 is a methyltransferase.", "Predicted structure and domain organization of rotavirus capping enzyme and innate immune antagonist VP3.", "Silencing the alarms: Innate immune antagonism by rotavirus NSP1 and VP3." ]

[ 1999, 2014, 2015 ]

3

[]

0

null

[ "Rotavirus" ]

[ 3776 ]

1

[]

0

true

Family

Protein VP3, rotavirus

VP3_Rotav

3

IPR011182

11,182

L-aspartate dehydrogenase

L-Asp_DH

Family

3,261

false

This group contains aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P) + cofactor) and a C-terminal α/β domain [ ]. This suggested that TM1643 may be a dehyd...

[ "GO:0033735", "GO:0009435" ]

[ "aspartate dehydrogenase [NAD(P)+] activity", "NAD+ biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF" ]

[ "PIRSF005227" ]

[ "Asp_dh_NAD_syn" ]

[ 3261 ]

1

[ "EC" ]

[ "1.4.1.21" ]

[ "EC:1.4.1.21" ]

1

[ "1h2h", "1j5p", "2dc1" ]

3

[ "PUB00014412" ]

[ "12496312" ]

[ "Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643." ]

[ 2003 ]

1

[]

[ "IPR020626" ]

0

1

0

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

[ 346, 2456, 422, 37 ]

4

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

[ 1, 2, 1, 2, 1 ]

5

true

Family

L-aspartate dehydrogenase

L-Asp_DH

8

IPR011184

11,184

DNA mismatch repair Msh2-type

DNA_mismatch_repair_Msh2

Family

8,602

false

Mismatch repair (MMR) is one of five major DNA repair pathways, the others being homologous recombination repair, non-homologous end joining, nucleotide excision repair, and base excision repair. The mismatch repair system recognises and repairs mispaired or unpaired nucleotides that result from errors in DNA replicati...

[ "GO:0005524", "GO:0030983", "GO:0006298" ]

[ "ATP binding", "mismatched DNA binding", "mismatch repair" ]

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

3

[ "PIRSF" ]

[ "PIRSF005813" ]

[ "MSH2" ]

[ 8602 ]

1

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

[ "R-BTA-5358565", "R-BTA-5358606", "R-DDI-5358565", "R-DDI-5358606", "R-DME-5358565", "R-HSA-5358565", "R-HSA-5358606", "R-HSA-5632927", "R-HSA-5632928", "R-HSA-5632968", "R-HSA-6796648", "R-HSA-912446", "R-MMU-5358565", "R-MMU-5358606", "R-RNO-5358565", "R-SCE-5358565", "R-SCE-535860...

[ "REACTOME:R-BTA-5358565", "REACTOME:R-BTA-5358606", "REACTOME:R-DDI-5358565", "REACTOME:R-DDI-5358606", "REACTOME:R-DME-5358565", "REACTOME:R-HSA-5358565", "REACTOME:R-HSA-5358606", "REACTOME:R-HSA-5632927", "REACTOME:R-HSA-5632928", "REACTOME:R-HSA-5632968", "REACTOME:R-HSA-6796648", "REACTOM...

19

[ "2o8b", "2o8c", "2o8d", "2o8e", "2o8f", "3thw", "3thx", "3thy", "3thz", "8ag6", "8olx", "8om5", "8om9", "8oma", "8omo", "8omq", "8r7c", "8r7e", "8r7v", "8rau", "8rav", "8raw", "8rax", "8raz", "8rb0", "8rb1", "8rb2", "8rz7", "8rz8", "8rz9" ]

30

[ "PUB00004486", "PUB00014545" ]

[ "9722651", "12222686" ]

[ "A phylogenomic study of the MutS family of proteins.", "DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1 heterodimers." ]

[ 1998, 2002 ]

2

[ "IPR045076" ]

[]

1

0

1

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

[ 91, 8491, 5, 2, 13 ]

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...

[ 15, 2, 7, 4, 33, 9, 1, 3, 7, 3, 1, 19 ]

12

true

Family

DNA mismatch repair Msh2-type

DNA_mismatch_repair_Msh2

4

IPR011188

11,188

Peptidoglycan synthesis regulatory protein ReoY-like

ReoY-like

Family

1,618

false

This family includes Peptidoglycan synthesis regulatory protein ReoY ( ) which is involved in the PASTA kinase-mediated signalling pathway regulating peptidoglycan synthesis to maintain cell wall integrity [ ]. It modulates peptidoglycan (PG) synthesis pathway committed-step enzyme MurA [ ]. ReoY positively modulates C...

[]

0

[ "HAMAP", "PIRSF" ]

[ "MF_00760", "PIRSF007165" ]

[ "UPF0302", "UCP007165" ]

[ 1112, 1614 ]

2

[]

0

[ "3do9" ]

1

[ "PUB00104135", "PUB00163192" ]

[ "32469310", "37688380" ]

[ "PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM.", "PASTA-kinase-mediated signaling drives accumulation of the peptidoglycan synthesis protein MurAA to promote cephalosporin resistance in Enterococcus faecalis." ]

[ 2020, 2023 ]

2

[]

0

null

[ "Bacillota", "Bacillus phage G", "metagenomes" ]

[ 1614, 2, 2 ]

3

[]

0

true

Family

Peptidoglycan synthesis regulatory protein ReoY-like

ReoY-like

2

IPR011189

11,189

Uncharacterised conserved protein, caspase-like

UCP_caspase_lke

Family

400

false

This group represents a family of cyanobacterial proteins, which have no known function. The N-terminal region, of members of this family, has homology to the caspase-hemoglobinase domain [ ].

[]

0

[ "PIRSF" ]

[ "PIRSF007398" ]

[ "Sll0148_caspase" ]

[ 400 ]

1

[]

0

[]

0

[ "PUB00015612" ]

[ "11835511" ]

[ "Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins." ]

[ 2002 ]

1

[]

0

null

[ "Cyanobacteriota" ]

[ 400 ]

1

[]

0

true

Family

Uncharacterised conserved protein, caspase-like

UCP_caspase_lke

4

IPR011191

11,191

Uncharacterised protein family Treponema vWA

Uncharacterised_Tp_vWA

Family

27

false

Members of this group are related to the 76kDa protein of unknown function from Treponema. The proteins contain a vWA domain.

[]

0

[ "PIRSF" ]

[ "PIRSF008381" ]

[ "TP0020_vWA" ]

[ 27 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Spirochaetales" ]

[ 27 ]

1

[]

0

true

Family

Uncharacterised protein family Treponema vWA

Uncharacterised_Tp_vWA

5

IPR011192

11,192

Rubisco LSMT methyltransferase, plant

Rubisco_LSMT_MeTrfase_plant

Family

830

false

In pea (Pisum sativum), the protein-lysine methyltransferase (PsLSMT, also known as RBCMT) catalyses the trimethylation of Lys-14 in the large subunit (LS) of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) [ ]. Arabidopsis homologue of RBCMT, LSMT, is a protein-lysine methyltransferase methylating chloroplas...

[ "GO:0030785", "GO:0009507" ]

[ "[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity", "chloroplast" ]

[ "molecular_function", "cellular_component" ]

2

[ "PIRSF", "PROFILE" ]

[ "PIRSF009328", "PS51583" ]

[ "RMT_SET", "SAM_MT127" ]

[ 799, 459 ]

2

[]

0

[ "1mlv", "1ozv", "1p0y", "2h21", "2h23", "2h2e", "2h2j" ]

7

[ "PUB00014357", "PUB00096033" ]

[ "1525466", "22547063" ]

[ "RUBISCO: structure and mechanism.", "Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants." ]

[ 1992, 2012 ]

2

[]

0

null

[ "Tracheophyta" ]

[ 830 ]

1

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

[ 8, 4, 5 ]

3

true

Family

Rubisco LSMT methyltransferase, plant

Rubisco_LSMT_MeTrfase_plant

2

IPR011193

11,193

Ornithine/lysine/arginine decarboxylase

Orn/lys/arg_de-COase

Family

11,279

false

This family is composed of ornithine decarboxylases (ODC), arginine decarboxylases (ADC) and lysine decarboxylases (LDC), and belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase domain superfamily (fold I) [ ]. These enzymes catalyse the decarboxylation of ornithine, arginine, or lysine, respe...

[ "GO:0016831", "GO:0006520", "GO:0005737" ]

[ "carboxy-lyase activity", "amino acid metabolic process", "cytoplasm" ]

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

3

[ "PIRSF", "PANTHER" ]

[ "PIRSF009393", "PTHR45229" ]

[ "Orn_decarb", "" ]

[ 9966, 11278 ]

2

[ "EC" ]

[ "4.1.1" ]

[ "EC:4.1.1" ]

1

[ "1c4k", "1ord", "2vyc", "3n75", "3q16", "4upb", "4upf", "5fkx", "5fkz", "5fl2", "5xx1", "6q6i", "6q7l", "6q7m", "6y3x", "6yn5", "6yn6", "7p9b", "7pk6", "9e0m", "9e0o", "9e0q" ]

22

[ "PUB00001452", "PUB00006301", "PUB00006322", "PUB00014378", "PUB00014382", "PUB00014393", "PUB00014437" ]

[ "8181483", "8112347", "7748903", "7663340", "9405048", "9063963", "7961515" ]

[ "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.", "Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families.", "Pyridoxal phosphate-dependent enzymes.", "Structural motifs for pyridoxal-5'-phosphate bi...

[ 1994, 1994, 1995, 1995, 1997, 1996, 1994 ]

7

[]

[ "IPR027568", "IPR027605" ]

0

2

0

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

[ 11089, 108, 32, 50 ]

4

[ "Escherichia coli (strain K12)" ]

[ 5 ]

1

true

Family

Ornithine/lysine/arginine decarboxylase

Orn/lys/arg_de-COase

5

IPR011194

11,194

Uncharacterised protein family UPF0306

UPF0306

Family

1,634

false

There are currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this group are restricted to the Proteobacteria.

[]

0

[ "HAMAP", "PIRSF" ]

[ "MF_00764", "PIRSF009554" ]

[ "UPF0306", "UCP009554" ]

[ 1307, 1631 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 1630, 4 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family UPF0306

UPF0306

6

IPR011197

11,197

Uncharacterised conserved protein UCP012318

UCP012318

Family

4,504

false

This is a family of uncharacterised proteins from Proteobacteria and plants.

[]

0

[ "PIRSF" ]

[ "PIRSF012318" ]

[ "UCP012318" ]

[ 4504 ]

1

[]

0

[]

0

[]

0

[ "IPR007402" ]

[]

1

0

1

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

[ 3930, 506, 68 ]

3

[ "Arabidopsis thaliana", "Danio rerio" ]

[ 4, 2 ]

2

true

Family

Uncharacterised conserved protein UCP012318

UCP012318

4

IPR011199

11,199

Bacillithiol biosynthesis BshC

Bacillithiol_biosynth_BshC

Family

4,031

false

Members of this protein family include BshC, which is an enzyme required for bacillithiol biosynthesis and described as a cysteine-adding enzyme [ ]. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes.

[]

0

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

[ "MF_01867", "PIRSF012535", "TIGR03998" ]

[ "BshC", "UCP012535", "thiol_BshC" ]

[ 3963, 3643, 4023 ]

3

[ "GP", "GP" ]

[ "GenProp0927", "GenProp1505" ]

[ "GP:GenProp0927", "GP:GenProp1505" ]

2

[ "4wbd" ]

1

[ "PUB00055031" ]

[ "20308541" ]

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

[ 2010 ]

1

[]

0

null

[ "Bacteria", "Protostomia", "ecological metagenomes" ]

[ 4012, 2, 17 ]

3

[]

0

true

Family

Bacillithiol biosynthesis BshC

Bacillithiol_biosynth_BshC

7

IPR011200

11,200

Uncharacterised conserved protein UCP012608

UCP012608

Family

3,955

false

Family of uncharacterised bacterial proteins.

