LiteFold/InterPro · Datasets at Hugging Face

IPR023041

23,041

Glucose receptor Git3-like, N-terminal

Glucose_rcpt_Git3-like_N

Domain

1,937

false

This entry contains the conserved N-terminal uncharacterised region belonging to the G-protein coupled receptors Git3, GPR1, GPR2, and GPR3 that are involved in glucose sensing and signaling pathways. Git3, found in Schizosaccharomyces pombe, is one of six proteins required for glucose-triggered adenylate cyclase activ...

[]

0

[ "PFAM" ]

[ "PF11710" ]

[ "Git3" ]

[ 1937 ]

1

[]

0

[]

0

[ "PUB00053759", "PUB00160293", "PUB00160297", "PUB00160298" ]

[ "11014802", "38649409", "10361302", "15494315" ]

[ "Glucose monitoring in fission yeast via the Gpa2 galpha, the git5 Gbeta and the git3 putative glucose receptor.", "The nematode-trapping fungus Arthrobotrys oligospora detects prey pheromones via G protein-coupled receptors.", "A Saccharomyces cerevisiae G-protein coupled receptor, Gpr1, is specifically requir...

[ 2000, 2024, 1999, 2004 ]

4

[]

0

null

[ "Eukaryota" ]

[ 1937 ]

1

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

[ 1, 1, 1 ]

3

true

Domain

Glucose receptor Git3-like, N-terminal

Glucose_rcpt_Git3-like_N

5

IPR023042

23,042

Peptidase M17, leucine aminopeptidase

Peptidase_M17_leu_NH2_pept

Family

21,827

false

The majority of members of this family are zinc-dependent exopeptidases belonging to MEROPS peptidase family M17 (leucyl aminopeptidase, clan MF). This family excludes pepB aminopeptidases, which are also members of MEROPS family M17 (see ).

[]

0

[ "HAMAP" ]

[ "MF_00181" ]

[ "Cytosol_peptidase_M17" ]

[ 21827 ]

1

[ "EC", "EC" ]

[ "3.4.11.1", "3.4.11.10" ]

[ "EC:3.4.11.1", "EC:3.4.11.10" ]

2

[ "1bll", "1bpm", "1bpn", "1gyt", "1lam", "1lan", "1lap", "1lcp", "2ewb", "2j9a", "3h8e", "3h8f", "3h8g", "3jru", "3kqx", "3kqz", "3kr4", "3kr5", "3pei", "3t8w", "4k3n", "4ksi", "4r6t", "4r76", "4r7m", "4zi6", "4zla", "5d8n", "6ee2", "6ome", "6wvv", "7k5k"...

43

[ "PUB00000202", "PUB00000522", "PUB00001416", "PUB00003579", "PUB00004713", "PUB00011211", "PUB00011212", "PUB00011213", "PUB00011215", "PUB00014575" ]

[ "1908238", "8439290", "1555602", "7674922", "2395881", "8703509", "10449417", "10970742", "8506345", "2670557" ]

[ "Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase.", "Evolutionary families of peptidases.", "Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants.", "Evolutio...

[ 1991, 1993, 1992, 1995, 1990, 1996, 1999, 2000, 1993, 1989 ]

10

[ "IPR011356" ]

[]

1

0

1

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

[ 68, 18671, 2725, 363 ]

4

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

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

8

true

Family

Peptidase M17, leucine aminopeptidase

Peptidase_M17_leu_NH2_pept

6

IPR023043

23,043

NAD(P)H-quinone oxidoreductase subunit 3, bacterial/plastid

NAD(P)H_OxRDtase_bac/plastid

Family

28,652

false

This family represents the subunit 3 of complex I.

[ "GO:0016651" ]

[ "oxidoreductase activity, acting on NAD(P)H" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01394" ]

[ "NDH1_NuoA" ]

[ 28652 ]

1

[ "EC" ]

[ "7.1.1.-" ]

[ "EC:7.1.1.-" ]

1

[ "3rko", "4he8", "4hea", "6hum", "6i0d", "6i1p", "6khi", "6khj", "6l7o", "6l7p", "6nbq", "6nbx", "6nby", "6q8o", "6q8w", "6q8x", "6tjv", "6x89", "6y11", "6ziy", "6zjl", "6zjn", "6zjy", "7a23", "7a24", "7aqq", "7ar7", "7ar8", "7arb", "7eu3", "7f9o", "7nyh"...

68

[ "PUB00005074", "PUB00043561", "PUB00045437" ]

[ "1470679", "10940377", "18394423" ]

[ "The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.", "The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.", "Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)." ]

[ 1992, 2000, 2008 ]

3

[ "IPR000440" ]

[]

1

0

1

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

[ 15012, 13087, 149, 404 ]

4

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

[ 6, 1, 4, 4 ]

4

true

Family

NAD(P)H-quinone oxidoreductase subunit 3, bacterial/plastid

NAD(P)H_OxRDtase_bac/plastid

2

IPR023045

23,045

Molybdenum cofactor biosynthesis C

MoaC

Family

22,425

false

The majority of molybdenum-containing enzymes utilise a molybdenum cofactor (MoCF or Moco) consisting of a Mo atom coordinated via a cis-dithiolene moiety to molybdopterin (MPT). MoCF is ubiquitous in nature, and the pathway for MoCF biosynthesis is conserved in all three domains of life. MoCF-containing enzymes functi...

[ "GO:0006777" ]

[ "Mo-molybdopterin cofactor biosynthetic process" ]

[ "biological_process" ]

1

[ "NCBIFAM" ]

[ "TIGR00581" ]

[ "moaC" ]

[ 22425 ]

1

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

[ "4.6.1.17", "GenProp0466", "GenProp1711", "PWY-6823", "R-BTA-947581", "R-DME-947581", "R-HSA-947581", "R-MMU-947581" ]

[ "EC:4.6.1.17", "GP:GenProp0466", "GP:GenProp1711", "METACYC:PWY-6823", "REACTOME:R-BTA-947581", "REACTOME:R-DME-947581", "REACTOME:R-HSA-947581", "REACTOME:R-MMU-947581" ]

8

[ "1ekr", "1eks", "2eey", "2ekn", "2ide", "2iih", "2ohd", "3jqj", "3jqk", "3jqm", "4fdf", "4pya", "4pyd" ]

13

[ "PUB00015635", "PUB00015921", "PUB00034757", "PUB00034758", "PUB00034759" ]

[ "12372836", "8528286", "12114025", "17198377", "16784786" ]

[ "In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli.", "Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamo...

[ 2002, 1995, 2002, 2007, 2006 ]

5

[]

[ "IPR023047", "IPR047594" ]

0

2

0

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

[ 757, 18313, 2989, 366 ]

4

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

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

10

true

Family

Molybdenum cofactor biosynthesis C

MoaC

8

IPR023047

23,047

Probable cyclic pyranopterin monophosphate synthase accessory protein, archaea

Mo_CF_biosynth-C_arc

Family

687

false

This entry contains probable cyclic pyranopterin monophosphate synthase accessory protein (also known as molybdenum cofactor biosynthesis protein C, or MoaC) from archaea. Members of this entry seem to be an outgroup of the eukaryotic and bacterial branch. Members of this MoaC family are involved in molybdenum cofactor...

[]

0

[ "HAMAP", "CDD" ]

[ "MF_01224_A", "cd01419" ]

[ "MoaC_A", "MoaC_A" ]

[ 662, 611 ]

2

[ "EC", "METACYC" ]

[ "4.6.1.17", "PWY-6823" ]

[ "EC:4.6.1.17", "METACYC:PWY-6823" ]

2

[ "2ekn", "2ohd" ]

2

[ "PUB00079808" ]

[ "11913130" ]

[ "Biosynthesis and molecular biology of the molybdenum cofactor (Moco)." ]

[ 2002 ]

1

[ "IPR023045" ]

[]

1

0

1

[ "Archaea", "ecological metagenomes" ]

[ 683, 4 ]

2

[]

0

true

Family

Probable cyclic pyranopterin monophosphate synthase accessory protein, archaea

Mo_CF_biosynth-C_arc

3

IPR023048

23,048

NADH:quinone oxidoreductase, FMN-dependent

NADH:quinone_OxRdtase_FMN_depd

Family

18,204

false

This entry represents FMN-dependent NADH:quinone oxidoreductases (also known as FMN-dependent NADH-azoreductases) which function as quinone reductases that provides resistance to thiol-specific stress caused by electrophilic quinones [ ]. These enzymes also exhibit azoreductase activity, catalysing the reductive cleava...

[ "GO:0010181", "GO:0016655" ]

[ "FMN binding", "oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP" ]

[ "MF_01216" ]

[ "Azoreductase_type1" ]

[ 18204 ]

1

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

[ "1.6.5.-", "1.7.1.17", "PWY-2261", "PWY-6370" ]

[ "EC:1.6.5.-", "EC:1.7.1.17", "METACYC:PWY-2261", "METACYC:PWY-6370" ]

4

[ "1t5b", "1tik", "1v4b", "2d5i", "2hpv", "2v9c", "2z98", "2z9b", "2z9c", "2z9d", "3keg", "3lt5", "3p0r", "3r6w", "3u7i", "3w77", "3w78", "3w79", "3w7a", "4c0w", "4c0x", "4c14", "4ese", "4m0c", "4n65", "4n9q", "5jro", "6dxp", "6jxn", "6jxs", "6qu0", "7awv"...

36

[ "PUB00049638", "PUB00096689", "PUB00096690" ]

[ "17904577", "17284825", "24915188" ]

[ "Molecular cloning, characterisation and ligand-bound structure of an azoreductase from Pseudomonas aeruginosa.", "Characterization of a NADH:dichloroindophenol oxidoreductase from Bacillus subtilis.", "Identification of NAD(P)H quinone oxidoreductase activity in azoreductases from P. aeruginosa: azoreductases ...

[ 2007, 2007, 2014 ]

3

[]

0

null

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

[ 18081, 62, 3, 1, 57 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

NADH:quinone oxidoreductase, FMN-dependent

NADH:quinone_OxRdtase_FMN_depd

5

IPR023049

23,049

Glucose-1-phosphate adenylyltransferase GlgC, bacterial

GlgC_bac

Family

13,291

false

This entry represent glucose-1-phosphate adenylyltransferase, also called ADP-glucose pyrophosphorylase [ ]. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This entry describes the GlgC subunit only.

[ "GO:0008878", "GO:0005978" ]

[ "glucose-1-phosphate adenylyltransferase activity", "glycogen biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_00624" ]

[ "GlgC" ]

[ 13291 ]

1

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

[ "2.7.7.27", "PWY-622", "PWY-7902" ]

[ "EC:2.7.7.27", "METACYC:PWY-622", "METACYC:PWY-7902" ]

3

[ "3brk", "5l6s", "5l6v", "5mni", "5w5r", "5w5t", "5w6j", "6r8b", "6r8u", "6shj", "6shn", "6shq", "6si8", "6v96", "6v99", "6v9a", "6vr0" ]

17

[ "PUB00068785" ]

[ "7079236" ]

[ "[Clinical aspect of undifferentiated thyroid tumor (author's transl)]" ]

[ 1982 ]

1

[ "IPR011831" ]

[]

1

0

1

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

[ 13158, 6, 127 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glucose-1-phosphate adenylyltransferase GlgC, bacterial

GlgC_bac

7

IPR023050

23,050

Bifunctional protein PyrR

PyrR

Family

10,409

false

The PyrR protein from Bacillus subtilis and many other bacteria is a bifunctional protein. Its primary function is the regulation of expression of pyrimidine biosynthetic (pyr) genes by binding to specific sites on pyr mRNA in a uridine nucleotide-dependent manner and altering the folding of downstream RNA to promote t...

