LiteFold/InterPro · Datasets at Hugging Face

IPR020456

20,456

Acylphosphatase

Family

20,155

false

Acylphosphatase ( ) is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [ ], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [ ]. The enzyme has a mainly β-sheet structure with 2 short α-helical segments....

[ "GO:0003998" ]

[ "acylphosphatase activity" ]

[ "molecular_function" ]

1

[ "PRINTS", "PANTHER", "PANTHER" ]

[ "PR00112", "PTHR10029", "PTHR47268" ]

[ "ACYLPHPHTASE", "", "" ]

[ 10956, 3950, 16099 ]

3

[ "EC" ]

[ "3.6.1.7" ]

[ "EC:3.6.1.7" ]

1

[ "1aps", "1ulr", "1urr", "1v3z", "1w2i", "1y9o", "2acy", "2bjd", "2bje", "2fhm", "2gv1", "2hlt", "2hlu", "2k7j", "2k7k", "2lxf", "2vh7", "2w4c", "2w4d", "2w4p", "3br8", "3tnv", "3toq", "3trg", "4hi1", "4hi2", "4oix", "4oj1", "4oj3", "4ojg", "4ojh", "6cbu"...

35

[ "PUB00002331", "PUB00002351", "PUB00003238" ]

[ "2830253", "1664426", "2538623" ]

[ "The primary structure of chicken muscle acylphosphatase isozyme Ch1.", "The primary structure of two molecular species of porcine organ-common type acylphosphatase.", "Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy." ]

[ 1987, 1991, 1989 ]

3

[]

[ "IPR028627" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "ssRNA phage SRR6254351_1", "unclassified sequences" ]

[ 982, 14008, 4935, 1, 229 ]

5

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

[ 6, 4, 11, 1, 11, 4, 1, 5, 10, 9 ]

10

true

Family

Acylphosphatase

6

IPR020457

20,457

Zinc finger, B-box, chordata

Znf_B-box_chordata

Domain

1,601

false

This entry represents B-box-type zinc finger domains, which are around 40 residues in length. Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead bindi...

[ "GO:0008270" ]

[ "zinc ion binding" ]

[ "molecular_function" ]

1

[ "PRINTS" ]

[ "PR01406" ]

[ "BBOXZNFINGER" ]

[ 1601 ]

1

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

[ "2.3.2.27", "PWY-7511", "R-BTA-3134975", "R-BTA-9755511", "R-BTA-983168", "R-HSA-1834941", "R-HSA-3134975", "R-HSA-3232142", "R-HSA-877300", "R-HSA-8948751", "R-HSA-9635465", "R-HSA-9755511", "R-HSA-983168", "R-MMU-3134975", "R-MMU-3232142", "R-MMU-8948751", "R-MMU-9755511", "R-MMU...

[ "EC:2.3.2.27", "METACYC:PWY-7511", "REACTOME:R-BTA-3134975", "REACTOME:R-BTA-9755511", "REACTOME:R-BTA-983168", "REACTOME:R-HSA-1834941", "REACTOME:R-HSA-3134975", "REACTOME:R-HSA-3232142", "REACTOME:R-HSA-877300", "REACTOME:R-HSA-8948751", "REACTOME:R-HSA-9635465", "REACTOME:R-HSA-9755511", ...

18

[ "2dq5", "2yvr", "5jpx", "5k3q", "5va4" ]

5

[ "PUB00014077", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812", "PUB00040284", "PUB00040653", "PUB00042940" ]

[ "12665246", "17210253", "15963892", "15718139", "10529348", "11179890", "17428496", "16529770", "16434393" ]

[ "Zinc fingers--folds for many occasions.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting a grip on RNA.", "Zinc finger peptides for the regulation of gene expression.", "Zinc finger proteins: new ...

[ 2002, 2007, 2005, 2005, 1999, 2001, 2007, 2006, 2006 ]

9

[ "IPR000315" ]

[]

1

0

1

[ "Vertebrata" ]

[ 1601 ]

1

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

[ 19, 13, 11 ]

3

true

Domain

Zinc finger, B-box, chordata

Znf_B-box_chordata

4

IPR020458

20,458

Zinc finger, DksA/TraR C4-type conserved site

Znf_DskA_TraR_CS

Conserved_site

18,287

false

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b...

[]

0

[ "PROSITE" ]

[ "PS01102" ]

[ "ZF_DKSA_1" ]

[ 18287 ]

1

[]

0

[ "1tjl", "2kgo", "5vsw", "5w1s", "5w1t", "6n57", "6n58", "6psq", "6psr", "6pss", "6pst", "6psu", "6psv", "6psw", "7khe", "7khi" ]

16

[ "PUB00001850", "PUB00002103", "PUB00014077", "PUB00015435", "PUB00015436", "PUB00015437", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]

[ "8063112", "2180916", "12665246", "15294156", "15294157", "12775693", "17210253", "15963892", "15718139", "10529348", "11179890" ]

[ "Sequence of the rec-2 locus of Haemophilus influenzae: homologies to comE-ORF3 of Bacillus subtilis and msbA of Escherichia coli.", "Identification and characterization of a new Escherichia coli gene that is a dosage-dependent suppressor of a dnaK deletion mutation.", "Zinc fingers--folds for many occasions.",...

[ 1994, 1990, 2002, 2004, 2004, 2003, 2007, 2005, 2005, 1999, 2001 ]

11

[]

0

null

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

[ 17875, 35, 55, 322 ]

4

[ "Escherichia coli (strain K12)" ]

[ 3 ]

1

true

Conserved_site

Zinc finger, DksA/TraR C4-type conserved site

Znf_DskA_TraR_CS

6

IPR020459

20,459

AMP-binding

Domain

13,961

false

A number of prokaryotic and eukaryotic enzymes, which appear to act via an ATP-dependent covalent binding of AMP to their substrate, share a region of sequence similarity [ , , ]. This region is a Ser/Thr/Gly-rich domain that is further characterised by a conserved Pro-Lys-Gly triplet. The family of enzymes includes Py...

[]

0

[ "PRINTS" ]

[ "PR00154" ]

[ "AMPBINDING" ]

[ 13961 ]

1

[]

0

[ "1amu", "3vnq", "3vnr", "3vns", "4d4g", "4d4h", "4d4i", "4d56", "4d57", "5n81", "5n82", "5n9w", "5n9x", "6lta", "6ltb", "6ltc", "6ltd", "6o6e", "7ly4", "7ly5", "7ly7", "7thq", "7ywj", "7ywk", "8g95", "8g96", "8g97", "8g98", "8glc", "8hlk", "8p5o", "8www"...

35

[ "PUB00001189", "PUB00002125", "PUB00004359", "PUB00005277", "PUB00092576", "PUB00101120", "PUB00101121" ]

[ "2118102", "2254270", "2911486", "8805533", "26473393", "15699031", "11208777" ]

[ "The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases.", "Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708.", "Prote...

[ 1990, 1990, 1989, 1996, 2016, 2005, 2001 ]

7

[ "IPR000873" ]

[]

1

0

1

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

[ 32, 11804, 1967, 158 ]

4

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

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

7

true

Domain

AMP-binding

5

IPR020460

20,460

Zinc finger, DksA/TraR C4-type, bacteria

Znf_C4-type_bac

Domain

6,216

false

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b...

[]

0

[ "PRINTS" ]

[ "PR00618" ]

[ "DKSAZNFINGER" ]

[ 6216 ]

1

[]

0

[ "1tjl", "2kgo", "5vsw", "5w1s", "5w1t", "6n57", "6n58", "6psq", "6psr", "6pss", "6pst", "6psu", "6psv", "6psw", "7khe", "7khi" ]

16

[ "PUB00001850", "PUB00002103", "PUB00014077", "PUB00015435", "PUB00015436", "PUB00015437", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]

[ "8063112", "2180916", "12665246", "15294156", "15294157", "12775693", "17210253", "15963892", "15718139", "10529348", "11179890" ]

[ "Sequence of the rec-2 locus of Haemophilus influenzae: homologies to comE-ORF3 of Bacillus subtilis and msbA of Escherichia coli.", "Identification and characterization of a new Escherichia coli gene that is a dosage-dependent suppressor of a dnaK deletion mutation.", "Zinc fingers--folds for many occasions.",...

[ 1994, 1990, 2002, 2004, 2004, 2003, 2007, 2005, 2005, 1999, 2001 ]

11

[ "IPR000962" ]

[]

1

0

1

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

[ 6122, 7, 39, 48 ]

4

[ "Escherichia coli (strain K12)" ]

[ 3 ]

1

true

Domain

Zinc finger, DksA/TraR C4-type, bacteria

Znf_C4-type_bac

2

IPR020461

20,461

High affinity nerve growth factor receptor NTRK1

NTRK1

Family

776

false

Neurotrophins are a family of secreted proteins that regulate development, maintenance and function of vertebrate nervous systems. They act via two different classes of receptor: p75NTR (a member of the TNF receptor superfamily), and neurotrophic tyrosine kinase receptors (NTRKs) - also known as tropomyosin-related kin...

[ "GO:0004714", "GO:0005030", "GO:0006468", "GO:0007169", "GO:0005886" ]

[ "transmembrane receptor protein tyrosine kinase activity", "neurotrophin receptor activity", "protein phosphorylation", "cell surface receptor protein tyrosine kinase signaling pathway", "plasma membrane" ]

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

5

[ "PRINTS" ]

[ "PR01940" ]

[ "NTKRECEPTOR1" ]

[ 776 ]

1

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

[ "2.7.10.1", "R-HSA-167021", "R-HSA-167044", "R-HSA-170968", "R-HSA-170984", "R-HSA-177504", "R-HSA-187024", "R-HSA-187042", "R-HSA-187706", "R-HSA-198203", "R-HSA-198745", "R-MMU-170968", "R-MMU-170984", "R-MMU-177504", "R-MMU-187042", "R-MMU-198203", "R-RNO-170968", "R-RNO-170984"...

[ "EC:2.7.10.1", "REACTOME:R-HSA-167021", "REACTOME:R-HSA-167044", "REACTOME:R-HSA-170968", "REACTOME:R-HSA-170984", "REACTOME:R-HSA-177504", "REACTOME:R-HSA-187024", "REACTOME:R-HSA-187042", "REACTOME:R-HSA-187706", "REACTOME:R-HSA-198203", "REACTOME:R-HSA-198745", "REACTOME:R-MMU-170968", "R...

21

[]

0

[ "PUB00046048", "PUB00046049", "PUB00046084", "PUB00046087", "PUB00046088" ]

[ "7605062", "11520916", "17192812", "16919030", "9547236" ]

[ "Functional interactions of neurotrophins and neurotrophin receptors.", "Neurotrophins: roles in neuronal development and function.", "Transcriptional regulation of Trk family neurotrophin receptors.", "Expression of nerve growth factor and its high-affinity receptor, tyrosine kinase A proteins, in the human ...

[ 1995, 2001, 2007, 2006, 1998 ]

5

[ "IPR020777" ]

[]

1

0

1

[ "Euteleostomi" ]

[ 776 ]

1

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

[ 2, 6, 1, 5 ]

4

true

Family

High affinity nerve growth factor receptor NTRK1

NTRK1

2

IPR020462

20,462

Interleukin-11B, fish

IL-11B_fish

Family

53

false

Interleukins (IL) are a group of cytokines that play an important role in the immune system. They modulate inflammation and immunity by regulating growth, mobility and differentiation of lymphoid and other cells. Interleukin-11 (IL-11) is a pleiotropic cytokine that stimulates megakaryocytopoiesis, resulting in increas...

[]

0

[ "PRINTS" ]

[ "PR01946" ]

[ "IL11BFISH" ]

[ 53 ]

1

[]

0

[]

0

[ "PUB00013131", "PUB00046036", "PUB00046037", "PUB00046038", "PUB00046050" ]

[ "9416001", "15992047", "15720388", "16003467", "18538848" ]

[ "Interleukin-11.", "The therapeutic utility of Interleukin-11 in the treatment of inflammatory disease.", "Cloning and expression of the first nonmammalian interleukin-11 gene in rainbow trout Oncorhynchus mykiss.", "Multiple and highly divergent IL-11 genes in teleost fish.", "Teleostean IL11b exhibits com...

[ 1997, 1998, 2005, 2005, 2008 ]

5

[ "IPR022356" ]

[]

1

0

1

[ "Percomorphaceae" ]

[ 53 ]

1

[]

0

true

Family

Interleukin-11B, fish

IL-11B_fish

7

IPR020464

20,464

LanC-like protein, eukaryotic

LanC-like_prot_euk

Family

5,019

false

The LanC-like protein superfamily encompasses a highly divergent group of peptide-modifying enzymes, including the eukaryotic and bacterial lanthionine synthetase C-like proteins (LanC) [ , , ]; subtilin biosynthesis protein SpaC from Bacillus subtilis [ , ]; epidermin biosynthesis protein EpiC from Staphylococcus epid...

[]

0

[ "PRINTS" ]

[ "PR01951" ]

[ "LANCEUKARYTE" ]

[ 5019 ]

1

[]

0

[ "3e6u", "3e73", "3t33", "6wq1", "8czk", "8czl", "8d0v", "8d19" ]

8

[ "PUB00002161", "PUB00008599", "PUB00011680", "PUB00018966", "PUB00035552", "PUB00040886", "PUB00046016", "PUB00046017", "PUB00046018", "PUB00046021", "PUB00046022", "PUB00046023", "PUB00046024", "PUB00046051", "PUB00091679" ]

[ "1735728", "1539969", "8161176", "1740156", "17347412", "16527981", "11474189", "10944443", "12566319", "1482192", "9512664", "18086512", "17894782", "7689965", "22891245" ]

[ "The subtilin gene of Bacillus subtilis ATCC 6633 is encoded in an operon that contains a homolog of the hemolysin B transport protein.", "Analysis of genes involved in biosynthesis of the lantibiotic subtilin.", "Regulation of nisin biosynthesis and immunity in Lactococcus lactis 6F3.", "Analysis of genes in...

[ 1992, 1992, 1994, 1992, 2007, 2006, 2001, 2000, 2003, 1992, 1998, 2008, 2007, 1993, 2012 ]

15

[ "IPR007822" ]

[]

1

0

1

[ "Bacillales", "Eukaryota" ]

[ 2, 5017 ]

2

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

[ 18, 4, 2, 9, 5, 7, 11, 6 ]

8

true

Family

LanC-like protein, eukaryotic

LanC-like_prot_euk

7

IPR020465

20,465

Tumour necrosis factor receptor 10

TNFR_10

Family

389

false

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain - a region that contains many cysteine residues arranged in a specific repetitive pattern [ ]. The cysteines allow formation of ...

[ "GO:0045569" ]

[ "TRAIL binding" ]

[ "molecular_function" ]

1

[ "PIRSF", "PRINTS" ]

[ "PIRSF037867", "PR01956" ]

[ "CD261_antigen", "TNFACTORR10" ]

[ 89, 383 ]

2

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

[ "R-HSA-140534", "R-HSA-202733", "R-HSA-3371378", "R-HSA-5213460", "R-HSA-5218900", "R-HSA-6803211", "R-HSA-69416", "R-HSA-75158", "R-MMU-202733", "R-MMU-3371378", "R-MMU-5218900", "R-MMU-69416", "R-MMU-75158" ]

[ "REACTOME:R-HSA-140534", "REACTOME:R-HSA-202733", "REACTOME:R-HSA-3371378", "REACTOME:R-HSA-5213460", "REACTOME:R-HSA-5218900", "REACTOME:R-HSA-6803211", "REACTOME:R-HSA-69416", "REACTOME:R-HSA-75158", "REACTOME:R-MMU-202733", "REACTOME:R-MMU-3371378", "REACTOME:R-MMU-5218900", "REACTOME:R-MMU...

13

[ "1d0g", "1d4v", "1du3", "1za3", "2h9g", "3x3f", "4i9x", "4n90", "4od2", "5cir", "6t3j", "8dpx" ]

12

[ "PUB00000892", "PUB00046030", "PUB00046031", "PUB00046032", "PUB00046033", "PUB00046034", "PUB00046089", "PUB00046090" ]

[ "8387891", "7917108", "15500863", "11239407", "9826575", "9826574", "9314565", "9430226" ]

[ "Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation.", "Tumor necrosis factor receptor superfamily members and their ligands.", "Assembly of post-receptor signaling complexes for the tumor necrosis factor receptor superfamily.", "The TNF ...

[ 1993, 1994, 2004, 2001, 1998, 1998, 1997, 1997 ]

8

[]

0

null

[ "Euteleostomi" ]

[ 389 ]

1

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

[ 12, 1, 3 ]

3

true

Family

Tumour necrosis factor receptor 10

TNFR_10

3

IPR020466

20,466

Interleukin-15, mammal

IL-15_mml

Family

267

false

Interleukins (IL) are a group of cytokines that play an important role in the immune system. They modulate inflammation and immunity by regulating growth, mobility and differentiation of lymphoid and other cells. Interleukin-15 (IL-15) has a variety of biological functions, including stimulation and maintenance of cell...

[ "GO:0005576" ]

[ "extracellular region" ]

[ "cellular_component" ]

1

[ "PRINTS" ]

[ "PR01947" ]

[ "INTLKN15MAML" ]

[ 267 ]

1

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

[ "R-BTA-8983432", "R-HSA-8983432", "R-MMU-8983432", "R-RNO-8983432" ]

[ "REACTOME:R-BTA-8983432", "REACTOME:R-HSA-8983432", "REACTOME:R-MMU-8983432", "REACTOME:R-RNO-8983432" ]

4

[]

0

[ "PUB00019742", "PUB00046028", "PUB00046091" ]

[ "10689297", "10784451", "8543827" ]

[ "The emerging role of IL-15 in NK-cell development.", "Control of homeostasis of CD8+ memory T cells by opposing cytokines.", "Induction and regulation of IL-15 expression in murine macrophages." ]

[ 2000, 2000, 1996 ]

3

[ "IPR020439" ]

[]

1

0

1

[ "Eutheria" ]

[ 267 ]

1

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

[ 1, 6, 3 ]

3

true

Family

Interleukin-15, mammal

IL-15_mml

2

IPR020469

20,469

Cytochrome P450, CYP2 family

Cyt_P450_CYP2_fam

Family

387

false

P450 enzymes constitute a superfamily of haem-thiolate proteins [ ], widely distributed in bacteria, fungi, plants and animals. The enzymes are involved in metabolism of a plethora of both exogenous and endogenous compounds [ ]. Usually, they act as terminal oxidases in multi-component electron-transfer chains, called ...

[ "GO:0004497", "GO:0005506", "GO:0019825", "GO:0020037" ]

[ "monooxygenase activity", "iron ion binding", "oxygen binding", "heme binding" ]

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

4

[ "PRINTS" ]

[ "PR01957" ]

[ "EP450ICYP2F" ]

[ 387 ]

1

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

[ "1.14.14.1", "PWY-5451", "PWY-5665", "PWY-6398", "PWY-6992", "PWY-7466", "R-HSA-211935", "R-HSA-211981", "R-HSA-211999", "R-MMU-211935", "R-MMU-211981", "R-MMU-211999", "R-RNO-211935", "R-RNO-211981", "R-RNO-211999" ]

[ "EC:1.14.14.1", "METACYC:PWY-5451", "METACYC:PWY-5665", "METACYC:PWY-6398", "METACYC:PWY-6992", "METACYC:PWY-7466", "REACTOME:R-HSA-211935", "REACTOME:R-HSA-211981", "REACTOME:R-HSA-211999", "REACTOME:R-MMU-211935", "REACTOME:R-MMU-211981", "REACTOME:R-MMU-211999", "REACTOME:R-RNO-211935", ...

15

[]

0

[ "PUB00000052", "PUB00001116", "PUB00001400", "PUB00018631", "PUB00046092" ]

[ "3304150", "7678494", "1655423", "9972448", "9448722" ]

[ "P450 genes: structure, evolution, and regulation.", "The P450 superfamily: update on new sequences, gene mapping, accession numbers, early trivial names of enzymes, and nomenclature.", "Nomenclature Committee of the International Union of Biochemistry (NC-IUB). Nomenclature of electron-transfer proteins. Recom...

[ 1987, 1993, 1991, 1998, 1998 ]

5

[ "IPR002401" ]

[]

1

0

1

[ "Tetrapoda" ]

[ 387 ]

1

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

[ 3, 2, 5 ]

3

true

Family

Cytochrome P450, CYP2 family

Cyt_P450_CYP2_fam

7

IPR020470

20,470

Interleukin-13

IL-13

Family

246

false

This entry represents interleukin-13 (IL-13), it is a pleiotropic cytokine which may be important in the regulation of the inflammatory and immune responses [ ]. IL-13 inhibits inflammatory cytokine production and synergises with IL-2 in regulating interferon-gamma synthesis. The sequences of IL-4 and IL-13 are distant...