[]

0

[ "PFAM", "PIRSF" ]

[ "PF10094", "PIRSF012608" ]

[ "DUF2332", "UCP012608" ]

[ 3955, 1733 ]

2

[]

0

[]

0

[]

0

[]

0

null

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

[ 3826, 10, 57, 62 ]

4

[]

0

true

Family

Uncharacterised conserved protein UCP012608

UCP012608

6

IPR011201

11,201

Zinc-ribbon domain, bacteria

Zinc-ribbon_6_bact

Domain

3,657

false

This family appears to be a true zinc-ribbon, with two sets of putative zinc-binding domains in tandem.

[]

0

[ "PFAM" ]

[ "PF10005" ]

[ "Zn_ribbon_DZR_6" ]

[ 3657 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Tanacetum cinerariifolium", "metagenomes" ]

[ 3632, 1, 24 ]

3

[]

0

true

Domain

Zinc-ribbon domain, bacteria

Zinc-ribbon_6_bact

5

IPR011204

11,204

Virulence protein RhuM-like

Virulence_RhuM-like

Family

7,065

false

There are currently no experimental data for members of this group or their homologues. However, these proteins are implicated in virulence/pathogenicity because RhuM is encoded in the SPI-3 pathogenicity island in Salmonella typhimurium [ , ].

[]

0

[ "PFAM", "PIRSF" ]

[ "PF13310", "PIRSF015268" ]

[ "Virulence_RhuM", "Virulence_RhuM" ]

[ 7065, 3856 ]

2

[]

0

[]

0

[ "PUB00014372", "PUB00014435" ]

[ "9922266", "12775700" ]

[ "The SPI-3 pathogenicity island of Salmonella enterica.", "Variation between pathogenic serovars within Salmonella pathogenicity islands." ]

[ 1999, 2003 ]

2

[]

0

null

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

[ 6749, 10, 107, 13, 186 ]

5

[]

0

true

Family

Virulence protein RhuM-like

Virulence_RhuM-like

2

IPR011205

11,205

Uncharacterised conserved protein UCP015417, vWA

UCP015417_vWA

Family

4,627

false

This is a family of uncharacterised proteins, the majority of which contain a C-terminal vWA domain.

[]

0

[ "PIRSF", "PANTHER" ]

[ "PIRSF015417", "PTHR31373" ]

[ "T31B5_30_vWA", "" ]

[ 3240, 4627 ]

2

[]

0

[]

0

[]

0

[]

0

null

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

[ 197, 3999, 2, 333, 96 ]

5

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

[ 21, 14, 13 ]

3

true

Family

Uncharacterised conserved protein UCP015417, vWA

UCP015417_vWA

9

IPR011206

11,206

Citrate lyase beta subunit-like

Citrate_lyase_beta/mcl1/mcl2

Family

28,714

false

This entry represents a group of proteins belonging to the HpcH/HpaI aldolase family. Proteins in this entry include citrate lyase subunit beta, malyl-CoA lyase and (3S)-malyl-CoA thioesterase. This entry also includes beta-methylmalyl-CoA lyase (rrnAC0690) from Haloarcula marismortui. Citrate lyase catalyses the magne...

[]

0

[ "PIRSF" ]

[ "PIRSF015582" ]

[ "Cit_lyase_B" ]

[ 28714 ]

1

[ "EC" ]

[ "4.1.3" ]

[ "EC:4.1.3" ]

1

[ "1sgj", "1u5h", "1u5v", "1z6k", "3qll", "3qqw", "4l7z", "4l80", "4l9y", "4l9z", "5ugr", "5vxc", "5vxo", "5vxs", "6aq4", "6arb", "6as5", "6chu", "6cj3", "6cj4", "6kin", "6kkh", "8khl", "8wco", "9nzb" ]

25

[ "PUB00014726", "PUB00014742", "PUB00070126", "PUB00070127", "PUB00070128" ]

[ "11741334", "10924139", "21252347", "15687206", "20047909" ]

[ "Molecular cloning of novel mouse and human putative citrate lyase beta-subunit.", "Biosynthesis of the prosthetic group of citrate lyase.", "A methylaspartate cycle in haloarchaea.", "L-malyl-coenzyme A/beta-methylmalyl-coenzyme A lyase is involved in acetate assimilation of the isocitrate lyase-negative bac...

[ 2001, 2000, 2011, 2005, 2010 ]

5

[]

[ "IPR006475", "IPR039480", "IPR040186" ]

0

3

0

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

[ 626, 24985, 2777, 326 ]

4

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

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

7

true

Family

Citrate lyase beta subunit-like

Citrate_lyase_beta/mcl1/mcl2

2

IPR011207

11,207

Orthopoxvirus protein F1

Orthopox_F1

Family

137

false

The poxvirus F1 family members are related to Vaccinia virus protein F1L, also known as Apoptosis regulator OPG045, which plays a role in evading host innate immune response by inhibiting host inflammasome activation [ ]. F1interacts with and inhibits NLR-mediated interleukin-1 beta/IL1B production in infected cells. F...

[ "GO:0033668" ]

[ "symbiont-mediated suppression of host apoptosis" ]

[ "biological_process" ]

1

[ "PIRSF" ]

[ "PIRSF015971" ]

[ "VAC_F1L" ]

[ 137 ]

1

[]

0

[]

0

[ "PUB00088293", "PUB00088294" ]

[ "23603272", "16439990" ]

[ "Vaccinia virus F1L protein promotes virulence by inhibiting inflammasome activation.", "Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis." ]

[ 2013, 2006 ]

2

[ "IPR021119" ]

[]

1

0

1

[ "Orthopoxvirus" ]

[ 137 ]

1

[]

0

true

Family

Orthopoxvirus protein F1

Orthopox_F1

3

IPR011213

11,213

Nicotinic acid mononucleotide biosynthesis protein

NMN_biosyn

Family

1,937

false

This group contains uncharacterised proteins that are implicated in nicotinic acid mononucleotide (NMN) biosynthesis based on the genomic context of the corresponding genes (operon structure, gene neighbourhood) [ ]. The Rhizobium loti (Mesorhizobium loti) member (Msi362, ORF1) is encoded by the symbiosis island that c...

[]

0

[ "PIRSF" ]

[ "PIRSF019423" ]

[ "NMN_biosyn" ]

[ 1937 ]

1

[]

0

[ "7q91", "7q92", "7q93", "7q94" ]

4

[ "PUB00014358", "PUB00014453" ]

[ "12003951", "11320134" ]

[ "Comparative sequence analysis of the symbiosis island of Mesorhizobium loti strain R7A.", "The bio operon on the acquired symbiosis island of Mesorhizobium sp. strain R7A includes a novel gene involved in pimeloyl-CoA synthesis." ]

[ 2002, 2001 ]

2

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 1922, 15 ]

2

[]

0

true

Family

Nicotinic acid mononucleotide biosynthesis protein

NMN_biosyn

3

IPR011214

11,214

Uncharacterised conserved protein UCP020967

UCP020967

Family

1,822

false

Family of uncharacterised bacterial proteins.

[]

0

[ "PIRSF" ]

[ "PIRSF020967" ]

[ "UCP020967" ]

[ 1822 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Acinetobacter phage vB_AbaM_ME3", "Bacteria", "ecological metagenomes" ]

[ 1, 1818, 3 ]

3

[]

0

true

Family

Uncharacterised conserved protein UCP020967

UCP020967

8

IPR011215

11,215

Cysteine protease StiP, N-terminal domain

StiP_N

Domain

3,027

false

This entry represents the N-terminal domain of Cysteine protease StiP from Acinetobacter baylyi, which may play a role in regulating cell morphology in response to stressful conditions which likely cause oxidative damage. StiP has been shown to posses cysteine protease activity [ ]. This domain is also found centrally ...

[]

0

[ "PFAM" ]

[ "PF11202" ]

[ "StiP" ]

[ 3027 ]

1

[]

0

[]

0

[ "PUB00066658", "PUB00069487" ]

[ "23044854", "24206355" ]

[ "Ter-dependent stress response systems: novel pathways related to metal sensing, production of a nucleoside-like metabolite, and DNA-processing.", "Acinetobacter baylyi long-term stationary-phase protein StiP is a protease required for normal cell morphology and resistance to tellurite." ]

[ 2012, 2013 ]

2

[]

0

null

[ "Acinetobacter phage vB_AbaM_ME3", "Bacteria", "Rhabditida", "metagenomes" ]

[ 1, 3018, 2, 6 ]

4

[]

0

true

Domain

Cysteine protease StiP, N-terminal domain

StiP_N

6

IPR011217

11,217

Virginiamycin B lyase Vgb

Vgb_bact

Family

1,314

false

Streptogramins consist of a mixture of two components: cyclic polyunsaturated macrolactones (group A) and cyclic hexadepsipeptides (group B). The latter are cyclized through an ester bond between the hydroxyl group of an N-terminal threonine and the C-terminal carboxyl [ ]. Inactivation of the B streptogramins (e.g., v...

[ "GO:0000287", "GO:0016835", "GO:0017001", "GO:0046677" ]

[ "magnesium ion binding", "carbon-oxygen lyase activity", "antibiotic catabolic process", "response to antibiotic" ]

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

4

[ "HAMAP", "PIRSF" ]

[ "MF_01282", "PIRSF026412" ]

[ "VirginiamycinB_lyase", "Streptogrm_lyase" ]

[ 894, 1232 ]

2

[ "EC", "METACYC" ]

[ "4.2.99.-", "PWY-5397" ]

[ "EC:4.2.99.-", "METACYC:PWY-5397" ]

2

[ "2qc5", "2z2n", "2z2o", "2z2p" ]

4

[ "PUB00014395", "PUB00014436" ]

[ "11467949", "3149758" ]

[ "Vgb from Staphylococcus aureus inactivates streptogramin B antibiotics by an elimination mechanism not hydrolysis.", "Nucleotide sequence of a staphylococcal plasmid gene, vgb, encoding a hydrolase inactivating the B components of virginiamycin-like antibiotics." ]

[ 2001, 1988 ]

2

[]

0

null

[ "Bacteria", "mine drainage metagenome" ]

[ 1313, 1 ]

2

[]

0

true

Family

Virginiamycin B lyase Vgb

Vgb_bact

5

IPR011218

11,218

Insecticidal delta endotoxin

Insecticidal_delta_endotoxin

Family

28

false

This group represents an insecticidal delta endotoxin from bacteria. The spore-forming bacterium Bacillus thuringiensis produces several plasmid-encoded delta-endotoxins in large quantities during sporulation, which are packaged into intracellular inclusions as protoxins. The subsequent ingestion of the inclusions by i...

[]

0

[ "PIRSF" ]

[ "PIRSF026584" ]

[ "Delta_tox" ]

[ 28 ]

1

[]

0

[ "4rhz" ]

1

[ "PUB00014563" ]

[ "11964120" ]

[ "Sporulation and delta-endotoxin synthesis by Bacillus thuringiensis." ]

[ 2002 ]

1

[ "IPR004991" ]

[]

1

0

1

[ "Bacillaceae" ]

[ 28 ]

1

[]

0

true

Family

Insecticidal delta endotoxin

Insecticidal_delta_endotoxin

2

IPR011219

11,219

Rubisco-cytochrome methylase MET

Rubisco-cyt_methylase_MET

Family

3

false

This group represents a predicted rubisco-cytochrome methylase, MET type. Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme in photosynthetic carbon assimilation. The enzyme is composed of large (rbcL) and small (rbcS) subunits, and has been found in algae, cryptophytes and land plants. This e...