[]

0

[ "HAMAP" ]

[ "MF_01219" ]

[ "PyrR" ]

[ 10409 ]

1

[ "EC", "METACYC" ]

[ "2.4.2.9", "PWY-7183" ]

[ "EC:2.4.2.9", "METACYC:PWY-7183" ]

2

[ "1a3c", "1a4x", "1non", "1ufr", "1w30", "1xz8", "1xzn", "2igb", "4p3k", "4p80", "4p81", "4p82", "4p83", "4p84", "4p86", "5iao" ]

16

[ "PUB00053983" ]

[ "12482852" ]

[ "Kinetic studies of the uracil phosphoribosyltransferase reaction catalyzed by the Bacillus subtilis pyrimidine attenuation regulatory protein PyrR." ]

[ 2003 ]

1

[]

0

null

[ "Bacteria", "Candidatus Iainarchaeum sp.", "Geodia barretti", "unclassified sequences" ]

[ 10095, 1, 7, 306 ]

4

[]

0

true

Family

Bifunctional protein PyrR

PyrR

9

IPR023051

23,051

Low affinity potassium transport system protein Kup

Kup

Family

12,111

false

This entry represents potassium transport Kup system proteins. These proteins are involved in the uptake of K+ ions under hyper-osmotic stress [ ] and likely operate as K+:H+ symporters. Kup proteins are composed of two domains--an integral membrane domain that has 12 putative trans-membrane sections and a hydrophilic ...

[]

0

[ "HAMAP" ]

[ "MF_01522" ]

[ "Kup" ]

[ 12111 ]

1

[]

0

[]

0

[ "PUB00053980" ]

[ "10214935" ]

[ "Kup is the major K+ uptake system in Escherichia coli upon hyper-osmotic stress at a low pH." ]

[ 1999 ]

1

[ "IPR003855" ]

[]

1

0

1

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

[ 11964, 43, 33, 71 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Low affinity potassium transport system protein Kup

Kup

6

IPR023052

23,052

Cell division protein SepF

Cell_div_SepF

Family

12,048

false

This entry represents a cell division protein, designated SepF, which is conserved in Gram-positive bacteria. SepF accumulates at the cell division site in an FtsZ-dependent manner and is required for proper septum formation [ ]. Mutants are viable but the formation of the septum is much slower and occurs with a very a...

[ "GO:0090529" ]

[ "cell septum assembly" ]

[ "biological_process" ]

1

[ "HAMAP", "PANTHER" ]

[ "MF_01197", "PTHR35798" ]

[ "SepF", "" ]

[ 11148, 12048 ]

2

[]

0

[ "3p04", "3zih", "3zii", "6sat", "6scp", "6scq", "6scs", "8hzq", "8hzt" ]

9

[ "PUB00043574" ]

[ "16420366" ]

[ "SepF, a novel FtsZ-interacting protein required for a late step in cell division." ]

[ 2006 ]

1

[ "IPR007561" ]

[]

1

0

1

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

[ 11784, 14, 250 ]

3

[]

0

true

Family

Cell division protein SepF

Cell_div_SepF

5

IPR023053

23,053

Small ribosomal subunit protein uS14, bacteria

Ribosomal_uS14_bact

Family

9,702

false

This entry includes bacterial small ribosomal subunit protein uS14. In bacteria the gene coding for ribosomal protein S14 has been subject to horizontal gene transfer, subsequent differential gene loss and insertions/deletions near the N terminus. Different groups have been described according to this [ ]. This family ...

[]

0

[ "HAMAP", "NCBIFAM" ]

[ "MF_01364_B", "NF005974" ]

[ "Ribosomal_uS14_2_B", "PRK08061.1" ]

[ 9357, 9702 ]

2

[]

0

[ "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"...

564

[ "PUB00004441", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00015636", "PUB00043008", "PUB00053984", "PUB00104044", "PUB00104296" ]

[ "8441676", "11297922", "11290319", "11114498", "12904577", "15049826", "11102698", "11574053", "9746356" ]

[ "Zinc finger-like motifs in rat ribosomal proteins S27 and S29.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Comparative genomics of bacterial zinc regulons: enhanced ion transport, pathogenesis, and r...

[ 1993, 2001, 2001, 2000, 2003, 2004, 2000, 2001, 1998 ]

9

[ "IPR001209" ]

[]

1

0

1

[ "Ascaris suum", "Bacteria", "unclassified sequences" ]

[ 1, 9578, 123 ]

3

[]

0

true

Family

Small ribosomal subunit protein uS14, bacteria

Ribosomal_uS14_bact

6

IPR023055

23,055

Putative competence-damage inducible protein, Archaea

CinA_Arc

Family

81

false

This entry represents a putative competence-damage inducible protein from Archaea, related to CinA from bacteria ( ).

[]

0

[ "HAMAP" ]

[ "MF_00226_A" ]

[ "CinA_A" ]

[ 81 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Archaea" ]

[ 81 ]

1

[]

0

true

Family

Putative competence-damage inducible protein, Archaea

CinA_Arc

3

IPR023057

23,057

Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme

GlnE

Family

15,665

false

This entry represents GlnE family proteins. These proteins adenylate and deadenylate glutamate-ammonia ligases: ATP + {L-Glutamate:ammonia ligase (ADP-forming)} = Diphosphate + Adenylyl-{L-Glutamate:Ammonia ligase (ADP-forming)} The two activities are functionally the reverse of one another and must be controlled by th...

[ "GO:0008882" ]

[ "[glutamate-ammonia-ligase] adenylyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "PANTHER" ]

[ "MF_00802", "PTHR30621" ]

[ "GlnE", "" ]

[ 11449, 15665 ]

2

[ "EC", "EC" ]

[ "2.7.7.42", "2.7.7.89" ]

[ "EC:2.7.7.42", "EC:2.7.7.89" ]

2

[ "1v4a", "3k7d" ]

2

[ "PUB00084183" ]

[ "11585846" ]

[ "The story of glutamine synthetase regulation." ]

[ 2001 ]

1

[]

0

null

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

[ 15404, 26, 235 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme

GlnE

3

IPR023059

23,059

Foldase protein PrsA

Foldase_PrsA

Family

3,751

false

The PrsA protein of Bacillus subtilis is an essential membrane-bound lipoprotein that is assumed to assist post-translocational folding of exported proteins and stabilise them in the compartment between the cytoplasmic membrane and cell wall. This folding activity is consistent with the homology of a segment of PrsA wi...

[ "GO:0003755" ]

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

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01145" ]

[ "Foldase_PrsA" ]

[ 3751 ]

1

[ "EC" ]

[ "5.2.1.8" ]

[ "EC:5.2.1.8" ]

1

[ "4wo7", "5htf", "5tvl", "6vj4", "6vj6", "7l75", "9ibn" ]

7

[ "PUB00053986" ]

[ "14976191" ]

[ "Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis." ]

[ 2004 ]

1

[]

0

null

[ "Bacteria", "Rhamnusium bicolor", "Siphoviridae sp. ctHip2", "metagenomes" ]

[ 3746, 1, 1, 3 ]

4

[]

0

true

Family

Foldase protein PrsA

Foldase_PrsA

6

IPR023060

23,060

Membrane insertase YidC/YidC1/YidC2, Firmicutes

YidC/YidC1/YidC2_Firmicutes

Family

4,642

false

This family includes membrane insertase YidC, YidC1 (also called MisCB), and YidC2 (also called MisCA). Members in this family are required for the insertion of integral membrane proteins into the membrane. They may also be involved in protein secretion processes. Besides having the membrane insertase function, Bacillu...

[ "GO:0032977", "GO:0016020" ]

[ "membrane insertase activity", "membrane" ]

[ "molecular_function", "cellular_component" ]

2

[ "HAMAP" ]

[ "MF_01811" ]

[ "YidC_type2" ]

[ 4642 ]

1

[]

0

[ "3wo6", "3wo7" ]

2

[ "PUB00003117", "PUB00060579", "PUB00060580" ]

[ "1487728", "11889108", "12586834" ]

[ "Structure and function of the spoIIIJ gene of Bacillus subtilis: a vegetatively expressed gene that is essential for sigma G activity at an intermediate stage of sporulation.", "Analysis of the Bacillus subtilis spoIIIJ gene and its Paralogue gene, yqjG.", "Complementary impact of paralogous Oxa1-like proteins...

[ 1992, 2002, 2003 ]

3

[ "IPR001708" ]

[]

1

0

1

[ "Bacteria" ]

[ 4642 ]

1

[]

0

true

Family

Membrane insertase YidC/YidC1/YidC2, Firmicutes

YidC/YidC1/YidC2_Firmicutes

9

IPR023061

23,061

Selenophosphate synthetase, class I

SelD_I

Family

9,031

false

The UGA (TGA) codon is normally a termination codon, however it is also used as a selenocysteine (Sec) codon by numerous organisms [ ]. Sec is the 21st amino acid that is inserted into selenoproteins (protein that includes a selenocysteine (Se-Cys) amino acid residue). The synthesis of Sec and its incorporation into pr...

[ "GO:0004756", "GO:0005524", "GO:0016260" ]

[ "selenide, water dikinase activity", "ATP binding", "L-selenocysteine biosynthetic process" ]

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

3

[ "HAMAP" ]

[ "MF_00625" ]

[ "SelD" ]

[ 9031 ]

1

[ "EC", "METACYC" ]

[ "2.7.9.3", "PWY-6281" ]

[ "EC:2.7.9.3", "METACYC:PWY-6281" ]

2

[ "2yye", "2zod", "3u0o" ]

3

[ "PUB00000070", "PUB00014691", "PUB00072493", "PUB00072494", "PUB00072501" ]

[ "2142875", "8986768", "8811175", "2405383", "1557403" ]

[ "Selenium biochemistry.", "Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism?", "Selenocysteine.", "In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD ...

[ 1990, 1996, 1996, 1990, 1992 ]

5

[ "IPR004536" ]

[]

1

0

1

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

[ 8909, 33, 18, 71 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Selenophosphate synthetase, class I

SelD_I

1

IPR023064

23,064

D-ribose pyranase

D-ribose_pyranase

Family

6,213

false

D-ribose pyranase catalyses the interconversion of beta-pyran and beta-furan forms of D-ribose.

[ "GO:0016872" ]

[ "intramolecular lyase activity" ]

[ "molecular_function" ]

1

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

[ "MF_01661", "NF008761", "PTHR37831" ]

[ "D_rib_pyranase", "PRK11797.1", "" ]

[ 5445, 6014, 6211 ]

3

[ "EC" ]

[ "5.4.99.62" ]

[ "EC:5.4.99.62" ]

1

[ "1ogc", "1ogd", "1oge", "1ogf", "3e7n", "3p12", "3p13" ]

7

[ "PUB00010214", "PUB00020761", "PUB00020762", "PUB00029425" ]

[ "11320319", "15876375", "15060078", "12738765" ]

[ "Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli RbsD, a component of the ribose-transport system with unknown biochemical function.", "Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase.", "NMR application probes a novel and ubiqu...

[ 2001, 2005, 2004, 2003 ]

4

[ "IPR007721" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Plasmodiophora brassicae", "metagenomes" ]

[ 8, 6160, 1, 44 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-ribose pyranase

D-ribose_pyranase

1

IPR023065

23,065

Uncharacterised protein family ApaG

Uncharacterised_ApaG

Family

6,929

false

This entry represents the bacterial protein ApaG that contains a single ApaG domain, which is ~125 amino acids in length. The Salmonella typhimurium ApaG domain protein, CorD, is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different ApaG proteins show a fold of several β-sheets. The ApaG d...

[]

0

[ "HAMAP" ]

[ "MF_00791" ]

[ "ApaG" ]

[ 6929 ]

1

[]

0

[ "1tza", "1xq4", "1xvs", "2f1e" ]

4

[ "PUB00009972", "PUB00016988", "PUB00016989" ]

[ "1779764", "10945468", "15213450" ]

[ "Magnesium transport in Salmonella typhimurium: the influence of new mutations conferring Co2+ resistance on the CorA Mg2+ transport system.", "cDNA cloning and expression analysis of new members of the mammalian F-box protein family.", "1H, 15N and 13C resonance assignments of the ApaG protein of the phytopath...