[]

0

[ "PFAM", "PRINTS", "PANTHER" ]

[ "PF03487", "PR01929", "PTHR48486" ]

[ "IL13", "INTRLEUKIN13", "" ]

[ 246, 234, 236 ]

3

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

[ "R-BTA-6785807", "R-CFA-6785807", "R-HSA-6785807", "R-HSA-9012546", "R-MMU-6785807", "R-RNO-6785807", "R-SSC-6785807" ]

[ "REACTOME:R-BTA-6785807", "REACTOME:R-CFA-6785807", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-9012546", "REACTOME:R-MMU-6785807", "REACTOME:R-RNO-6785807", "REACTOME:R-SSC-6785807" ]

7

[ "1ga3", "1ijz", "1ik0", "3bpo", "3g6d", "3l5w", "3l5x", "3lb6", "4i77", "4ps4", "5e4e", "5knh", "5l6y", "7rew", "8blq" ]

15

[ "PUB00004143" ]

[ "8096327" ]

[ "Interleukin-13 is a new human lymphokine regulating inflammatory and immune responses." ]

[ 1993 ]

1

[ "IPR001325" ]

[]

1

0

1

[ "Euteleostomi" ]

[ 246 ]

1

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

[ 4, 1, 2 ]

3

true

Family

Interleukin-13

IL-13

3

IPR020471

20,471

Aldo-keto reductase

AKR

Family

173,020

false

In general, the aldo-keto reductase (AKR) protein superfamily members reduce carbonyl substrates such as: sugar aldehydes, keto-steroids, keto-prostaglandins, retinals, quinones, and lipid peroxidation by-products [ , ]. However, there are some exceptions, such as the reduction of steroid double bonds catalysed by AKR1...

[ "GO:0016491" ]

[ "oxidoreductase activity" ]

[ "molecular_function" ]

1

[ "PIRSF", "PRINTS", "PANTHER", "PANTHER", "PANTHER" ]

[ "PIRSF000097", "PR00069", "PTHR11732", "PTHR42686", "PTHR43827" ]

[ "AKR", "ALDKETRDTASE", "", "", "" ]

[ 79415, 156246, 36063, 13252, 52780 ]

5

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

[ "1.1.1", "R-BTA-156590", "R-BTA-193368", "R-BTA-193775", "R-BTA-193807", "R-BTA-2162123", "R-BTA-5365859", "R-BTA-5661270", "R-BTA-975634", "R-BTA-9757110", "R-DDI-156590", "R-DDI-193144", "R-DDI-193368", "R-DDI-193775", "R-DDI-193807", "R-DDI-196108", "R-DDI-2162123", "R-DDI-53658...

[ "EC:1.1.1", "REACTOME:R-BTA-156590", "REACTOME:R-BTA-193368", "REACTOME:R-BTA-193775", "REACTOME:R-BTA-193807", "REACTOME:R-BTA-2162123", "REACTOME:R-BTA-5365859", "REACTOME:R-BTA-5661270", "REACTOME:R-BTA-975634", "REACTOME:R-BTA-9757110", "REACTOME:R-DDI-156590", "REACTOME:R-DDI-193144", "...

105

[ "1a80", "1abn", "1ads", "1ae4", "1afs", "1ah0", "1ah3", "1ah4", "1az1", "1az2", "1c9w", "1cwn", "1dla", "1ef3", "1eko", "1el3", "1frb", "1gve", "1hqt", "1hw6", "1iei", "1ihi", "1j96", "1jez", "1k8c", "1lqa", "1lwi", "1m9h", "1mar", "1mi3", "1mrq", "1mzr"...

448

[ "PUB00002548", "PUB00002751", "PUB00005156", "PUB00096110" ]

[ "2498333", "1447221", "1621098", "25304492" ]

[ "The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.", "The crystal structure of the aldose reductase.NADPH binary complex.", "An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic...

[ 1989, 1992, 1992, 2015 ]

4

[]

[ "IPR044477", "IPR044478", "IPR044479", "IPR044480", "IPR044481", "IPR044482", "IPR044483", "IPR044484", "IPR044485", "IPR044486", "IPR044487", "IPR044488", "IPR044489", "IPR044490", "IPR044491", "IPR044494", "IPR044495", "IPR044496", "IPR044497", "IPR044498", "IPR044499", "...

0

25

0

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

[ 2762, 103802, 65400, 18, 1038 ]

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",...

[ 73, 15, 16, 21, 7, 37, 50, 11, 71, 88, 7, 7, 110 ]

13

true

Family

Aldo-keto reductase

AKR

1

IPR020472

20,472

PAC1/LIS1-like, WD-40 repeat

WD40_PAC1

Repeat

299,542

false

This entry represents the WD-40 repeats in PAC1/LIS1 receptors, a class B G-protein-coupled receptor (GPCR) and similar GPCR related proteins. This entry also includes small ribosomal subunit proteins RACK1 and other scaffolding proteins such as CIAO1 and MDV1. WD-40 repeats (also known as WD or beta-transducin repeats...

[]

0

[ "PRINTS" ]

[ "PR00320" ]

[ "GPROTEINBRPT" ]

[ 299542 ]

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-1296041", "R-BTA-141430", "R-BTA-141444", "R-BTA-1538133", "R-BTA-159227", "R-BTA-159230", "R-BTA-159231", "R-BTA-159236", "R-BTA-1632852", "R-BTA-165159", "R-BTA-166208", "R-BTA-170822", "R-BTA-174184", "R-BTA-176409", "R-BTA-179409", "R-BTA-191859", "R-BTA-202040", "R-BTA-...

[ "REACTOME:R-BTA-1296041", "REACTOME:R-BTA-141430", "REACTOME:R-BTA-141444", "REACTOME:R-BTA-1538133", "REACTOME:R-BTA-159227", "REACTOME:R-BTA-159230", "REACTOME:R-BTA-159231", "REACTOME:R-BTA-159236", "REACTOME:R-BTA-1632852", "REACTOME:R-BTA-165159", "REACTOME:R-BTA-166208", "REACTOME:R-BTA-...

923

[ "1a0r", "1b9x", "1b9y", "1erj", "1gg2", "1got", "1gp2", "1nex", "1nr0", "1omw", "1p22", "1pev", "1tbg", "1trj", "1vyh", "1xhm", "2bcj", "2cnx", "2co0", "2g99", "2g9a", "2gnq", "2h13", "2h14", "2h68", "2h6k", "2h6n", "2h6q", "2h9l", "2h9m", "2h9n", "2h9p"...

2,615

[ "PUB00005491", "PUB00015237", "PUB00094364" ]

[ "10322433", "11814058", "30069656" ]

[ "The WD repeat: a common architecture for diverse functions.", "WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases.", "WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions." ]

[ 1999, 2001, 2018 ]

3

[]

0

null

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

[ 37, 15301, 284074, 12, 118 ]

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...

[ 449, 51, 217, 118, 350, 231, 36, 238, 338, 31, 43, 686 ]

12

true

Repeat

PAC1/LIS1-like, WD-40 repeat

WD40_PAC1

6

IPR020475

20,475

Endothelin

Family

2,985

false

Endothelins are small proteins that play an important role in the regulation of the cardiovascular system [ , , ]. They are the most potent vasoconstrictors known, they stimulate cardiac constriction, regulate release of vasoactive substances, and stimulate mitogenesis in blood vessels in primary culture. They also sti...

[]

0

[ "PRINTS", "PANTHER" ]

[ "PR00365", "PTHR13874" ]

[ "ENDOTHELIN", "" ]

[ 2865, 2960 ]

2

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

[ "R-BTA-375276", "R-BTA-416476", "R-CFA-375276", "R-CFA-416476", "R-HSA-375276", "R-HSA-416476", "R-HSA-9856649", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476", "R-SSC-375276", "R-SSC-416476" ]

[ "REACTOME:R-BTA-375276", "REACTOME:R-BTA-416476", "REACTOME:R-CFA-375276", "REACTOME:R-CFA-416476", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476", "REACTOME:R-SSC-37...

13

[ "1edn", "1t7h", "1v6r", "5glh", "6dk5", "6igk", "8hcq", "8hcx", "8iy5", "8iy6", "8xgr", "8xvh", "8xvi", "8xwp", "8xwq", "8zrt" ]

16

[ "PUB00001506", "PUB00001510", "PUB00005553" ]

[ "2168326", "1916094", "2690429" ]

[ "Cellular signaling by peptides of the endothelin gene family.", "Endothelins.", "Molecular biology and biochemistry of the endothelins." ]

[ 1990, 1991, 1989 ]

3

[]

0

null

[ "Deerpox virus (strain W-1170-84)", "Vertebrata" ]

[ 1, 2984 ]

2

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

[ 8, 8, 6, 8 ]

4

true

Family

Endothelin

8

IPR020476

20,476

NUDIX hydrolase

Nudix_hydrolase

Domain

111,799

false

Recently, the generic name 'NUDIX hydrolases' (NUcleoside DIphosphate linke to some other moeity X) has been coined for this domain family [ ]. The family can be divided into a number of subgroups, of which MutT anti-mutagenic activity represents only one type; most of the rest hydrolyse diverse nucleoside diphosphate ...

[]

0

[ "PRINTS" ]

[ "PR00502" ]

[ "NUDIXFAMILY" ]

[ 111799 ]

1

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

[ "3.6.1", "3.6.1.-", "PWY-5757", "PWY-6147", "PWY-6383", "PWY-6797", "PWY-7206", "PWY-7419", "PWY-7539", "PWY-7719", "PWY-7821", "PWY-8289", "R-BTA-3299685", "R-CEL-2393930", "R-CFA-2393930", "R-DRE-2393930", "R-HSA-2393930", "R-MMU-1855167", "R-MMU-2393930", "R-MMU-9748787", ...

[ "EC:3.6.1", "EC:3.6.1.-", "METACYC:PWY-5757", "METACYC:PWY-6147", "METACYC:PWY-6383", "METACYC:PWY-6797", "METACYC:PWY-7206", "METACYC:PWY-7419", "METACYC:PWY-7539", "METACYC:PWY-7719", "METACYC:PWY-7821", "METACYC:PWY-8289", "REACTOME:R-BTA-3299685", "REACTOME:R-CEL-2393930", "REACTOME:...

22

[ "1f3y", "1iry", "1jkn", "1mut", "1ppx", "1pun", "1puq", "1pus", "1sjy", "1soi", "1su2", "1sz3", "1tum", "1v8i", "1v8l", "1v8m", "1v8n", "1v8r", "1v8s", "1v8t", "1vc8", "1vc9", "1vcd", "2azw", "2b06", "2dsb", "2dsc", "2dsd", "2fml", "2kdv", "2kdw", "2rrk"...

335

[ "PUB00006662" ]

[ "8810257" ]

[ "The MutT proteins or \"Nudix\" hydrolases, a family of versatile, widely distributed, \"housecleaning\" enzymes." ]

[ 1996 ]

1

[ "IPR000086" ]

[]

1

0

1

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

[ 1888, 97772, 10710, 195, 1234 ]

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",...

[ 26, 3, 9, 3, 5, 8, 15, 2, 10, 20, 25 ]

11

true

Domain

NUDIX hydrolase

Nudix_hydrolase

6

IPR020479

20,479

Homeodomain, metazoa

HD_metazoa

Domain

93,458

false

This entry represents the homeodomain (HD), a protein domain of approximately 60 residues that usually binds DNA. It is encoded by the homeobox sequence [ , ], which was first identified in a number of Drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including ...

[ "GO:0003677" ]

[ "DNA binding" ]

[ "molecular_function" ]

1

[ "PRINTS" ]

[ "PR00024" ]

[ "HOMEOBOX" ]

[ 93458 ]

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-DME-8853884", "R-DRE-9762293", "R-GGA-9762293", "R-HSA-2032785", "R-HSA-210745", "R-HSA-210746", "R-HSA-210747", "R-HSA-381771", "R-HSA-5578768", "R-HSA-5617472", "R-HSA-8939902", "R-HSA-9010553", "R-HSA-9733709", "R-HSA-9762293", "R-HSA-9823739", "R-HSA-9830364", "R-HSA-9830674",...

[ "REACTOME:R-DME-8853884", "REACTOME:R-DRE-9762293", "REACTOME:R-GGA-9762293", "REACTOME:R-HSA-2032785", "REACTOME:R-HSA-210745", "REACTOME:R-HSA-210746", "REACTOME:R-HSA-210747", "REACTOME:R-HSA-381771", "REACTOME:R-HSA-5578768", "REACTOME:R-HSA-5617472", "REACTOME:R-HSA-8939902", "REACTOME:R-...

24

[ "1ahd", "1b72", "1b8i", "1du0", "1enh", "1ftt", "1ftz", "1hdd", "1hom", "1ig7", "1jgg", "1nk2", "1nk3", "1p7i", "1p7j", "1puf", "1qry", "1san", "1vnd", "1ztr", "2cra", "2djn", "2dmt", "2e1o", "2h1k", "2hdd", "2hoa", "2hos", "2hot", "2jwt", "2kt0", "2l7f"...

106

[ "PUB00000591", "PUB00005390", "PUB00075496", "PUB00126359", "PUB00153777" ]

[ "2568852", "1357790", "19734295", "26464018", "17963489" ]

[ "The structure and function of the homeodomain.", "The homeobox in perspective.", "A comprehensive classification and evolutionary analysis of plant homeobox genes.", "Homeodomain proteins: an update.", "Classification and nomenclature of all human homeobox genes." ]

[ 1989, 1992, 2009, 2016, 2007 ]

5

[ "IPR001356" ]

[ "IPR000747" ]

1

0

[ "Eukaryota" ]

[ 93458 ]

1

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

[ 34, 219, 106, 248, 180, 198 ]

6

true

Domain

Homeodomain, metazoa

HD_metazoa

3

IPR020481

20,481

Intracellular proteinase inhibitor BsuPI

Intracell_prot_inh_BsuPI

Domain

1,192

false

This is a bacterial domain which has been named BsuPI in Bacillus subtilis. This domain is found in , where it has been suggested to regulate the major intracellular proteinase (ISP-1) activity in vivo [ ]. The structure of proteins in this family adopt a β barrel topology.

[]

0

[ "PFAM" ]

[ "PF12690" ]

[ "BsuPI" ]

[ 1192 ]

1

[]

0

[ "3isy" ]

1

[ "PUB00046108" ]

[ "8226659" ]

[ "Characterization of the gene encoding an intracellular proteinase inhibitor of Bacillus subtilis and its role in regulation of the major intracellular proteinase." ]

[ 1993 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211)", "ecological metagenomes" ]

[ 162, 1014, 1, 15 ]

4

[]

0

true

Domain

Intracellular proteinase inhibitor BsuPI

Intracell_prot_inh_BsuPI

2

IPR020483

20,483

Uncharacterised protein family YgbA

Uncharacterised_YgbA

Family

2,880

false

This entry contains proteins with no known function.

[]

0

[ "NCBIFAM", "PFAM" ]

[ "NF007714", "PF11756" ]

[ "PRK10410.1-2", "YgbA_NO" ]

[ 2590, 2880 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "Promethearchaeum syntrophicum", "metagenomes" ]

[ 2845, 3, 1, 31 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family YgbA

Uncharacterised_YgbA

1

IPR020484

20,484

Protein of unknown function DUF5503

DUF5503

Family

52

false

This is a family of unknown function found in Enterobacteriaceae. This family includes uncharacterised protein YedM.

[]

0

[ "PFAM" ]

[ "PF17607" ]

[ "DUF5503" ]

[ 52 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Enterobacteriaceae" ]

[ 52 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Protein of unknown function DUF5503

DUF5503

4

IPR020485

20,485

Stationary phase protein 4

Spg4

Family

62

false

Saccharomyces cerevisiae respond and cope to starvation by ceasing growth and entering a non-proliferating state referred to as stationary phase [ ]. Expression of SPG4 has been shown to be higher in stressed cells, and stationary phase cells compared to active cells. It is not required for growth on non-fermentable ca...

[]

0

[ "PFAM" ]

[ "PF17325" ]

[ "SPG4" ]

[ 62 ]

1

[]

0

[]

0

[ "PUB00074983", "PUB00085357" ]

[ "15456898", "27558777" ]

[ "Genomic analysis of stationary-phase and exit in Saccharomyces cerevisiae: gene expression and identification of novel essential genes.", "Quantitative proteomic comparison of stationary/G0 phase cells and tetrads in budding yeast." ]

[ 2004, 2016 ]

2

[]

0

null

[ "Saccharomycetes" ]

[ 62 ]

1

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

[ 1 ]

1

true

Family

Stationary phase protein 4

Spg4

9

IPR020489

20,489

Uncharacterised protein family YejG

Uncharacterised_YejG

Family

1,079

false

This entry contains proteins with no known function.

[]

0

[ "NCBIFAM", "PFAM" ]

[ "NF008811", "PF13989" ]

[ "PRK11835.1", "YejG" ]

[ 1052, 1079 ]

2

[]

0

[ "6bi6" ]

1

[]

0

[]

0

null

[ "Bacteria" ]

[ 1079 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family YejG

Uncharacterised_YejG

6

IPR020490

20,490

Uncharacterised protein family YaiZ

Uncharacterised_YaiZ

Family

726

false

This entry contains membrane proteins with no known function.

[]

0

[ "PFAM" ]

[ "PF10953" ]

[ "DUF2754" ]

[ 726 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Gammaproteobacteria" ]

[ 726 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family YaiZ

Uncharacterised_YaiZ

8

IPR020491

20,491

Biogenesis of lysosome-related organelles complex 1 subunit BLI1

BLI1

Family

64

false

This entry represents biogenesis of lysosome-related organelles complex 1 subunit BLI1. The complex is found on tubular endosomes and plays an important role in the biogenesis of lysosome-related organelles, possibly by facilitating cargo sorting into tubular carriers [ ].

[]

0

[ "PFAM" ]

[ "PF17324" ]

[ "BLI1" ]

[ 64 ]

1

[]

0

[]

0

[ "PUB00074975" ]

[ "25898163" ]

[ "BORC and BLOC-1: Shared Subunits in Trafficking Complexes." ]

[ 2015 ]

1

[]

0

null

[ "Saccharomycetaceae" ]

[ 64 ]

1

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

[ 1 ]

1

true

Family

Biogenesis of lysosome-related organelles complex 1 subunit BLI1

BLI1

2

IPR020493

20,493

Uncharacterised protein family HI0310

Uncharacterised_HI0310

Family

595

false

This entry contains proteins with no known function.

[]

0

[ "PFAM" ]

[ "PF17274" ]

[ "DUF5339" ]

[ 595 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria" ]

[ 595 ]

1

[]

0

true

Family

Uncharacterised protein family HI0310

Uncharacterised_HI0310

3

IPR020496

20,496

Sigma-M inhibitor YhdK

YhdK

Family

66

false

Extracytoplasmic function (ECF) sigma factors are a diverse family of proteins within the class of the sigma 70 subunit of RNA polymerase. Most members are known to regulate gene expression in response to stress conditions. The Bacillus subtilis genome encodes at least 17 distinct sigma factors, seven of which are memb...

[]

0

[ "PFAM" ]

[ "PF17453" ]

[ "Sigma_M_inh" ]

[ 66 ]

1

[]

0

[]

0

[ "PUB00034427", "PUB00046113" ]

[ "10216858", "14993308" ]

[ "Sigma M, an ECF RNA polymerase sigma factor of Bacillus subtilis 168, is essential for growth and survival in high concentrations of salt.", "Interaction of Bacillus subtilis extracytoplasmic function (ECF) sigma factors with the N-terminal regions of their potential anti-sigma factors." ]

[ 1999, 2004 ]

2

[]

0

null

[ "Bacillales" ]

[ 66 ]

1

[]

0

true

Family

Sigma-M inhibitor YhdK

YhdK

2

IPR020497

20,497

Protein of unknown function DUF5440

DUF5440

Family

13

false

This is a family of unknown function found in Proteobacteria.