[]

0

[ "PIRSF" ]

[ "PIRSF026986" ]

[ "MET_SET" ]

[ 3 ]

1

[]

0

[]

0

[ "PUB00014426", "PUB00014562" ]

[ "11323671", "10742049" ]

[ "The highly reduced genome of an enslaved algal nucleus.", "A nucleomorph-encoded CbbX and the phylogeny of RuBisCo regulators." ]

[ 2001, 2000 ]

2

[]

0

null

[ "Eukaryota" ]

[ 3 ]

1

[ "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 2 ]

1

true

Family

Rubisco-cytochrome methylase MET

Rubisco-cyt_methylase_MET

7

IPR011220

11,220

Uncharacterised conserved protein UCP028205

UCP028205

Family

837

false

This is a family of uncharacterised bacterial proteins, restricted to the Proteobacteria.

[]

0

[ "PIRSF" ]

[ "PIRSF028205" ]

[ "UCP028205" ]

[ 837 ]

1

[]

0

[ "3buu" ]

1

[]

0

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 828, 9 ]

2

[]

0

true

Family

Uncharacterised conserved protein UCP028205

UCP028205

6

IPR011222

11,222

Double-stranded DNA virus, group I, capsid

dsDNA_vir_gr_I_capsid

Homologous_superfamily

12,300

false

This entry represents viral capsid proteins from group I dsDNA viruses, including Papovaviridae-like Polyomaviruses and Papillomaviruses. Virus-encoded capsid proteins play a major role in the life cycles of all viruses. Structures have been determined for the major capsid protein VP1 (viral protein 1) from Murine poly...

[ "GO:0005198", "GO:0019028" ]

[ "structural molecule activity", "viral capsid" ]

[ "molecular_function", "cellular_component" ]

2

[ "SSF" ]

[ "SSF88648" ]

[ "" ]

[ 12300 ]

1

[]

0

[ "1cn3", "1dzl", "1sid", "1sie", "1sva", "1vpn", "1vps", "2r5h", "2r5i", "2r5j", "2r5k", "3bwq", "3bwr", "3iyj", "3iys", "3j6r", "3j7g", "3j8v", "3j8w", "3j8z", "3jba", "3nxd", "3nxg", "3s7v", "3s7x", "4fmg", "4fmh", "4fmi", "4fmj", "4jcd", "4jce", "4jcf"...

145

[ "PUB00003160", "PUB00006154", "PUB00024376", "PUB00035302", "PUB00035621", "PUB00035622" ]

[ "7561785", "9628860", "10882140", "12620808", "12928495", "17446671" ]

[ "Organization of the major and minor capsid proteins in human papillomavirus type 33 virus-like particles.", "Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry.", "Structure of small virus-like particles assembled from the...

[ 1995, 1998, 2000, 2003, 2003, 2006 ]

6

[]

0

null

[ "Eukaryota", "Papovaviricetes" ]

[ 5, 12295 ]

2

[ "Homo sapiens" ]

[ 3 ]

1

true

Homologous_superfamily

Double-stranded DNA virus, group I, capsid

dsDNA_vir_gr_I_capsid

2

IPR011223

11,223

Uncharacterised conserved protein UCP028770

UCP028770

Family

1,696

false

This is a family of uncharacterised bacterial proteins, restricted to the Gammaproteobacteria.

[]

0

[ "PFAM", "PIRSF" ]

[ "PF11742", "PIRSF028770" ]

[ "DUF3302", "UCP028770" ]

[ 1696, 1271 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "unclassified sequences" ]

[ 1684, 12 ]

2

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Uncharacterised conserved protein UCP028770

UCP028770

1

IPR011224

11,224

Ribosomal RNA large subunit methyltransferase M

rRNA_MeTrfase_M

Family

4,121

false

This entry represents the ribosomal RNA large subunit methyltransferase M (RlmM), previously known as YdgE. RlmM specifically catalyses the 2'-O-methylation of nucleotide C2498 in the peptidyl transferase loop of 23S rRNA [ ].

[ "GO:0008168" ]

[ "methyltransferase activity" ]

[ "molecular_function" ]

1

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

[ "MF_01551", "NF008734", "PIRSF028774" ]

[ "23SrRNA_methyltr_M", "PRK11760.1", "UCP028774" ]

[ 3854, 4120, 3953 ]

3

[ "EC" ]

[ "2.1.1.186" ]

[ "EC:2.1.1.186" ]

1

[ "4atn", "4auk", "4b17" ]

3

[ "PUB00053913" ]

[ "19400805" ]

[ "YgdE is the 2'-O-ribose methyltransferase RlmM specific for nucleotide C2498 in bacterial 23S rRNA." ]

[ 2009 ]

1

[]

0

null

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

[ 4093, 7, 21 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ribosomal RNA large subunit methyltransferase M

rRNA_MeTrfase_M

3

IPR011225

11,225

Type IV secretory pathway, VirJ component

IV_sec_VirJ

Family

2,250

false

Type IV secretion systems are virulence determinants in many bacteria and share homology with many conjugal transfer systems. The VirB system of Agrobacterium tumefaciens, which delivers both virulence proteins and oncogenic T-DNA to plant hosts, is the best studied Type IV secretion system. This group contains the Vir...

[]

0

[ "PIRSF" ]

[ "PIRSF029063" ]

[ "IV_sec_VirJ" ]

[ 2250 ]

1

[]

0

[ "9rc4" ]

1

[ "PUB00012242", "PUB00014385", "PUB00014402", "PUB00014405", "PUB00014422" ]

[ "12207700", "7494475", "8491736", "7765595", "7860597" ]

[ "Agrobacterium type IV secretion is a two-step process in which export substrates associate with the virulence protein VirJ in the periplasm.", "An Agrobacterium virulence factor encoded by a Ti plasmid gene or a chromosomal gene is required for T-DNA transfer into plants.", "Isolation and characterization of a...

[ 2002, 1995, 1993, 1994, 1995 ]

5

[]

0

null

[ "Bacteria", "Eukaryota", "Plasmid Ti", "ecological metagenomes" ]

[ 2242, 2, 1, 5 ]

4

[]

0

true

Family

Type IV secretory pathway, VirJ component

IV_sec_VirJ

6

IPR011226

11,226

ATP-grasp family

ATP-grasp_fam

Family

1,320

false

This entry represents a family of bacterial proteins that contain an ATP-grasp domain. They are related to carbamoyl phosphate synthetases. Their genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved i...

[]

0

[ "PIRSF" ]

[ "PIRSF029120" ]

[ "UCP029120" ]

[ 1320 ]

1

[]

0

[]

0

[ "PUB00066658" ]

[ "23044854" ]

[ "Ter-dependent stress response systems: novel pathways related to metal sensing, production of a nucleoside-like metabolite, and DNA-processing." ]

[ 2012 ]

1

[]

0

null

[ "Bacteria", "marine sediment metagenome" ]

[ 1319, 1 ]

2

[]

0

true

Family

ATP-grasp family

ATP-grasp_fam

9

IPR011228

11,228

Uncharacterised conserved protein UCP029766

UCP029766

Family

1,065

false

This family is a group of uncharacterised conserved proteins from the Gammaproteobacteria.

[]

0

[ "NCBIFAM", "PIRSF" ]

[ "NF011783", "PIRSF029766" ]

[ "PRK15247.1", "UCP029766" ]

[ 695, 1031 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria" ]

[ 1065 ]

1

[]

0

true

Family

Uncharacterised conserved protein UCP029766

UCP029766

5

IPR011229

11,229

Cell cycle protein GpsB

Cell_cycle_GpsB

Family

2,476

false

This entry contains GpsB (also known as YpsB), which is a cell cycle protein and a component of the divisome. It associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, it is a key component of the system ...

[]

0

[ "HAMAP", "PIRSF" ]

[ "MF_02011", "PIRSF029938" ]

[ "GpsB", "UCP029938" ]

[ 1575, 2320 ]

2

[]

0

[ "4ug1", "4ug3", "8e2b", "8e2c", "9pv2" ]

5

[ "PUB00070823", "PUB00070824" ]

[ "18363795", "18776011" ]

[ "Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis.", "Cytological characterization of YpsB, a novel component of the Bacillus subtilis divisome." ]

[ 2008, 2008 ]

2

[ "IPR007793" ]

[]

1

0

1

[ "Bacteria", "Zophobas morio", "metagenomes" ]

[ 2471, 1, 4 ]

3

[]

0

true

Family

Cell cycle protein GpsB

Cell_cycle_GpsB

3

IPR011230

11,230

Probable inactive purple acid phosphatase 14/16/28/29

PAP14/16/28/29

Family

2,428

false

This group of conserved proteins from plants and some bacteria contain one copy of the calcineurin-like phosphoesterase domain [ ]. Members from Arabidopsi lack the conserved His residue essential for phosphatase activity.

[]

0

[ "PIRSF" ]

[ "PIRSF030250" ]

[ "Ptase_At2g46880" ]

[ 2428 ]

1

[]

0

[]

0

[ "PUB00014394" ]

[ "8683579" ]

[ "Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures." ]

[ 1996 ]

1

[]

0

null

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

[ 666, 1758, 4 ]

3

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

[ 15, 9, 11 ]

3

true

Family

Probable inactive purple acid phosphatase 14/16/28/29

PAP14/16/28/29

9

IPR011231

11,231

Bacteriophage VT1-Sakai, H0018

Phage_VT1-Sakai_H0018

Family

2,624

false

This entry represents a large family of phage proteins. These proteins form a trimeric arrangement which stabilises the phage capsid. The proteins have what is known as a β-tulip fold. This entry is represented by Bacteriophage VT1-Sakai, H0018. The characteristics of the protein distribution suggest prophage matches i...

[]

0

[ "PFAM", "PIRSF" ]

[ "PF09956", "PIRSF030771" ]

[ "Phage_cement_2", "UCP030771" ]

[ 2624, 1337 ]

2

[]

0

[ "9gay", "9gaz", "9gb0" ]

3

[]

0

[]

0

null

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

[ 2331, 8, 5, 213, 67 ]

5

[]

0

true

Family

Bacteriophage VT1-Sakai, H0018

Phage_VT1-Sakai_H0018

3

IPR011233

11,233

Probable tellurium resistance transcriptional regulator TerW

TerW

Family

216

false

This group represents Probable tellurium resistance transcriptional regulator TerW from the IncHI2 R478 plasmid in Serratia marcescens that specifies resistance to tellurite (Te(r)), to some bacteriophages (Phi) and to pore-forming colicins (PacB) [ ]. TerW binds specifically to the potential promoter region of the ter...

[]

0

[ "PIRSF" ]

[ "PIRSF030837" ]

[ "TerW" ]

[ 216 ]

1

[]

0

[]

0

[ "PUB00014419", "PUB00103677" ]

[ "8981981", "16937251" ]

[ "Characterization of a region of the IncHI2 plasmid R478 which protects Escherichia coli from toxic effects specified by components of the tellurite, phage, and colicin resistance cluster.", "Analysis of the tellurite resistance determinant on the pNT3B derivative of the pTE53 plasmid from uropathogenic Escherich...

[ 1997, 2006 ]

2

[]

0

null

[ "Enterobacterales" ]

[ 216 ]

1

[]

0

true

Family

Probable tellurium resistance transcriptional regulator TerW

TerW

9

IPR011238

11,238

Bacterial microcompartment shell protein PduT

Micro_shell_prot_PduT

Family

1,597

false

Members of this group are bacterial microcompartment shell proteins: PduT of Salmonella enterica and its orthologs in the propriondiol and ethanolamine operons of bacteria [ , , , ]. Some non-autotrophic organisms form polyhedral organelles, enterosomes [ ], that resemble the carboxysomes found in autotrophs, particula...