[ 1991, 2000, 2004 ]

3

[]

0

null

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

[ 6797, 42, 90 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised protein family ApaG

Uncharacterised_ApaG

8

IPR023066

23,066

Quinolinate synthase A, type 2

Quinolinate_synth_type2

Family

6,452

false

This entry represents a group of bacterial type 2 quinolinate synthetases (NadA). Quinolinate synthetase catalyses the second step of the de novo biosynthetic pathway of pyridine nucleotide formation. In particular, quinolinate synthetase is involved in the condensation of dihydroxyacetone phosphate and iminoaspartate ...

[ "GO:0016765" ]

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

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00568" ]

[ "NadA_type2" ]

[ 6452 ]

1

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

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

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

5

[ "1wzu", "4hhe", "4p3x", "4zk6", "5f33", "5f35", "5f3d", "5ktm", "5ktn", "5kto", "5ktp", "5ktr", "5kts", "5ktt", "5lqm", "5lqs", "6f48", "6f4d", "6f4l", "6g74", "6i0k", "6i0p", "6i0r", "6nso", "6nsu", "6or8", "6ora", "7p4m", "7p4p", "7p4q" ]

30

[ "PUB00009471" ]

[ "10648170" ]

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

[ 2000 ]

1

[ "IPR003473" ]

[]

1

0

1

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

[ 347, 6009, 13, 1, 82 ]

5

[]

0

true

Family

Quinolinate synthase A, type 2

Quinolinate_synth_type2

5

IPR023067

23,067

DNA protection during starvation protein, gammaproteobacteria

Dps_gammaproteobac

Family

919

false

This group belongs to the ferritin domain superfamily and has the ferritin-like structural fold. Ferritins constitute a broad superfamily of iron storage proteins, widespread in all domains of life [ , ]. Ferritins and bacterioferritins have essentially the same architecture, assembling in a 24mer cluster to form a hol...

[ "GO:0016722" ]

[ "oxidoreductase activity, acting on metal ions" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01441" ]

[ "Dps" ]

[ 919 ]

1

[]

0

[ "1dps", "1f30", "1f33", "1jre", "1jts", "1l8h", "1l8i", "3ak8", "3ak9", "4dyu", "5xgo", "6b0d", "6gcm", "6zgl", "7aqs", "8ouc", "8pv9" ]

17

[ "PUB00001907", "PUB00016778", "PUB00016788", "PUB00016824", "PUB00016848", "PUB00016871", "PUB00054022" ]

[ "1340475", "11230141", "15365182", "12727864", "10403254", "12730463", "19231146" ]

[ "A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli.", "Regulated phase transitions of bacterial chromatin: a non-enzymatic pathway for generic DNA protection.", "Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA ...

[ 1992, 2001, 2004, 2003, 1999, 2003, 2010 ]

7

[ "IPR002177" ]

[]

1

0

1

[ "Bacteria", "Eukaryota" ]

[ 917, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

DNA protection during starvation protein, gammaproteobacteria

Dps_gammaproteobac

4

IPR023068

23,068

CCA-adding enzyme, firmicutes

CCA-adding_enz_firmicutes

Family

2,734

false

This family consists of CCA tRNA adenylyltransferases from the firmicutes [ , ]. CCA tRNA nucleotidyltransferase, also known as CCA-adding enzyme, are responsible for the synthesis and repair of the 3' terminal CCA sequence of tRNA molecules. They are encoded by essential genes in almost all organisms and add the three...

[ "GO:0004810", "GO:0001680" ]

[ "CCA tRNA nucleotidyltransferase activity", "tRNA 3'-terminal CCA addition" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01263" ]

[ "CCA_bact_type3" ]

[ 2734 ]

1

[ "EC" ]

[ "2.7.7.72" ]

[ "EC:2.7.7.72" ]

1

[ "1miv", "1miw", "1miy" ]

3

[ "PUB00015829", "PUB00059199" ]

[ "12526808", "9829937" ]

[ "Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP.", "The Bacillus subtilis nucleotidyltransferase is a tRNA CCA-adding enzyme." ]

[ 2002, 1998 ]

2

[]

0

null

[ "Bacteria", "Trichuris trichiura", "human gut metagenome" ]

[ 2732, 1, 1 ]

3

[]

0

true

Family

CCA-adding enzyme, firmicutes

CCA-adding_enz_firmicutes

5

IPR023069

23,069

Chaperone TorD

Chaperone_TorD

Family

1,445

false

The TorD protein, after which this family is named, is involved in the maturation of the the trimethylamine N-oxide reductase TorA in Escherichia coli [ ]. TorA is a molybdenum-containing enzyme which requires the the insertion of a bis(molybdopterin guanine dinucleotide) molybdenum (bis(MGD)Mo) cofactor in its catalyt...

[]

0

[ "HAMAP", "NCBIFAM" ]

[ "MF_01150", "NF003442" ]

[ "TorD", "PRK04976.1" ]

[ 1308, 1443 ]

2

[]

0

[ "1n1c" ]

1

[ "PUB00012283" ]

[ "12766163" ]

[ "Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA." ]

[ 2003 ]

1

[ "IPR020945" ]

[]

1

0

1

[ "Bacteria" ]

[ 1445 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Chaperone TorD

Chaperone_TorD

7

IPR023070

23,070

DnaA initiator-associating protein

DiaA

Family

1,024

false

This entry represents DnaA initiator-associating proteins which are required for the timely initiation of chromosomal replication [ ].

[]

0

[ "HAMAP", "NCBIFAM" ]

[ "MF_01157", "NF008138" ]

[ "SIS_DiaA", "PRK10886.1" ]

[ 882, 1024 ]

2

[ "GP" ]

[ "GenProp1210" ]

[ "GP:GenProp1210" ]

1

[ "2yva", "4u6n" ]

2

[ "PUB00053988" ]

[ "15326179" ]

[ "DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication." ]

[ 2004 ]

1

[ "IPR035461" ]

[]

1

0

1

[ "Bacteria" ]

[ 1024 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

DnaA initiator-associating protein

DiaA

5

IPR023071

23,071

Transcriptional regulator, SlyA

Tscrpt_reg_SlyA

Family

1,076

false

This entry represents transcriptional regulators SlyA. In Escherichia coli, SlyA activates expression of genes such as molecular chaperones (groL, groS, dnaK, grpE, and cbpA), proteins involved in acid resistance (hdeA, hdeB, and gadA), the starvation lipoprotein slp, virulence protein hlyE/clyA. Represses expression o...

[]

0

[ "HAMAP" ]

[ "MF_01819" ]

[ "HTH_type_SlyA" ]

[ 1076 ]

1

[]

0

[ "3deu", "3q5f", "3qpt", "4aih", "4aij", "4aik" ]

6

[ "PUB00053989", "PUB00053990", "PUB00053991" ]

[ "8861216", "11053378", "12057949" ]

[ "Induction of haemolytic activity in Escherichia coli by the slyA gene product.", "Silencing and activation of ClyA cytotoxin expression in Escherichia coli.", "Differential regulation of multiple proteins of Escherichia coli and Salmonella enterica serovar Typhimurium by the transcriptional regulator SlyA." ]

[ 1996, 2000, 2002 ]

3

[ "IPR039422" ]

[]

1

0

1

[ "Glossina", "Pseudomonadota" ]

[ 2, 1074 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Transcriptional regulator, SlyA

Tscrpt_reg_SlyA

9

IPR023072

23,072

Acetyltransferase, YpeA

Acetyltransferase_YpeA

Family

994

false

This entry represents acetyltransferases, YpeA.

[ "GO:0016747" ]

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

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01127" ]

[ "Acetyltransf_YpeA" ]

[ 994 ]

1

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

[ "2.3.1.-", "PWY-3602", "PWY-361", "PWY-4801", "PWY-4922", "PWY-5048", "PWY-5139", "PWY-5268", "PWY-5284", "PWY-5292", "PWY-5307", "PWY-5313", "PWY-5317", "PWY-5318", "PWY-5353", "PWY-5400", "PWY-5473", "PWY-5475", "PWY-5477", "PWY-5660", "PWY-5679", "PWY-5710", "PWY-5794"...

[ "EC:2.3.1.-", "METACYC:PWY-3602", "METACYC:PWY-361", "METACYC:PWY-4801", "METACYC:PWY-4922", "METACYC:PWY-5048", "METACYC:PWY-5139", "METACYC:PWY-5268", "METACYC:PWY-5284", "METACYC:PWY-5292", "METACYC:PWY-5307", "METACYC:PWY-5313", "METACYC:PWY-5317", "METACYC:PWY-5318", "METACYC:PWY-53...

219

[ "2pdo", "4qus", "4qvt" ]

3

[]

0

[]

0

null

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

[ 1, 993 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Acetyltransferase, YpeA

Acetyltransferase_YpeA

3

IPR023073

23,073

DNA polymerase, error-prone

DnaE2

Family

9,916

false

The error-prone DNA polymerase is involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.

[ "GO:0003887" ]

[ "DNA-directed DNA polymerase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_01902" ]

[ "DNApol_error_prone" ]

[ 9916 ]

1

[ "EC" ]

[ "2.7.7.7" ]

[ "EC:2.7.7.7" ]

1

[]

0

[]

0

[ "IPR004805" ]

[]

1

0

1

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

[ 9819, 16, 81 ]

3

[]

0

true

Family

DNA polymerase, error-prone

DnaE2

8

IPR023074

23,074

Hydroxymethylglutaryl-CoA reductase, class I/II, catalytic domain superfamily

HMG_CoA_Rdtase_cat_sf

Homologous_superfamily

15,149

false

There are two distinct classes of hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase enzymes: class I consists of eukaryotic and most archaeal enzymes ( ), while class II consists of prokaryotic enzymes ( ) [ , ]. Class I HMG-CoA reductases catalyse the NADP-dependent synthesis of mevalonate from 3-hydroxy-3-methylgl...

[ "GO:0004420" ]

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

[ "molecular_function" ]

1

[ "CATHGENE3D" ]

[ "G3DSA:3.90.770.10" ]

[ "" ]

[ 15149 ]

1

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

[ "1.1.1.34", "PWY-6174", "PWY-7391", "PWY-7524", "PWY-8125", "PWY-922", "R-BTA-191273", "R-DDI-191273", "R-DME-191273", "R-HSA-191273", "R-HSA-1989781", "R-HSA-2426168", "R-HSA-9619665", "R-MMU-191273", "R-RNO-191273", "R-SCE-191273", "R-SPO-191273" ]

[ "EC:1.1.1.34", "METACYC:PWY-6174", "METACYC:PWY-7391", "METACYC:PWY-7524", "METACYC:PWY-8125", "METACYC:PWY-922", "REACTOME:R-BTA-191273", "REACTOME:R-DDI-191273", "REACTOME:R-DME-191273", "REACTOME:R-HSA-191273", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-2426168", "REACTOME:R-HSA-9619665", ...

17

[ "1dq8", "1dq9", "1dqa", "1hw8", "1hw9", "1hwi", "1hwj", "1hwk", "1hwl", "1qax", "1qay", "1r31", "1r7i", "1t02", "2q1l", "2q6b", "2q6c", "2r4f", "3bgl", "3cct", "3ccw", "3ccz", "3cd0", "3cd5", "3cd7", "3cda", "3cdb", "3qae", "3qau", "4i4b", "4i56", "4i64"...

53

[ "PUB00019711", "PUB00036052", "PUB00036053", "PUB00036054" ]

[ "15535874", "10068515", "10600463", "15028676" ]

[ "The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases.", "Sequence comparisons reveal two classes of 3-hydroxy-3-methylglutaryl coenzyme A reductase.", "Expression and characterization of the HMG-CoA reductase of the thermophilic archaeon Sulfolobus solfataricus.", "Class II 3-hydroxy-3-methylglutar...

[ 2004, 1999, 1999, 2004 ]

4

[]

0

null

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

[ 966, 5931, 8110, 3, 139 ]

5

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

[ 6, 1, 7, 3, 7, 6, 1, 12, 7, 2, 1, 28 ]

12

true

Homologous_superfamily

Hydroxymethylglutaryl-CoA reductase, class I/II, catalytic domain superfamily

HMG_CoA_Rdtase_cat_sf

6

IPR023076

23,076

Hydroxymethylglutaryl-CoA reductase, class I/II, conserved site

HMG_CoA_Rdtase_CS

Conserved_site

12,226

false

There are two distinct classes of hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase enzymes: class I consists of eukaryotic and most archaeal enzymes ( ), while class II consists of prokaryotic enzymes ( ) [ , ]. Class I HMG-CoA reductases catalyse the NADP-dependent synthesis of mevalonate from 3-hydroxy-3-methylgl...