[]

0

[ "PFAM" ]

[ "PF17509" ]

[ "DUF5440" ]

[ 13 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Birmingham IncP-alpha plasmid", "Pseudomonadati" ]

[ 1, 12 ]

2

[]

0

true

Family

Protein of unknown function DUF5440

DUF5440

6

IPR020500

20,500

Anti-RecBCD protein 2, bacteriophage P22

Phage_P22_anti-RecBCD_p2

Family

575

false

This phage protein modulates the activity of the host recBCD nuclease promoting phage growth and recombination and protects the linear double stranded DNA from exonuclease degradation [ , ].

[]

0

[ "PFAM" ]

[ "PF11043" ]

[ "Anti-RecBCD_p2" ]

[ 575 ]

1

[]

0

[ "8b1t", "8b1u" ]

2

[ "PUB00046144", "PUB00097480" ]

[ "3660589", "10669596" ]

[ "Sequence of the bacteriophage P22 anti-recBCD (abc) genes and properties of P22 abc region deletion mutants.", "Bacteriophage P22 Abc2 protein binds to RecC increases the 5' strand nicking activity of RecBCD and together with lambda bet, promotes Chi-independent recombination." ]

[ 1987, 2000 ]

2

[]

0

null

[ "Caudoviricetes", "Enterobacteriaceae" ]

[ 31, 544 ]

2

[]

0

true

Family

Anti-RecBCD protein 2, bacteriophage P22

Phage_P22_anti-RecBCD_p2

3

IPR020501

20,501

Uncharacterised protein family AF1218

Uncharacterised_AF1218

Family

243

false

This entry includes Uncharacterized protein AF_1218 found in archaea. Some members have a winged helix DNA-binding domain like.

[]

0

[ "PFAM" ]

[ "PF10826" ]

[ "DUF2551" ]

[ 243 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Cylicocyclus nassatus", "Methanobacteriota", "ecological metagenomes" ]

[ 1, 235, 7 ]

3

[]

0

true

Family

Uncharacterised protein family AF1218

Uncharacterised_AF1218

2

IPR020502

20,502

Late transcription unit B

LtuB

Family

28

false

Chlamydiae possess an intracellular developmental cycle defined by the interconversion of infectious, metabolically inactive elementary bodies and noninfectious, dividing reticulate bodies. The predicted peptides encoded by late genes ltuA and ltuB do not resemble known proteins, and their function is not known. The tr...

[]

0

[ "PFAM" ]

[ "PF17455" ]

[ "LtuB" ]

[ 28 ]

1

[]

0

[]

0

[ "PUB00052315" ]

[ "7543468" ]

[ "Characterization of late gene promoters of Chlamydia trachomatis." ]

[ 1995 ]

1

[]

0

null

[ "Chlamydia" ]

[ 28 ]

1

[]

0

true

Family

Late transcription unit B

LtuB

1

IPR020503

20,503

Uncharacterised protein family Rv2561

Uncharacterised_Rv2561

Family

804

false

This entry contains proteins with no known function.

[]

0

[ "PFAM" ]

[ "PF10851" ]

[ "DUF2652" ]

[ 804 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 792, 12 ]

2

[]

0

true

Family

Uncharacterised protein family Rv2561

Uncharacterised_Rv2561

4

IPR020504

20,504

Protein of unknown function DUF5500

DUF5500

Family

29

false

This is a family of unknown function found in Herpesvirus. The family includes uncharacterised protein UL19.

[]

0

[ "PFAM" ]

[ "PF17604" ]

[ "DUF5500" ]

[ 29 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Cytomegalovirus" ]

[ 29 ]

1

[]

0

true

Family

Protein of unknown function DUF5500

DUF5500

8

IPR020507

20,507

Protein of unknown function DUF5517

DUF5517

Family

13

false

This is a family of unknown function found in Fuselloviridae. Structure analysis suggest a role in viral assembly.

[]

0

[ "PFAM" ]

[ "PF17639" ]

[ "DUF5517" ]

[ 13 ]

1

[]

0

[ "4lid" ]

1

[]

0

[]

0

null

[ "Fuselloviridae", "Sulfolobaceae" ]

[ 8, 5 ]

2

[]

0

true

Family

Protein of unknown function DUF5517

DUF5517

6

IPR020510

20,510

Poly-beta-1,6-N-acetyl-D-glucosamine synthesis protein IcaD

IcaD

Family

113

false

IcaD is essential for the synthesis of poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also known as PIA), a biofilm adhesin polysaccharide. IcaD is required for full IcaA N-acetylglucosaminyltransferase activity [ ]. This entry is specific to Staphylococcaceae.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF27790", "TIGR03932" ]

[ "IcaD", "PIA_icaD" ]

[ 112, 64 ]

2

[]

0

[]

0

[ "PUB00046114" ]

[ "9660830" ]

[ "Characterization of the N-acetylglucosaminyltransferase activity involved in the biosynthesis of the Staphylococcus epidermidis polysaccharide intercellular adhesin." ]

[ 1998 ]

1

[]

0

null

[ "Bacteria", "human gut metagenome" ]

[ 112, 1 ]

2

[]

0

true

Family

Poly-beta-1,6-N-acetyl-D-glucosamine synthesis protein IcaD

IcaD

7

IPR020511

20,511

Uncharacterised protein family HI0941

Uncharacterised_HI0941

Family

193

false

This entry contains proteins with no known function.

[]

0

[ "PFAM" ]

[ "PF17344" ]

[ "DUF5374" ]

[ 193 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Pasteurellaceae" ]

[ 193 ]

1

[]

0

true

Family

Uncharacterised protein family HI0941

Uncharacterised_HI0941

8

IPR020513

20,513

Uncharacterised protein family, inner membrane YaiY

Uncharacterised_IM_YaiY

Family

695

false

This entry contains membrane proteins with no known function.

[ "GO:0016020" ]

[ "membrane" ]

[ "cellular_component" ]

1

[ "PFAM" ]

[ "PF10954" ]

[ "DUF2755" ]

[ 695 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Pseudomonadati", "human gut metagenome" ]

[ 693, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family, inner membrane YaiY

Uncharacterised_IM_YaiY

9

IPR020516

20,516

Uncharacterised protein family YxcD

Uncharacterised_YxcD

Family

875

false

This entry contains proteins with no known function.

[]

0

[ "PFAM" ]

[ "PF10850" ]

[ "DUF2653" ]

[ 875 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacilli" ]

[ 875 ]

1

[]

0

true

Family

Uncharacterised protein family YxcD

Uncharacterised_YxcD

5

IPR020518

20,518

Transcription regulator PrtN

Tscrpt_reg_PrtN

Family

1,684

false

PrtN is a transcriptional activator for pyocin synthesis genes [ ], and probably acts by binding to the sequences conserved in their 5' non-coding regions (P box) [ ].

[ "GO:0006355" ]

[ "regulation of DNA-templated transcription" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF11112" ]

[ "PyocinActivator" ]

[ 1684 ]

1

[]

0

[]

0

[ "PUB00052312", "PUB00058169" ]

[ "8444788", "16109947" ]

[ "Regulation of pyocin genes in Pseudomonas aeruginosa by positive (prtN) and negative (prtR) regulatory genes.", "PtrB of Pseudomonas aeruginosa suppresses the type III secretion system under the stress of DNA damage." ]

[ 1993, 2005 ]

2

[]

0

null

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

[ 1660, 16, 8 ]

3

[]

0

true

Family

Transcription regulator PrtN

Tscrpt_reg_PrtN

3

IPR020519

20,519

Divergent protein kinase domain 2A/B

DIPK2A/B

Family

2,210

false

DIPK2A, also known as DIA1 (deleted in autism protein 1), may play a role in cardiomyocyte proliferation through paracrine signaling and activation of the PPI3K-AKT-CDK7 signaling cascade [ ]. This entry also includes DIPK2B, whose function is not clear.

[]

0

[ "PANTHER" ]

[ "PTHR32073" ]

[ "" ]

[ 2210 ]

1

[]

0

[]

0

[ "PUB00089889" ]

[ "23784961" ]

[ "C3orf58, a novel paracrine protein, stimulates cardiomyocyte cell-cycle progression through the PI3K-AKT-CDK7 pathway." ]

[ 2013 ]

1

[]

0

null

[ "Eumetazoa" ]

[ 2210 ]

1

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

[ 7, 1, 8, 4, 5 ]

5

true

Family

Divergent protein kinase domain 2A/B

DIPK2A/B

6

IPR020527

20,527

UL17, Cytomegalovirus

UL17_Cytomegalovir

Family

25

false

This family consists of UL17 proteins from Cytomegalovirus, mainly from Human cytomegalovirus (HCMV), also known as Human herpesvirus 5 (HHV-5). Its function is not known [ ].

[]

0

[ "PFAM" ]

[ "PF17640" ]

[ "UL17" ]

[ 25 ]

1

[ "REACTOME" ]

[ "R-HSA-9609690" ]

[ "REACTOME:R-HSA-9609690" ]

1

[]

0

[ "PUB00083276" ]

[ "14623981" ]

[ "Functional profiling of a human cytomegalovirus genome." ]

[ 2003 ]

1

[]

0

null

[ "Cytomegalovirus" ]

[ 25 ]

1

[]

0

true

Family

UL17, Cytomegalovirus

UL17_Cytomegalovir

3

IPR020529

20,529

Origin recognition complex, subunit 6, metazoa/plant

ORC6_met/pln

Family

2,087

false

The Origin Recognition Complex (ORC) is a six-subunit ATP-dependent DNA-binding complex encoded by ORC1-6 [ ]. ORC is a central component for eukaryotic DNA replication, and binds chromatin at replication origins throughout the cell cycle [ ]. ORC directs DNA replication throughout the genome and is required for its in...

[ "GO:0006260", "GO:0005664" ]

[ "DNA replication", "nuclear origin of replication recognition complex" ]

[ "biological_process", "cellular_component" ]

2

[ "PANTHER" ]

[ "PTHR13394" ]

[ "" ]

[ 2087 ]

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-176187", "R-BTA-68616", "R-BTA-68689", "R-BTA-68949", "R-BTA-68962", "R-DDI-68616", "R-DDI-68689", "R-DDI-68962", "R-DME-176187", "R-DME-68616", "R-DME-68689", "R-DME-68949", "R-DME-68962", "R-HSA-113507", "R-HSA-176187", "R-HSA-68616", "R-HSA-68689", "R-HSA-68867", "R-HSA...

[ "REACTOME:R-BTA-176187", "REACTOME:R-BTA-68616", "REACTOME:R-BTA-68689", "REACTOME:R-BTA-68949", "REACTOME:R-BTA-68962", "REACTOME:R-DDI-68616", "REACTOME:R-DDI-68689", "REACTOME:R-DDI-68962", "REACTOME:R-DME-176187", "REACTOME:R-DME-68616", "REACTOME:R-DME-68689", "REACTOME:R-DME-68949", "R...

30

[ "3m03", "6kvg", "7jgr", "7jgs", "7jk2", "7jk3", "7jk4", "7jk5", "7jk6", "8s0b", "8s0d" ]

11

[ "PUB00052559", "PUB00052560", "PUB00052561", "PUB00052562", "PUB00052563", "PUB00052564", "PUB00052565", "PUB00052566", "PUB00052567", "PUB00052568", "PUB00052569", "PUB00052570", "PUB00052571", "PUB00052572", "PUB00052573", "PUB00052574", "PUB00052575", "PUB00052576", "PUB000525...

[ "17241905", "17825065", "1579162", "7585959", "16716188", "7892251", "7781615", "16228006", "10966477", "12045100", "15680967", "11572976", "11429609", "16024805", "8622770", "9171055", "9038340", "11459976", "15610739", "16387651", "17053779", "9442876", "31160578", "3...

[ "Multiple functions of the origin recognition complex.", "Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: interaction between subunits and identification of binding proteins.", "ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex....

[ 2007, 2007, 1992, 1995, 2006, 1995, 1995, 2005, 2000, 2002, 2005, 2001, 2001, 2005, 1996, 1997, 1997, 2001, 2004, 2006, 2006, 1997, 2019, 2020 ]

24

[]

0

null

[ "Eukaryota" ]

[ 2087 ]

1

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

[ 4, 1, 1, 5, 6, 1, 5, 1, 5 ]

9

true

Family

Origin recognition complex, subunit 6, metazoa/plant

ORC6_met/pln

8

IPR020532

20,532

Cycloeucalenol cycloisomerase

Cycloeucalenol_cycloisomerase

Family

1,005

false

This entry represents the enzyme cycloeucalenol cycloisomerase ( ) and is involved in the synthesis of plant sterols, by converting pentacyclic cyclopropyl sterols to tetracyclic sterols [ ]. In Arabidopsis thaliana (Mouse-ear cress), cycloeucalenol cycloisomerase functions during and just after division and supports g...

[ "GO:0047793" ]

[ "cycloeucalenol cycloisomerase activity" ]

[ "molecular_function" ]

1

[ "PANTHER" ]

[ "PTHR35136" ]

[ "" ]

[ 1005 ]

1

[]

0

[]

0

[ "PUB00046127", "PUB00052426" ]

[ "10788449", "18223643" ]

[ "Functional cloning of an Arabidopsis thaliana cDNA encoding cycloeucalenol cycloisomerase.", "Sterol-dependent endocytosis mediates post-cytokinetic acquisition of PIN2 auxin efflux carrier polarity." ]

[ 2000, 2008 ]

2

[]

0

null

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

[ 33, 971, 1 ]

3

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

[ 7, 5, 5 ]

3

true

Family

Cycloeucalenol cycloisomerase

Cycloeucalenol_cycloisomerase

9

IPR020533

20,533

Developmental regulator, ULTRAPETALA

Developmental_reg_ULTRAPETALA

Family

1,149

false

This entry represents a developmental regulator that acts as a key negative regulator of cell accumulation in shoot and floral meristems. Negatively regulates the size of the WUSCHEL (WUS)-expressing organising centre in inflorescence meristems. May act by down-regulating expression of WUS and can compensate for mutant...

[]

0

[ "PANTHER" ]

[ "PTHR34053" ]

[ "" ]

[ 1149 ]

1

[]

0

[]

0

[ "PUB00052440" ]

[ "15673576" ]

[ "ULTRAPETALA1 encodes a SAND domain putative transcriptional regulator that controls shoot and floral meristem activity in Arabidopsis." ]

[ 2005 ]

1

[]

0

null

[ "Streptophyta" ]

[ 1149 ]

1

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

[ 8, 5, 7 ]

3

true

Family

Developmental regulator, ULTRAPETALA

Developmental_reg_ULTRAPETALA

9

IPR020534

20,534

Uncharacterised protein family YqxA

Uncharacterised_YqxA

Family

806

false

This entry contains proteins from bacillales with no known function. Members are predicted to contain predicted transmembrane regions.

[]

0

[ "PFAM" ]

[ "PF12438" ]

[ "DUF3679" ]

[ 806 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacillales" ]

[ 806 ]

1

[]

0

true

Family

Uncharacterised protein family YqxA

Uncharacterised_YqxA

1

IPR020536

20,536

Thil, AANH domain

ThiI_AANH

Domain

11,875

false

This entry represents the AANH domain. Three domains of ThiI are essential for the thiolation of tRNA: a THUMP domain that binds tRNA (see ) [ ], an AANH domain ( ) that activates the uridine residue by adenylylation [ ], and a rhodanese-like domain ( ) that transfers sulfur to the activated uridine residue [ ]. Neithe...

[ "GO:0004810" ]

[ "CCA tRNA nucleotidyltransferase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "CDD" ]

[ "PF02568", "cd01712" ]

[ "ThiI", "PPase_ThiI" ]

[ 11875, 9656 ]

2

[ "EC" ]

[ "2.8.1.4" ]

[ "EC:2.8.1.4" ]

1

[ "1vbk", "2c5s", "4kr6", "4kr7", "4kr9" ]

5

[ "PUB00008209", "PUB00017402", "PUB00039897", "PUB00057394", "PUB00057395", "PUB00060442" ]

[ "9209060", "11443125", "16343540", "16855700", "18604845", "21724998" ]

[ "Characterization of thiI, a new gene involved in thiazole biosynthesis in Salmonella typhimurium.", "The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA.", "Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domain."...

[ 1997, 2001, 2006, 2006, 2008, 2011 ]

6

[]

0

null

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

[ 945, 10634, 94, 5, 197 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Thil, AANH domain

ThiI_AANH

9

IPR020537

20,537

ATP synthase, F0 complex, subunit C, DCCD-binding site

ATP_synth_F0_csu_DDCD_BS

Binding_site

41,372

false

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

[]

0

[ "PROSITE" ]

[ "PS00605" ]

[ "ATPASE_C" ]

[ 41372 ]

1

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

[ "R-BTA-1268020", "R-BTA-163210", "R-BTA-8949613", "R-CEL-1268020", "R-CEL-163210", "R-CEL-8949613", "R-HSA-1268020", "R-HSA-163210", "R-HSA-8949613", "R-MMU-1268020", "R-MMU-163210", "R-MMU-8949613", "R-RNO-1268020", "R-RNO-163210", "R-RNO-8949613" ]

[ "REACTOME:R-BTA-1268020", "REACTOME:R-BTA-163210", "REACTOME:R-BTA-8949613", "REACTOME:R-CEL-1268020", "REACTOME:R-CEL-163210", "REACTOME:R-CEL-8949613", "REACTOME:R-HSA-1268020", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "REACTOME:R-MMU-1268020", "REACTOME:R-MMU-163210", "REACTOME:R-...

15

[ "1a91", "1aty", "1c0v", "1c17", "1c99", "1ijp", "1qo1", "1wu0", "1yce", "2w5j", "2wgm", "2wie", "2wpd", "2x2v", "2xnd", "2xok", "2xqs", "2xqt", "2xqu", "3u2f", "3u2y", "3u32", "3ud0", "3v3c", "3zk1", "3zk2", "3zo6", "3zry", "4b2q", "4bem", "4cbj", "4cbk"...

320

[ "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020632", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]

[ "11309608", "15473999", "15078220", "14630314", "20450191", "18937357", "1385979", "9741106" ]

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

[ 2001, 2004, 2004, 2003, 2010, 2008, 1992, 1998 ]

8

[]

0

null

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

[ 20045, 20955, 1, 371 ]

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",...

[ 7, 1, 3, 3, 1, 8, 4, 2, 6, 10, 1, 1, 4 ]

13

true

Binding_site

ATP synthase, F0 complex, subunit C, DCCD-binding site

ATP_synth_F0_csu_DDCD_BS

5

IPR020539

20,539

Ribonuclease P, conserved site

RNase_P_CS

Conserved_site

15,566

false

Ribonuclease P ( ) (RNase P) [ , , ] is a site specific endonuclease that generates mature tRNAs by catalysing the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. In bacteria RNase P is known to be composed of two components: a...

[ "GO:0004526" ]

[ "ribonuclease P activity" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS00648" ]

[ "RIBONUCLEASE_P" ]

[ 15566 ]

1

[ "EC" ]

[ "3.1.26.5" ]

[ "EC:3.1.26.5" ]

1

[ "1a6f", "1d6t", "1nz0", "2ljp", "3q1q", "3q1r", "4jg4", "6cqc", "6d1r", "6max", "6ov1", "7uo0", "7uo1", "7uo2", "7uo5" ]

15

[ "PUB00002589", "PUB00002604", "PUB00004402" ]

[ "1700778", "1689306", "1374553" ]

[ "Ribonuclease P. Postscript.", "Ribonuclease P: function and variation.", "Ribonuclease P RNA and protein subunits from bacteria." ]

[ 1990, 1990, 1992 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "candidate division MSBL1 archaeon SCGC-AAA382N08", "unclassified sequences", "uncultured marine phage" ]

[ 15291, 42, 1, 231, 1 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Conserved_site

Ribonuclease P, conserved site

RNase_P_CS

6

IPR020541

20,541

Chorismate synthase, conserved site

Chorismate_synthase_CS

Conserved_site

28,838

false

Chorismate synthase (CS; 5-enolpyruvylshikimate-3-phosphate phospholyase; 1-carboxyvinyl-3-phosphoshikimate phosphate-lyase; E.C. 4.2.3.5) catalyzes the seventh and final step in the shikimate pathway which is used in prokaryotes, fungi and plants for the biosynthesis of aromatic amino acids. It catalyzes the 1,4-trans...