[]

0

[ "PIRSF" ]

[ "PIRSF034834" ]

[ "PduT" ]

[ 1597 ]

1

[]

0

[ "3n79", "3nwg", "3pac", "3vcd", "4ddf", "4nwn", "5dih", "5dii", "6fdb", "6n06", "6n0f", "6n0g", "8t6n", "8uf0", "8ui2", "8ukm", "8un1" ]

17

[ "PUB00002263", "PUB00003863", "PUB00009955", "PUB00011184", "PUB00013595", "PUB00013596", "PUB00014337", "PUB00014338", "PUB00015063", "PUB00015064", "PUB00015065", "PUB00015066", "PUB00097925" ]

[ "7868611", "7934888", "10464203", "10498708", "11844753", "8071226", "15012219", "9891798", "11722879", "15317775", "12648839", "12923081", "30833088" ]

[ "Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster.", "Isolation and characterization of a carboxysome shell gene from Thiobacillus neapolitanus.", "The 17-gene ethanolamine (eut) operon of Salmo...

[ 1995, 1994, 1999, 1999, 2002, 1994, 1999, 1998, 2001, 2004, 2003, 2003, 2019 ]

13

[]

[ "IPR013501" ]

0

1

0

[ "Bacteria", "metagenomes" ]

[ 1571, 26 ]

2

[]

0

true

Family

Bacterial microcompartment shell protein PduT

Micro_shell_prot_PduT

8

IPR011239

11,239

Phosphoesterase cyanobacterial, all2852

Pesterase_cyn

Family

235

false

This group represents a predicted phosphoesterase, all members are Cyanobacteria.

[]

0

[ "PIRSF" ]

[ "PIRSF035427" ]

[ "All2852" ]

[ 235 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Cyanophyceae" ]

[ 235 ]

1

[]

0

true

Family

Phosphoesterase cyanobacterial, all2852

Pesterase_cyn

4

IPR011240

11,240

Phosphoesterase-related protein YunD

Pesterase_YunD

Family

2,174

false

These conserved proteins from Gram-positive bacteria possess most of the motifs characteristic of a variety of enzymatically active phosphoesterases [ ], including acid and alkaline phosphatases, phosphoprotein phosphatases, 5'-nucleotidase, bis(5'-nucleosyl)-tetraphosphatase (symmetrical), sphingomyelin phosphodiester...

[]

0

[ "PIRSF" ]

[ "PIRSF036361" ]

[ "YunD" ]

[ 2174 ]

1

[]

0

[]

0

[ "PUB00014394" ]

[ "8683579" ]

[ "Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures." ]

[ 1996 ]

1

[ "IPR006179" ]

[]

1

0

1

[ "Bacilli" ]

[ 2174 ]

1

[]

0

true

Family

Phosphoesterase-related protein YunD

Pesterase_YunD

6

IPR011241

11,241

Bifunctional acetylglutamate kinase/N-acetyl-gamma-glutamyl-phosphate reductase

NAGK/NAGSA

Family

1,377

false

This group represents a bifunctional acetylglutamate kinase ( )/N-acetyl-gamma-glutamyl-phosphate reductase ( ), which is found in fungi. It contains an N-terminal acetylglutamate kinase (also known as N-acetyl-L-glutamate kinase, NAGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (NAGSA) domain ...

[ "GO:0003942", "GO:0003991", "GO:0006526", "GO:0005739" ]

[ "N-acetyl-gamma-glutamyl-phosphate reductase activity", "acetylglutamate kinase activity", "L-arginine biosynthetic process", "mitochondrion" ]

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

4

[ "PIRSF" ]

[ "PIRSF036440" ]

[ "ARG5-6" ]

[ 1377 ]

1

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

[ "1.2.1.38", "2.7.2.8", "PWY-5154", "R-DDI-70635", "R-SCE-70635", "R-SPO-70635" ]

[ "EC:1.2.1.38", "EC:2.7.2.8", "METACYC:PWY-5154", "REACTOME:R-DDI-70635", "REACTOME:R-SCE-70635", "REACTOME:R-SPO-70635" ]

6

[]

0

[ "PUB00014450", "PUB00085083" ]

[ "11553611", "1313366" ]

[ "A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis: acetylglutamate synthase activity requires complex formation with acetylglutamate kinase.", "Cloning and sequencing of arg3 and arg11 genes of Schizosaccharomyces pombe on a 10-kb DNA fragment. Heterologous expression and mi...

[ 2001, 1992 ]

2

[]

0

null

[ "Eukaryota", "Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2)" ]

[ 1376, 1 ]

2

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

[ 1, 1, 1 ]

3

true

Family

Bifunctional acetylglutamate kinase/N-acetyl-gamma-glutamyl-phosphate reductase

NAGK/NAGSA

6

IPR011242

11,242

Acetylglutamate kinase ArgB, GNAT domain-containing

ArgB_GNAT

Family

762

false

N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for...

[ "GO:0003991", "GO:0006526", "GO:0005737" ]

[ "acetylglutamate kinase activity", "L-arginine biosynthetic process", "cytoplasm" ]

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

3

[ "PIRSF" ]

[ "PIRSF036441" ]

[ "NAGK_DUF619" ]

[ 762 ]

1

[ "EC", "METACYC" ]

[ "2.7.2.8", "PWY-5154" ]

[ "EC:2.7.2.8", "METACYC:PWY-5154" ]

2

[ "3s6g", "3s6h", "3s6k", "3s7y", "3zzi", "4ab7", "4kzt" ]

7

[ "PUB00014499" ]

[ "12633501" ]

[ "N-acetylglutamate and its changing role through evolution." ]

[ 2003 ]

1

[]

0

null

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

[ 629, 131, 2 ]

3

[ "Homo sapiens", "Rattus norvegicus" ]

[ 1, 1 ]

2

true

Family

Acetylglutamate kinase ArgB, GNAT domain-containing

ArgB_GNAT

7

IPR011243

11,243

N-acetylglutamate synthase, animal

GlcNAc_Synth_met

Family

308

false

N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for...

[ "GO:0004042", "GO:0006526" ]

[ "L-glutamate N-acetyltransferase activity", "L-arginine biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF" ]

[ "PIRSF036442" ]

[ "NAGS_animal" ]

[ 308 ]

1

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

[ "2.3.1.1", "PWY-5154", "R-DRE-70635", "R-HSA-70635", "R-MMU-70635" ]

[ "EC:2.3.1.1", "METACYC:PWY-5154", "REACTOME:R-DRE-70635", "REACTOME:R-HSA-70635", "REACTOME:R-MMU-70635" ]

5

[]

0

[ "PUB00014442", "PUB00014499" ]

[ "12049647", "12633501" ]

[ "Identification, cloning and expression of the mouse N-acetylglutamate synthase gene.", "N-acetylglutamate and its changing role through evolution." ]

[ 2002, 2003 ]

2

[]

0

null

[ "Gnathostomata" ]

[ 308 ]

1

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

[ 2, 2, 1, 1 ]

4

true

Family

N-acetylglutamate synthase, animal

GlcNAc_Synth_met

5

IPR011244

11,244

Bifunctional argininosuccinate lyase/acetyltransferase

ASAL_AGS_AcTrfase

Family

469

false

This group represents a predicted bifunctional argininosuccinate lyase/acetyltransferase from Gammaproteobacteria.

[ "GO:0004056", "GO:0016746", "GO:0006526", "GO:0005737" ]

[ "argininosuccinate lyase activity", "acyltransferase activity", "L-arginine biosynthetic process", "cytoplasm" ]

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

4

[ "PIRSF" ]

[ "PIRSF036456" ]

[ "ASAL_AGS" ]

[ 469 ]

1

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

[ "2.3.1.-", "4.3.2.1", "PWY-3602", "PWY-361", "PWY-4801", "PWY-4922", "PWY-4983", "PWY-4984", "PWY-5", "PWY-5048", "PWY-5139", "PWY-5154", "PWY-5268", "PWY-5284", "PWY-5292", "PWY-5307", "PWY-5313", "PWY-5317", "PWY-5318", "PWY-5353", "PWY-5400", "PWY-5473", "PWY-5475", ...

[ "EC:2.3.1.-", "EC:4.3.2.1", "METACYC:PWY-3602", "METACYC:PWY-361", "METACYC:PWY-4801", "METACYC:PWY-4922", "METACYC:PWY-4983", "METACYC:PWY-4984", "METACYC:PWY-5", "METACYC:PWY-5048", "METACYC:PWY-5139", "METACYC:PWY-5154", "METACYC:PWY-5268", "METACYC:PWY-5284", "METACYC:PWY-5292", "M...

225

[]

0

[ "PUB00014557", "PUB00014560" ]

[ "14609201", "408599" ]

[ "Interdomain communications in bifunctional enzymes: how are different activities coordinated?", "The genetic organization of arginine biosynthesis in Pseudomonas aeruginosa." ]

[ 2003, 1977 ]

2

[]

0

null

[ "Bacteria", "marine sediment metagenome" ]

[ 467, 2 ]

2

[]

0

true

Family

Bifunctional argininosuccinate lyase/acetyltransferase

ASAL_AGS_AcTrfase

7

IPR011245

11,245

Butyrate kinase

Butyrate_kin

Family

3,415

false

Butyrate kinase is an enzyme that facilitates the formation of butyryl-CoA by phosphorylating butyrate in the presence of ATP to form butyryl phosphate [ ]. The final steps in butyrate synthesis by anaerobic bacteria can occur via butyrate kinase and phosphotransbutyrylase or via butyryl-CoA:acetate CoA-transferase, th...

[ "GO:0005524", "GO:0047761", "GO:0016310", "GO:0005737" ]

[ "ATP binding", "butyrate kinase activity", "phosphorylation", "cytoplasm" ]

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

4

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

[ "MF_00542", "NF002834", "PIRSF036458", "TIGR02707", "cd24011" ]

[ "Butyrate_kinase", "PRK03011.1-5", "Butyrate_kin", "butyr_kinase", "ASKHA_NBD_BK" ]

[ 3400, 3393, 3306, 3285, 3391 ]

5

[ "EC", "GP" ]

[ "2.7.2.7", "GenProp0910" ]

[ "EC:2.7.2.7", "GP:GenProp0910" ]

2

[ "1saz", "1x9j" ]

2

[ "PUB00001831", "PUB00014559", "PUB00046639" ]

[ "8396545", "15028695", "12777787" ]

[ "Cloning and sequence analysis of the genes encoding phosphotransbutyrylase and butyrate kinase from Clostridium acetobutylicum NCIMB 8052.", "Restricted distribution of the butyrate kinase pathway among butyrate-producing bacteria from the human colon.", "Crystallization of butyrate kinase 2 from Thermotoga ma...

[ 1993, 2004, 2003 ]

3

[ "IPR000890" ]

[]

1

0

1

[ "Bacteria", "Candidatus Methanolliviera hydrocarbonicum", "Trichuris trichiura", "metagenomes" ]

[ 3345, 1, 1, 68 ]

4

[]

0

true

Family

Butyrate kinase

Butyrate_kin

6

IPR011246

11,246

Bifunctional diaminopimelate decarboxylase/aspartate kinase

DAP_dec_asp_kin

Family

558

false

This group represents a predicted bifunctional diaminopimelate decarboxylase/aspartate kinase from the Gammaproteobacteria. Bifunctional enzymes permit the direct channelling of intermediates between catalytic centres involved in consecutive reactions in a pathway, offering an efficient means of directing the flow of c...

[]

0

[ "NCBIFAM", "PIRSF" ]

[ "NF006515", "PIRSF036459" ]

[ "PRK08961.1", "DAP_dec_asp_kin" ]

[ 557, 509 ]

2

[]

0

[]

0

[ "PUB00014557", "PUB00014558" ]

[ "14609201", "9559056" ]

[ "Interdomain communications in bifunctional enzymes: how are different activities coordinated?", "Enzymology of bacterial lysine biosynthesis." ]

[ 2003, 1998 ]

2

[]

0

null

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

[ 552, 2, 4 ]

3

[]

0

true

Family

Bifunctional diaminopimelate decarboxylase/aspartate kinase

DAP_dec_asp_kin

5

IPR011247

11,247

Chemotaxis protein-glutamate methylesterase

Chemotax_prot-Glu_Me-esterase

Family

1,428

false

In bacterial chemotaxis, cellular movement is directed in response to chemical gradients. Transmembrane chemoreceptors that sense the stimuli are coupled (via a coupling protein, CheW) with a signal transduction histidine kinase (CheA). CheA phosphorylates response regulators CheB and CheY. Phosphorylated CheY binds to...