[ "GO:0004420" ]

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

[ "molecular_function" ]

1

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

[ "PS00066", "PS00318", "PS01192" ]

[ "HMG_COA_REDUCTASE_1", "HMG_COA_REDUCTASE_2", "HMG_COA_REDUCTASE_3" ]

[ 9283, 9659, 8213 ]

3

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

[ "1.1.1.34", "PWY-6174", "PWY-7391", "PWY-7524", "PWY-8125", "PWY-922", "R-BTA-191273", "R-DDI-191273", "R-DME-191273", "R-HSA-191273", "R-HSA-1989781", "R-HSA-2426168", "R-HSA-9619665", "R-MMU-191273", "R-RNO-191273", "R-SCE-191273", "R-SPO-191273" ]

[ "EC:1.1.1.34", "METACYC:PWY-6174", "METACYC:PWY-7391", "METACYC:PWY-7524", "METACYC:PWY-8125", "METACYC:PWY-922", "REACTOME:R-BTA-191273", "REACTOME:R-DDI-191273", "REACTOME:R-DME-191273", "REACTOME:R-HSA-191273", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-2426168", "REACTOME:R-HSA-9619665", ...

17

[ "1dq8", "1dq9", "1dqa", "1hw8", "1hw9", "1hwi", "1hwj", "1hwk", "1hwl", "1qax", "1qay", "1r31", "1r7i", "1t02", "2q1l", "2q6b", "2q6c", "2r4f", "3bgl", "3cct", "3ccw", "3ccz", "3cd0", "3cd5", "3cd7", "3cda", "3cdb", "3qae", "3qau", "4i4b", "4i56", "4i64"...

54

[ "PUB00002079", "PUB00019711", "PUB00036052", "PUB00036053", "PUB00036054" ]

[ "2656635", "15535874", "10068515", "10600463", "15028676" ]

[ "Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase.", "The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases.", "Sequence comparisons reveal two classes of 3-hydroxy-3-methylglutaryl coenzyme A reductase.", "Expression...

[ 1989, 2004, 1999, 1999, 2004 ]

5

[]

0

null

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

[ 929, 3545, 7654, 4, 94 ]

5

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

[ 6, 1, 7, 3, 7, 6, 1, 11, 7, 2, 1, 29 ]

12

true

Conserved_site

Hydroxymethylglutaryl-CoA reductase, class I/II, conserved site

HMG_CoA_Rdtase_CS

9

IPR023079

23,079

Sedoheptulose-1,7-bisphosphatase

SBPase

Family

2,251

false

This entry represents sedoheptulose-1,7-bisphosphatase. Sedoheptulose- 1,7-bisphosphate is involved in carbohydrate biosynthesis, catalysing the production of sedoheptulose 7-phosphate and phosphate from sedoheptulose- 1,7-bisphosphate and water. The enzyme shares a high degree of similarity with fructose-1,6-bisphosph...

[ "GO:0016791", "GO:0005975" ]

[ "phosphatase activity", "carbohydrate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PRINTS" ]

[ "PR01958" ]

[ "S17BPHPHTASE" ]

[ 2251 ]

1

[ "EC", "METACYC" ]

[ "3.1.3.11", "PWY-5484" ]

[ "EC:3.1.3.11", "METACYC:PWY-5484" ]

2

[ "4ir8", "5iz3", "7b2o", "7zuv" ]

4

[ "PUB00001414", "PUB00053714" ]

[ "1374332", "8392396" ]

[ "cDNA and gene sequences of wheat chloroplast sedoheptulose-1,7-bisphosphatase reveal homology with fructose-1,6-bisphosphatases.", "A light- and developmentally-regulated DNA-binding interaction is common to the upstream sequences of the wheat Calvin cycle bisphosphatase genes." ]

[ 1992, 1993 ]

2

[ "IPR000146" ]

[]

1

0

1

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

[ 147, 494, 1591, 19 ]

4

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

[ 2, 1, 3, 3 ]

4

true

Family

Sedoheptulose-1,7-bisphosphatase

SBPase

3

IPR023080

23,080

D-amino acid dehydrogenase DadA

DadA

Family

5,878

false

DadA is a dehydrogenase catalysing the deamination of D-amino acids yielding corresponding 2-oxo acids and hydrogen [ ]. D-Amino acids control growth phase-dependent cell wall remodelling and rigger biofilm disassembly [ ].

[ "GO:0008718", "GO:0019478" ]

[ "D-amino-acid dehydrogenase activity", "D-amino acid catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP" ]

[ "MF_01202" ]

[ "DadA" ]

[ 5878 ]

1

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

[ "1.4.99.-", "PWY-7431", "PWY-7690" ]

[ "EC:1.4.99.-", "METACYC:PWY-7431", "METACYC:PWY-7690" ]

3

[]

0

[ "PUB00074091", "PUB00074092" ]

[ "15358424", "21378189" ]

[ "Oxidation of 3,4-dehydro-D-proline and other D-amino acid analogues by D-alanine dehydrogenase from Escherichia coli.", "Regulation and characterization of the dadRAX locus for D-amino acid catabolism in Pseudomonas aeruginosa PAO1." ]

[ 2004, 2011 ]

2

[]

0

null

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

[ 5852, 4, 22 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-amino acid dehydrogenase DadA

DadA

9

IPR023081

23,081

Cell division protein FtsB

Cell_div_FtsB

Family

6,589

false

The proteins in this entry are represented by the Escherichia coli (strain K12) protein FtsB. FtsB is one of the three membrane proteins required for cell division in E. coli: FtsQ, FtsL and FtsB, all of these localize to the cell septum. FtsL and FtsB contain a leucine zipper-like sequence and are dependent on each ot...

[]

0

[ "HAMAP", "PANTHER" ]

[ "MF_00599", "PTHR37485" ]

[ "FtsB", "" ]

[ 5852, 6586 ]

2

[ "GP", "GP" ]

[ "GenProp1142", "GenProp1154" ]

[ "GP:GenProp1142", "GP:GenProp1154" ]

2

[ "6h9n", "8bh1", "8hhf", "8hhg", "8hhh", "8p1u" ]

6

[ "PUB00053999" ]

[ "15165235" ]

[ "A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region." ]

[ 2004 ]

1

[ "IPR007060" ]

[]

1

0

1

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

[ 6445, 5, 139 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Cell division protein FtsB

Cell_div_FtsB

7

IPR023082

23,082

Homeo-prospero domain

Homeo_prospero_dom

Domain

3,409

false

This entry represents the homeo-prospero domain. This domain consists of a homeodomain-homology N-terminal region and the prospero-specific C-terminal region. The structure of these two regions consists of a single structural unit (a homeo-prospero domain), in which the prospero domain region is in position to contribu...

[ "GO:0003677" ]

[ "DNA binding" ]

[ "molecular_function" ]

1

[ "PFAM", "PROFILE" ]

[ "PF05044", "PS51818" ]

[ "HPD", "HOMEO_PROSPERO" ]

[ 3409, 3393 ]

2

[]

0

[ "1mij", "1xpx", "2lmd" ]

3

[ "PUB00027356", "PUB00038342" ]

[ "12429095", "15837198" ]

[ "Structure of the DNA binding region of prospero reveals a novel homeo-prospero domain.", "Structural basis of Prospero-DNA interaction: implications for transcription regulation in developing cells." ]

[ 2002, 2005 ]

2

[]

0

null

[ "Bilateria" ]

[ 3409 ]

1

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

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

6

true

Domain

Homeo-prospero domain

Homeo_prospero_dom

3

IPR023083

23,083

Glycerol-3-phosphate O-acyltransferase, alpha-helical bundle, N-terminal

G3P_O-acylTrfase_N

Domain

883

false

Stromal glycerol-3-phosphate acyltransferases (GPAT) are responsible for the selective incorporation of saturated and unsaturated fatty-acyl chains into chloroplast membranes, which is an important determinant of a plant's ability to tolerate chilling temperatures [ ]. This entry represents the N-terminal four α helica...

[ "GO:0004366" ]

[ "glycerol-3-phosphate O-acyltransferase activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF14829" ]

[ "GPAT_N" ]

[ 883 ]

1

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

[ "2.3.1.15", "PWY-5667", "PWY-6453", "PWY-7411", "PWY-7587", "PWY-8051", "PWY-8053", "PWY-8055" ]

[ "EC:2.3.1.15", "METACYC:PWY-5667", "METACYC:PWY-6453", "METACYC:PWY-7411", "METACYC:PWY-7587", "METACYC:PWY-8051", "METACYC:PWY-8053", "METACYC:PWY-8055" ]

8

[ "1iuq", "1k30", "8ia1" ]

3

[ "PUB00021867" ]

[ "14684887" ]

[ "Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea." ]

[ 2004 ]

1

[]

0

null

[ "Viridiplantae" ]

[ 883 ]

1

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

[ 3, 3, 21 ]

3

true

Domain

Glycerol-3-phosphate O-acyltransferase, alpha-helical bundle, N-terminal

G3P_O-acylTrfase_N

2

IPR023084

23,084

Proteinase inhibitor I11, ecotin, gammaproteobacteria

Prot_inh_ecotin_gammaproteobac

Family

1,273

false

This entry represents bacterial proteinase inhibitors that belong to MEROPS inhibitor family I11, clan IN. Ecotins are dimeric periplasmic proteins from Escherichia coli and related Gram-negative bacteria that have been shown to be potent inhibitors of many trypsin-fold serine proteases of widely varying substrate spec...

[ "GO:0004867" ]

[ "serine-type endopeptidase inhibitor activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "CDD" ]

[ "MF_00706", "cd00242" ]

[ "Ecotin", "Ecotin" ]

[ 1268, 1092 ]

2

[]

0

[ "1azz", "1ecy", "1ecz", "1ezs", "1ezu", "1id5", "1ifg", "1n8o", "1p0s", "1slu", "1slv", "1slw", "1slx", "1xx9", "1xxd", "1xxf", "2y6t", "4iw4", "4niy", "7cbk", "7pqn", "7pqo" ]

22

[ "PUB00014133", "PUB00014201", "PUB00019495" ]

[ "14705960", "14705961", "11513582" ]

[ "Evolutionary families of peptidase inhibitors.", "The periplasmic serine protease inhibitor ecotin protects bacteria against neutrophil elastase.", "Crystal structure of thrombin-ecotin reveals conformational changes and extended interactions." ]

[ 2004, 2004, 2001 ]

3

[ "IPR005658" ]

[]

1

0

1

[ "Bacteria", "Leishmania major" ]

[ 1272, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Proteinase inhibitor I11, ecotin, gammaproteobacteria

Prot_inh_ecotin_gammaproteobac

8

IPR023085

23,085

UDP-N-acetyl-D-mannosaminuronic acid transferase

UDP-ManNAcA_Trfase_WecG

Family

1,395

false

This entry represents UDP-N-acetyl-D-mannosaminuronic acid transferases that belong to the glycosyltransferase 26 family. It has been proposed that these proteins catalyze the synthesis of Und-PP-GlcNAc-ManNAcA (Lipid II), the second lipid-linked intermediate involved in enterobacterial common antigen synthesis.

[ "GO:0016758", "GO:0009246" ]

[ "hexosyltransferase activity", "enterobacterial common antigen biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01001", "NF002980" ]

[ "WecG_RffM", "PRK03692.1" ]

[ 1307, 1395 ]

2

[ "EC" ]

[ "2.4.1.180" ]

[ "EC:2.4.1.180" ]

1

[]

0

[ "PUB00079560", "PUB00104139" ]

[ "3275612", "36006410" ]

[ "Characterization of an Escherichia coli rff mutant defective in transfer of N-acetylmannosaminuronic acid (ManNAcA) from UDP-ManNAcA to a lipid-linked intermediate involved in enterobacterial common antigen synthesis.", "Subcellular localization of the enterobacterial common antigen GT-E-like glycosyltransferase...