[ "GO:0004107", "GO:0009073" ]

[ "chorismate synthase activity", "aromatic amino acid family biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE", "PROSITE", "PROSITE" ]

[ "PS00787", "PS00788", "PS00789" ]

[ "CHORISMATE_SYNTHASE_1", "CHORISMATE_SYNTHASE_2", "CHORISMATE_SYNTHASE_3" ]

[ 25569, 24989, 23916 ]

3

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

[ "4.2.3.5", "PWY-6163", "R-MTU-964903" ]

[ "EC:4.2.3.5", "METACYC:PWY-6163", "REACTOME:R-MTU-964903" ]

3

[ "1q1l", "1qxo", "1r52", "1r53", "1sq1", "1um0", "1umf", "1ztb", "2g85", "2o11", "2o12", "2qhf", "4bai", "4baj", "4ecd", "4lj2", "4o90", "4ob9", "5wuy", "5z9a", "7rca" ]

21

[ "PUB00002667", "PUB00003811", "PUB00030073", "PUB00030439", "PUB00030526", "PUB00031826", "PUB00039012", "PUB00079715", "PUB00079716", "PUB00079717", "PUB00079718", "PUB00079719" ]

[ "1718979", "1837329", "14705034", "14656434", "14573601", "15095868", "16459102", "17348836", "17662045", "8674765", "18279385", "17326665" ]

[ "Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers.", "Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae.", "Crystal structure of chorismate syntha...

[ 1991, 1991, 2004, 2003, 2004, 2004, 2006, 2007, 2007, 1996, 2008, 2007 ]

12

[]

0

null

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

[ 827, 24336, 3056, 6, 613 ]

5

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

[ 6, 1, 1, 2, 1, 1, 21 ]

7

true

Conserved_site

Chorismate synthase, conserved site

Chorismate_synthase_CS

8

IPR020545

20,545

Aspartate carbamoyltransferase regulatory subunit, N-terminal

Asp_carbamoyltransf_reg_N

Domain

4,644

false

Aspartate carbamoyltransferase (aspartate transcarbamylase, ATCase) is an allosteric enzyme that plays a central role in the regulation of the pyrimidine pathway in bacteria. The holoenzyme is a dodecamer composed of six catalytic chains, each with an active site, and six regulatory chains lacking catalytic activity [ ...

[]

0

[ "PFAM" ]

[ "PF01948" ]

[ "PyrI" ]

[ 4644 ]

1

[]

0

[ "1acm", "1at1", "1d09", "1ezz", "1f1b", "1i5o", "1nbe", "1pg5", "1q95", "1r0b", "1r0c", "1raa", "1rab", "1rac", "1rad", "1rae", "1raf", "1rag", "1rah", "1rai", "1sku", "1tth", "1tu0", "1tug", "1xjw", "1za1", "1za2", "2a0f", "2air", "2at1", "2atc", "2be7"...

66

[ "PUB00006327", "PUB00006462", "PUB00006470", "PUB00014302" ]

[ "7791626", "10600394", "10651286", "11323717" ]

[ "Cooperativity in enzyme function: equilibrium and kinetic aspects.", "Intramolecular signal transmission in enterobacterial aspartate transcarbamylases II. Engineering co-operativity and allosteric regulation in the aspartate transcarbamylase of Erwinia herbicola.", "Insights into the mechanisms of catalysis a...

[ 1995, 1999, 1999, 2001 ]

4

[]

0

null

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

[ 864, 3652, 23, 105 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Aspartate carbamoyltransferase regulatory subunit, N-terminal

Asp_carbamoyltransf_reg_N

8

IPR020546

20,546

ATP synthase, F1 complex, delta/epsilon subunit, N-terminal

ATP_synth_F1_dsu/esu_N

Domain

44,085

false

This family represents subunits called delta (in mitochondrial ATPase) or epsilon (in bacteria or chloroplast ATPase). The interaction site of subunit C of the F0 complex with the delta or epsilon subunit of the F1 complex may be important for connecting the rotor of F1 (gamma subunit) to the rotor of F0 (C subunit) [ ...

[ "GO:0015986" ]

[ "proton motive force-driven ATP synthesis" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF02823" ]

[ "ATP-synt_DE_N" ]

[ 44085 ]

1

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

[ "GenProp0128", "R-BTA-163210", "R-BTA-8949613", "R-CEL-163210", "R-CEL-8949613", "R-HSA-163210", "R-HSA-8949613", "R-MMU-163210", "R-MMU-8949613", "R-RNO-163210", "R-RNO-8949613" ]

[ "GP:GenProp0128", "REACTOME:R-BTA-163210", "REACTOME:R-BTA-8949613", "REACTOME:R-CEL-163210", "REACTOME:R-CEL-8949613", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "REACTOME:R-MMU-163210", "REACTOME:R-MMU-8949613", "REACTOME:R-RNO-163210", "REACTOME:R-RNO-8949613" ]

11

[ "1aqt", "1bsh", "1bsn", "1e79", "1fs0", "1h8e", "1qo1", "2ck3", "2e5y", "2hld", "2jdi", "2qe7", "2rq6", "2rq7", "2v7q", "2w6h", "2w6i", "2w6j", "2wpd", "2wss", "2xnd", "2xok", "3fks", "3oaa", "3oe7", "3oee", "3oeh", "3ofn", "3zia", "3zry", "4asu", "4b2q"...

294

[ "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020606", "PUB00035968", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]

[ "11309608", "15473999", "15078220", "12887009", "16707672", "20450191", "18937357", "1385979", "9741106" ]

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

[ 2001, 2004, 2004, 2003, 2006, 2010, 2008, 1992, 1998 ]

9

[]

0

null

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

[ 28, 24685, 18875, 497 ]

4

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

[ 6, 1, 1, 1, 1, 2, 5, 1, 9, 6, 1, 1, 12 ]

13

true

Domain

ATP synthase, F1 complex, delta/epsilon subunit, N-terminal

ATP_synth_F1_dsu/esu_N

1

IPR020547

20,547

ATP synthase epsilon subunit, C-terminal domain

ATP_synth_F1_esu_C

Domain

26,097

false

This entry represents the C-terminal long α-helix domain of ATPase subunit epsilon (in bacteria or chloroplast ATPase) from bacteria and plants [ ]. The interaction site of subunit C of the F0 complex with the delta or epsilon subunit of the F1 complex may be important for connecting the rotor of F1 (gamma subunit) to ...

[]

0

[ "PFAM", "PFAM" ]

[ "PF00401", "PF27469" ]

[ "ATP-synt_DE", "ATP_synt_eps_C" ]

[ 24858, 1239 ]

2

[]

0

[ "1aqt", "1bsh", "1bsn", "1fs0", "1qo1", "2e5t", "2e5u", "2e5y", "2qe7", "2rq6", "2rq7", "3oaa", "4xd7", "5hkk", "5ik2", "5t4o", "5t4p", "5t4q", "5zwl", "6fkf", "6fkh", "6fki", "6n2y", "6n2z", "6n30", "6oqr", "6oqs", "6oqt", "6oqu", "6oqv", "6oqw", "6pqv"...

64

[ "PUB00019175", "PUB00020606", "PUB00035968" ]

[ "9331422", "12887009", "16707672" ]

[ "Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli.", "ATP synthases: insights into their motor functions from sequence and structural analyses.", "Inhibition of ATP hydrolysis by thermoalkaliphilic F1Fo-ATP synthase is controlled by the C terminus of the ep...

[ 1997, 2003, 2006 ]

3

[]

0

null

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

[ 11141, 14766, 190 ]

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" ]

[ 4, 1, 1, 6, 7 ]

5

true

Domain

ATP synthase epsilon subunit, C-terminal domain

ATP_synth_F1_esu_C

1

IPR020548

20,548

Fructose-1,6-bisphosphatase, active site

Fructose_bisphosphatase_AS

Active_site

13,311

false

This entry represents fructose-1,6-bisphosphatase (FBPase), a critical regulatory enzyme in gluconeogenesis that catalyses the removal of 1-phosphate from fructose 1,6-bis-phosphate to form fructose 6-phosphate [ , ]. It is involved in many different metabolic pathways and found in most organisms. FBPase requires metal...

[ "GO:0042578", "GO:0005975" ]

[ "phosphoric ester hydrolase activity", "carbohydrate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE" ]

[ "PS00124" ]

[ "FBPASE" ]

[ 13311 ]

1

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

[ "3.1.3.11", "PWY-5484", "R-BTA-70263", "R-DDI-70263", "R-HSA-70263", "R-MMU-70263", "R-RNO-70263", "R-SCE-70263", "R-SPO-70263", "R-SSC-70263" ]

[ "EC:3.1.3.11", "METACYC:PWY-5484", "REACTOME:R-BTA-70263", "REACTOME:R-DDI-70263", "REACTOME:R-HSA-70263", "REACTOME:R-MMU-70263", "REACTOME:R-RNO-70263", "REACTOME:R-SCE-70263", "REACTOME:R-SPO-70263", "REACTOME:R-SSC-70263" ]

10

[ "1bk4", "1cnq", "1d9q", "1dbz", "1dcu", "1eyi", "1eyj", "1eyk", "1fbc", "1fbd", "1fbe", "1fbf", "1fbg", "1fbh", "1fbp", "1fj6", "1fj9", "1fpb", "1fpd", "1fpe", "1fpf", "1fpg", "1fpi", "1fpj", "1fpk", "1fpl", "1frp", "1fsa", "1fta", "1kz8", "1lev", "1nuw"...

151

[ "PUB00000153", "PUB00000179", "PUB00000219", "PUB00001414", "PUB00003256", "PUB00004864" ]

[ "2159755", "3008716", "8382485", "1374332", "2157849", "7761465" ]

[ "Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase.", "Amino acid sequence homology among fructose-1,6-bisphosphatases.", "Structural similarities between fructose-1,6-bisphosphatase and inositol monophosphatase.", "cDNA and gene sequences of wheat chloroplast sedoheptulose-1,7-bisphospha...

[ 1990, 1986, 1993, 1992, 1990, 1995 ]

6

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Homavirus sp.", "metagenomes" ]

[ 65, 5595, 7588, 1, 62 ]

5

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

[ 8, 1, 4, 3, 1, 5, 4, 2, 9, 5, 1, 1, 22 ]

13

true

Active_site

Fructose-1,6-bisphosphatase, active site

Fructose_bisphosphatase_AS

2

IPR020549

20,549

Endoribonuclease YbeY, conserved site

YbeY_CS

Conserved_site

23,362

false

YbeY is a single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. It acts together with the RNase R to eliminate defective 70S ribosomes, but not properly matured 70S ribosomes or individual subunits, by a process mediated...

[]

0

[ "PROSITE" ]

[ "PS01306" ]

[ "UPF0054" ]

[ 23362 ]

1

[]

0

[ "1oz9", "1tvi", "1xax", "1xm5", "7y7o" ]

5

[ "PUB00038326", "PUB00064741", "PUB00064742", "PUB00064743" ]

[ "16511207", "20639334", "20807199", "23273979" ]

[ "The ybeY protein from Escherichia coli is a metalloprotein.", "The heat shock protein YbeY is required for optimal activity of the 30S ribosomal subunit.", "Role of Escherichia coli YbeY, a highly conserved protein, in rRNA processing.", "Conserved Bacterial RNase YbeY Plays Key Roles in 70S Ribosome Quality...

[ 2005, 2010, 2010, 2013 ]

4

[]

0

null

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

[ 20840, 2080, 2, 440 ]

4

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

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

8

true

Conserved_site

Endoribonuclease YbeY, conserved site

YbeY_CS

5

IPR020550

20,550

Inositol monophosphatase, conserved site

Inositol_monophosphatase_CS

Conserved_site

44,723

false

This entry represents a conserved signature pattern found within the inositol monophosphatase family of proteins. It is suggested [ ] that these proteins may act by enhancing the synthesis or degradation of phosphorylated messenger molecules. It has been shown that several proteins share two sequence motifs [ ]. Two of...

[ "GO:0046854" ]

[ "phosphatidylinositol phosphate biosynthetic process" ]

[ "biological_process" ]

1

[ "PROSITE" ]

[ "PS00630" ]

[ "IMP_2" ]

[ 44723 ]

1

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

[ "3.1.3", "R-BTA-156584", "R-BTA-1855183", "R-CEL-1855183", "R-DDI-156584", "R-DDI-1855183", "R-DME-156584", "R-DRE-156584", "R-HSA-156584", "R-HSA-1855183", "R-MMU-156584", "R-MMU-1855183", "R-RNO-156584", "R-RNO-1855183", "R-SCE-1855183", "R-SSC-156584", "R-XTR-156584" ]

[ "EC:3.1.3", "REACTOME:R-BTA-156584", "REACTOME:R-BTA-1855183", "REACTOME:R-CEL-1855183", "REACTOME:R-DDI-156584", "REACTOME:R-DDI-1855183", "REACTOME:R-DME-156584", "REACTOME:R-DRE-156584", "REACTOME:R-HSA-156584", "REACTOME:R-HSA-1855183", "REACTOME:R-MMU-156584", "REACTOME:R-MMU-1855183", ...

17

[ "1awb", "1dk4", "1g0h", "1g0i", "1ima", "1imb", "1imc", "1imd", "1ime", "1imf", "1inp", "1jp4", "1k9y", "1k9z", "1ka0", "1ka1", "1lbv", "1lbw", "1lbx", "1lby", "1lbz", "1qgx", "2bji", "2czh", "2czi", "2czk", "2ddk", "2fvz", "2hhm", "2p3n", "2p3v", "2q74"...

66

[ "PUB00000822", "PUB00001628", "PUB00004864" ]

[ "2553271", "1660408", "7761465" ]

[ "Neural and developmental actions of lithium: a unifying hypothesis.", "Diverse proteins homologous to inositol monophosphatase.", "Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure." ]

[ 1989, 1991, 1995 ]

3

[]

0

null

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

[ 221, 28984, 14963, 555 ]

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",...

[ 12, 4, 9, 16, 2, 14, 18, 2, 17, 26, 3, 1, 21 ]

13

true

Conserved_site

Inositol monophosphatase, conserved site

Inositol_monophosphatase_CS

1

IPR020552

20,552

Inositol monophosphatase, lithium-sensitive

Inositol_monoPase_Li-sen

Family

4,502

false

It has been shown that several proteins share two sequence motifs [ ]. Two of these proteins, vertebrate and plant inositol monophosphatase ( ), and vertebrate inositol polyphosphate 1-phosphatase ( ), are enzymes of the inositol phosphate second messenger signalling pathway, and share similar enzyme activity. Both enz...

[ "GO:0046854" ]

[ "phosphatidylinositol phosphate biosynthetic process" ]

[ "biological_process" ]

1

[ "PRINTS" ]

[ "PR00378" ]

[ "LIIMPHPHTASE" ]

[ 4502 ]

1

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

[ "3.1.3.25", "PWY-2301", "PWY-4702", "PWY-6363", "R-BTA-1855183", "R-CEL-1855183", "R-HSA-1855183", "R-MMU-1855183", "R-RNO-1855183" ]

[ "EC:3.1.3.25", "METACYC:PWY-2301", "METACYC:PWY-4702", "METACYC:PWY-6363", "REACTOME:R-BTA-1855183", "REACTOME:R-CEL-1855183", "REACTOME:R-HSA-1855183", "REACTOME:R-MMU-1855183", "REACTOME:R-RNO-1855183" ]

9

[ "1awb", "1ima", "1imb", "1imc", "1imd", "1ime", "1imf", "2bji", "2czh", "2czi", "2czk", "2ddk", "2fvz", "2hhm", "4as4", "4as5", "6giu", "6gj0", "6zk0", "7vce" ]

20

[ "PUB00000822", "PUB00001628", "PUB00004864", "PUB00032773", "PUB00046132" ]

[ "2553271", "1660408", "7761465", "15858264", "10822345" ]

[ "Neural and developmental actions of lithium: a unifying hypothesis.", "Diverse proteins homologous to inositol monophosphatase.", "Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure.", "High-resolution structure of myo-in...

[ 1989, 1991, 1995, 2005, 2000 ]

5

[ "IPR033942" ]

[]

1

0

1

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

[ 253, 4244, 1, 4 ]

4

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

[ 3, 1, 3, 11, 9, 12, 3, 8, 1 ]

9

true

Family

Inositol monophosphatase, lithium-sensitive

Inositol_monoPase_Li-sen

1

IPR020554

20,554

Uncharacterised protein family UPF0021, conserved site

UPF0021_CS

Conserved_site

1,984

false

The following uncharacterised proteins have been shown to share regions of similarities, yeast chromosome VII hypothetical protein YGL211w; Dictyostelium discoideum (Slime mold) protein veg136; and Methanocaldococcus jannaschii (Methanococcus jannaschii) hypothetical proteins MJ1157 and MJ1478. The signature in this en...

[]

0

[ "PROSITE" ]

[ "PS01263" ]

[ "UPF0021" ]

[ 1984 ]

1

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

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

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

18

[]

0

[]

0

[]

0

null

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

[ 135, 20, 1827, 2 ]

4

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

[ 3, 1, 1, 1, 1 ]

5

true

Conserved_site

Uncharacterised protein family UPF0021, conserved site

UPF0021_CS

2

IPR020555

20,555

2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, conserved site

MECDP_synthase_CS

Conserved_site

21,114

false

IspF is a MECDP (2-C-methyl-D-erythritol 2,4-cyclodiphosphate) synthetase, also known as YgbB. It is an enzyme in the non-mevalonate pathway of isoprenoid synthesis. Isoprenoids are essential in all organisms, and can also be synthesized through the mevalonate pathway. The non-mevolante route is used by many bacteria a...

[ "GO:0008685" ]

[ "2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS01350" ]

[ "ISPF" ]

[ 21114 ]

1

[ "EC", "METACYC" ]

[ "4.6.1.12", "PWY-7560" ]

[ "EC:4.6.1.12", "METACYC:PWY-7560" ]

2

[ "1gx1", "1h47", "1h48", "1iv1", "1iv2", "1iv3", "1iv4", "1jn1", "1jy8", "1knj", "1knk", "1t0a", "1u3l", "1u3p", "1u40", "1u43", "1vh8", "1vha", "1w55", "1w57", "1yqn", "2amt", "2gzl", "2pmp", "2uzh", "3b6n", "3elc", "3eor", "3ern", "3esj", "3f0d", "3f0e"...

71

[ "PUB00021869", "PUB00056865" ]

[ "12499535", "15233799" ]

[ "Structure and catalytic mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) synthase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis.", "Biosynthesis of isoprenoids: a bifunctional IspDF enzyme from Campylobacter jejuni." ]

[ 2003, 2004 ]

2

[]

0

null

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

[ 4, 19658, 998, 454 ]

4

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

[ 5, 1, 2, 8 ]

4

true

Conserved_site

2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, conserved site

MECDP_synthase_CS

1

IPR020556

20,556

Amidase, conserved site

Amidase_CS

Conserved_site

65,654

false

Amidase signature (AS) enzymes are a large group of hydrolytic enzymes that contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being found in both prokaryotes and eukaryotes. AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has dive...

[]

0

[ "PROSITE" ]

[ "PS00571" ]

[ "AMIDASES" ]

[ 65654 ]

1

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

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

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

7

[ "1mt5", "2dc0", "2df4", "2dqn", "2f2a", "2g5h", "2g5i", "2gi3", "2vya", "2wap", "2wj1", "2wj2", "3a1k", "3a2p", "3al0", "3h0l", "3h0m", "3h0r", "3ip4", "3k7f", "3k83", "3k84", "3kfu", "3lj6", "3lj7", "3oj8", "3ppm", "3pr0", "3qj8", "3qj9", "3qk5", "3qkv"...

46

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

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

[ "Probing the Ser-Ser-Lys catalytic triad mechanism of peptide amidase: computational studies of the ground state, transition state, and intermediate.", "A second fatty acid amide hydrolase with variable distribution among placental mammals.", "Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalyti...

[ 2004, 2006, 2002, 2002 ]

4

[]

0

null

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

[ 1123, 45530, 18088, 1, 912 ]

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...

[ 12, 5, 13, 1, 3, 4, 3, 8, 3, 2, 3, 19 ]

12

true

Conserved_site

Amidase, conserved site

Amidase_CS

6

IPR020557

20,557

Fumarate lyase, conserved site

Fumarate_lyase_CS

Conserved_site

110,436

false

A number of enzymes, belonging to the lyase class, for which fumarate is a substrate, have been shown to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes [ ]. The following are examples of members of this family: : 3-carboxymuconate lacton...

[ "GO:0003824" ]

[ "catalytic activity" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS00163" ]

[ "FUMARATE_LYASES" ]

[ 110436 ]

1

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

[ "4.3.2.1", "PWY-4983", "PWY-4984", "PWY-5", "PWY-5154", "PWY-7400", "R-BTA-70635", "R-CEL-71403", "R-CEL-73817", "R-CEL-9837999", "R-DDI-71403", "R-DDI-9837999", "R-DRE-71403", "R-GGA-419140", "R-GGA-421203", "R-HSA-70635", "R-HSA-71403", "R-HSA-73817", "R-HSA-9837999", "R-MMU-...