[]

0

[ "PIRSF" ]

[ "PIRSF036461" ]

[ "Chmtx_methlestr" ]

[ 1428 ]

1

[]

0

[]

0

[ "PUB00011107", "PUB00015775" ]

[ "10049806", "11912013" ]

[ "Structural analysis of bacterial chemotaxis proteins: components of a dynamic signaling system.", "Exploiting genome sequence: predictions for mechanisms of Campylobacter chemotaxis." ]

[ 1998, 2002 ]

2

[]

0

null

[ "Bacteria", "Pleodorina starrii", "marine sediment metagenome" ]

[ 1425, 1, 2 ]

3

[]

0

true

Family

Chemotaxis protein-glutamate methylesterase

Chemotax_prot-Glu_Me-esterase

7

IPR011248

11,248

Serine/alanine racemase

Serine/alanine_racemase

Family

54

false

This family represents a serine/alanine racemase from Enterococcus spp [ , ]. Vancomycin resistance in Enterococcus gallinarum results from the production of UDP-MurNAc-pentapeptide[D-Ser]. VanT, a membrane-bound serine racemase, is one of three proteins essential for this resistance. VanT also has alanine racemase act...

[ "GO:0016855", "GO:0030170", "GO:0046677", "GO:0016020" ]

[ "racemase and epimerase activity, acting on amino acids and derivatives", "pyridoxal phosphate binding", "response to antibiotic", "membrane" ]

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

4

[ "PIRSF" ]

[ "PIRSF036464" ]

[ "Ser_ala_racem" ]

[ 54 ]

1

[ "EC" ]

[ "5.1.1.-" ]

[ "EC:5.1.1.-" ]

1

[]

0

[ "PUB00014380", "PUB00014409", "PUB00014498" ]

[ "12615855", "10878136", "10209740" ]

[ "Role of the transmembrane domain of the VanT serine racemase in resistance to vancomycin in Enterococcus gallinarum BM4174.", "Serine and alanine racemase activities of VanT: a protein necessary for vancomycin resistance in Enterococcus gallinarum BM4174.", "Characterization and modelling of VanT: a novel, mem...

[ 2003, 2000, 1999 ]

3

[ "IPR000821" ]

[]

1

0

1

[ "Bacillota" ]

[ 54 ]

1

[]

0

true

Family

Serine/alanine racemase

Serine/alanine_racemase

7

IPR011249

11,249

Metalloenzyme, LuxS/M16 peptidase-like

Metalloenz_LuxS/M16

Homologous_superfamily

126,429

false

This entry represents domains with a two-layer α/β structure found in metalloenzymes such as LuxS (S-ribosylhomocysteinase; ) and metallopeptidases belonging to MEROPS peptidase family M16. These domains share the same active site motif of HxxEH located in the first core helix, but differ in one of the metal-binding re...

[ "GO:0046872" ]

[ "metal ion binding" ]

[ "molecular_function" ]

1

[ "SSF" ]

[ "SSF63411" ]

[ "" ]

[ 126429 ]

1

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

[ "4.4.1.21", "PWY-6151", "PWY-6153", "PWY-6154", "R-BTA-5689880", "R-BTA-611105", "R-BTA-77387", "R-BTA-8949664", "R-BTA-9033241", "R-BTA-9837999", "R-BTA-9865881", "R-CEL-611105", "R-CEL-8949664", "R-CEL-9837999", "R-CEL-9865881", "R-DDI-611105", "R-DDI-9033241", "R-DDI-9837999", ...

[ "EC:4.4.1.21", "METACYC:PWY-6151", "METACYC:PWY-6153", "METACYC:PWY-6154", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-77387", "REACTOME:R-BTA-8949664", "REACTOME:R-BTA-9033241", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9865881", "REACTOME:R-CEL-611105", "REACTOME:R-C...

56

[ "1bcc", "1be3", "1bgy", "1ezv", "1hr6", "1hr7", "1hr8", "1hr9", "1ie0", "1inn", "1j6v", "1j6w", "1j6x", "1j98", "1joe", "1jqw", "1jvi", "1kb9", "1kyo", "1l0l", "1l0n", "1ntk", "1ntm", "1ntz", "1nu1", "1p84", "1pp9", "1ppj", "1q2l", "1qcr", "1sqb", "1sqp"...

313

[ "PUB00010202", "PUB00025993", "PUB00032627" ]

[ "11470436", "11553770", "15751951" ]

[ "Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences.", "Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site.", "Crystal structure of S-ribosylhomocysteinase (LuxS) in complex with a catalytic 2-ketone intermed...

[ 2001, 2001, 2005 ]

3

[]

0

null

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

[ 44, 78473, 46056, 230, 1626 ]

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",...

[ 69, 18, 17, 11, 4, 92, 29, 6, 45, 45, 8, 6, 178 ]

13

true

Homologous_superfamily

Metalloenzyme, LuxS/M16 peptidase-like

Metalloenz_LuxS/M16

8

IPR011252

11,252

Fibrogen-binding domain 1

Fibrogen-bd_dom1

Homologous_superfamily

6,110

false

This superfamily represents fibrinogen-binding domain 1. In proteins such as fibrinogen-binding adhesion SdrG and clumping factor A, there are two fibrinogen-binding domains with similar core β-sandwich topologies, but with different modulations in their structure. This entry represents the first domain, while represen...

[ "GO:0007155" ]

[ "cell adhesion" ]

[ "biological_process" ]

1

[ "CATHGENE3D" ]

[ "G3DSA:2.60.40.1280" ]

[ "" ]

[ 6110 ]

1

[]

0

[ "1n67", "1r17", "1r19", "2f68", "2f6a", "2ral", "2vr3", "2y7l", "2y7m", "2y7n", "2y7o", "2ylh", "2z1p", "3asw", "3at0", "3au0", "3irp", "3irz", "3is0", "3is1", "3v10", "4b5z", "4b60", "4f1z", "4f20", "4f24", "4f27", "4jdz", "4je0", "4le8", "4leb", "4lee"...

48

[ "PUB00027570", "PUB00030473" ]

[ "12485987", "14567919" ]

[ "A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A.", "A \"dock, lock, and latch\" structural model for a staphylococcal adhesin binding to fibrinogen." ]

[ 2002, 2003 ]

2

[]

0

null

[ "Bacteria", "Caudoviricetes", "Fungi", "metagenomes" ]

[ 5603, 15, 485, 7 ]

4

[ "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 1 ]

1

true

Homologous_superfamily

Fibrogen-binding domain 1

Fibrogen-bd_dom1

7

IPR011254

11,254

Prismane-like superfamily

Prismane-like_sf

Homologous_superfamily

12,090

false

Prismane (hybrid-cluster) proteins are present in a wide range of bacteria and archaea, and are characterised by their two Fe/S centres: a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O] cluster [ ]. Prismane proteins contain four domains: two spectrin repeat-like 3-helical bundle domains, and two α/β domains with Ro...

[ "GO:0003824", "GO:0016491" ]

[ "catalytic activity", "oxidoreductase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "SSF" ]

[ "SSF56821" ]

[ "" ]

[ 12090 ]

1

[ "EC", "REACTOME" ]

[ "1.7.99.1", "R-SCE-6791226" ]

[ "EC:1.7.99.1", "REACTOME:R-SCE-6791226" ]

2

[ "1e1d", "1e2u", "1e9v", "1gn9", "1gnl", "1gnt", "1jqk", "1mjg", "1oa0", "1oa1", "1oao", "1ru3", "1su6", "1su7", "1su8", "1suf", "1upx", "1w9m", "2xgj", "2yiv", "2z8y", "3b51", "3b52", "3b53", "3cf4", "3git", "3i01", "3i04", "3i39", "3s2x", "4qu4", "4u4c"...

153

[ "PUB00007375" ]

[ "10651802" ]

[ "The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]." ]

[ 2000 ]

1

[]

0

null

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

[ 1060, 8929, 1496, 605 ]

4

[ "Arabidopsis thaliana", "Danio rerio", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Zea mays" ]

[ 7, 3, 1, 4, 1, 37 ]

6

true

Homologous_superfamily

Prismane-like superfamily

Prismane-like_sf

5

IPR011257

11,257

DNA glycosylase

DNA_glycosylase

Homologous_superfamily

141,759

false

DNA glycosylases act to repair oxidative damage in DNA. These proteins are redundant as there are several different types of DNA glycosylases that are able to compensate for one another. Examples include the endonuclease III subfamily, the mismatch glycosylases subfamily, the 3-methyladenine DNA glycosylases I subfamil...

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

[ "catalytic activity", "DNA repair" ]

[ "molecular_function", "biological_process" ]

2

[ "SSF" ]

[ "SSF48150" ]

[ "" ]

[ 141759 ]

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...

[ "3.2.2", "4.2.99.18", "R-BTA-110329", "R-BTA-110357", "R-CEL-110329", "R-CEL-110357", "R-DME-110329", "R-DME-110330", "R-DME-110331", "R-DME-110357", "R-GGA-110329", "R-HSA-110328", "R-HSA-110329", "R-HSA-110330", "R-HSA-110331", "R-HSA-110357", "R-HSA-5649702", "R-HSA-9608287", ...

[ "EC:3.2.2", "EC:4.2.99.18", "REACTOME:R-BTA-110329", "REACTOME:R-BTA-110357", "REACTOME:R-CEL-110329", "REACTOME:R-CEL-110357", "REACTOME:R-DME-110329", "REACTOME:R-DME-110330", "REACTOME:R-DME-110331", "REACTOME:R-DME-110357", "REACTOME:R-GGA-110329", "REACTOME:R-HSA-110328", "REACTOME:R-HS...

39

[ "1diz", "1ebm", "1fn7", "1hu0", "1kea", "1kg2", "1kg3", "1kg4", "1kg5", "1kg6", "1kg7", "1ko9", "1kqj", "1lmz", "1lwv", "1lww", "1lwy", "1m3h", "1m3q", "1mpg", "1mud", "1mun", "1muy", "1n39", "1n3a", "1n3c", "1ngn", "1nku", "1orn", "1orp", "1p59", "1p7m"...

197

[ "PUB00014479" ]

[ "14637253" ]

[ "DNA N-glycosylase deficient mice: a tale of redundancy." ]

[ 2003 ]

1

[]

0

null

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

[ 3909, 106422, 29297, 47, 2084 ]

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",...

[ 92, 1, 9, 5, 4, 44, 14, 7, 62, 18, 4, 4, 165 ]

13

true

Homologous_superfamily

DNA glycosylase

DNA_glycosylase

8

IPR011258

11,258

BPG-independent PGAM, N-terminal

BPG-indep_PGM_N

Domain

19,210

false

This family represents the N-terminal region of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (or phosphoglyceromutase or BPG-independent PGAM) protein ( ). The family is found in conjunction with Metalloenzyme (located in the C-terminal region of the protein).

[ "GO:0004619", "GO:0030145", "GO:0006007", "GO:0005737" ]

[ "phosphoglycerate mutase activity", "manganese ion binding", "glucose catabolic process", "cytoplasm" ]

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

4

[ "PFAM" ]

[ "PF06415" ]

[ "iPGM_N" ]

[ 19210 ]

1

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

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

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

13

[ "1ejj", "1eqj", "1o98", "1o99", "2ify", "3igy", "3igz", "3nvl", "4my4", "4nwj", "4nwx", "4qax", "5kgl", "5kgm", "5kgn", "5vpu", "7knf", "7kng", "7tl7", "7tl8" ]

20

[]

0

[]

0

null

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

[ 442, 15109, 3407, 252 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 5, 1, 1, 1, 8, 32 ]

6

true

Domain

BPG-independent PGAM, N-terminal

BPG-indep_PGM_N

5

IPR011259

11,259

Ezrin/radixin/moesin, C-terminal

ERM_C_dom

Domain

9,712

false

This entry represents the C-terminal domain of ERM family of proteins which corresponds to the actin-binding tail domain [ , ]. The ERM family consists of three closely-related proteins, ezrin, radixin and moesin [ ]. Ezrin was first identified as a constituent of microvilli [ ], radixin as a barbed, end-capping actin-...