[ 1988, 2022 ]

2

[ "IPR004629" ]

[]

1

0

1

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

[ 1392, 2, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

UDP-N-acetyl-D-mannosaminuronic acid transferase

UDP-ManNAcA_Trfase_WecG

4

IPR023086

23,086

Phosphoglycerate mutase, GpmB, probable

Phosphoglycerate_mutase_GpmB

Family

1,197

false

This entry represents probable phosphoglycerate mutases (PGAM) that belong to the GpmB subfamily.

[ "GO:0004619", "GO:0006096" ]

[ "phosphoglycerate mutase activity", "glycolytic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01040", "NF002901" ]

[ "PGAM_GpmB", "PRK03482.1" ]

[ 1099, 1197 ]

2

[ "EC" ]

[ "5.4.2.-" ]

[ "EC:5.4.2.-" ]

1

[]

0

[]

0

[ "IPR013078" ]

[]

1

0

1

[ "Bacteria", "Ecdysozoa" ]

[ 1194, 3 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Phosphoglycerate mutase, GpmB, probable

Phosphoglycerate_mutase_GpmB

9

IPR023087

23,087

Flagellar motor switch protein FliG, C-terminal

Flg_Motor_Flig_C

Domain

13,454

false

The flagellar motor switch in Escherichia coli and Salmonella typhimurium regulates the direction of flagellar rotation and hence controls swimming behaviour [ ]. The switch is a complex apparatus that responds to signals transduced by the chemotaxis sensory signalling system during chemotactic behaviour [ ]. CheY, the...

[]

0

[ "PFAM" ]

[ "PF01706" ]

[ "FliG_C" ]

[ 13454 ]

1

[]

0

[ "1lkv", "1qc7", "3ajc", "3hjl", "3usw", "3usy", "4fhr", "8ucs", "8umd", "8umx", "8uox", "8upl", "8vib", "8vid", "8vkq", "8vkr", "8wiw", "8wo5", "8woe", "8xp0", "8xp1", "8yjt", "8z4d", "8z4g", "9n49", "9n4z" ]

26

[ "PUB00001834", "PUB00002083", "PUB00002290", "PUB00004294", "PUB00004790" ]

[ "8224881", "2656645", "8631704", "10440379", "1631122" ]

[ "Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG.", "Flagellar switch of Salmonella typhimurium: gene sequences and deduced protein sequences.", "A mutational analysis of the interaction between FliG and FliM, two compone...

[ 1993, 1989, 1996, 1999, 1992 ]

5

[]

0

null

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

[ 13215, 31, 208 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Flagellar motor switch protein FliG, C-terminal

Flg_Motor_Flig_C

6

IPR023088

23,088

3'5'-cyclic nucleotide phosphodiesterase

PDEase

Family

46,533

false

The cyclic nucleotide phosphodiesterases (PDE) comprise a group of enzymes that degrade the phosphodiester bond in the second messenger molecules cAMP and cGMP. They are divided into 11 families. They regulate the localisation, duration and amplitude of cyclic nucleotide signalling within subcellular domains. PDEs are ...

[ "GO:0008081" ]

[ "phosphoric diester hydrolase activity" ]

[ "molecular_function" ]

1

[ "PRINTS" ]

[ "PR00387" ]

[ "PDIESTERASE1" ]

[ 46533 ]

1

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

[ "3.1.4", "R-BTA-111957", "R-BTA-418457", "R-BTA-418555", "R-BTA-445355", "R-BTA-9013422", "R-CEL-111957", "R-CEL-165160", "R-CEL-180024", "R-CEL-418457", "R-CEL-418555", "R-CEL-9860927", "R-CFA-2485179", "R-CFA-2514859", "R-CFA-4086398", "R-CFA-418457", "R-CFA-445355", "R-CFA-90134...

[ "EC:3.1.4", "REACTOME:R-BTA-111957", "REACTOME:R-BTA-418457", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-445355", "REACTOME:R-BTA-9013422", "REACTOME:R-CEL-111957", "REACTOME:R-CEL-165160", "REACTOME:R-CEL-180024", "REACTOME:R-CEL-418457", "REACTOME:R-CEL-418555", "REACTOME:R-CEL-9860927", "RE...

62

[ "1f0j", "1mkd", "1oyn", "1ptw", "1q9m", "1rkp", "1ro6", "1ro9", "1ror", "1t9r", "1t9s", "1taz", "1tb5", "1tb7", "1tbb", "1tbf", "1udt", "1udu", "1uho", "1xlx", "1xlz", "1xm4", "1xm6", "1xmu", "1xmy", "1xn0", "1xom", "1xon", "1xoq", "1xor", "1xos", "1xot"...

709

[ "PUB00043423", "PUB00043424", "PUB00043425", "PUB00154469" ]

[ "18447606", "18367027", "18436153", "34170501" ]

[ "Roflumilast: an oral, once-daily selective PDE-4 inhibitor for the management of COPD and asthma.", "Phosphodiesterase 5 inhibition in essential hypertension.", "Type 3 phosphodiesterase inhibitors may be protective against cerebrovascular events in patients with claudication.", "Photoreceptor Phosphodiester...

[ 2008, 2008, 2008, 2022 ]

4

[]

0

null

[ "Eukaryota", "viral metagenome" ]

[ 46532, 1 ]

2

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 16, 229, 32, 100, 105, 158, 1 ]

7

true

Family

3'5'-cyclic nucleotide phosphodiesterase

PDEase

7

IPR023089

23,089

YozE SAM-like domain

YozE_SAM-like

Domain

2,756

false

YozE-like is a family of Firmicute proteins that carries a four-helix motif similar to sterile alpha motif (SAM) domains. The family is suggested to fall into two subfamilies, possibly with differing functions based on the different surface charges on the three structural representatives, YozE, MW0776 and MW1311. This ...

[]

0

[ "PFAM" ]

[ "PF06855" ]

[ "YozE_SAM_like" ]

[ 2756 ]

1

[]

0

[ "2fj6", "2kvs", "2o6k" ]

3

[ "PUB00075372" ]

[ "22843344" ]

[ "Three structural representatives of the PF06855 protein domain family from Staphyloccocus aureus and Bacillus subtilis have SAM domain-like folds and different functions." ]

[ 2012 ]

1

[]

0

null

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

[ 2, 2745, 4, 2, 3 ]

5

[]

0

true

Domain

YozE SAM-like domain

YozE_SAM-like

4

IPR023090

23,090

UPF0702, alpha/beta domain superfamily

UPF0702_alpha/beta_dom_sf

Homologous_superfamily

19,121

false

This superfamily represents a 2 layer α/β sandwich domain that is found in an uncharacterised protein family. This domain is often tandemly repeated.

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:3.30.240.20" ]

[ "" ]

[ 19121 ]

1

[]

0

[ "3c6f" ]

1

[]

0

[]

0

null

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

[ 47, 18911, 68, 95 ]

4

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

[ 1, 1 ]

2

true

Homologous_superfamily

UPF0702, alpha/beta domain superfamily

UPF0702_alpha/beta_dom_sf

5

IPR023091

23,091

Metalloprotease catalytic domain superfamily, predicted

MetalPrtase_cat_dom_sf_prd

Homologous_superfamily

28,140

false

This superfamily represents a domain found in a number of predicted metalloproteases. The crystal structure of the protein from the hyperthermophilic bacteria Aquifex aeolicus has been determined. The overall fold consists of one central α-helix surrounded by a four-stranded β-sheet and four other α-helices. Structure-...

[ "GO:0004222" ]

[ "metalloendopeptidase activity" ]

[ "molecular_function" ]

1

[ "CATHGENE3D" ]

[ "G3DSA:3.40.390.30" ]

[ "" ]

[ 28140 ]

1

[]

0

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

5

[ "PUB00027806" ]

[ "12832766" ]

[ "Structure of the hypothetical protein AQ_1354 from Aquifex aeolicus." ]

[ 2003 ]

1

[]

0

null

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

[ 25217, 2304, 4, 615 ]

4

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

[ 5, 3, 1, 2, 1, 8, 2, 17 ]

8

true

Homologous_superfamily

Metalloprotease catalytic domain superfamily, predicted

MetalPrtase_cat_dom_sf_prd

4

IPR023093

23,093

ScpA-like, C-terminal

ScpA-like_C

Homologous_superfamily

16,919

false

This superfamily represents a conserved C-terminal region found in bacterial segregation and condensation protein A (ScpA) as well as in eukaryotic cohesins of the Rad21 and Scc1 families. ScpA participates in chromosomal partition during cell division. It may act via the formation of a condensin-like complex containin...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.10.580" ]

[ "" ]

[ 16919 ]

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-2467813", "R-BTA-2468052", "R-BTA-2470946", "R-BTA-2500257", "R-BTA-3108214", "R-CEL-2468052", "R-CEL-2470946", "R-CEL-2500257", "R-CEL-3108214", "R-HSA-1221632", "R-HSA-2467813", "R-HSA-2468052", "R-HSA-2470946", "R-HSA-2500257", "R-HSA-3108214", "R-HSA-9018519", "R-MMU-24678...

[ "REACTOME:R-BTA-2467813", "REACTOME:R-BTA-2468052", "REACTOME:R-BTA-2470946", "REACTOME:R-BTA-2500257", "REACTOME:R-BTA-3108214", "REACTOME:R-CEL-2468052", "REACTOME:R-CEL-2470946", "REACTOME:R-CEL-2500257", "REACTOME:R-CEL-3108214", "REACTOME:R-HSA-1221632", "REACTOME:R-HSA-2467813", "REACTOM...

27

[ "1w1w", "4i99", "5h66", "5h67", "5xg3", "5xns", "6qpq", "6qpw", "6wg3", "6wge", "6yuf", "6zz6", "7w1m", "7zjs", "8p0a", "8pq5", "8ro6", "8ro7", "8ro8", "8ro9", "8roa", "8rob", "8roc", "8rod", "8roe", "8rof", "8rog" ]

27

[]

0

[]

0

null

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

[ 692, 7611, 8418, 198 ]

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...

[ 25, 6, 2, 3, 7, 9, 2, 13, 4, 1, 2, 46 ]

12

true

Homologous_superfamily

ScpA-like, C-terminal

ScpA-like_C

5

IPR023095

23,095

Adenine-specific methyltransferase, domain 2

Ade_MeTrfase_dom_2

Homologous_superfamily

13,363

false

This superfamily represents the α-helical domain (also refered as domain 2) found in the adenine-specific N(4)/N(6)-methyltransferase family. It is around 100 amino acids in length.

[ "GO:0009007" ]

[ "site-specific DNA-methyltransferase (adenine-specific) activity" ]

[ "molecular_function" ]

1

[ "CATHGENE3D" ]

[ "G3DSA:1.10.1020.10" ]

[ "" ]

[ 13363 ]

1

[ "EC" ]

[ "2.1.1.72" ]

[ "EC:2.1.1.72" ]

1

[ "1q0s", "1q0t", "1yf3", "1yfj", "1yfl", "2dpm", "2g1p", "2ore", "4gbe", "4gol", "4gom", "4gon", "4goo", "4rtj", "4rtk", "4rtl", "4rtm", "4rtn", "4rto", "4rtp", "4rtq", "4rtr", "4rts", "7m6b" ]

24

[]

0

[]

0

null

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

[ 387, 11980, 72, 659, 265 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Homologous_superfamily

Adenine-specific methyltransferase, domain 2

Ade_MeTrfase_dom_2

1

IPR023096

23,096

Phosphoglucose isomerase, C-terminal

G6P_Isomerase_C

Homologous_superfamily

22,593

false

Phosphoglucose isomerase ( ) (PGI) [ , ] is a dimeric enzyme that catalyses the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. PGI is involved in different pathways: in most higher organisms it is involved in glycolysis; in mammals it is involved in gluconeogenesis; in plants in carbohydrate ...