[ "EC:4.3.2.1", "METACYC:PWY-4983", "METACYC:PWY-4984", "METACYC:PWY-5", "METACYC:PWY-5154", "METACYC:PWY-7400", "REACTOME:R-BTA-70635", "REACTOME:R-CEL-71403", "REACTOME:R-CEL-73817", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-71403", "REACTOME:R-DDI-9837999", "REACTOME:R-DRE-71403", "REACTO...

36

[ "1aos", "1auw", "1c3c", "1c3u", "1dcn", "1dof", "1f1o", "1fuo", "1fup", "1fuq", "1fur", "1hy0", "1hy1", "1j3u", "1jsw", "1kq7", "1q5n", "1re5", "1tj7", "1tju", "1tjv", "1tjw", "1u15", "1u16", "1vdk", "1xwo", "1yfe", "1yfm", "1yis", "2e9f", "2fel", "2fen"...

112

[ "PUB00000374", "PUB00000586", "PUB00004940", "PUB00083219", "PUB00083220" ]

[ "1390752", "3282546", "1574589", "26639528", "27750034" ]

[ "3-Carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: a new reaction in the evolution of a mechanistic motif.", "Two biochemically distinct classes of fumarase in Escherichia coli.", "De novo purine nucleotide biosynthesis.", "Ustilago maydis pro...

[ 1992, 1988, 1992, 2016, 2016 ]

5

[]

0

null

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

[ 1383, 91766, 15810, 13, 1464 ]

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",...

[ 27, 2, 6, 16, 6, 30, 9, 3, 11, 12, 3, 4, 34 ]

13

true

Conserved_site

Fumarate lyase, conserved site

Fumarate_lyase_CS

9

IPR020559

20,559

Phosphoribosylglycinamide synthetase, conserved site

PRibGlycinamide_synth_CS

Conserved_site

26,158

false

Phosphoribosylglycinamide synthetase ( ) (GARS) (phosphoribosylamine glycine ligase) [ ] catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by phosphoribosylglycinamide synthetase is the ATP-dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide: ...

[ "GO:0004637", "GO:0009113" ]

[ "phosphoribosylamine-glycine ligase activity", "purine nucleobase biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE" ]

[ "PS00184" ]

[ "GARS" ]

[ 26158 ]

1

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

[ "6.3.4.13", "PWY-6121", "PWY-6122", "PWY-6277", "R-BTA-73817", "R-DME-73817", "R-GGA-419140", "R-HSA-73817", "R-MMU-73817", "R-SCE-73817", "R-SPO-73817" ]

[ "EC:6.3.4.13", "METACYC:PWY-6121", "METACYC:PWY-6122", "METACYC:PWY-6277", "REACTOME:R-BTA-73817", "REACTOME:R-DME-73817", "REACTOME:R-GGA-419140", "REACTOME:R-HSA-73817", "REACTOME:R-MMU-73817", "REACTOME:R-SCE-73817", "REACTOME:R-SPO-73817" ]

11

[ "1vkz", "2ip4", "2qk4", "2xcl", "2xd4", "2yrw", "2yrx", "2ys6", "2ys7", "2yw2", "2yya", "3lp8", "3mjf", "5vev", "7lvo" ]

15

[ "PUB00002527", "PUB00075622", "PUB00075625" ]

[ "2687276", "2147474", "3097325" ]

[ "Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli.", "De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-gly...

[ 1989, 1990, 1986 ]

3

[]

0

null

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

[ 659, 20530, 4511, 2, 456 ]

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",...

[ 3, 1, 4, 5, 1, 5, 4, 1, 5, 5, 1, 1, 15 ]

13

true

Conserved_site

Phosphoribosylglycinamide synthetase, conserved site

PRibGlycinamide_synth_CS

9

IPR020560

20,560

Phosphoribosylglycinamide synthetase, C-domain

PRibGlycinamide_synth_C-dom

Domain

31,722

false

Phosphoribosylglycinamide synthetase ( ) (GARS) (phosphoribosylamine glycine ligase) [ ] catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by phosphoribosylglycinamide synthetase is the ATP-dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide: ...

[ "GO:0004637", "GO:0009113" ]

[ "phosphoribosylamine-glycine ligase activity", "purine nucleobase biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "SMART" ]

[ "PF02843", "SM01210" ]

[ "GARS_C", "GARS_C" ]

[ 31281, 31708 ]

2

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

[ "6.3.4.13", "PWY-6121", "PWY-6122", "PWY-6277", "R-BTA-73817", "R-DDI-73817", "R-DME-73817", "R-GGA-419140", "R-HSA-73817", "R-MMU-73817", "R-SCE-73817", "R-SPO-73817" ]

[ "EC:6.3.4.13", "METACYC:PWY-6121", "METACYC:PWY-6122", "METACYC:PWY-6277", "REACTOME:R-BTA-73817", "REACTOME:R-DDI-73817", "REACTOME:R-DME-73817", "REACTOME:R-GGA-419140", "REACTOME:R-HSA-73817", "REACTOME:R-MMU-73817", "REACTOME:R-SCE-73817", "REACTOME:R-SPO-73817" ]

12

[ "1gso", "1vkz", "2ip4", "2qk4", "2xcl", "2xd4", "2yrw", "2yrx", "2ys6", "2ys7", "2yw2", "2yya", "3lp8", "3mjf", "5vev", "7lvo" ]

16

[ "PUB00002527", "PUB00075622", "PUB00075625" ]

[ "2687276", "2147474", "3097325" ]

[ "Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli.", "De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-gly...

[ 1989, 1990, 1986 ]

3

[]

0

null

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

[ 1039, 24965, 5136, 15, 567 ]

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",...

[ 3, 1, 4, 5, 1, 4, 3, 1, 5, 5, 1, 1, 14 ]

13

true

Domain

Phosphoribosylglycinamide synthetase, C-domain

PRibGlycinamide_synth_C-dom

4

IPR020561

20,561

Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain

PRibGlycinamid_synth_ATP-grasp

Domain

32,796

false

Phosphoribosylglycinamide synthetase ( ) (GARS) (phosphoribosylamine glycine ligase) [ ] catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by phosphoribosylglycinamide synthetase is the ATP-dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide: ...

[]

0

[ "PFAM" ]

[ "PF01071" ]

[ "GARS_A" ]

[ 32796 ]

1

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

[ "6.3.4.13", "PWY-6121", "PWY-6122", "PWY-6277", "R-BTA-73817", "R-DDI-73817", "R-DME-73817", "R-GGA-419140", "R-HSA-73817", "R-MMU-73817", "R-SCE-73817", "R-SPO-73817" ]

[ "EC:6.3.4.13", "METACYC:PWY-6121", "METACYC:PWY-6122", "METACYC:PWY-6277", "REACTOME:R-BTA-73817", "REACTOME:R-DDI-73817", "REACTOME:R-DME-73817", "REACTOME:R-GGA-419140", "REACTOME:R-HSA-73817", "REACTOME:R-MMU-73817", "REACTOME:R-SCE-73817", "REACTOME:R-SPO-73817" ]

12

[ "1gso", "1vkz", "2ip4", "2qk4", "2xcl", "2xd4", "2yrw", "2yrx", "2ys6", "2ys7", "2yw2", "2yya", "3ln6", "3lp8", "3mjf", "4dim", "5vev", "7lvo" ]

18

[ "PUB00002527", "PUB00075622", "PUB00075625" ]

[ "2687276", "2147474", "3097325" ]

[ "Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli.", "De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-gly...

[ 1989, 1990, 1986 ]

3

[ "IPR011761" ]

[]

1

0

1

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

[ 1049, 25639, 5470, 8, 630 ]

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",...

[ 3, 1, 4, 5, 1, 10, 5, 1, 5, 5, 1, 1, 15 ]

13

true

Domain

Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain

PRibGlycinamid_synth_ATP-grasp

5

IPR020562

20,562

Phosphoribosylglycinamide synthetase, N-terminal

PRibGlycinamide_synth_N

Domain

31,406

false

This entry represents the N-domain, which is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase ( ). Phosphoribosylglycinamide synthetase ( ) (GARS) (phosphoribosylamine glycine ligase) [ ] catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by phos...

[ "GO:0004637", "GO:0009113" ]

[ "phosphoribosylamine-glycine ligase activity", "purine nucleobase biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF02844" ]

[ "GARS_N" ]

[ 31406 ]

1

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

[ "6.3.4.13", "PWY-6121", "PWY-6122", "PWY-6277", "R-BTA-73817", "R-DDI-73817", "R-DME-73817", "R-GGA-419140", "R-HSA-73817", "R-MMU-73817", "R-SCE-73817", "R-SPO-73817" ]

[ "EC:6.3.4.13", "METACYC:PWY-6121", "METACYC:PWY-6122", "METACYC:PWY-6277", "REACTOME:R-BTA-73817", "REACTOME:R-DDI-73817", "REACTOME:R-DME-73817", "REACTOME:R-GGA-419140", "REACTOME:R-HSA-73817", "REACTOME:R-MMU-73817", "REACTOME:R-SCE-73817", "REACTOME:R-SPO-73817" ]

12

[ "1gso", "1vkz", "2ip4", "2qk4", "2xcl", "2xd4", "2yrw", "2yrx", "2ys6", "2ys7", "2yw2", "2yya", "3lp8", "3mjf", "5vev", "7lvo" ]

16

[ "PUB00002527", "PUB00075622", "PUB00075625" ]

[ "2687276", "2147474", "3097325" ]

[ "Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli.", "De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-gly...

[ 1989, 1990, 1986 ]

3

[]

0

null

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

[ 863, 24753, 5246, 4, 540 ]

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",...

[ 3, 1, 4, 4, 1, 9, 6, 1, 5, 5, 1, 1, 13 ]

13

true

Domain

Phosphoribosylglycinamide synthetase, N-terminal

PRibGlycinamide_synth_N

8

IPR020563

20,563

Crossover junction endodeoxyribonuclease RuvC, magnesium-binding site

X-over_junc_endoDNase_Mg_BS

Binding_site

18,584

false

The Escherichia coli RuvC gene is involved in DNA repair and in the late step of RecE and RecF pathway recombination [ ]. RuvC protein ( ) cleaves cruciform junctions, which are formed by the extrusion of inverted repeat sequences from a super-coiled plasmid and which are structurally analogous to Holliday junctions, b...

[ "GO:0008821" ]

[ "crossover junction DNA endonuclease activity" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS01321" ]

[ "RUVC" ]

[ 18584 ]

1

[ "EC" ]

[ "3.1.21.10" ]

[ "EC:3.1.21.10" ]

1

[ "1hjr", "6lw3" ]

2

[ "PUB00001215", "PUB00003328" ]

[ "1661673", "8057369" ]

[ "Escherichia coli RuvC protein is an endonuclease that resolves the Holliday structure.", "Preliminary crystallographic study of Escherichia coli RuvC protein. An endonuclease specific for Holliday junctions." ]

[ 1991, 1994 ]

2

[]

0

null

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

[ 18077, 6, 26, 46, 429 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Binding_site

Crossover junction endodeoxyribonuclease RuvC, magnesium-binding site

X-over_junc_endoDNase_Mg_BS

6

IPR020565

20,565

Imidazoleglycerol-phosphate dehydratase, conserved site

ImidazoleglycerP_deHydtase_CS

Conserved_site

25,491

false

Imidazoleglycerol-phosphate dehydratase (IGPD; ) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by...

[ "GO:0004424", "GO:0000105" ]

[ "imidazoleglycerol-phosphate dehydratase activity", "L-histidine biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE", "PROSITE" ]

[ "PS00954", "PS00955" ]

[ "IGP_DEHYDRATASE_1", "IGP_DEHYDRATASE_2" ]

[ 23669, 24030 ]

2

[ "EC" ]

[ "4.2.1.19" ]

[ "EC:4.2.1.19" ]

1

[ "1rhy", "2ae8", "2f1d", "4gqu", "4lom", "4lpf", "4mu0", "4mu1", "4mu3", "4mu4", "4qnj", "4qnk", "5dnl", "5dnx", "5ekw", "5el9", "5elw", "5xds", "5zqn", "6ezj", "6ezm", "6fwh", "6khh", "6yjh", "7ddv", "7dnq", "7fcy", "7oj5", "8qav", "8qaw", "8qax", "8qay"...

36

[ "PUB00009674", "PUB00022600", "PUB00040491", "PUB00046135", "PUB00079788", "PUB00079789", "PUB00079790", "PUB00079791", "PUB00079792", "PUB00079793", "PUB00079794", "PUB00079795" ]

[ "3007936", "14724278", "16338409", "15042344", "10885480", "16511155", "10450980", "8066131", "3001645", "9767718", "8511965", "2664449" ]

[ "Gene structure in the histidine operon of Escherichia coli. Identification and nucleotide sequence of the hisB gene.", "Crystal structure of imidazole glycerol-phosphate dehydratase: duplication of an unusual fold.", "Structure and mechanism of imidazoleglycerol-phosphate dehydratase.", "Molecular evolution ...

[ 1986, 2004, 2005, 2004, 2000, 2005, 1999, 1994, 1985, 1998, 1993, 1989 ]

12

[]

0

null

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

[ 719, 21500, 2815, 457 ]

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" ]

[ 11, 1, 1, 4, 1, 1, 11 ]

7

true

Conserved_site

Imidazoleglycerol-phosphate dehydratase, conserved site

ImidazoleglycerP_deHydtase_CS

1

IPR020566

20,566

Histidine biosynthesis bifunctional protein HisB

His_synth_bifunc_HisB

Family

5,464

false

This entry represents the histidine biosynthesis bifunctional protein HisB [ , ], which contains an N-terminal histidinol phosphate phosphatase ( ) and a C-terminal imidazoleglycerol-phosphate dehydratase ( ) [ ]. HisB catalyses steps 6 and 8 of L-histidine biosynthesis. The N-terminal histidinol phosphate phosphatase ...

[ "GO:0004401", "GO:0004424", "GO:0000105" ]

[ "histidinol-phosphatase activity", "imidazoleglycerol-phosphate dehydratase activity", "L-histidine biosynthetic process" ]

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

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01022", "NF003937" ]

[ "Bifunc_HisB", "PRK05446.1" ]

[ 5367, 5458 ]

2

[ "EC", "EC" ]

[ "3.1.3.15", "4.2.1.19" ]

[ "EC:3.1.3.15", "EC:4.2.1.19" ]

2

[]

0

[ "PUB00040771", "PUB00046135", "PUB00060953", "PUB00060954" ]

[ "16966333", "15042344", "13763426", "4349042" ]

[ "Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway.", "Molecular evolution of hisB genes.", "Enzyme complementation in mixed extracts of mutants from the Salmonella histidine B locus.", "Some properties of the catalytic sites of imidazoleglycerol phosphate de...

[ 2006, 2004, 1961, 1973 ]

4

[ "IPR000807" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta", "metagenomes" ]

[ 5427, 5, 32 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Histidine biosynthesis bifunctional protein HisB

His_synth_bifunc_HisB

6

IPR020568

20,568

Ribosomal protein uS5 domain 2-type superfamily

Ribosomal_Su5_D2-typ_SF

Homologous_superfamily

676,141

false

The founding member of this superfamily is the second domain of the small ribosomal subunit protein uS5. This domain adopts α/β fold consisting of four-stranded mixed β-sheet and two helices packed on one side of it. Typical features for this superfamily are the psi-loop between strands 2 and 3; and the left-handed cro...

[]

0

[ "SSF" ]

[ "SSF54211" ]

[ "" ]

[ 676141 ]

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-1227986", "R-BTA-1474151", "R-BTA-156827", "R-BTA-156902", "R-BTA-1679131", "R-BTA-168928", "R-BTA-1799339", "R-BTA-191273", "R-BTA-2029482", "R-BTA-203615", "R-BTA-2565942", "R-BTA-3371497", "R-BTA-3371511", "R-BTA-3371568", "R-BTA-3371571", "R-BTA-380259", "R-BTA-380270", ...

[ "REACTOME:R-BTA-1227986", "REACTOME:R-BTA-1474151", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-156902", "REACTOME:R-BTA-1679131", "REACTOME:R-BTA-168928", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-191273", "REACTOME:R-BTA-2029482", "REACTOME:R-BTA-203615", "REACTOME:R-BTA-2565942", "REACTOME:R-B...

545

[ "1a6f", "1b62", "1b63", "1bkn", "1d6t", "1dar", "1dv4", "1e3h", "1e3p", "1ea6", "1efg", "1eg0", "1ei1", "1elo", "1fi4", "1fjg", "1fka", "1fnm", "1fwk", "1fwl", "1h72", "1h73", "1h74", "1h7s", "1h7u", "1hk7", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95"...

2,843

[ "PUB00015644", "PUB00016021", "PUB00022600", "PUB00024488", "PUB00029653", "PUB00030777", "PUB00034480", "PUB00034481", "PUB00034482", "PUB00035354", "PUB00035569", "PUB00038434" ]

[ "11188689", "12672694", "14724278", "11574484", "14767080", "14665623", "8722013", "17081993", "15544330", "15039704", "17174896", "15632161" ]

[ "Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily.", "XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators.", "Crystal structure of imidazole glycerol-phosphate dehydratas...

[ 2000, 2003, 2004, 2001, 2004, 2004, 1995, 2006, 2004, 2004, 2006, 2005 ]

12

[]

0

null

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

[ 13636, 474883, 177005, 796, 9821 ]

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",...

[ 333, 62, 86, 45, 20, 256, 161, 30, 195, 187, 32, 28, 532 ]

13

true

Homologous_superfamily

Ribosomal protein uS5 domain 2-type superfamily

Ribosomal_Su5_D2-typ_SF

9

IPR020573

20,573

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, non-repeat region

UDP_GlcNAc_AcTrfase_non-rep

Domain

15,069

false

This entry represents the non-repeating region of the enzyme. UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase ( ) catalyses an early step in lipid A biosynthesis [ ]: UDP-3-O-(3-hydroxytetradecanoyl)glucosamine + (R)-3-hydroxytetradecanoyl- [acyl carrier protein] = UDP-2,3-bis(3-hydroxytetradecanoyl)glucosam...

[ "GO:0016747", "GO:0009245" ]

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

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF04613" ]

[ "LpxD" ]

[ 15069 ]

1

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

[ "2.3.1.191", "PWY-8073", "PWY-8245", "PWY-8283" ]

[ "EC:2.3.1.191", "METACYC:PWY-8073", "METACYC:PWY-8245", "METACYC:PWY-8283" ]

4

[ "2iu8", "2iu9", "2iua", "3eh0", "3pmo", "4e75", "4e79", "4ihf", "4ihg", "4ihh", "6p83", "6p84", "6p85", "6p86", "6p87", "6p88", "6p89", "6p8a", "6p8b", "6uec", "6ued" ]

21

[ "PUB00010088" ]

[ "8366125" ]

[ "The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis." ]

[ 1993 ]

1

[]

0

null

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

[ 11, 14754, 25, 279 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, non-repeat region

UDP_GlcNAc_AcTrfase_non-rep

6

IPR020574

20,574

Small ribosomal subunit protein uS9, conserved site

Ribosomal_uS9_CS

Conserved_site

32,445

false

This entry represents a conserved region, found in small ribosomal subunit protein uS9, containing many charged residues and located in the central section of these proteins. uS9 proteins adopt a β/α/β fold similar to that found in numerous RNA/DNA-binding proteins, as well as in kinases from the GHMP kinase family [ ]...

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

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

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

3

[ "PROSITE" ]

[ "PS00360" ]

[ "RIBOSOMAL_S9" ]

[ 32445 ]

1

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

[ "R-BTA-156827", "R-BTA-1799339", "R-BTA-5389840", "R-BTA-5419276", "R-BTA-6791226", "R-BTA-72649", "R-BTA-72689", "R-BTA-72695", "R-BTA-72702", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-BTA-9937383", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72649", "R-CEL-72689", "R-CEL-7269...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-5389840", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72695", "REACTOME:R-BTA-72702", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-9759...

112

[ "1fjg", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xmo", "1xmq", "1xnq", "1xnr", "2e5l", "2f4v"...

1,874

[ "PUB00001585", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00034480" ]

[ "2332055", "11297922", "11290319", "11114498", "8722013" ]

[ "The primary structure of rat ribosomal protein S16.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Structures of prokaryotic ribosomal proteins: implications for RNA binding and evolution." ]

[ 1990, 2001, 2001, 2000, 1995 ]

5

[]

0

null

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

[ 815, 21680, 9451, 499 ]

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",...