[]

0

[ "PFAM" ]

[ "PF00769" ]

[ "ERM_C" ]

[ 9712 ]

1

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

[ "R-BTA-373752", "R-DME-2029482", "R-DME-373752", "R-DME-5627123", "R-HSA-2029482", "R-HSA-373752", "R-HSA-437239", "R-HSA-5627123", "R-HSA-8950505", "R-HSA-9662360", "R-HSA-9662361", "R-HSA-9725370", "R-MMU-2029482", "R-MMU-373752", "R-MMU-437239", "R-MMU-5627123", "R-RNO-2029482", ...

[ "REACTOME:R-BTA-373752", "REACTOME:R-DME-2029482", "REACTOME:R-DME-373752", "REACTOME:R-DME-5627123", "REACTOME:R-HSA-2029482", "REACTOME:R-HSA-373752", "REACTOME:R-HSA-437239", "REACTOME:R-HSA-5627123", "REACTOME:R-HSA-8950505", "REACTOME:R-HSA-9662360", "REACTOME:R-HSA-9662361", "REACTOME:R-...

20

[ "1ef1", "2i1j", "2i1k", "4rm8", "4rm9", "4zrj", "7edr" ]

7

[ "PUB00000467", "PUB00003053", "PUB00003059", "PUB00005477", "PUB00041575", "PUB00095065", "PUB00095066", "PUB00098611", "PUB00098656", "PUB00098657", "PUB00098658" ]

[ "3046603", "6885906", "2500445", "9048483", "17134719", "27405666", "21167305", "27364155", "9298994", "9616160", "17061246" ]

[ "A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation.", "Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells.", "A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-c...

[ 1988, 1983, 1989, 1997, 2007, 2016, 2011, 2016, 1997, 1998, 2007 ]

11

[]

0

null

[ "Eukaryota", "Pseudomonadati" ]

[ 9710, 2 ]

2

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

[ 6, 19, 8, 20, 19, 23 ]

6

true

Domain

Ezrin/radixin/moesin, C-terminal

ERM_C_dom

8

IPR011260

11,260

RNA polymerase, alpha subunit, C-terminal

RNAP_asu_C

Domain

40,843

false

The core of the bacterial RNA polymerase (RNAP) consists of four subunits, two alpha, a beta and a beta', which are conserved from bacteria to mammals. The alpha subunit (RpoA) initiates RNAP assembly by dimerising to form a platform on which the beta subunits can interact. The alpha subunit consists of a N-terminal do...

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

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

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

3

[ "PFAM" ]

[ "PF03118" ]

[ "RNA_pol_A_CTD" ]

[ 40843 ]

1

[ "EC", "REACTOME" ]

[ "2.7.7.6", "R-HSA-9639775" ]

[ "EC:2.7.7.6", "REACTOME:R-HSA-9639775" ]

2

[ "1coo", "1doq", "1hqm", "1i6v", "1iw7", "1l9u", "1l9z", "1lb2", "1smy", "1xs9", "1ynj", "1ynn", "1z3e", "1zyr", "2a68", "2a69", "2a6e", "2a6h", "2be5", "2cw0", "2gho", "2jzb", "2max", "2o5i", "2o5j", "2ppb", "3aoh", "3aoi", "3dxj", "3eql", "3gfk", "3ihq"...

580

[ "PUB00005211", "PUB00014541" ]

[ "7491496", "12202833" ]

[ "Solution structure of the activator contact domain of the RNA polymerase alpha subunit.", "Structural basis of transcription activation: the CAP-alpha CTD-DNA complex." ]

[ 1995, 2002 ]

2

[]

0

null

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

[ 26367, 13929, 2, 16, 529 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 1, 6, 2 ]

4

true

Domain

RNA polymerase, alpha subunit, C-terminal

RNAP_asu_C

4

IPR011262

11,262

DNA-directed RNA polymerase, insert domain

DNA-dir_RNA_pol_insert

Domain

52,086

false

DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerase...

[ "GO:0003899", "GO:0046983", "GO:0006351" ]

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

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

3

[ "PFAM" ]

[ "PF01000" ]

[ "RNA_pol_A_bac" ]

[ 52086 ]

1

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

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

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

169

[ "1bdf", "1hqm", "1i3q", "1i50", "1i6h", "1i6v", "1iw7", "1k83", "1l9u", "1l9z", "1nik", "1nt9", "1pqv", "1r5u", "1r9s", "1r9t", "1sfo", "1smy", "1twa", "1twc", "1twf", "1twg", "1twh", "1wcm", "1y1v", "1y1w", "1y1y", "1y77", "1ynj", "1ynn", "1zyr", "2a68"...

1,184

[ "PUB00000061", "PUB00005231", "PUB00013987", "PUB00033173" ]

[ "3052291", "9657722", "11453250", "10499798" ]

[ "Structure and function of bacterial sigma factors.", "Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain.", "Functional analysis of RNA polymerase II Rpb3 mutants of the fission yeast Schizosaccharomyces pombe.", "Crystal structure of Thermus aquaticus core RNA polymerase at...

[ 1988, 1998, 2001, 1999 ]

4

[]

0

null

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

[ 919, 26041, 24622, 7, 497 ]

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",...

[ 24, 2, 3, 2, 1, 10, 11, 2, 11, 10, 2, 2, 11 ]

13

true

Domain

DNA-directed RNA polymerase, insert domain

DNA-dir_RNA_pol_insert

6

IPR011263

11,263

DNA-directed RNA polymerase, RpoA/D/Rpb3-type

DNA-dir_RNA_pol_RpoA/D/Rpb3

Domain

53,550

false

The core of the bacterial RNA polymerase (RNAP) consists of four subunits, two alpha, a beta and a beta', which are conserved from bacteria to mammals. The alpha subunit (RpoA) initiates RNAP assembly by dimerising to form a platform on which the beta subunits can interact, and plays a direct role in promoter recogniti...

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

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

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "SMART" ]

[ "PF01193", "SM00662" ]

[ "RNA_pol_L", "RPOLD" ]

[ 51817, 52798 ]

2

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

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

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

169

[ "1bdf", "1hqm", "1i3q", "1i50", "1i6h", "1i6v", "1iw7", "1k83", "1l9u", "1l9z", "1nik", "1nt9", "1pqv", "1r5u", "1r9s", "1r9t", "1sfo", "1smy", "1twa", "1twc", "1twf", "1twg", "1twh", "1wcm", "1y1v", "1y1w", "1y1y", "1y77", "1ynj", "1ynn", "1zyr", "2a68"...

1,184

[ "PUB00013992", "PUB00013994", "PUB00013995" ]

[ "10972792", "12860379", "12694606" ]

[ "UPs and downs in bacterial transcription initiation: the role of the alpha subunit of RNA polymerase in promoter recognition.", "Functional interaction of the subunit 3 of RNA polymerase II (RPB3) with transcription factor-4 (ATF4).", "Archaeal chromatin and transcription." ]

[ 2000, 2003, 2003 ]

3

[]

0

null

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

[ 934, 26259, 25521, 35, 801 ]

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",...

[ 24, 2, 3, 3, 1, 15, 12, 2, 13, 11, 2, 2, 10 ]

13

true

Domain

DNA-directed RNA polymerase, RpoA/D/Rpb3-type

DNA-dir_RNA_pol_RpoA/D/Rpb3

2

IPR011264

11,264

Betaine aldehyde dehydrogenase

BADH

Family

4,522

false

Under osmotic stress, betaine aldehyde dehydrogenase oxidises glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in Gram-positive and Gram-negative bact...

[ "GO:0008802", "GO:0046872", "GO:0019285" ]

[ "betaine-aldehyde dehydrogenase (NAD+) activity", "metal ion binding", "glycine betaine biosynthetic process from choline" ]

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

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00804", "TIGR01804" ]

[ "BADH", "BADH" ]

[ 3328, 4454 ]

2

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

[ "1.2.1.8", "GenProp0147", "PWY-3722", "PWY-3981", "PWY-5760", "PWY-6054", "PWY-6055", "PWY-7494" ]

[ "EC:1.2.1.8", "GP:GenProp0147", "METACYC:PWY-3722", "METACYC:PWY-3981", "METACYC:PWY-5760", "METACYC:PWY-6054", "METACYC:PWY-6055", "METACYC:PWY-7494" ]

8

[ "2wme", "2wox", "2xdr", "3r31", "3zqa", "4caz", "4cbb", "4mpb", "4mpy", "4nea", "4nu9", "4q92", "4qje", "4qn2", "4qto", "4zwl", "4zxu", "5dib", "5eyu", "5ez4", "6bjp", "6bpg", "6wsa", "6wsb", "7swk", "8skf", "8u9b", "8uzi", "8uzk", "8uzm", "8uzn", "8uzo"...

37

[ "PUB00013491", "PUB00013492", "PUB00013493", "PUB00058453" ]

[ "3065456", "10094709", "9141699", "21732915" ]

[ "Molecular cloning, physical mapping and expression of the bet genes governing the osmoregulatory choline-glycine betaine pathway of Escherichia coli.", "The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization.", "Molecular characterization of the bet genes encod...

[ 1988, 1999, 1997, 2011 ]

4

[]

0

null

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

[ 4508, 6, 8 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Betaine aldehyde dehydrogenase

BADH

3

IPR011265

11,265

GABA permease

GABA_permease

Family

2,165

false

GABA permease (gabP) catalyses the translocation of 4-aminobutyrate (GABA) across the plasma membrane, with homologues expressed in Gram-negative and Gram-positive organisms. This permease is a highly hydrophobic transmembrane protein consisting of 12 transmembrane domains with hydrophilic N- and C-terminal ends [ ]. I...

[ "GO:0015185", "GO:0015812", "GO:0016020" ]

[ "gamma-aminobutyric acid transmembrane transporter activity", "gamma-aminobutyric acid transport", "membrane" ]

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

3

[ "NCBIFAM" ]

[ "TIGR01773" ]

[ "GABAperm" ]

[ 2165 ]

1

[ "GP" ]

[ "GenProp0233" ]

[ "GP:GenProp0233" ]

1

[]

0

[ "PUB00000167", "PUB00013485", "PUB00013486" ]

[ "8297211", "9677314", "9685361" ]

[ "Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gabP and expression of the GABA permease gene.", "4-Aminobutyrate (GABA) transporters from the amine-polyamine-choline superfamily: substrate specificity and ligand recognition profile of the 4-aminob...

[ 1993, 1998, 1998 ]

3

[]

0

null

[ "Bacteria", "Timema californicum" ]

[ 2164, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

GABA permease

GABA_permease

9

IPR011266

11,266

Fibrinogen-binding domain 2

Adhesin_Fg-bd_dom_2

Domain

1,190

false

This entry represents the fibrinogen-binding domain from bacterial proteins such as fibrinogen-binding adhesion SdrG and clumping factor A. In both SdrG and clumping factor A, there are two fibrinogen-binding domains with similar core β-sandwich topologies, but with different modulations in their structure. This entry ...

[ "GO:0007155", "GO:0005618" ]

[ "cell adhesion", "cell wall" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF10425" ]

[ "SdrG_C_C" ]

[ 1190 ]

1

[]

0

[ "1n67", "1r17", "1r19", "2ral", "2vr3", "3asw", "3at0", "3au0", "3irp", "3irz", "3is0", "3is1", "4b5z", "4b60", "4f1z", "4f20", "4f24", "4f27", "4jdz", "4je0", "4mbo", "4mbr", "4rmb", "5cf3", "5cfa", "5ihw", "5jq6", "5wta", "5wtb", "6leb", "6lxh", "6lxs"...