[ "GO:0004347", "GO:0006096" ]

[ "glucose-6-phosphate isomerase activity", "glycolytic process" ]

[ "molecular_function", "biological_process" ]

2

[ "CATHGENE3D" ]

[ "G3DSA:1.10.1390.10" ]

[ "" ]

[ 22593 ]

1

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

[ "5.3.1.9", "PWY-3801", "PWY-5054", "PWY-5384", "PWY-5514", "PWY-5659", "PWY-6142", "PWY-621", "PWY-622", "PWY-6981", "PWY-6992", "PWY-7238", "PWY-7347", "PWY-7385", "PWY-8013", "R-BTA-5628897", "R-BTA-6798695", "R-BTA-70171", "R-BTA-70263", "R-DDI-5628897", "R-DDI-6798695", ...

[ "EC:5.3.1.9", "METACYC:PWY-3801", "METACYC:PWY-5054", "METACYC:PWY-5384", "METACYC:PWY-5514", "METACYC:PWY-5659", "METACYC:PWY-6142", "METACYC:PWY-621", "METACYC:PWY-622", "METACYC:PWY-6981", "METACYC:PWY-6992", "METACYC:PWY-7238", "METACYC:PWY-7347", "METACYC:PWY-7385", "METACYC:PWY-801...

51

[ "1dqr", "1g98", "1gzd", "1gzv", "1hm5", "1hox", "1iat", "1iri", "1jiq", "1jlh", "1koj", "1n8t", "1nuh", "1q50", "1t10", "1u0e", "1u0f", "1u0g", "1xtb", "2cvp", "2cxn", "2cxo", "2cxp", "2cxq", "2cxr", "2cxs", "2cxt", "2cxu", "2o2c", "2o2d", "2wu8", "3hjb"...

64

[ "PUB00003422", "PUB00004511", "PUB00006445", "PUB00006471", "PUB00011130" ]

[ "1593646", "6115414", "10318897", "10653639", "10770936" ]

[ "Anomalous phylogeny involving the enzyme glucose-6-phosphate isomerase.", "Glucose-6-phosphate isomerase.", "The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin.", "Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that mo...

[ 1992, 1981, 1999, 2000, 2000 ]

5

[]

0

null

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

[ 2, 16341, 6040, 210 ]

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",...

[ 3, 2, 5, 1, 1, 6, 2, 1, 7, 4, 1, 1, 7 ]

13

true

Homologous_superfamily

Phosphoglucose isomerase, C-terminal

G6P_Isomerase_C

9

IPR023098

23,098

L-serine kinase SerK/SbnI, C-terminal

SerK/SbnI_C

Homologous_superfamily

399

false

This superfamily represents a structural α-β domain [ ] found in the C-terminal region of free serine kinase (SerK) from Thermococcus kodakarensis and SbnI from Staphylococcus aureus [ ]. SerK converts ADP and l-serine (Ser) into AMP and O-phospho-l-serine (Sep), which is a precursor of l-cysteine [ ].

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:3.30.1760.10" ]

[ "" ]

[ 399 ]

1

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

[ "2.7.1.225", "PWY-7694", "PWY-7706", "PWY-8008", "PWY-8381" ]

[ "EC:2.7.1.225", "METACYC:PWY-7694", "METACYC:PWY-7706", "METACYC:PWY-8008", "METACYC:PWY-8381" ]

5

[ "1vk1", "5ujd", "5uje", "5x0b", "5x0e", "5x0f", "5x0g", "5x0j", "5x0k", "6nr6" ]

10

[ "PUB00046765", "PUB00091306", "PUB00092872" ]

[ "17729285", "28358477", "29483190" ]

[ "Crystal structure solution of a ParB-like nuclease at atomic resolution.", "Structural Study on the Reaction Mechanism of a Free Serine Kinase Involved in Cysteine Biosynthesis.", "SbnI is a free serine kinase that generates O -phospho-l-serine for staphyloferrin B biosynthesis in Staphylococcus aureus." ]

[ 2008, 2017, 2018 ]

3

[]

0

null

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

[ 159, 219, 14, 7 ]

4

[]

0

true

Homologous_superfamily

L-serine kinase SerK/SbnI, C-terminal

SerK/SbnI_C

9

IPR023099

23,099

Glycoside hydrolase, family 46, N-terminal

Glyco_hydro_46_N

Homologous_superfamily

2,047

false

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

[ "GO:0016977", "GO:0005975" ]

[ "chitosanase activity", "carbohydrate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "CATHGENE3D" ]

[ "G3DSA:3.30.386.10" ]

[ "" ]

[ 2047 ]

1

[ "EC" ]

[ "3.2.1.132" ]

[ "EC:3.2.1.132" ]

1

[ "1chk", "1qgi", "2d05", "4ily", "4olt", "4qwp", "5hwa", "6lwu", "6x2q", "7c6c", "7c6d", "7xh0" ]

12

[ "PUB00004870", "PUB00005266", "PUB00030255", "PUB00036505", "PUB00079509", "PUB00079510", "PUB00079511" ]

[ "7624375", "8535779", "10521473", "8564542", "9723170", "8564539", "12369923" ]

[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism.", "X-ray structure...

[ 1995, 1995, 1999, 1996, 1998, 1996, 2000 ]

7

[]

0

null

[ "Bacteria", "Eukaryota", "Methanosarcina", "Viruses", "uncultured organism" ]

[ 1668, 341, 7, 29, 2 ]

5

[]

0

true

Homologous_superfamily

Glycoside hydrolase, family 46, N-terminal

Glyco_hydro_46_N

2

IPR023100

23,100

D-aminoacylase, insert domain superfamily

D-aminoacylase_insert_dom_sf

Homologous_superfamily

6,572

false

This superfamily represents the insert found in the catalytic domain. This insert, composed of two α-helices and four β-strands, goes across the active site and is involved in substrate-mediated conformational change. D-aminoacylase hydrolyses a wide variety of N-acyl derivatives of neutral D-amino acids, in a zinc-dep...

[ "GO:0016811" ]

[ "hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides" ]

[ "molecular_function" ]

1

[ "CATHGENE3D" ]

[ "G3DSA:3.30.1490.130" ]

[ "" ]

[ 6572 ]

1

[]

0

[ "1m7j", "1rjp", "1rjq", "1rjr", "1rk5", "1rk6", "1v4y", "1v51", "3gip", "3giq", "9g5m", "9gv8", "9kb1", "9kb3", "9kb4" ]

15

[ "PUB00014261" ]

[ "12454005" ]

[ "Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanism." ]

[ 2003 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Caudovirales sp. ctTVN2", "Eukaryota", "metagenomes" ]

[ 73, 6202, 1, 98, 198 ]

5

[]

0

true

Homologous_superfamily

D-aminoacylase, insert domain superfamily

D-aminoacylase_insert_dom_sf

1

IPR023101

23,101

AF1862-like domain superfamily

AF1862-like_dom_sf

Homologous_superfamily

848

false

The CRISPR-Cas system is a prokaryotic defence mechanism against foreign genetic elements. The key elements of this defence system are the Cas proteins and the CRISPR RNA. This superfamily represents the structural domain found in a family of Cas proteins as represented by TM1791.1 from Thermotoga maritima and AF1862 f...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.10.520.30", "SSF158568" ]

[ "", "" ]

[ 783, 837 ]

2

[]

0

[ "2oeb", "2zop", "3x1l", "4gkf", "6s6b", "6s8b", "6s8e", "6s91", "6sh8", "6shb", "6sic", "9arw" ]

12

[ "PUB00043286", "PUB00043287", "PUB00043288", "PUB00060621", "PUB00071890" ]

[ "17442114", "17379808", "16545108", "21699496", "24459147" ]

[ "Evolutionary conservation of sequence and secondary structures in CRISPR repeats.", "CRISPR provides acquired resistance against viruses in prokaryotes.", "A putative RNA-interference-based immune system in prokaryotes: computational analysis of the predicted enzymatic machinery, functional analogies with euka...

[ 2007, 2007, 2006, 2011, 2014 ]

5

[]

0

null

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

[ 123, 712, 13 ]

3

[]

0

true

Homologous_superfamily

AF1862-like domain superfamily

AF1862-like_dom_sf

7

IPR023104

23,104

ITPase-like domain superfamily

ITPase-like_dom_sf

Homologous_superfamily

24

false

This superfamily represents a structural domain found in a family of proteins with unknown function.

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.287.780" ]

[ "" ]

[ 24 ]

1

[]

0

[ "2js3" ]

1

[]

0

[]

0

null

[ "Pseudomonadota" ]

[ 24 ]

1

[]

0

true

Homologous_superfamily

ITPase-like domain superfamily

ITPase-like_dom_sf

2

IPR023105

23,105

YkvR-like superfamily

YkvR-like_sf

Homologous_superfamily

407

false

This domain superfamily is found in proteins with unknown function that appears to be restricted to Bacillaceae. Some members in this family of proteins are annotated as YkvR however this cannot be confirmed.

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:2.40.30.80", "SSF159173" ]

[ "", "" ]

[ 406, 392 ]

2

[]

0

[ "2jn9" ]

1

[]

0

[]

0

null

[ "Bacillota" ]

[ 407 ]

1

[]

0

true

Homologous_superfamily

YkvR-like superfamily

YkvR-like_sf

7

IPR023107

23,107

Atu2299-like domain superfamily

Atu2299-like_dom_sf

Homologous_superfamily

220

false

This superfamily represents a domain found in a family of protein of approx. 100 residues. The proteins contain up to five α helices and up to seven β strands and are probably monomeric. Their function is unknown.

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:3.10.550.10" ]

[ "" ]

[ 220 ]

1

[]

0

[ "2hly" ]

1

[]

0

[]

0

null

[ "Bacteria", "unclassified sequences" ]

[ 217, 3 ]

2

[]

0

true

Homologous_superfamily

Atu2299-like domain superfamily

Atu2299-like_dom_sf

4

IPR023108

23,108

Domain of unknown function, DUF3216

DUF3216

Domain

43

false

This domain is found in a family of proteins with unknown function and appears to be restricted to the Thermococcaceae.

[]

0

[ "PFAM" ]

[ "PF11505" ]

[ "DUF3216" ]

[ 43 ]

1

[]

0

[ "2hjm" ]

1

[]

0

[]

0

null

[ "Thermococcaceae" ]

[ 43 ]

1

[]

0

true

Domain

Domain of unknown function, DUF3216

DUF3216

2

IPR023110

23,110

PH1570-like domain

PH1570-like_domain

Domain

45

false

This domain is found in a family of proteins that include a hypothetical protein from Pyrococcus horikoshii, which has no known function. It contains six α helices and eight β strands and is thought to be monomeric.

[]

0

[ "PFAM" ]

[ "PF09638" ]

[ "Ph1570" ]

[ 45 ]

1

[]

0

[ "2hq4" ]

1

[]

0

[]

0

null

[ "Thermococcaceae" ]

[ 45 ]

1

[]

0

true

Domain

PH1570-like domain

PH1570-like_domain

2

IPR023111

23,111

Titin-like domain superfamily

Titin-like_dom_sf

Homologous_superfamily

862

false

The domain found in this superfamily is associated with telethonin, which is found at the Z-disc of sarcomeres. It is the phosphorylation target of the kinase domain of titin, and is thought to play a role in muscle development [ , ]. Deletion of the C terminus of titin, including the kinase domain, has been found to i...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:2.20.160.10" ]

[ "" ]

[ 862 ]

1

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

[ "R-BTA-390522", "R-HSA-390522", "R-MMU-390522" ]

[ "REACTOME:R-BTA-390522", "REACTOME:R-HSA-390522", "REACTOME:R-MMU-390522" ]

3

[ "1ya5", "2f8v" ]

2

[ "PUB00034631", "PUB00035182", "PUB00035183", "PUB00035184", "PUB00040581" ]

[ "9804419", "10481174", "14600266", "12379311", "16713295" ]

[ "Structural basis for activation of the titin kinase domain during myofibrillogenesis.", "Titin: a molecular control freak.", "A targeted deletion of the C-terminal end of titin, including the titin kinase domain, impairs myofibrillogenesis.", "Telethonin protein expression in neuromuscular disorders.", "Ev...