[ 16, 1, 1, 2, 1, 7, 7, 2, 10, 14, 3, 3, 16 ]

13

true

Conserved_site

Small ribosomal subunit protein uS9, conserved site

Ribosomal_uS9_CS

1

IPR020575

20,575

Heat shock protein Hsp90, N-terminal

Hsp90_N

Domain

40,449

false

Prokaryotes and eukaryotes respond to heat shock and other forms of environmental stress by inducing synthesis of heat-shock proteins (hsp) [ ]. The 90kDa heat shock protein, Hsp90, is one of the most abundant proteins in eukaryotic cells, comprising 1-2% of cellular proteins under non-stress conditions [ ]. Its contri...

[]

0

[ "PRINTS", "CDD" ]

[ "PR00775", "cd16927" ]

[ "HEATSHOCK90", "HATPase_Hsp90-like" ]

[ 40164, 34642 ]

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-1227986", "R-BTA-1474151", "R-BTA-1679131", "R-BTA-168928", "R-BTA-2029482", "R-BTA-203615", "R-BTA-2565942", "R-BTA-3371497", "R-BTA-3371511", "R-BTA-3371568", "R-BTA-3371571", "R-BTA-380259", "R-BTA-380270", "R-BTA-380284", "R-BTA-380320", "R-BTA-381426", "R-BTA-399954", "...

[ "REACTOME:R-BTA-1227986", "REACTOME:R-BTA-1474151", "REACTOME:R-BTA-1679131", "REACTOME:R-BTA-168928", "REACTOME:R-BTA-2029482", "REACTOME:R-BTA-203615", "REACTOME:R-BTA-2565942", "REACTOME:R-BTA-3371497", "REACTOME:R-BTA-3371511", "REACTOME:R-BTA-3371568", "REACTOME:R-BTA-3371571", "REACTOME:...

276

[ "1a4h", "1ah6", "1ah8", "1am1", "1amw", "1bgq", "1byq", "1osf", "1qy8", "1qye", "1tbw", "1tc0", "1tc6", "1u0z", "1u2o", "1us7", "1uy6", "1uy7", "1uy8", "1uy9", "1uyc", "1uyd", "1uye", "1uyf", "1uyg", "1uyh", "1uyi", "1uyk", "1uyl", "1uym", "1y4s", "1y4u"...

640

[ "PUB00000102", "PUB00002788", "PUB00005421", "PUB00014968", "PUB00112352", "PUB00112353", "PUB00112354", "PUB00141629", "PUB00141630", "PUB00141631", "PUB00141642" ]

[ "2853609", "8419347", "7914036", "15069952", "19697319", "24462206", "26464709", "26616658", "26884463", "26929380", "22008467" ]

[ "The heat-shock proteins.", "Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases.", "Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones.", "Hsp90 isoforms: functions, expression and clinical importance.", "Hsp90 and ...

[ 1988, 1993, 1994, 2004, 2010, 2014, 2015, 2015, 2016, 2016, 2012 ]

11

[ "IPR003594" ]

[]

1

0

1

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

[ 27, 18869, 21297, 11, 245 ]

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",...

[ 33, 4, 7, 7, 1, 49, 31, 1, 31, 20, 2, 1, 97 ]

13

true

Domain

Heat shock protein Hsp90, N-terminal

Hsp90_N

5

IPR020578

20,578

Aminotransferase class-V, pyridoxal-phosphate binding site

Aminotrans_V_PyrdxlP_BS

Binding_site

77,731

false

This entry represents a conserved region surrounding the lysine residue that binds the pyridoxal-phosphate [ ]. Aminotransferases share certain mechanistic features with other pyridoxal- phosphate dependent enzymes, such as the covalent binding of the pyridoxal- phosphate group to a lysine residue. On the basis of sequ...

[]

0

[ "PROSITE" ]

[ "PS00595" ]

[ "AA_TRANSFER_CLASS_5" ]

[ 77731 ]

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-977347", "R-DDI-1362409", "R-DDI-947581", "R-DDI-977347", "R-DDI-9865881", "R-DME-1362409", "R-DME-389661", "R-DME-9033241", "R-DME-947581", "R-DME-977347", "R-DME-9865881", "R-HSA-1362409", "R-HSA-389661", "R-HSA-9033241", "R-HSA-947581", "R-HSA-977347", "R-HSA-9854311", "R...

[ "REACTOME:R-CEL-977347", "REACTOME:R-DDI-1362409", "REACTOME:R-DDI-947581", "REACTOME:R-DDI-977347", "REACTOME:R-DDI-9865881", "REACTOME:R-DME-1362409", "REACTOME:R-DME-389661", "REACTOME:R-DME-9033241", "REACTOME:R-DME-947581", "REACTOME:R-DME-977347", "REACTOME:R-DME-9865881", "REACTOME:R-HS...

40

[ "1bjn", "1bjo", "1bt4", "1c0n", "1elq", "1elu", "1h0c", "1i29", "1iug", "1j04", "1jf9", "1kmj", "1kmk", "1p3w", "1vjo", "1w23", "1w3u", "2bhx", "2bi1", "2bi2", "2bi3", "2bi5", "2bi9", "2bia", "2bie", "2big", "2c0r", "2ch1", "2ch2", "2huf", "2hui", "2huu"...

168

[ "PUB00001654" ]

[ "8482384" ]

[ "Homology of the NifS family of proteins to a new class of pyridoxal phosphate-dependent enzymes." ]

[ 1993 ]

1

[]

0

null

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

[ 1364, 63398, 11864, 7, 1098 ]

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",...

[ 9, 3, 5, 5, 4, 12, 9, 1, 7, 13, 2, 2, 18 ]

13

true

Binding_site

Aminotransferase class-V, pyridoxal-phosphate binding site

Aminotrans_V_PyrdxlP_BS

1

IPR020579

20,579

Exonuclease VII, large subunit, C-terminal

Exonuc_VII_lsu_C

Domain

25,094

false

Exonuclease VII ( ) is composed of two nonidentical subunits; one large subunit and 4 small ones [ ]. Exonuclease VII catalyses exonucleolytic cleavage in either 5'-3' or 3'-5' direction to yield 5'-phosphomononucleotides. The large subunit also contains the OB-fold domains that bind to nucleic acids at the N terminus....

[ "GO:0008855" ]

[ "exodeoxyribonuclease VII activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF02601" ]

[ "Exonuc_VII_L" ]

[ 25094 ]

1

[ "EC" ]

[ "3.1.11.6" ]

[ "EC:3.1.11.6" ]

1

[ "8txr" ]

1

[ "PUB00008230" ]

[ "6284744" ]

[ "Subunit structure of Escherichia coli exonuclease VII." ]

[ 1982 ]

1

[]

0

null

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

[ 24141, 52, 272, 39, 590 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Exonuclease VII, large subunit, C-terminal

Exonuc_VII_lsu_C

9

IPR020581

20,581

Glycine cleavage system P protein

GDC_P

Family

33,633

false

The P protein, also known as Glycine dehydrogenase (decarboxylating), is part of the glycine decarboxylase multienzyme complex (GDC), also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T [ ]. The P protein ( ) binds the alpha-amino group of glycine through its pyrid...

[ "GO:0004375", "GO:0006546" ]

[ "glycine dehydrogenase (decarboxylating) activity", "glycine catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PANTHER", "CDD" ]

[ "PTHR11773", "cd00613" ]

[ "", "GDC-P" ]

[ 29189, 27085 ]

2

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

[ "1.4.4.2", "GenProp0178", "R-DDI-6783984", "R-HSA-6783984", "R-MMU-6783984", "R-SCE-6783984", "R-SPO-6783984" ]

[ "EC:1.4.4.2", "GP:GenProp0178", "REACTOME:R-DDI-6783984", "REACTOME:R-HSA-6783984", "REACTOME:R-MMU-6783984", "REACTOME:R-SCE-6783984", "REACTOME:R-SPO-6783984" ]

7

[ "1wyt", "1wyu", "1wyv", "4lgl", "4lhc", "4lhd", "6i33", "6i34", "6i35" ]

9

[ "PUB00009491", "PUB00038183" ]

[ "8181752", "15791207" ]

[ "Characterization of the Escherichia coli gcv operon.", "Structure of P-protein of the glycine cleavage system: implications for nonketotic hyperglycinemia." ]

[ 1994, 2005 ]

2

[]

[ "IPR003437", "IPR023010", "IPR023012" ]

0

3

0

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

[ 746, 25631, 6445, 5, 806 ]

5

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

[ 10, 2, 2, 1, 1, 10, 3, 1, 14, 8, 1, 1, 7 ]

13

true

Family

Glycine cleavage system P protein

GDC_P

6

IPR020584

20,584

DNA recombination/repair protein RecA, conserved site

DNA_recomb/repair_RecA_CS

Conserved_site

33,278

false

The recA gene product is a multifunctional enzyme that plays a role in homologous recombination, DNA repair and induction of the SOS response [ ]. In homologous recombination, the protein functions as a DNA-dependent ATPase, promoting synapsis, heteroduplex formation and strand exchange between homologous DNAs [ ]. Rec...

[ "GO:0003677", "GO:0005524", "GO:0008094", "GO:0006259" ]

[ "DNA binding", "ATP binding", "ATP-dependent activity, acting on DNA", "DNA metabolic process" ]

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

4

[ "PROSITE" ]

[ "PS00321" ]

[ "RECA_1" ]

[ 33278 ]

1

[]

0

[ "1g18", "1g19", "1mo3", "1mo4", "1mo5", "1mo6", "1n03", "1rea", "1u94", "1u98", "1u99", "1ubc", "1ube", "1ubf", "1ubg", "1xms", "1xmv", "1xp8", "2g88", "2odn", "2odw", "2oe2", "2oep", "2oes", "2ofo", "2reb", "2rec", "2zr0", "2zr7", "2zr9", "2zra", "2zrb"...

84

[ "PUB00002285", "PUB00003439", "PUB00003747", "PUB00004797", "PUB00004946", "PUB00043276" ]

[ "7592482", "8587109", "1896024", "1518831", "9187054", "12045091" ]

[ "Bacterial classifications derived from recA protein sequence comparisons.", "The RecA protein as a model molecule for molecular systematic studies of bacteria: comparison of trees of RecAs and 16S rRNAs from the same species.", "Characterization of recA genes and recA mutants of Rhizobium meliloti and Rhizobiu...

[ 1995, 1995, 1991, 1992, 1997, 2002 ]

6

[]

0

null

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

[ 30738, 1979, 41, 520 ]

4

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

[ 8, 1, 10, 16 ]

4

true

Conserved_site

DNA recombination/repair protein RecA, conserved site

DNA_recomb/repair_RecA_CS

5

IPR020587

20,587

DNA recombination and repair protein RecA, monomer-monomer interface

RecA_monomer-monomer_interface

Domain

47,177

false

The recA gene product is a multifunctional enzyme that plays a role in homologous recombination, DNA repair and induction of the SOS response [ ]. In homologous recombination, the protein functions as a DNA-dependent ATPase, promoting synapsis, heteroduplex formation and strand exchange between homologous DNAs [ ]. Rec...

[ "GO:0003677", "GO:0005524", "GO:0008094", "GO:0006259" ]

[ "DNA binding", "ATP binding", "ATP-dependent activity, acting on DNA", "DNA metabolic process" ]

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

4

[ "PROFILE" ]

[ "PS50163" ]

[ "RECA_3" ]

[ 47177 ]

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-5685938", "R-BTA-5685942", "R-BTA-5693568", "R-BTA-5693579", "R-BTA-5693616", "R-BTA-912446", "R-CFA-5685938", "R-CFA-5685942", "R-CFA-5693568", "R-CFA-5693579", "R-CFA-5693616", "R-CFA-912446", "R-DME-5693616", "R-GGA-265976", "R-GGA-351433", "R-GGA-5685938", "R-GGA-5685942",...

[ "REACTOME:R-BTA-5685938", "REACTOME:R-BTA-5685942", "REACTOME:R-BTA-5693568", "REACTOME:R-BTA-5693579", "REACTOME:R-BTA-5693616", "REACTOME:R-BTA-912446", "REACTOME:R-CFA-5685938", "REACTOME:R-CFA-5685942", "REACTOME:R-CFA-5693568", "REACTOME:R-CFA-5693579", "REACTOME:R-CFA-5693616", "REACTOME...

45

[ "1g18", "1g19", "1mo3", "1mo4", "1mo5", "1mo6", "1n03", "1n0w", "1pzn", "1rea", "1szp", "1t4g", "1u94", "1u98", "1u99", "1ubc", "1ube", "1ubf", "1ubg", "1v5w", "1xms", "1xmv", "1xp8", "1xu4", "2b21", "2bke", "2dfl", "2f1h", "2f1i", "2f1j", "2fpk", "2fpl"...

234

[ "PUB00002285", "PUB00003439", "PUB00003747", "PUB00004797", "PUB00004946", "PUB00043276" ]

[ "7592482", "8587109", "1896024", "1518831", "9187054", "12045091" ]

[ "Bacterial classifications derived from recA protein sequence comparisons.", "The RecA protein as a model molecule for molecular systematic studies of bacteria: comparison of trees of RecAs and 16S rRNAs from the same species.", "Characterization of recA genes and recA mutants of Rhizobium meliloti and Rhizobiu...

[ 1995, 1995, 1991, 1992, 1997, 2002 ]

6

[]

0

null

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

[ 979, 33431, 11247, 743, 777 ]

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",...

[ 23, 3, 4, 2, 1, 7, 5, 1, 23, 7, 2, 2, 48 ]

13

true

Domain

DNA recombination and repair protein RecA, monomer-monomer interface

RecA_monomer-monomer_interface

4

IPR020588

20,588

DNA recombination and repair protein RecA-like, ATP-binding domain

RecA_ATP-bd

Domain

97,811

false

The recA gene product is a multifunctional enzyme that plays a role in homologous recombination, DNA repair and induction of the SOS response [ ]. In homologous recombination, the protein functions as a DNA-dependent ATPase, promoting synapsis, heteroduplex formation and strand exchange between homologous DNAs [ ]. Rec...

[ "GO:0003677", "GO:0005524", "GO:0140664", "GO:0006281" ]

[ "DNA binding", "ATP binding", "ATP-dependent DNA damage sensor activity", "DNA repair" ]

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

4

[ "PROFILE" ]

[ "PS50162" ]

[ "RECA_2" ]

[ 97811 ]

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-5685938", "R-BTA-5685942", "R-BTA-5693568", "R-BTA-5693579", "R-BTA-5693616", "R-BTA-912446", "R-CFA-5685938", "R-CFA-5685942", "R-CFA-5693568", "R-CFA-5693579", "R-CFA-5693616", "R-CFA-912446", "R-DME-5693616", "R-GGA-265976", "R-GGA-351433", "R-GGA-5685938", "R-GGA-5685942",...

[ "REACTOME:R-BTA-5685938", "REACTOME:R-BTA-5685942", "REACTOME:R-BTA-5693568", "REACTOME:R-BTA-5693579", "REACTOME:R-BTA-5693616", "REACTOME:R-BTA-912446", "REACTOME:R-CFA-5685938", "REACTOME:R-CFA-5685942", "REACTOME:R-CFA-5693568", "REACTOME:R-CFA-5693579", "REACTOME:R-CFA-5693616", "REACTOME...

45

[ "1g18", "1g19", "1mo3", "1mo4", "1mo5", "1mo6", "1n03", "1n0w", "1pzn", "1rea", "1szp", "1t4g", "1u94", "1u98", "1u99", "1ubc", "1ube", "1ubf", "1ubg", "1v5w", "1xms", "1xmv", "1xp8", "1xu4", "2b21", "2bke", "2cvf", "2cvh", "2dfl", "2f1h", "2f1i", "2f1j"...

244

[ "PUB00002285", "PUB00003439", "PUB00003747", "PUB00004797", "PUB00004946", "PUB00043276" ]

[ "7592482", "8587109", "1896024", "1518831", "9187054", "12045091" ]

[ "Bacterial classifications derived from recA protein sequence comparisons.", "The RecA protein as a model molecule for molecular systematic studies of bacteria: comparison of trees of RecAs and 16S rRNAs from the same species.", "Characterization of recA genes and recA mutants of Rhizobium meliloti and Rhizobiu...

[ 1995, 1995, 1991, 1992, 1997, 2002 ]

6

[]

0

null

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

[ 2125, 68273, 25657, 505, 1251 ]

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",...

[ 75, 4, 15, 38, 2, 40, 23, 3, 43, 35, 4, 4, 94 ]

13

true

Domain

DNA recombination and repair protein RecA-like, ATP-binding domain

RecA_ATP-bd

2

IPR020590

20,590

Guanylate kinase, conserved site

Guanylate_kinase_CS

Conserved_site

65,105

false

Guanylate kinase ( ) (GK) [ ] catalyzes the ATP-dependent phosphorylation of GMP into GDP. It is essential for recycling GMP and indirectly, cGMP. In prokaryotes (such as Escherichia coli), lower eukaryotes (such as yeast) and in vertebrates, GK is a highly conserved monomeric protein of about 200 amino acids. GK has b...

[]

0

[ "PROSITE" ]

[ "PS00856" ]

[ "GUANYLATE_KINASE_1" ]

[ 65105 ]

1

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

[ "2.7.4.8", "PWY-7221", "PWY-8289", "R-BTA-499943", "R-BTA-9013149", "R-BTA-9013404", "R-BTA-9013406", "R-BTA-9013408", "R-BTA-9013423", "R-BTA-9748787", "R-CEL-212676", "R-CEL-438066", "R-CEL-451308", "R-CEL-6794361", "R-CEL-8849932", "R-CFA-399719", "R-CFA-438066", "R-CFA-451308",...

[ "EC:2.7.4.8", "METACYC:PWY-7221", "METACYC:PWY-8289", "REACTOME:R-BTA-499943", "REACTOME:R-BTA-9013149", "REACTOME:R-BTA-9013404", "REACTOME:R-BTA-9013406", "REACTOME:R-BTA-9013408", "REACTOME:R-BTA-9013423", "REACTOME:R-BTA-9748787", "REACTOME:R-CEL-212676", "REACTOME:R-CEL-438066", "REACTO...

103

[ "1ex6", "1ex7", "1gky", "1jxm", "1jxo", "1kgd", "1kjw", "1lvg", "1s4q", "1s96", "1z6g", "1z8f", "1znw", "1znx", "1zny", "1znz", "2an9", "2anb", "2anc", "2f3r", "2f3t", "2j41", "2qor", "2xkx", "3lnc", "3ney", "3tau", "3tr0", "3tvt", "3uat", "3w9y", "3wp0"...

68

[ "PUB00000870", "PUB00001440", "PUB00003284", "PUB00003556", "PUB00005396" ]

[ "1310897", "8097461", "1314905", "8155583", "1329277" ]

[ "A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene.", "Purification and sequence determination of guanylate kinase from pig brain.", "Refined structure of the complex between guanylate kinase and its sub...

[ 1992, 1993, 1992, 1993, 1992 ]

5

[]

0

null

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

[ 22424, 42189, 1, 78, 413 ]

5

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

[ 10, 11, 431, 38, 1, 115, 65, 1, 5, 108, 1, 1, 15 ]

13

true

Conserved_site

Guanylate kinase, conserved site

Guanylate_kinase_CS

7

IPR020591

20,591

Chromosomal replication control, initiator DnaA-like

Chromosome_initiator_DnaA-like

Family

29,510

false

The bacterial DnaA protein [ , , ] plays an important role in initiating and regulating chromosomal replication. DnaA is an ATP- and DNA-binding protein. It binds specifically to 9 bp nucleotide repeats known as dnaA boxes which are found in the chromosome origin of replication (oriC). DnaA contains two conserved regio...

[]

0

[ "PRINTS" ]

[ "PR00051" ]

[ "DNAA" ]

[ 29510 ]

1

[]

0

[ "1l8q", "2hcb", "2z4r", "2z4s", "3bos", "3r8f", "3sc3", "5x06", "8btg", "8bv3" ]

10

[ "PUB00000665", "PUB00001793", "PUB00003815", "PUB00005517" ]

[ "8110826", "2172087", "1779750", "2558436" ]

[ "The initiator protein DnaA: evolution, properties and function.", "Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli.", "Structure and function of DnaA and the DnaA-box in eubacteria: evolutionary relationships of bacterial re...