34

[]

0

[]

0

null

[ "Bacteria", "human gut metagenome" ]

[ 1187, 3 ]

2

[]

0

true

Domain

Fibrinogen-binding domain 2

Adhesin_Fg-bd_dom_2

7

IPR011267

11,267

Vegetative storage protein

Veg_Stor_Prot

Family

30

false

These vegatative storage proteins are close relatives of the plant acid phosphatases ( ) and are limited to members of the Phaseoleae including Glycine max (Soybean) and Phaseolus vulgaris (Kidney bean). These proteins are highly expressed in the leaves of repeatedly depodded plants [ , ]. Vegetative storage protein (V...

[ "GO:0045735" ]

[ "nutrient reservoir activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR01680" ]

[ "Veg_Stor_Prot" ]

[ 30 ]

1

[]

0

[]

0

[ "PUB00008422", "PUB00014554", "PUB00014555" ]

[ "1639823", "12354941", "12232060" ]

[ "The soybean vegetative storage proteins VSP alpha and VSP beta are acid phosphatases active on polyphosphates.", "Novel Regulation of Vegetative Storage Protein Genes.", "Purification of the Major Soybean Leaf Acid Phosphatase That Is Increased by Seed-Pod Removal." ]

[ 1992, 1990, 1994 ]

3

[ "IPR014403" ]

[]

1

0

1

[ "Phaseoleae" ]

[ 30 ]

1

[]

0

true

Family

Vegetative storage protein

Veg_Stor_Prot

5

IPR011268

11,268

Purine nucleoside phosphorylase

Purine_phosphorylase

Family

19,248

false

This entry consists of three clades of purine phosphorylases based on a neighbour-joining tree using the MTAP family as an out group. The highest-branching clade ( ) consists of a group of sequences from both Gram-positive and Gram-negative bacteria which have been shown to act as purine nucleotide phosphorylases but w...

[ "GO:0004731", "GO:0006139" ]

[ "purine-nucleoside phosphorylase activity", "nucleobase-containing compound metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]

[ "PIRSF000477", "PTHR11904", "TIGR01697", "cd09009" ]

[ "PurNPase", "", "PNPH-PUNA-XAPA", "PNP-EcPNPII_like" ]

[ 16935, 19202, 18037, 18652 ]

4

[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "RE...

[ "2.4.2.1", "GenProp1235", "GenProp1255", "GenProp1278", "GenProp1469", "GenProp1528", "GenProp1568", "GenProp1611", "GenProp1753", "PWY-4202", "PWY-5532", "PWY-5695", "PWY-6608", "PWY-6609", "PWY-6611", "PWY-6620", "PWY-6627", "PWY-6644", "PWY-7179", "PWY-8440", "R-HSA-679869...

[ "EC:2.4.2.1", "GP:GenProp1235", "GP:GenProp1255", "GP:GenProp1278", "GP:GenProp1469", "GP:GenProp1528", "GP:GenProp1568", "GP:GenProp1611", "GP:GenProp1753", "METACYC:PWY-4202", "METACYC:PWY-5532", "METACYC:PWY-5695", "METACYC:PWY-6608", "METACYC:PWY-6609", "METACYC:PWY-6611", "METACYC...

41

[ "1a9o", "1a9p", "1a9q", "1a9r", "1a9s", "1a9t", "1b8n", "1b8o", "1c3x", "1fxu", "1g2o", "1i80", "1lv8", "1lvu", "1m73", "1n3i", "1pbn", "1pf7", "1pwy", "1qe5", "1rct", "1rfg", "1rr6", "1rsz", "1rt9", "1tcu", "1tcv", "1td1", "1ula", "1ulb", "1v2h", "1v3q"...

134

[ "PUB00002584", "PUB00013820", "PUB00023847", "PUB00028036" ]

[ "2104852", "10537218", "10600382", "15808857" ]

[ "Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.", "Nucleosides as a carbon source in Bacillus subtilis: characterization of the drm-pupG operon.", "Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for...

[ 1990, 1999, 1999, 2005 ]

4

[]

[ "IPR010943", "IPR011269", "IPR011270" ]

0

3

0

[ "Archaea", "Bacteria", "Eukaryota", "Singapore grouper iridovirus", "metagenomes" ]

[ 3, 13533, 5367, 2, 343 ]

5

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 2, 47, 10, 1, 8, 5, 7, 1, 1 ]

9

true

Family

Purine nucleoside phosphorylase

Purine_phosphorylase

2

IPR011269

11,269

Putative purine nucleotide phosphorylase

PUNP

Family

4,252

false

This entry describes purine nucleotide phosphorylases (PNPs). Some proteins in this entry have been shown to act on inosine and guanosine, though their physiological substrates and role in vivo are not known [ , ]. Closely related clades act on inosine and guanosine (PNPH, ), and xanthosine, inosine and guanosine (XAPA...

[ "GO:0004731", "GO:0006139" ]

[ "purine-nucleoside phosphorylase activity", "nucleobase-containing compound metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01698" ]

[ "PUNP" ]

[ 4252 ]

1

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

[ "2.4.2.1", "PWY-4202", "PWY-5532", "PWY-5695", "PWY-6608", "PWY-6609", "PWY-6611", "PWY-6620", "PWY-6627", "PWY-6644", "PWY-7179", "PWY-8440" ]

[ "EC:2.4.2.1", "METACYC:PWY-4202", "METACYC:PWY-5532", "METACYC:PWY-5695", "METACYC:PWY-6608", "METACYC:PWY-6609", "METACYC:PWY-6611", "METACYC:PWY-6620", "METACYC:PWY-6627", "METACYC:PWY-6644", "METACYC:PWY-7179", "METACYC:PWY-8440" ]

12

[ "1c3x", "1g2o", "1i80", "1n3i", "1qe5", "3iom", "3ix2", "3scz", "4uc0", "7zsq", "7zsr", "8c25" ]

12

[ "PUB00023847", "PUB00028037", "PUB00028038" ]

[ "10600382", "11444965", "9598071" ]

[ "Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs.", "Purine nucleoside phosphorylase from Mycobacterium tuberculosis. Analysis of inhibition by a transition-state analogue and dissection by parts.", "Cellulomonas sp. pur...

[ 1999, 2001, 1998 ]

3

[ "IPR011268" ]

[]

1

0

1

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

[ 4209, 4, 39 ]

3

[]

0

true

Family

Putative purine nucleotide phosphorylase

PUNP

8

IPR011270

11,270

Purine nucleoside phosphorylase I, inosine/guanosine-specific

Pur_Nuc_Pase_Ino/Guo-sp

Family

10,099

false

This entry represents a family of bacterial and metazoan purine phosphorylases acting primarily on inosine and guanosine and not acting on adenosine. PNP-I refers to the nomenclature from Bacillus stearothermophilus (Geobacillus stearothermophilus) [ ] where PHP-II refers to the nucleotidase acting on adenosine as the ...

[ "GO:0004731", "GO:0006139" ]

[ "purine-nucleoside phosphorylase activity", "nucleobase-containing compound metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01700" ]

[ "PNPH" ]

[ 10099 ]

1

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

[ "2.4.2.1", "GenProp1235", "GenProp1255", "GenProp1278", "GenProp1469", "GenProp1528", "GenProp1568", "GenProp1753", "PWY-4202", "PWY-5532", "PWY-5695", "PWY-6608", "PWY-6609", "PWY-6611", "PWY-6620", "PWY-6627", "PWY-6644", "PWY-7179", "PWY-8440", "R-HSA-6798695", "R-HSA-7421...

[ "EC:2.4.2.1", "GP:GenProp1235", "GP:GenProp1255", "GP:GenProp1278", "GP:GenProp1469", "GP:GenProp1528", "GP:GenProp1568", "GP:GenProp1753", "METACYC:PWY-4202", "METACYC:PWY-5532", "METACYC:PWY-5695", "METACYC:PWY-6608", "METACYC:PWY-6609", "METACYC:PWY-6611", "METACYC:PWY-6620", "METAC...

36

[ "1a9o", "1a9p", "1a9q", "1a9r", "1a9s", "1a9t", "1b8n", "1b8o", "1fxu", "1lv8", "1lvu", "1m73", "1pbn", "1pf7", "1pwy", "1rct", "1rfg", "1rr6", "1rsz", "1rt9", "1tcu", "1tcv", "1td1", "1ula", "1ulb", "1v2h", "1v3q", "1v41", "1v45", "1v48", "1vfn", "1vmk"...

114

[ "PUB00002584", "PUB00013820", "PUB00013854", "PUB00013855" ]

[ "2104852", "10537218", "9058965", "9020983" ]

[ "Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.", "Nucleosides as a carbon source in Bacillus subtilis: characterization of the drm-pupG operon.", "Cloning and expression of purine nucleoside phosphorylase I gene from Bacillus stearothermophilus TH 6-2.", ...

[ 1990, 1999, 1997, 1997 ]

4

[ "IPR011268" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Singapore grouper iridovirus", "metagenomes" ]

[ 6610, 3433, 2, 54 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 2, 45, 8, 5, 4, 5, 1 ]

7

true

Family

Purine nucleoside phosphorylase I, inosine/guanosine-specific

Pur_Nuc_Pase_Ino/Guo-sp

3

IPR011273

11,273

Malate dehydrogenase, NADP-dependent, plants

Malate_DH_NADP-dep_pln

Family

739

false

This entry represents the NADP-dependent malate dehydrogenase found in plants, mosses and green algae and localised to the chloroplast. Malate dehydrogenase converts oxaloacetate into malate, a critical step in the C4 cycle which allows circumvention of the effects of photorespiration. Malate is subsequently transporte...

[ "GO:0046554", "GO:0006108" ]

[ "L-malate dehydrogenase (NADP+) activity", "malate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01757" ]

[ "Malate-DH_plant" ]

[ 739 ]

1

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

[ "1.1.1.82", "PWY-241", "PWY-7117" ]

[ "EC:1.1.1.82", "METACYC:PWY-241", "METACYC:PWY-7117" ]

3

[ "1civ", "7mdh" ]

2

[ "PUB00013757" ]

[ "10194350" ]

[ "Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form." ]

[ 1999 ]

1

[ "IPR010945" ]

[]

1

0

1

[ "Viridiplantae" ]

[ 739 ]

1

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

[ 6, 2, 7 ]

3

true

Family

Malate dehydrogenase, NADP-dependent, plants

Malate_DH_NADP-dep_pln

5

IPR011274

11,274

Malate dehydrogenase, NAD-dependent, cytosolic

Malate_DH_NAD-dep_euk

Family

3,536

false

Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate [ ]. There are several isoforms of MDH, differing in their subcellular localization and their specificit...

[ "GO:0030060", "GO:0006108" ]

[ "L-malate dehydrogenase (NAD+) activity", "malate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM", "CDD" ]

[ "TIGR01758", "cd01336" ]

[ "MDH_euk_cyt", "MDH_cytoplasmic_cytosolic" ]

[ 3334, 3470 ]

2

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

[ "1.1.1.37", "GenProp0033", "GenProp1584", "GenProp1612", "GenProp1693", "PWY-1622", "PWY-5392", "PWY-561", "PWY-5690", "PWY-6728", "PWY-6969", "PWY-7115", "PWY-7383", "PWY-8086", "R-BTA-9856872", "R-CEL-9856872", "R-DDI-9856872", "R-GGA-352875", "R-HSA-9856872", "R-MMU-9856872"...