[ 1998, 1999, 2003, 2002, 2006 ]

5

[]

0

null

[ "Vertebrata" ]

[ 862 ]

1

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

[ 25, 5, 3, 3 ]

4

true

Homologous_superfamily

Titin-like domain superfamily

Titin-like_dom_sf

2

IPR023113

23,113

Telomere-binding protein, beta subunit domain superfamily

TEBP_beta_dom_sf

Homologous_superfamily

30

false

Telomeres are specialised protein-DNA complexes that compose the ends of eukaryotic chromosomes. Telomeres protect chromosome termini from degradation and recombination and act together with telomerase to ensure complete genome replication. TEBP beta forms a complex with TEBP alpha and this complex is able to recognise...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:2.40.200.10" ]

[ "" ]

[ 30 ]

1

[]

0

[ "1jb7", "1otc", "1pa6", "1ph1", "1ph2", "1ph3", "1ph4", "1ph5", "1ph6", "1ph7", "1ph8", "1ph9", "1phj", "2i0q" ]

14

[ "PUB00013133" ]

[ "9875850" ]

[ "Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA." ]

[ 1998 ]

1

[]

0

null

[ "Spirotrichea" ]

[ 30 ]

1

[]

0

true

Homologous_superfamily

Telomere-binding protein, beta subunit domain superfamily

TEBP_beta_dom_sf

5

IPR023115

23,115

Translation initiation factor IF- 2, domain 3

TIF_IF2_dom3

Domain

39,107

false

Initiation factor 2 (IF-2) is one of the three factors required for the initiation of protein biosynthesis in bacteria [ ]. IF-2 promotes the GTP-dependent binding of the initiator tRNA to the small subunit of the ribosome. IF-2 is a protein of about 70 to 95kDa that contains a central GTP-binding domain flanked by a h...

[]

0

[ "PFAM" ]

[ "PF11987" ]

[ "IF-2" ]

[ 39107 ]

1

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

[ "R-DDI-72706", "R-HSA-5368286", "R-HSA-72706", "R-MMU-72706", "R-RNO-72706", "R-SCE-72706", "R-SPO-72706" ]

[ "REACTOME:R-DDI-72706", "REACTOME:R-HSA-5368286", "REACTOME:R-HSA-72706", "REACTOME:R-MMU-72706", "REACTOME:R-RNO-72706", "REACTOME:R-SCE-72706", "REACTOME:R-SPO-72706" ]

7

[ "1g7r", "1g7s", "1g7t", "1z9b", "1zo1", "3izy", "3j4j", "3jcj", "3jcn", "3wbi", "3wbj", "3wbk", "4kjz", "4n3g", "4n3n", "4n3s", "4ncf", "4ncl", "4ncn", "4ujc", "4ujd", "4v8z", "5fg3", "5lmv", "5me0", "5me1", "6gaw", "6gaz", "6gb2", "6o7k", "6o9k", "6rw5"...

60

[ "PUB00011836", "PUB00035262", "PUB00085958" ]

[ "11114334", "10200264", "15755955" ]

[ "X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding.", "Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2.", "Initiation of protein synthesis in bacteria." ...

[ 2000, 1999, 2005 ]

3

[]

0

null

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

[ 935, 26327, 11191, 3, 651 ]

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",...

[ 44, 2, 3, 10, 1, 5, 6, 2, 14, 9, 2, 2, 34 ]

13

true

Domain

Translation initiation factor IF- 2, domain 3

TIF_IF2_dom3

8

IPR023116

23,116

Phosphonoacetate hydrolase, insert domain superfamily

Phosphonoacetate_hydro_insert

Homologous_superfamily

2,163

false

Phosphonates are organic compounds with a direct C-P bond that is far less labile than the C-O-P bonds of phosphate attachment sites. Phosphonoacetate hydrolase specifically cleaves the C-P bond in phosphonoacetate [ ]. This superfamily represents a short α/β 2 layer sandwich domain inserted towards the C terminus of t...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:3.30.1360.110" ]

[ "" ]

[ 2163 ]

1

[ "EC" ]

[ "3.11.1.2" ]

[ "EC:3.11.1.2" ]

1

[ "1ei6", "3szy", "3szz", "3t00", "3t01", "3t02" ]

6

[ "PUB00015581" ]

[ "9300819" ]

[ "Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving enzyme and its expression in Escherichia coli and Pseudomonas putida." ]

[ 1997 ]

1

[]

0

null

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

[ 5, 1914, 220, 24 ]

4

[]

0

true

Homologous_superfamily

Phosphonoacetate hydrolase, insert domain superfamily

Phosphonoacetate_hydro_insert

9

IPR023117

23,117

PA1123-like domain

PA1123-like_domain

Domain

563

false

This domain contains three α helices and six β strands. It is found in a protein that is produced from gene PA1123 of Pseudomonas. The protein PA1123 appears to be present in the biofilm layer and may be a lipoprotein.

[]

0

[ "PFAM" ]

[ "PF09634" ]

[ "DUF2025" ]

[ 563 ]

1

[]

0

[ "2hg6" ]

1

[]

0

[]

0

null

[ "Pseudomonadaceae" ]

[ 563 ]

1

[]

0

true

Domain

PA1123-like domain

PA1123-like_domain

2

IPR023118

23,118

YqaI domain superfamily

YqaI_dom_sf

Homologous_superfamily

332

false

This superfamily represents a domain consisting of an α helix and four β strands. It is found in the hypothetical protein YqaI, which is expressed in bacteria, particularly Bacillus subtilis.

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.30.40.30", "SSF160713" ]

[ "", "" ]

[ 306, 312 ]

2

[]

0

[ "2dsm" ]

1

[]

0

[]

0

null

[ "Bacillati", "Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)", "Viruses" ]

[ 323, 1, 8 ]

3

[]

0

true

Homologous_superfamily

YqaI domain superfamily

YqaI_dom_sf

1

IPR023120

23,120

Winged helix-turn-helix transcription repressor, HrcA, inserted dimerising domain superfamily

WHTH_transcript_rep_HrcA_IDD

Homologous_superfamily

15,014

false

Prokaryotic cells have a defence mechanism against a sudden heat-shock stress. Commonly, they induce a set of proteins that protect cellular proteins from being denatured by heat. Among such proteins are the GroE and DnaK chaperones whose transcription is regulated by a heat-shock repressor protein HrcA. HrcA is a wing...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:3.30.390.60" ]

[ "" ]

[ 15014 ]

1

[]

0

[ "1stz" ]

1

[ "PUB00037641", "PUB00053432", "PUB00053433" ]

[ "15979091", "19277496", "12486078" ]

[ "Crystal structure of a heat-inducible transcriptional repressor HrcA from Thermotoga maritima: structural insight into DNA binding and dimerization.", "Reduction-sensitive and cysteine residue-mediated Streptococcus pneumoniae HrcA oligomerization in vitro.", "Identification of a helix-turn-helix motif of Baci...

[ 2005, 2009, 2003 ]

3

[]

0

null

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

[ 14706, 15, 293 ]

3

[]

0

true

Homologous_superfamily

Winged helix-turn-helix transcription repressor, HrcA, inserted dimerising domain superfamily

WHTH_transcript_rep_HrcA_IDD

8

IPR023121

23,121

ApoC-II domain superfamily

ApoC-II_dom_sf

Homologous_superfamily

470

false

This domain superfamily is found in apolipoprotein CII (apoC-II). ApoC-II is a surface constituent of plasma lipoproteins and the activator for lipoprotein lipase (LPL). It is therefore central for lipid transport in blood. Lipoprotein lipase is a key enzyme in the regulation of triglyceride levels in human serum [ ]. ...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.1440.10" ]

[ "" ]

[ 470 ]

1

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

[ "R-BTA-8963888", "R-BTA-8963901", "R-BTA-8964058", "R-BTA-975634", "R-CFA-8963888", "R-CFA-8963901", "R-CFA-8964058", "R-CFA-975634", "R-HSA-8963888", "R-HSA-8963889", "R-HSA-8963901", "R-HSA-8964058", "R-HSA-9029569", "R-HSA-975634", "R-MMU-8963888", "R-MMU-8963901", "R-MMU-8964058"...

[ "REACTOME:R-BTA-8963888", "REACTOME:R-BTA-8963901", "REACTOME:R-BTA-8964058", "REACTOME:R-BTA-975634", "REACTOME:R-CFA-8963888", "REACTOME:R-CFA-8963901", "REACTOME:R-CFA-8964058", "REACTOME:R-CFA-975634", "REACTOME:R-HSA-8963888", "REACTOME:R-HSA-8963889", "REACTOME:R-HSA-8963901", "REACTOME:...

22

[ "1by6", "1i5j", "1o8t", "1soh" ]

4

[ "PUB00010498", "PUB00025907", "PUB00029348" ]

[ "10903476", "11331005", "12590574" ]

[ "Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine.", "NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.", "Global structure and dynamics of human apolipoprotein CII in complex wi...

[ 2000, 2001, 2003 ]

3

[]

0

null

[ "Bacteroidota", "Bilateria" ]

[ 3, 467 ]

2

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

[ 14, 1, 6, 2, 1 ]

5

true

Homologous_superfamily

ApoC-II domain superfamily

ApoC-II_dom_sf

2

IPR023122

23,122

NE1680-like superfamily

NE1680-like_sf

Homologous_superfamily

557

false

This superfamily represents a domain of ~86 residues which consists of two α helices and four β strands. Its function is unknown.

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.10.510.10", "SSF160766" ]

[ "", "" ]

[ 557, 557 ]

2

[]

0

[ "2hfq" ]

1

[]

0

[]

0

null

[ "Nitrososphaerota", "Pseudomonadati", "ecological metagenomes" ]

[ 84, 462, 11 ]

3

[]

0

true

Homologous_superfamily

NE1680-like superfamily

NE1680-like_sf

5

IPR023123

23,123

Tubulin, C-terminal

Tubulin_C

Homologous_superfamily

56,742

false

Microtubules are polymers of tubulin, a dimer of two 55kDa subunits, designated alpha and beta [ , ]. Within the microtubule lattice, α-β heterodimers associate in a head-to-tail fashion, giving rise to microtubule polarity. Fluorescent labelling studies have suggested that tubulin is oriented in microtubules with beta...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.287.600" ]

[ "" ]

[ 56742 ]

1

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

[ "R-BTA-114608", "R-BTA-190840", "R-BTA-2132295", "R-BTA-2467813", "R-BTA-2500257", "R-BTA-2565942", "R-BTA-3371497", "R-BTA-380259", "R-BTA-380270", "R-BTA-380284", "R-BTA-380320", "R-BTA-5610787", "R-BTA-5617833", "R-BTA-5620912", "R-BTA-5620924", "R-BTA-5626467", "R-BTA-5663220", ...

[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-190840", "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-2467813", "REACTOME:R-BTA-2500257", "REACTOME:R-BTA-2565942", "REACTOME:R-BTA-3371497", "REACTOME:R-BTA-380259", "REACTOME:R-BTA-380270", "REACTOME:R-BTA-380284", "REACTOME:R-BTA-380320", "REACTOME:R-BT...

233

[ "1ffx", "1ia0", "1jff", "1sa0", "1sa1", "1tub", "1tvk", "1z2b", "1z5v", "1z5w", "2bto", "2btq", "2e4h", "2hxf", "2hxh", "2p4n", "2wbe", "2xrp", "3cb2", "3dco", "3du7", "3e22", "3edl", "3hkb", "3hkc", "3hkd", "3hke", "3iz0", "3j1t", "3j1u", "3j2u", "3j6e"...

783

[ "PUB00000039", "PUB00000721", "PUB00000978", "PUB00002443", "PUB00006112", "PUB00020380", "PUB00039756", "PUB00072957", "PUB00072959", "PUB00099927" ]

[ "3896122", "8274140", "2194680", "3680207", "8102497", "11030624", "15967998", "12486237", "25169981", "26234217" ]

[ "Molecular biology and genetics of tubulin.", "Gamma-tubulin: the hub of cellular microtubule assemblies.", "Diversity among tubulin subunits: toward what functional end?", "Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate.", "Localization of an exchangeable GT...