[ 1994, 1990, 1991, 1989 ]

4

[]

[ "IPR001957", "IPR017788" ]

0

2

0

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

[ 28809, 58, 34, 11, 598 ]

5

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Chromosomal replication control, initiator DnaA-like

Chromosome_initiator_DnaA-like

5

IPR020592

20,592

Small ribosomal subunit protein bS16, conserved site

Ribosomal_bS16_CS

Conserved_site

24,031

false

This signature pattern covers a conserved region located in the N-terminal extremity of the small ribosomal subunit protein bS16 family. Ribosomal protein S16 (also known as bS16) is one of the proteins from the small ribosomal subunit. It belongs to a family of ribosomal proteins which, on the basis of sequence simila...

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

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

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

3

[ "PROSITE" ]

[ "PS00732" ]

[ "RIBOSOMAL_S16" ]

[ 24031 ]

1

[]

0

[ "2ykr", "3iy8", "3j9w", "3j9y", "3j9z", "3ja1", "3jbu", "3jbv", "3jcd", "3jce", "3jcj", "3jcn", "4a2i", "4adv", "4u1u", "4u1v", "4u20", "4u24", "4u25", "4u26", "4u27", "4v47", "4v48", "4v4h", "4v4q", "4v4v", "4v4w", "4v50", "4v52", "4v53", "4v54", "4v55"...

658

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

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

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

[ 2001, 2001, 2000, 2008 ]

4

[]

0

null

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

[ 11576, 1, 12260, 1, 193 ]

5

[ "Arabidopsis thaliana", "Danio rerio", "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)", "Zea mays" ]

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

7

true

Conserved_site

Small ribosomal subunit protein bS16, conserved site

Ribosomal_bS16_CS

5

IPR020593

20,593

Gamma-glutamyl phosphate reductase GPR, conserved site

G-glutamylP_reductase_CS

Conserved_site

25,585

false

This entry represents a conserved region that contains two histidine residues. This region is located in the last third of GPR. Gamma-glutamyl phosphate reductase ( ) (GPR) is the enzyme that catalyzes the second step in the biosynthesis of proline from glutamate, the NADP-dependent reduction of L-glutamate 5-phosphate...

[ "GO:0004350", "GO:0055129" ]

[ "glutamate-5-semialdehyde dehydrogenase activity", "L-proline biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE" ]

[ "PS01223" ]

[ "PROA" ]

[ 25585 ]

1

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

[ "1.2.1.41", "PWY-6922", "R-CEL-8964539", "R-CEL-9837999", "R-HSA-8964539", "R-HSA-9837999", "R-MMU-8964539", "R-MMU-9837999", "R-SCE-8964539", "R-SCE-9837999", "R-SPO-8964539", "R-SPO-9837999" ]

[ "EC:1.2.1.41", "METACYC:PWY-6922", "REACTOME:R-CEL-8964539", "REACTOME:R-CEL-9837999", "REACTOME:R-HSA-8964539", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-8964539", "REACTOME:R-MMU-9837999", "REACTOME:R-SCE-8964539", "REACTOME:R-SCE-9837999", "REACTOME:R-SPO-8964539", "REACTOME:R-SPO-9837999" ...

12

[ "1o20", "1vlu", "2h5g", "4ghk", "7f5t", "7f5u", "7f5v", "7f5x", "7wx3", "7wx4", "7wxf", "7wxg", "7wxh", "7wxi", "8j0e", "8j0f", "8j0g", "8j27", "8j28", "8y2h", "8zok", "8zon", "8zoo" ]

23

[ "PUB00004804", "PUB00005656" ]

[ "1384052", "8896266" ]

[ "A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants.", "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII." ]

[ 1992, 1996 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Hyperionvirus sp.", "unclassified sequences" ]

[ 164, 20142, 4895, 1, 383 ]

5

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

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

13

true

Conserved_site

Gamma-glutamyl phosphate reductase GPR, conserved site

G-glutamylP_reductase_CS

7

IPR020594

20,594

Large ribosomal subunit protein bL9, bacteria/chloroplast

Ribosomal_bL9_bact/chp

Family

25,235

false

This entry represents the large ribosomal subunit protein bL9. In Escherichia coli, bL9 is known to bind directly to the 23S rRNA. It belongs to a family of ribosomal proteins grouped on the basis of sequence similarities [ ]. The crystal structure of Bacillus stearothermophilus bL9 shows the 149-residue protein compri...

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

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

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

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00503", "TIGR00158" ]

[ "Ribosomal_bL9", "L9" ]

[ 24759, 25219 ]

2

[]

0

[ "1cqu", "1div", "1nkw", "1nwx", "1nwy", "1sm1", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xbp", "2hba", "2hbb", "2hvf", "2j28", "2rdo", "3bbx", "3iy9", "3j5l", "3j7z", "3j8g", "3j9y", "3j9z", "3ja1", "3jbu", "3jbv", "3jcd", "3jce", "3jcj", "3jcn", "487d"...

946

[ "PUB00001252", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00007073" ]

[ "8306963", "11297922", "11290319", "11114498", "12051860" ]

[ "Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "pH-dependent stability and folding kinetics of a protein with an unu...

[ 1994, 2001, 2001, 2000, 2002 ]

5

[ "IPR000244" ]

[]

1

0

1

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

[ 23676, 1034, 525 ]

3

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

[ 4, 1, 3, 3 ]

4

true

Family

Large ribosomal subunit protein bL9, bacteria/chloroplast

Ribosomal_bL9_bact/chp

8

IPR020595

20,595

MnmG-related, conserved site

MnmG-rel_CS

Conserved_site

29,601

false

MnmG (also known as GidA) is a tRNA modification enzyme found in bacteria and mitochondria. Though its precise molecular function of these proteins is not known, it is involved in the 5-carboxymethylaminomethyl modification of the wobble uridine base in some tRNAs [ , ]. Sequence variations in the human mitochondrial p...

[]

0

[ "PROSITE", "PROSITE" ]

[ "PS01280", "PS01281" ]

[ "GIDA_1", "GIDA_2" ]

[ 24140, 26692 ]

2

[ "REACTOME" ]

[ "R-HSA-6787450" ]

[ "REACTOME:R-HSA-6787450" ]

1

[ "2zxh", "2zxi", "3ces", "3cp2", "3cp8", "3g05", "3g5q", "3g5r", "3g5s", "8zu0", "9hip", "9hiq", "9hir" ]

13

[ "PUB00043571", "PUB00043572", "PUB00043573" ]

[ "15509579", "11544186", "15542390" ]

[ "Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases.", "Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift.", "Phenotype of non-syndro...

[ 2005, 2001, 2004 ]

3

[]

0

null

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

[ 25488, 3755, 1, 2, 355 ]

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)", "Rattus norvegicus", "Saccharomyces cerevisiae (stra...

[ 6, 1, 8, 1, 1, 17, 2, 1, 2, 1, 1, 7 ]

12

true

Conserved_site

MnmG-related, conserved site

MnmG-rel_CS

7

IPR020596

20,596

Ribosomal RNA adenine methylase transferase, conserved site

rRNA_Ade_Mease_Trfase_CS

Conserved_site

35,939

false

This entry represents a highly conserved region located in the N-terminal section that is probably involved in S-adenosyl methionine (SAM) binding. The bacterial enzyme KsgA catalyses the transfer of a total of four methyl groups from S-adenosyl-l-methionine (S-AdoMet) to two adjacent adenosine bases in 16S rRNA. This ...

[ "GO:0000179", "GO:0000154" ]

[ "rRNA (adenine-N6,N6-)-dimethyltransferase activity", "rRNA modification" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE" ]

[ "PS01131" ]

[ "RRNA_A_DIMETH" ]

[ 35939 ]

1

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

[ "2.1.1", "2.1.1.182", "R-HSA-2151201", "R-HSA-6790901", "R-HSA-6793080" ]

[ "EC:2.1.1", "EC:2.1.1.182", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-6790901", "REACTOME:R-HSA-6793080" ]

5

[ "1qam", "1qan", "1qao", "1qaq", "1qyr", "1yb2", "1yub", "1zq9", "2erc", "2zul", "2zwv", "3dmf", "3dmg", "3dmh", "3ftc", "3ftd", "3fte", "3ftf", "3fut", "3fuu", "3fuv", "3fuw", "3fux", "3fyc", "3fyd", "3grr", "3gru", "3grv", "3gry", "3r9x", "3tpz", "3tqs"...

98

[ "PUB00014820", "PUB00072555", "PUB00101503", "PUB00101504", "PUB00101505" ]

[ "15136037", "23804760", "4336392", "4329247", "6575236" ]

[ "Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli.", "Structural basis for S-adenosylmethionine binding and methyltransferase activity by mitochondrial transcription factor B1.", "Mechanism of kasugamycin resistance in Escherichia coli.", "Change in methy...

[ 2004, 2013, 1972, 1971, 1983 ]

5

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Plasmid pAM-beta-1", "unclassified Caudoviricetes", "unclassified sequences" ]

[ 868, 27586, 6928, 1, 2, 554 ]

6

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

[ 17, 2, 4, 2, 1, 13, 2, 1, 7, 6, 1, 1, 12 ]

13

true

Conserved_site

Ribosomal RNA adenine methylase transferase, conserved site

rRNA_Ade_Mease_Trfase_CS

9

IPR020598

20,598

Ribosomal RNA adenine methylase transferase, N-terminal

rRNA_Ade_methylase_Trfase_N

Domain

41,145

false

This entry represents the N-terminal domain of rRNA adenine methylase transferases. The bacterial enzyme KsgA catalyses the transfer of a total of four methyl groups from S-adenosyl-l-methionine (S-AdoMet) to two adjacent adenosine bases in 16S rRNA. This enzyme and the resulting modified adenosine bases appear to be c...

[ "GO:0000179", "GO:0000154" ]

[ "rRNA (adenine-N6,N6-)-dimethyltransferase activity", "rRNA modification" ]

[ "molecular_function", "biological_process" ]

2

[ "SMART" ]

[ "SM00650" ]

[ "rADc" ]

[ 41145 ]

1

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

[ "2.1.1", "2.1.1.182", "R-BTA-163282", "R-HSA-163282", "R-HSA-2151201", "R-HSA-6790901", "R-HSA-6793080", "R-MMU-163282", "R-RNO-163282" ]

[ "EC:2.1.1", "EC:2.1.1.182", "REACTOME:R-BTA-163282", "REACTOME:R-HSA-163282", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-6790901", "REACTOME:R-HSA-6793080", "REACTOME:R-MMU-163282", "REACTOME:R-RNO-163282" ]

9

[ "1qam", "1qan", "1qao", "1qaq", "1qyr", "1yub", "1zq9", "2erc", "2h1r", "3ftc", "3ftd", "3fte", "3ftf", "3fut", "3fuu", "3fuv", "3fuw", "3fux", "3fyc", "3fyd", "3grr", "3gru", "3grv", "3gry", "3r9x", "3tpz", "3tqs", "3uzu", "4adv", "4gc5", "4gc9", "4jxj"...

106

[ "PUB00014820", "PUB00072555", "PUB00101503", "PUB00101504", "PUB00101505" ]

[ "15136037", "23804760", "4336392", "4329247", "6575236" ]

[ "Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli.", "Structural basis for S-adenosylmethionine binding and methyltransferase activity by mitochondrial transcription factor B1.", "Mechanism of kasugamycin resistance in Escherichia coli.", "Change in methy...

[ 2004, 2013, 1972, 1971, 1983 ]

5

[]

0

null

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

[ 951, 30765, 8768, 2, 2, 657 ]

6

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

[ 17, 2, 13, 2, 1, 13, 5, 1, 9, 9, 1, 1, 19 ]

13

true

Domain

Ribosomal RNA adenine methylase transferase, N-terminal

rRNA_Ade_methylase_Trfase_N

8

IPR020599

20,599

Translation elongation factor P/YeiP

Transl_elong_fac_P/YeiP

Family

30,055

false

Members of this family possess translation elongation factor activity. They have been shown to stimulate efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro, possibly indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity a...

[]

0

[ "PIRSF", "PANTHER" ]

[ "PIRSF005901", "PTHR30053" ]

[ "EF-P", "" ]

[ 27831, 30055 ]

2

[]

0

[ "1ueb", "1yby", "3a5z", "3oyy", "3tre", "4v6a", "5j3b", "6enj", "6enu", "6j7m", "6rji", "6rk3", "6s8z", "8s8u", "8vwq", "8w2n" ]

16

[ "PUB00000702" ]

[ "9195040" ]

[ "Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction." ]

[ 1997 ]

1

[]

[ "IPR011768", "IPR011897" ]

0

2

0

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

[ 27514, 1900, 1, 639, 1 ]

5

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

[ 12, 2, 9, 11 ]

4

true

Family

Translation elongation factor P/YeiP

Transl_elong_fac_P/YeiP

7

IPR020600

20,600

Inosine monophosphate cyclohydrolase-like

IMP_cyclohydrolase-like

Domain

1,440

false

This entry represents inosine monophosphate (IMP) cyclohydrolase family, found in archaeal species, as well as some bacterial proteins of unknown function. IMP cyclohydrolase catalyses the cyclisation of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP, a reaction which is important in de novo purine biosynth...

[ "GO:0003937", "GO:0006164", "GO:0006188" ]

[ "IMP cyclohydrolase activity", "purine nucleotide biosynthetic process", "IMP biosynthetic process" ]

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

3

[ "PFAM" ]

[ "PF07826" ]

[ "IMP_cyclohyd" ]

[ 1440 ]

1

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

[ "3.5.4.10", "PWY-6123", "PWY-6124", "PWY-7234" ]

[ "EC:3.5.4.10", "METACYC:PWY-6123", "METACYC:PWY-6124", "METACYC:PWY-7234" ]

4

[ "1kuu", "2ntk", "2ntl", "2ntm" ]

4

[ "PUB00013793", "PUB00016548" ]

[ "11844782", "12012346" ]

[ "New class of IMP cyclohydrolases in Methanococcus jannaschii.", "Crystal structure of Methanobacterium thermoautotrophicum conserved protein MTH1020 reveals an NTN-hydrolase fold." ]

[ 2002, 2002 ]

2

[]

0

null

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

[ 455, 957, 28 ]

3

[]

0

true

Domain

Inosine monophosphate cyclohydrolase-like

IMP_cyclohydrolase-like

3

IPR020601

20,601

1-aminocyclopropane-1-carboxylate deaminase, bacterial

ACP_carboxylate_deaminase_bac

Family

1,253

false

1-aminocyclopropane-1-carboxylate deaminase ( ) is a pyridoxal phosphate-dependent enzyme which degrades 1-aminocyclopropane-1-carboxylate to ammonia and alpha-ketoglutarate. Some plant growth-promoting rhizobacteria can produce 1-aminocyclopropane-1-carboxylate deaminase to enhance plant growth [ , ]. This entry only ...

[ "GO:0008660", "GO:0030170", "GO:0009310" ]

[ "1-aminocyclopropane-1-carboxylate deaminase activity", "pyridoxal phosphate binding", "amine catabolic process" ]

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

3

[ "HAMAP" ]

[ "MF_00807" ]

[ "ACC_deaminase" ]

[ 1253 ]

1

[ "EC" ]

[ "3.5.99.7" ]

[ "EC:3.5.99.7" ]

1

[ "1rqx", "1tyz", "1tz2", "1tzj", "1tzk", "1tzm" ]

6

[ "PUB00046140", "PUB00063668", "PUB00063669" ]

[ "16524684", "22805914", "21523387" ]

[ "Reaction mechanisms of the bacterial enzyme 1-aminocyclopropane-1-carboxylate deaminase.", "Plant growth-promoting rhizobacteria (PGPR): emergence in agriculture.", "Metagenomic analysis of the 1-aminocyclopropane-1-carboxylate deaminase gene (acdS) operon of an uncultured bacterial endophyte colonizing Solanu...

[ 2006, 2012, 2011 ]

3

[ "IPR005965" ]

[]

1

0

1

[ "Bacteria", "Dikarya", "metagenomes" ]

[ 1228, 20, 5 ]

3

[]

0

true

Family

1-aminocyclopropane-1-carboxylate deaminase, bacterial

ACP_carboxylate_deaminase_bac

9

IPR020602

20,602

GTP cyclohydrolase I domain

GTP_CycHdrlase_I_dom

Domain

30,470

false

GTP cyclohydrolase I ( ) catalyses the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP [ ]. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. The comparison of the sequenc...

[]

0

[ "PFAM" ]

[ "PF01227" ]

[ "GTP_cyclohydroI" ]

[ 30470 ]

1

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

[ "3.5.4.16", "PWY-5663", "PWY-6147", "PWY-6703", "PWY-6983", "PWY-7442", "PWY-7852", "R-CEL-1474151", "R-DDI-1474151", "R-DME-1474151", "R-HSA-1474151", "R-MMU-1474151", "R-RNO-1474151", "R-SCE-1474151", "R-SPO-1474151" ]

[ "EC:3.5.4.16", "METACYC:PWY-5663", "METACYC:PWY-6147", "METACYC:PWY-6703", "METACYC:PWY-6983", "METACYC:PWY-7442", "METACYC:PWY-7852", "REACTOME:R-CEL-1474151", "REACTOME:R-DDI-1474151", "REACTOME:R-DME-1474151", "REACTOME:R-HSA-1474151", "REACTOME:R-MMU-1474151", "REACTOME:R-RNO-1474151", ...

15

[ "1a8r", "1a9c", "1fb1", "1fbx", "1gtp", "1is7", "1is8", "1n3r", "1n3s", "1n3t", "1wm9", "1wpl", "1wuq", "1wur", "4du6", "4uqf", "6z80", "6z85", "6z86", "6z87", "6z88", "6z89", "7ala", "7alb", "7alc", "7alq", "9p8z" ]

27

[ "PUB00000247", "PUB00022220", "PUB00035933" ]

[ "7542887", "12559918", "15767583" ]

[ "Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers.", "Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I.", "From cyclohydrolase to oxidoreductase: discovery of nitrile redu...

[ 1995, 2003, 2005 ]

3

[]

0

null

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

[ 241, 23544, 5911, 166, 608 ]

5

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

[ 4, 2, 2, 4, 1, 5, 3, 1, 4, 5, 1, 1, 8 ]

13

true

Domain

GTP cyclohydrolase I domain

GTP_CycHdrlase_I_dom

7

IPR020603

20,603

MraZ domain

MraZ_dom

Domain

19,558

false

This entry represents the 70 amino acid region found duplicated in the bacterial proteins MraZ [ ]. MraZ share protein structural similarity to the AbrB transition state regulator. MraZ from E. coli is a transcriptional regulator [ ].

[]

0

[ "PFAM" ]

[ "PF02381" ]

[ "MraZ" ]

[ 19558 ]

1

[]

0

[ "1n0e", "1n0f", "1n0g" ]

3

[ "PUB00028995", "PUB00074047" ]

[ "15146477", "24659771" ]

[ "Crystal structure of a protein associated with cell division from Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved sequence motif.", "The highly conserved MraZ protein is a transcriptional regulator in Escherichia coli." ]

[ 2004, 2014 ]

2

[ "IPR007159" ]

[]

1

0

1

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

[ 23, 19005, 25, 505 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

MraZ domain

MraZ_dom

6

IPR020605

20,605

Octanoyltransferase, conserved site

Octanoyltransferase_CS

Conserved_site

22,187

false

Lipoate-protein ligase B [ ] (gene lipB), alternatively known as octanoyltransferase ( ) is an enzyme that creates an amide linkage that joins the free carboxyl group of lipoic acid to the ε-amino group of a specific lysine residue in lipoate-dependent enzymes. octanoyl-[acyl-carrier-protein] + protein = protein N6-(oc...

[ "GO:0033819", "GO:0009249" ]

[ "lipoyl(octanoyl) transferase activity", "protein lipoylation" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE" ]

[ "PS01313" ]

[ "LIPB" ]

[ 22187 ]

1

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

[ "2.3.1.181", "PWY-6987", "PWY-7382", "R-DME-9857492", "R-DRE-9857492", "R-SCE-9857492", "R-SPO-9857492", "R-XTR-9857492" ]

[ "EC:2.3.1.181", "METACYC:PWY-6987", "METACYC:PWY-7382", "REACTOME:R-DME-9857492", "REACTOME:R-DRE-9857492", "REACTOME:R-SCE-9857492", "REACTOME:R-SPO-9857492", "REACTOME:R-XTR-9857492" ]

8

[ "1w66", "2qhs", "2qht", "2qhu", "2qhv" ]

5

[ "PUB00002260", "PUB00003773", "PUB00014819", "PUB00043601", "PUB00052307", "PUB00052308", "PUB00052309", "PUB00052310" ]

[ "8002607", "9268025", "11040290", "10966480", "1655709", "921841", "14700636", "11427685" ]

[ "Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein.", "Cloning and characterization of the lipoyl-protein ligase gene LIPB from the yeast Kluyveromyces lactis: synergistic respiratory deficiency due to mutations in LIPB and mi...