[ "EC:1.1.1.37", "GP:GenProp0033", "GP:GenProp1584", "GP:GenProp1612", "GP:GenProp1693", "METACYC:PWY-1622", "METACYC:PWY-5392", "METACYC:PWY-561", "METACYC:PWY-5690", "METACYC:PWY-6728", "METACYC:PWY-6969", "METACYC:PWY-7115", "METACYC:PWY-7383", "METACYC:PWY-8086", "REACTOME:R-BTA-985687...

23

[ "4mdh", "5mdh", "5nue", "5nuf", "7rm9", "7rrl", "9d2f", "9fqr" ]

8

[ "PUB00000309", "PUB00021813", "PUB00080844" ]

[ "2775751", "11389141", "9834842" ]

[ "Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution.", "Structural analyses of a malate dehydrogenase with a variable active site.", "Malate dehydrogenase: distribution, function and properties." ]

[ 1989, 2001, 1998 ]

3

[ "IPR010945" ]

[]

1

0

1

[ "Eukaryota" ]

[ 3536 ]

1

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

[ 14, 1, 9, 2, 3, 2, 6, 3, 16 ]

9

true

Family

Malate dehydrogenase, NAD-dependent, cytosolic

Malate_DH_NAD-dep_euk

9

IPR011275

11,275

Malate dehydrogenase, type 3

Malate_DH_type3

Family

9,217

false

This entry contains bacterial and archaeal malate dehydrogenases, which convert malate into oxaloacetate in the citric acid cycle. The critical residues which discriminate malate dehydrogenase from lactate dehydrogenase have been characterised [ ], and have been used to determine members of this group.

[ "GO:0016616" ]

[ "oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor" ]

[ "molecular_function" ]

1

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

[ "MF_00487", "TIGR01763", "cd01339" ]

[ "Malate_dehydrog_3", "MalateDH_bact", "LDH-like_MDH" ]

[ 7872, 7696, 9217 ]

3

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

[ "1.1.1.37", "GenProp0033", "PWY-1622", "PWY-5392", "PWY-561", "PWY-5690", "PWY-6728", "PWY-6969", "PWY-7115", "PWY-7383", "PWY-8086" ]

[ "EC:1.1.1.37", "GP:GenProp0033", "METACYC:PWY-1622", "METACYC:PWY-5392", "METACYC:PWY-561", "METACYC:PWY-5690", "METACYC:PWY-6728", "METACYC:PWY-6969", "METACYC:PWY-7115", "METACYC:PWY-7383", "METACYC:PWY-8086" ]

11

[ "1ceq", "1cet", "1d3a", "1guy", "1guz", "1gv0", "1gv1", "1hlp", "1ldg", "1oc4", "1pze", "1pzf", "1pzg", "1pzh", "1sov", "1sow", "1t24", "1t25", "1t26", "1t2c", "1t2d", "1t2e", "1u4o", "1u4s", "1u5a", "1u5c", "1ur5", "1uxg", "1uxh", "1uxi", "1uxj", "1uxk"...

94

[ "PUB00013812", "PUB00078870" ]

[ "11021970", "8577343" ]

[ "Analysis and prediction of functional sub-types from protein sequence alignments.", "A bradyzoite stage-specifically expressed gene of Toxoplasma gondii encodes a polypeptide homologous to lactate dehydrogenase." ]

[ 2000, 1995 ]

2

[ "IPR001557" ]

[]

1

0

1

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

[ 231, 8286, 399, 301 ]

4

[]

0

true

Family

Malate dehydrogenase, type 3

Malate_DH_type3

2

IPR011277

11,277

Chorismate mutase, T-protein

CM_T

Domain

2,371

false

This entry represents the chorismate mutase domain of the gamma proteobacterial 'T-protein' which consists of an N-terminal chorismate mutase domain and a C-terminal prephenate dehydrogenase domain.

[ "GO:0004106", "GO:0006571", "GO:0005737" ]

[ "chorismate mutase activity", "L-tyrosine biosynthetic process", "cytoplasm" ]

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

3

[ "NCBIFAM" ]

[ "TIGR01799" ]

[ "CM_T" ]

[ 2371 ]

1

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

[ "1.3.1.12", "5.4.99.5", "GenProp1234", "GenProp1251", "GenProp1309", "GenProp1538", "GenProp1708", "PWY-3461", "PWY-3462", "PWY-6120", "PWY-6627", "PWY-7303", "PWY-7626" ]

[ "EC:1.3.1.12", "EC:5.4.99.5", "GP:GenProp1234", "GP:GenProp1251", "GP:GenProp1309", "GP:GenProp1538", "GP:GenProp1708", "METACYC:PWY-3461", "METACYC:PWY-3462", "METACYC:PWY-6120", "METACYC:PWY-6627", "METACYC:PWY-7303", "METACYC:PWY-7626" ]

13

[]

0

[]

0

[ "IPR002701" ]

[]

1

0

1

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

[ 2368, 2, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Chorismate mutase, T-protein

CM_T

1

IPR011278

11,278

2-methylcitrate synthase/citrate synthase type I

2-MeCitrate/Citrate_synth_II

Family

11,036

false

Members of this family are dimeric enzymes with activity as 2-methylcitrate synthase, citrate synthase, or both. Many Gram-negative species have a hexameric citrate synthase, termed citrate synthase I. Members of this family appear as a second citrate synthase isozyme, but typically are associated with propionate metab...

[ "GO:0046912", "GO:0005737" ]

[ "acyltransferase activity, acyl groups converted into alkyl on transfer", "cytoplasm" ]

[ "molecular_function", "cellular_component" ]

2

[ "NCBIFAM" ]

[ "TIGR01800" ]

[ "cit_synth_II" ]

[ 11036 ]

1

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

[ "2.3.3.16", "GenProp0033", "GenProp0240", "GenProp1687", "GenProp1710" ]

[ "EC:2.3.3.16", "GP:GenProp0033", "GP:GenProp0240", "GP:GenProp1687", "GP:GenProp1710" ]

5

[ "1a59", "1aj8", "1iom", "1ixe", "1o7x", "1vgm", "1vgp", "2ibp", "2ifc", "2p2w", "2r26", "2r9e", "3hwk", "3o8j", "3tqg", "4ybo", "6abv", "6abw", "6abx", "6aby", "6s6f", "6s87", "8an1", "8bei", "8bp7", "8qwb", "8rjk", "8rjl" ]

28

[ "PUB00013490" ]

[ "9579066" ]

[ "Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships." ]

[ 1998 ]

1

[ "IPR024176" ]

[]

1

0

1

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

[ 582, 10296, 46, 112 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

2-methylcitrate synthase/citrate synthase type I

2-MeCitrate/Citrate_synth_II

9

IPR011280

11,280

Succinate dehydrogenase/fumarate reductase flavoprotein subunit, low-GC Gram-positive bacteria

Succ_DH/Fum_Rdt_flav_su

Family

8,049

false

This entry represents the succinate dehydrogenase flavoprotein subunit as found in the low-GC Gram-positive bacteria and a few other lineages. This enzyme may act in a complete or partial TCA cycle, or act in the opposite direction as fumarate reductase. In some but not all species, succinate dehydrogenase and fumarate...

[]

0

[ "NCBIFAM" ]

[ "TIGR01811" ]

[ "sdhA_Bsu" ]

[ 8049 ]

1

[ "GP", "GP" ]

[ "GenProp0033", "GenProp0756" ]

[ "GP:GenProp0033", "GP:GenProp0756" ]

2

[ "9lay", "9laz", "9lb0", "9lb1" ]

4

[ "PUB00017742" ]

[ "10802060" ]

[ "Adenylylsulfate reductases from archaea and bacteria are 1:1 alphabeta-heterodimeric iron-sulfur flavoenzymes--high similarity of molecular properties emphasizes their central role in sulfur metabolism." ]

[ 2000 ]

1

[ "IPR030664" ]

[]

1

0

1

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

[ 7944, 7, 98 ]

3

[]

0

true

Family

Succinate dehydrogenase/fumarate reductase flavoprotein subunit, low-GC Gram-positive bacteria

Succ_DH/Fum_Rdt_flav_su

1

IPR011281

11,281

Succinate dehydrogenase, flavoprotein subunit

Succ_DH_flav_su_fwd

Family

17,000

false

Succinate dehydrogenase and fumarate reductase are homologous enzymes reversible in principle but favoured under different circumstances. This entry represents a narrowly defined clade of the succinate dehydrogenase flavoprotein subunit as found in mitochondria, in Rickettsia, in Escherichia coli and other proteobacter...

[ "GO:0050660", "GO:0160308", "GO:0006099" ]

[ "flavin adenine dinucleotide binding", "succinate dehydrogenase (FAD) activity", "tricarboxylic acid cycle" ]

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

3

[ "NCBIFAM" ]

[ "TIGR01816" ]

[ "sdhA_forward" ]

[ 17000 ]

1

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

[ "1.3.5.1", "GenProp0033", "GenProp1112", "GenProp1493", "GenProp1515", "GenProp1693", "PWY-3781", "PWY-4302", "PWY-5392", "PWY-561", "PWY-5690", "PWY-5913", "PWY-6728", "PWY-6969", "PWY-7254", "PWY-7279", "PWY-7384", "PWY-8086", "R-CEL-71403", "R-CEL-9854311", "R-DDI-71403", ...

[ "EC:1.3.5.1", "GP:GenProp0033", "GP:GenProp1112", "GP:GenProp1493", "GP:GenProp1515", "GP:GenProp1693", "METACYC:PWY-3781", "METACYC:PWY-4302", "METACYC:PWY-5392", "METACYC:PWY-561", "METACYC:PWY-5690", "METACYC:PWY-5913", "METACYC:PWY-6728", "METACYC:PWY-6969", "METACYC:PWY-7254", "ME...

42

[ "1nek", "1nen", "1yq3", "1yq4", "1zoy", "1zp0", "2acz", "2fbw", "2h88", "2h89", "2wdq", "2wdr", "2wdv", "2wp9", "2wqy", "2ws3", "2wu2", "2wu5", "3abv", "3ae1", "3ae2", "3ae3", "3ae4", "3ae5", "3ae6", "3ae7", "3ae8", "3ae9", "3aea", "3aeb", "3aec", "3aed"...

77

[]

0

[ "IPR014006" ]

[]

1

0

1

[ "Bacteria", "Candidatus Methanoperedens nitratireducens", "Eukaryota", "unclassified sequences" ]

[ 11726, 2, 5156, 116 ]

4

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

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

13

true

Family

Succinate dehydrogenase, flavoprotein subunit

Succ_DH_flav_su_fwd

8

IPR011282

11,282

2-amino-3-ketobutyrate coenzyme A ligase

2am3keto_CoA_ligase

Family

10,439

false

2-amino-3-ketobutyrate coenzyme A ligase (KBL), also called glycine C-acetyltransferase, is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA, the second step in the conversion of L-threonine to glycine in both prokaryotes and eukaryotes [ , ].

[ "GO:0008890", "GO:0006567" ]

[ "glycine C-acetyltransferase activity", "L-threonine catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_00985", "TIGR01822" ]

[ "2am3keto_CoA_ligase", "2am3keto_CoA" ]

[ 10033, 10427 ]

2

[ "EC", "GP" ]

[ "2.3.1.29", "GenProp1646" ]

[ "EC:2.3.1.29", "GP:GenProp1646" ]

2

[ "1fc4", "3tqx", "7bxp", "7bxq", "7bxr", "7bxs", "7v58", "7v5i" ]

8

[ "PUB00074164", "PUB00074165" ]

[ "10712613", "2104756" ]

[ "Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs.", "2-Amino-3-ketobutyrate CoA ligase of Escherichia coli: stoichiometry of pyridoxal phosphate binding and location of the pyridoxyllysine peptide in the primary structure of the enzyme." ]

[ 2000, 1990 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "metagenomes" ]

[ 8665, 1687, 1, 86 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

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

7

true

Family

2-amino-3-ketobutyrate coenzyme A ligase

2am3keto_CoA_ligase

1