[ 1995, 1997, 2000, 2000, 1991, 1977, 2003, 2001 ]

8

[]

0

null

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

[ 72, 18061, 3593, 1, 460 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 11, 1, 3, 2, 1, 2, 1, 1, 3 ]

9

true

Conserved_site

Octanoyltransferase, conserved site

Octanoyltransferase_CS

9

IPR020606

20,606

Small ribosomal subunit protein uS7, conserved site

Ribosomal_uS7_CS

Conserved_site

47,944

false

This entry represents a conserved site located in the N-terminal section of the proteins. This entry includes the small ribosomal subunit protein uS7, formerly referred to as 30S ribosomal proteins S7 (bacterial, archaeal, plastid, mitochondrial), and eukaryotic 40S ribosomal proteins S5 (cytoplasmic) [ , , , ]. 30S ri...

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

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

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

3

[ "PROSITE" ]

[ "PS00052" ]

[ "RIBOSOMAL_S7" ]

[ 47944 ]

1

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

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

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

92

[ "1dv4", "1eg0", "1fjg", "1fka", "1hnw", "1hnx", "1hnz", "1hr0", "1hus", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1qd7", "1rss", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7"...

1,755

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

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

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

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

8

[]

0

null

[ "Archaea", "Bacillus phage BSP38", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 488, 1, 20456, 26699, 300 ]

5

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

[ 8, 1, 2, 4, 1, 5, 3, 1, 10, 5, 2, 3, 11 ]

13

true

Conserved_site

Small ribosomal subunit protein uS7, conserved site

Ribosomal_uS7_CS

4

IPR020608

20,608

RNA polymerase, subunit H/Rpb5, conserved site

RNA_pol_subH/Rpb5_CS

Conserved_site

3,494

false

Prokaryotes contain a single DNA-dependent RNA polymerase (RNAP; ) that is responsible for the transcription of all genes, while eukaryotes have three classes of RNAPs (I-III) that transcribe different sets of genes. Each class of RNA polymerase is an assemblage of ten to twelve different polypeptides. Certain subunits...

[]

0

[ "PROSITE" ]

[ "PS01110" ]

[ "RNA_POL_H_23KD" ]

[ 3494 ]

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

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

192

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

531

[ "PUB00003393", "PUB00004780", "PUB00008455", "PUB00008456" ]

[ "10191143", "1729711", "10841537", "10841538" ]

[ "RNA polymerase subunit H features a beta-ribbon motif within a novel fold that is present in archaea and eukaryotes.", "Component H of the DNA-dependent RNA polymerases of Archaea is homologous to a subunit shared by the three eucaryal nuclear RNA polymerases.", "Crystal structure of RPB5, a universal eukaryot...

[ 1999, 1992, 2000, 2000 ]

4

[]

0

null

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

[ 307, 3167, 6, 14 ]

4

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

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

12

true

Conserved_site

RNA polymerase, subunit H/Rpb5, conserved site

RNA_pol_subH/Rpb5_CS

2

IPR020610

20,610

Thiolase, active site

Thiolase_AS

Active_site

84,707

false

Two different types of thiolase [ , , ] are found both in eukaryotes and in prokaryotes: acetoacetyl-CoA thiolase ( ) and 3-ketoacyl-CoA thiolase ( ). 3-ketoacyl-CoA thiolase (also called thiolase I) has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-...

[ "GO:0016747" ]

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

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS00099" ]

[ "THIOLASE_3" ]

[ 84707 ]

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", "2.3.1.16", "PWY-481", "PWY-5109", "PWY-5136", "PWY-6080", "PWY-6435", "PWY-6443", "PWY-6458", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-6948", "PWY-7094", "PWY-7288", "PWY-7337", "PWY-7338", "PWY-7339", "PWY-7340", "PWY-735", "PWY-7606", "PWY-7654", "PWY-7726", ...

[ "EC:2.3.1", "EC:2.3.1.16", "METACYC:PWY-481", "METACYC:PWY-5109", "METACYC:PWY-5136", "METACYC:PWY-6080", "METACYC:PWY-6435", "METACYC:PWY-6443", "METACYC:PWY-6458", "METACYC:PWY-6944", "METACYC:PWY-6945", "METACYC:PWY-6946", "METACYC:PWY-6948", "METACYC:PWY-7094", "METACYC:PWY-7288", ...

121

[ "1afw", "1dlu", "1dlv", "1dm3", "1m1o", "1m1t", "1m3k", "1m3z", "1m4s", "1m4t", "1nl7", "1ou6", "1pxt", "1qfl", "1ulq", "1wdk", "1wdl", "1wdm", "1wl4", "1wl5", "2c7y", "2c7z", "2d3t", "2f2s", "2ib7", "2ib8", "2ib9", "2ibu", "2ibw", "2iby", "2iik", "2vtz"...

139

[ "PUB00001113", "PUB00002552", "PUB00003423", "PUB00052320" ]

[ "1755959", "2191949", "1354266", "15589695" ]

[ "Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier protein (SCPx) and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx.", "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural...

[ 1991, 1990, 1992, 2004 ]

4

[]

0

null

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

[ 637, 66548, 16753, 769 ]

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",...

[ 27, 3, 10, 5, 5, 26, 18, 3, 11, 40, 2, 1, 39 ]

13

true

Active_site

Thiolase, active site

Thiolase_AS

5

IPR020611

20,611

Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-1 conserved site

Cu2_ascorb_mOase_CS-1

Conserved_site

3,368

false

Copper type II, ascorbate-dependent monooxygenases [ ] are a class of enzymes that requires copper as a cofactor and which uses ascorbate as an electron donor. This family contains two related enzymes, dopamine-beta-monooxygenase ( ) and peptidyl-glycine alpha-amidating monooxygenase ( ). There are a few regions of seq...

[ "GO:0016715" ]

[ "oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS00084" ]

[ "CU2_MONOOXYGENASE_1" ]

[ 3368 ]

1

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

[ "1.14.17", "R-DME-209905", "R-HSA-209905", "R-MMU-209905", "R-RNO-209905" ]

[ "EC:1.14.17", "REACTOME:R-DME-209905", "REACTOME:R-HSA-209905", "REACTOME:R-MMU-209905", "REACTOME:R-RNO-209905" ]

5

[ "1opm", "1phm", "1sdw", "1yi9", "1yip", "1yjk", "1yjl", "3mib", "3mic", "3mid", "3mie", "3mif", "3mig", "3mih", "3mlj", "3mlk", "3mll", "3phm", "4e4z", "4zel", "5wkw", "5wm0", "6amp", "6an3", "8dsj", "8dsl", "8dsn" ]

27

[ "PUB00001578" ]

[ "2792366" ]

[ "Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain." ]

[ 1989 ]

1

[]

0

null

[ "Eukaryota", "Pseudomonadota" ]

[ 3362, 6 ]

2

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

[ 2, 4, 12, 5, 13 ]

5

true

Conserved_site

Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-1 conserved site

Cu2_ascorb_mOase_CS-1

4

IPR020612

20,612

Methylthiotransferase, conserved site

Methylthiotransferase_CS

Conserved_site

62,117

false

The methylthiotransferase (MTTase) or miaB-like family is named after the (dimethylallyl)adenosine tRNA MTTase miaB protein, which catalyses a C-H to C-S bond conversion in the methylthiolation of tRNA. A related bacterial enzyme rimO performs a similar methylthiolation, but on a protein substrate. RimO acts on the rib...

[ "GO:0051539" ]

[ "4 iron, 4 sulfur cluster binding" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS01278" ]

[ "MTTASE_RADICAL" ]

[ 62117 ]

1

[ "EC", "REACTOME" ]

[ "2.8.4", "R-HSA-6782315" ]

[ "EC:2.8.4", "REACTOME:R-HSA-6782315" ]

2

[ "2qgq", "4jc0", "7mjv", "7mjw", "7mjx", "7mjy", "7mjz", "9ccb" ]

8

[ "PUB00009728", "PUB00010539", "PUB00046148", "PUB00052321" ]

[ "11882645", "11222759", "18252828", "15289575" ]

[ "Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein.", "Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods.", "RimO, a MiaB-like enzyme, met...

[ 2002, 2001, 2008, 2004 ]

4

[]

0

null

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

[ 885, 54393, 5651, 4, 1184 ]

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" ]

[ 8, 2, 4, 2, 3, 6, 2, 6, 11, 13 ]

10

true

Conserved_site

Methylthiotransferase, conserved site

Methylthiotransferase_CS

6

IPR020613

20,613

Thiolase, conserved site

Thiolase_CS

Conserved_site

106,645

false

Two different types of thiolase [ , , ] are found both in eukaryotes and in prokaryotes: acetoacetyl-CoA thiolase ( ) and 3-ketoacyl-CoA thiolase ( ). 3-ketoacyl-CoA thiolase (also called thiolase I) has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-...

[ "GO:0016747" ]

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

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS00737" ]

[ "THIOLASE_2" ]

[ 106645 ]

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", "2.3.1.16", "PWY-481", "PWY-5109", "PWY-5136", "PWY-6080", "PWY-6435", "PWY-6443", "PWY-6458", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-6948", "PWY-7094", "PWY-7288", "PWY-7337", "PWY-7338", "PWY-7339", "PWY-7340", "PWY-735", "PWY-7606", "PWY-7654", "PWY-7726", ...

[ "EC:2.3.1", "EC:2.3.1.16", "METACYC:PWY-481", "METACYC:PWY-5109", "METACYC:PWY-5136", "METACYC:PWY-6080", "METACYC:PWY-6435", "METACYC:PWY-6443", "METACYC:PWY-6458", "METACYC:PWY-6944", "METACYC:PWY-6945", "METACYC:PWY-6946", "METACYC:PWY-6948", "METACYC:PWY-7094", "METACYC:PWY-7288", ...

137

[ "1afw", "1dlu", "1dlv", "1dm3", "1m1o", "1m1t", "1m3k", "1m3z", "1m4s", "1m4t", "1nl7", "1ou6", "1pxt", "1qfl", "1ulq", "1wdk", "1wdl", "1wdm", "1wl4", "1wl5", "2c7y", "2c7z", "2d3t", "2f2s", "2ib7", "2ib8", "2ib9", "2ibu", "2ibw", "2iby", "2iik", "2vtz"...

150

[ "PUB00001113", "PUB00002552", "PUB00003423", "PUB00052320" ]

[ "1755959", "2191949", "1354266", "15589695" ]

[ "Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier protein (SCPx) and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx.", "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural...

[ 1991, 1990, 1992, 2004 ]

4

[]

0

null

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

[ 916, 80997, 23615, 1117 ]

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",...

[ 22, 5, 12, 10, 5, 31, 19, 6, 11, 47, 2, 1, 47 ]

13

true

Conserved_site

Thiolase, conserved site

Thiolase_CS

6

IPR020615

20,615

Thiolase, acyl-enzyme intermediate active site

Thiolase_acyl_enz_int_AS

Active_site

78,840

false

Two different types of thiolase [ , , ] are found both in eukaryotes and in prokaryotes: acetoacetyl-CoA thiolase ( ) and 3-ketoacyl-CoA thiolase ( ). 3-ketoacyl-CoA thiolase (also called thiolase I) has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-...

[ "GO:0016747" ]

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

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS00098" ]

[ "THIOLASE_1" ]

[ 78840 ]

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", "2.3.1.16", "PWY-481", "PWY-5109", "PWY-5136", "PWY-6080", "PWY-6435", "PWY-6443", "PWY-6458", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-6948", "PWY-7094", "PWY-7288", "PWY-7337", "PWY-7338", "PWY-7339", "PWY-7340", "PWY-735", "PWY-7606", "PWY-7654", "PWY-7726", ...

[ "EC:2.3.1", "EC:2.3.1.16", "METACYC:PWY-481", "METACYC:PWY-5109", "METACYC:PWY-5136", "METACYC:PWY-6080", "METACYC:PWY-6435", "METACYC:PWY-6443", "METACYC:PWY-6458", "METACYC:PWY-6944", "METACYC:PWY-6945", "METACYC:PWY-6946", "METACYC:PWY-6948", "METACYC:PWY-7094", "METACYC:PWY-7288", ...

133

[ "1afw", "1dlu", "1dlv", "1dm3", "1m1t", "1m4s", "1m4t", "1nl7", "1ou6", "1pxt", "1qfl", "1ulq", "1wdk", "1wdl", "1wdm", "2c7y", "2c7z", "2d3t", "2f2s", "2ib7", "2ib8", "2ib9", "2ibu", "2ibw", "2iby", "2iik", "2vu0", "2vu1", "2vu2", "2wkt", "2wku", "2wkv"...

134

[ "PUB00001113", "PUB00002552", "PUB00003423", "PUB00052320" ]

[ "1755959", "2191949", "1354266", "15589695" ]

[ "Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier protein (SCPx) and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx.", "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural...

[ 1991, 1990, 1992, 2004 ]

4

[]

0

null

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

[ 345, 58081, 19790, 624 ]

4

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

[ 15, 5, 6, 11, 5, 34, 16, 5, 7, 31, 2, 22 ]

12

true

Active_site

Thiolase, acyl-enzyme intermediate active site

Thiolase_acyl_enz_int_AS

7

IPR020616

20,616

Thiolase, N-terminal

Thiolase_N

Domain

143,852

false

This entry represents the N-terminal domain of thiolases and related proteins. Two different types of thiolase [ , , ] are found both in eukaryotes and in prokaryotes: acetoacetyl-CoA thiolase ( ) and 3-ketoacyl-CoA thiolase ( ). 3-ketoacyl-CoA thiolase (also called thiolase I) has a broad chain-length specificity for ...

[ "GO:0016747" ]

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

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF00108" ]

[ "Thiolase_N" ]

[ 143852 ]

1

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

[ "2.3.1", "2.3.1.16", "GenProp0055", "GenProp1364", "PWY-481", "PWY-5109", "PWY-5136", "PWY-6080", "PWY-6435", "PWY-6443", "PWY-6458", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-6948", "PWY-7094", "PWY-7288", "PWY-7337", "PWY-7338", "PWY-7339", "PWY-7340", "PWY-735", "PWY-76...

[ "EC:2.3.1", "EC:2.3.1.16", "GP:GenProp0055", "GP:GenProp1364", "METACYC:PWY-481", "METACYC:PWY-5109", "METACYC:PWY-5136", "METACYC:PWY-6080", "METACYC:PWY-6435", "METACYC:PWY-6443", "METACYC:PWY-6458", "METACYC:PWY-6944", "METACYC:PWY-6945", "METACYC:PWY-6946", "METACYC:PWY-6948", "MET...

139

[ "1afw", "1dlu", "1dlv", "1dm3", "1m1o", "1m1t", "1m3k", "1m3z", "1m4s", "1m4t", "1nl7", "1ou6", "1pxt", "1qfl", "1ulq", "1wdk", "1wdl", "1wdm", "1wl4", "1wl5", "2c7y", "2c7z", "2d3t", "2f2s", "2ib7", "2ib8", "2ib9", "2ibu", "2ibw", "2iby", "2iik", "2vtz"...

185

[ "PUB00001113", "PUB00002552", "PUB00003423" ]

[ "1755959", "2191949", "1354266" ]

[ "Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier protein (SCPx) and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx.", "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural...

[ 1991, 1990, 1992 ]

3

[]

0

null

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

[ 3221, 110980, 27866, 1785 ]

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",...

[ 24, 5, 11, 12, 5, 49, 26, 6, 11, 51, 2, 1, 48 ]

13

true

Domain

Thiolase, N-terminal

Thiolase_N

3

IPR020617

20,617

Thiolase, C-terminal

Thiolase_C

Domain

123,122

false

This entry represents the C-terminal domain of thiolases and related proteins. Two different types of thiolase [ , , ] are found both in eukaryotes and in prokaryotes: acetoacetyl-CoA thiolase ( ) and 3-ketoacyl-CoA thiolase ( ). 3-ketoacyl-CoA thiolase (also called thiolase I) has a broad chain-length specificity for ...

[ "GO:0016747" ]

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

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF02803" ]

[ "Thiolase_C" ]

[ 123122 ]

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", "2.3.1.16", "PWY-481", "PWY-5109", "PWY-5136", "PWY-6080", "PWY-6435", "PWY-6443", "PWY-6458", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-6948", "PWY-7094", "PWY-7288", "PWY-7337", "PWY-7338", "PWY-7339", "PWY-7340", "PWY-735", "PWY-7606", "PWY-7654", "PWY-7726", ...

[ "EC:2.3.1", "EC:2.3.1.16", "METACYC:PWY-481", "METACYC:PWY-5109", "METACYC:PWY-5136", "METACYC:PWY-6080", "METACYC:PWY-6435", "METACYC:PWY-6443", "METACYC:PWY-6458", "METACYC:PWY-6944", "METACYC:PWY-6945", "METACYC:PWY-6946", "METACYC:PWY-6948", "METACYC:PWY-7094", "METACYC:PWY-7288", ...

131

[ "1afw", "1dlu", "1dlv", "1dm3", "1m1o", "1m1t", "1m3k", "1m3z", "1m4s", "1m4t", "1nl7", "1ou6", "1pxt", "1qfl", "1ulq", "1wdk", "1wdl", "1wdm", "1wl4", "1wl5", "2c7y", "2c7z", "2d3t", "2f2s", "2ib7", "2ib8", "2ib9", "2ibu", "2ibw", "2iby", "2iik", "2vtz"...

164

[ "PUB00001113", "PUB00002552", "PUB00003423" ]

[ "1755959", "2191949", "1354266" ]

[ "Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier protein (SCPx) and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx.", "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural...

[ 1991, 1990, 1992 ]

3

[]

0

null

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

[ 920, 97842, 23014, 1346 ]

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",...

[ 23, 4, 10, 6, 5, 26, 18, 5, 11, 40, 2, 1, 54 ]

13

true

Domain

Thiolase, C-terminal

Thiolase_C

1

IPR020618

20,618

Adenylate kinase isoenzyme 6

Adenyl_kinase_AK6

Family

5,644

false

Adenylate kinase isoenzyme 6 (AK6) is a broad-specificity nucleoside monophosphate (NMP) kinase that catalyses the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates [ ]. AMP and dAMP are the preferred substrates, but CMP and dCMP are also good substrates. All nucleo...

[ "GO:0004017", "GO:0005524", "GO:0016887" ]

[ "AMP kinase activity", "ATP binding", "ATP hydrolysis activity" ]

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

3

[ "HAMAP", "PANTHER" ]

[ "MF_00039", "PTHR12595" ]

[ "Adenylate_kinase_AK6", "" ]

[ 4815, 5572 ]

2

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

[ "2.7.4.3", "PWY-7219", "R-BTA-499943", "R-CEL-499943", "R-DDI-499943", "R-DME-499943", "R-HSA-499943", "R-MMU-499943", "R-PFA-499943", "R-RNO-499943", "R-SCE-499943", "R-SPO-499943" ]

[ "EC:2.7.4.3", "METACYC:PWY-7219", "REACTOME:R-BTA-499943", "REACTOME:R-CEL-499943", "REACTOME:R-DDI-499943", "REACTOME:R-DME-499943", "REACTOME:R-HSA-499943", "REACTOME:R-MMU-499943", "REACTOME:R-PFA-499943", "REACTOME:R-RNO-499943", "REACTOME:R-SCE-499943", "REACTOME:R-SPO-499943" ]

12

[ "1rkb", "1y63", "3iij", "3iik", "3iil", "3iim", "4cvn", "4cw7", "5jzv" ]

9

[ "PUB00030703", "PUB00056952", "PUB00068768" ]

[ "15630091", "22038794", "16079131" ]

[ "The crystal structure of human adenylate kinase 6: An adenylate kinase localized to the cell nucleus.", "hCINAP is an atypical mammalian nuclear adenylate kinase with an ATPase motif: Structural and functional studies.", "Characterization of hCINAP, a novel coilin-interacting protein encoded by a transcript fr...

[ 2005, 2011, 2005 ]

3

[]

0

null

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

[ 883, 9, 4723, 29 ]

4

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

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

12

true

Family

Adenylate kinase isoenzyme 6

Adenyl_kinase_AK6

3