[ 1985, 1993, 1990, 1987, 1993, 2000, 2005, 2002, 2014, 2015 ]

10

[]

0

null

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

[ 29, 56706, 6, 1 ]

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...

[ 48, 20, 36, 27, 91, 42, 4, 36, 68, 4, 4, 124 ]

12

true

Homologous_superfamily

Tubulin, C-terminal

Tubulin_C

8

IPR023124

23,124

DUF3239 domain superfamily

DUF3239_dom_sf

Homologous_superfamily

513

false

This domain superfamily is found in the protein family defined by ; these are putative membrane proteins, however this cannot be confirmed. Currently they have no known function.

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:2.40.410.10" ]

[ "" ]

[ 513 ]

1

[]

0

[ "3c8i" ]

1

[]

0

[]

0

null

[ "Bacteria", "Didymella rabiei", "freshwater metagenome" ]

[ 511, 1, 1 ]

3

[]

0

true

Homologous_superfamily

DUF3239 domain superfamily

DUF3239_dom_sf

5

IPR023126

23,126

HP0242-like superfamily

HP0242-like_sf

Homologous_superfamily

381

false

This domain superfamily is found in proteins of unknown function related to HP0242. The crystal structure of HP0242, a hypothetical protein from Helicobacter pylori (Campylobacter pylori) has been determined. It reveals an acid-adaptive protein possibly of physiological significance when H. pylori colonises the human s...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.10.3350.10", "SSF158752" ]

[ "", "" ]

[ 274, 381 ]

2

[]

0

[ "2bo3", "3mlg", "3mli", "4npx", "4u12" ]

5

[ "PUB00039697" ]

[ "16395670" ]

[ "Crystal structure of HP0242, a hypothetical protein from Helicobacter pylori with a novel fold." ]

[ 2006 ]

1

[]

0

null

[ "Campylobacterota", "Eukaryota", "ecological metagenomes" ]

[ 363, 4, 14 ]

3

[]

0

true

Homologous_superfamily

HP0242-like superfamily

HP0242-like_sf

7

IPR023128

23,128

Protein N-terminal glutamine amidohydrolase, alpha beta roll

Prot_N_Gln_amidohydro_ab_roll

Domain

2,855

false

This entry represents a structural domain found in the N-terminal glutamine amidohydrolase (Nt Q -amidase) family of proteins. These proteins contain a region of approximately 200 residues carrying several distinctive motifs including a WDYHV motif and one of three cysteines. Protein N-terminal glutamine amidohydrolase...

[]

0

[ "PFAM" ]

[ "PF09764" ]

[ "Nt_Gln_amidase" ]

[ 2855 ]

1

[ "EC", "METACYC" ]

[ "3.5.1.122", "PWY-7799" ]

[ "EC:3.5.1.122", "METACYC:PWY-7799" ]

2

[ "3c9q", "4w79", "6kgj", "8jjf", "8jjg", "8jjh", "8jji", "8jju", "8jjw", "8jjx", "8jjy", "8jjz", "8jk0", "8jk1", "8jk2" ]

15

[ "PUB00054026" ]

[ "19560421" ]

[ "Glutamine-specific N-terminal amidase, a component of the N-end rule pathway." ]

[ 2009 ]

1

[]

0

null

[ "Bacteria", "Clandestinovirus", "Eukaryota", "hydrothermal vent metagenome" ]

[ 42, 1, 2807, 5 ]

4

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

[ 5, 1, 1, 2, 5, 5, 1, 10, 9 ]

9

true

Domain

Protein N-terminal glutamine amidohydrolase, alpha beta roll

Prot_N_Gln_amidohydro_ab_roll

7

IPR023130

23,130

Ta0600-like superfamily

Ta0600-like_sf

Homologous_superfamily

1,870

false

This domain superfamily is functionally uncharacterised and found primarily in the UPF0147 family of proteins, which have no known function.

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.20.1440.50" ]

[ "" ]

[ 1870 ]

1

[]

0

[ "1tdp", "2bl7", "2bl8", "2fu2", "2qsb", "2qzg" ]

6

[]

0

[]

0

null

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

[ 531, 1290, 1, 48 ]

4

[]

0

true

Homologous_superfamily

Ta0600-like superfamily

Ta0600-like_sf

6

IPR023131

23,131

Mth639-like domain superfamily

Mth639-like_dom_sf

Homologous_superfamily

824

false

This domain superfamily is found in a prokaryotic family of proteins, which have no known function.

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:2.60.120.630" ]

[ "" ]

[ 824 ]

1

[]

0

[ "3cbn", "7y7n" ]

2

[]

0

[]

0

null

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

[ 750, 46, 28 ]

3

[]

0

true

Homologous_superfamily

Mth639-like domain superfamily

Mth639-like_dom_sf

3

IPR023132

23,132

Sama2622-like superfamily

Sama2622-like_sf

Homologous_superfamily

385

false

This domain superfamily is found in a family of proteins, which have no known function.

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.10.3440.10", "SSF158675" ]

[ "", "" ]

[ 218, 385 ]

2

[]

0

[ "2pv4" ]

1

[]

0

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 381, 4 ]

2

[]

0

true

Homologous_superfamily

Sama2622-like superfamily

Sama2622-like_sf

5

IPR023135

23,135

N6 adenine-specific DNA methyltransferase, TaqI class, C-terminal

N6_DNA_MeTrfase_TaqI_C

Homologous_superfamily

729

false

In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. There are 2 major classes of DNA methyltransferase that differ in the nature of the modifications they effect. The members of one class (C-MTases) methylate a ring carbon and form C5-methylcytosine (see ...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:3.90.220.10" ]

[ "" ]

[ 729 ]

1

[]

0

[ "1aqi", "1aqj", "1g38", "2adm", "2ibs", "2ibt", "2ih2", "2ih4", "2ih5", "2jg3", "2np6", "2np7" ]

12

[ "PUB00000092", "PUB00001770", "PUB00001857", "PUB00003225", "PUB00003245", "PUB00004831" ]

[ "7663118", "3248728", "7607512", "3323532", "2541254", "7971991" ]

[ "Structure and function of DNA methyltransferases.", "The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases.", "Sequence motifs characteristic for DNA [cytosine-N4] ...

[ 1995, 1988, 1995, 1987, 1989, 1994 ]

6

[]

0

null

[ "Archaea", "Bacteria", "Bilateria", "metagenomes", "uncultured archaeal virus" ]

[ 80, 618, 3, 27, 1 ]

5

[]

0

true

Homologous_superfamily

N6 adenine-specific DNA methyltransferase, TaqI class, C-terminal

N6_DNA_MeTrfase_TaqI_C

9

IPR023136

23,136

Api92-like domain superfamily

Api92-like_dom_sf

Homologous_superfamily

1,166

false

This domain superfamily is found in a family of hypothetical enterobacterial proteins of around 170 residues in length. Members of this family are found in Escherichia coli, Salmonella typhimurium and Shigella species. The function of this family is unknown.

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.3530.10" ]

[ "" ]

[ 1166 ]

1

[]

0

[ "2ijr" ]

1

[]

0

[]

0

null

[ "Pseudomonadota", "uncultured Caudovirales phage" ]

[ 1164, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Homologous_superfamily

Api92-like domain superfamily

Api92-like_dom_sf

5

IPR023137

23,137

BrxA superfamily

BrxA_sf

Homologous_superfamily

1,922

false

BrxA is part of the phage resistance system BREX (Bacteriophage Exclusion). It shares structural homology with the RNA-binding antitermination protein NusB [ ].

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.3540.10" ]

[ "" ]

[ 1922 ]

1

[]

0

[ "3bhw", "7zge" ]

2

[ "PUB00093365" ]

[ "25452498" ]

[ "BREX is a novel phage resistance system widespread in microbial genomes." ]

[ 2015 ]

1

[]

0

null

[ "Bacteria", "Caudoviricetes", "Methanobacteriota", "leotiomyceta", "metagenomes" ]

[ 1794, 3, 100, 2, 23 ]

5

[]

0

true

Homologous_superfamily

BrxA superfamily

BrxA_sf

3

IPR023138

23,138

NMB0513-like superfamily

NMB0513-like_sf

Homologous_superfamily

513

false

This domain is found in a family of proteins, which have no known function.

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.10.3510.10", "SSF160472" ]

[ "", "" ]

[ 499, 512 ]

2

[]

0

[ "2o5h" ]

1

[]

0

[]

0

null

[ "Bacteria", "Diploscapter pachys" ]

[ 512, 1 ]

2

[]

0

true

Homologous_superfamily

NMB0513-like superfamily

NMB0513-like_sf

1

IPR023139

23,139

PBDC1-like domain superfamily

PBDC1-like_dom_sf

Homologous_superfamily

3,340

false

This domain superfamily can be found in the PBDC1 (polysaccharide biosynthesis domain-containing protein 1) proteins from fungi and animals. Protein PBDC1 homolog from S. cerevisiae also known as Ypl225w (Chp1, Chaperone 1 for eEF1A) functions as a co-translational chaperone by forming dual interactions with the eEF1A ...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.3560.10" ]

[ "" ]

[ 3340 ]

1

[]

0

[ "2jyn" ]

1

[ "PUB00160075", "PUB00160942" ]

[ "39900909", "38360885" ]

[ "A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A.", "Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis." ]

[ 2025, 2024 ]

2

[]

0

null

[ "Eukaryota" ]

[ 3340 ]

1

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

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

9

true

Homologous_superfamily

PBDC1-like domain superfamily

PBDC1-like_dom_sf

7

IPR023140

23,140

Domain of unknown function DUF357

DUF357

Domain

933

false

This domain is found in a family of proteins, which have no known function. The members of this family fold into a three helical bundle that has some structural similarity to imunnoglobulin/albumin binding domains .

[]

0

[ "PFAM" ]

[ "PF04010" ]

[ "DUF357" ]

[ 933 ]

1

[]

0

[ "2oo2", "2pmr", "4fzo", "4fzp" ]

4

[]

0

[]

0

null

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

[ 901, 2, 30 ]

3

[]

0

true

Domain

Domain of unknown function DUF357

DUF357

9

IPR023141

23,141

Ammonia/methane monooxygenase, subunit B, hairpin domain superfamily

NH3_CH4_mOase_suB_hlx_hairpin

Homologous_superfamily

254

false

Ammonia monooxygenase and the particulate methane monooxygenase are both integral membrane proteins, occurring in ammonia oxidisers and methanotrophs respectively, which are thought to be evolutionarily related [ ]. These enzymes have a relatively wide substrate specificity and can catalyse the oxidation of a range of ...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.287.710" ]

[ "" ]

[ 254 ]

1

[]

0

[ "1yew", "3chx", "3rfr", "3rgb", "4phz", "4pi0", "4pi2", "6cxh", "7ev9", "7s4h", "7s4i", "7s4j", "7s4k", "7s4l", "7s4m", "7t4o", "7t4p", "7yzy", "8oyi", "8sqw", "8sr1", "8sr2", "8sr4", "8sr5", "9cl1", "9cl2", "9cl3", "9cl4", "9cl5", "9cl6" ]

30

[ "PUB00016963", "PUB00016964", "PUB00016965" ]

[ "7590173", "12209257", "15674245" ]

[ "Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related.", "Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea.", "Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane." ]

[ 1995, 2002, 2005 ]

3

[]

0

null

[ "Bacteria", "unclassified sequences" ]

[ 249, 5 ]

2

[]

0

true

Homologous_superfamily

Ammonia/methane monooxygenase, subunit B, hairpin domain superfamily

NH3_CH4_mOase_suB_hlx_hairpin

2

IPR023142

23,142

Microtubule-associated serine/threonine-protein kinase, pre-PK domain superfamily

MAST_pre-PK_dom_sf

Homologous_superfamily

8,676

false

This superfamily represents a four α-helical bundle domain found N-terminal to the protein kinase domain in microtubule-associated serine/threonine-protein kinases.

[ "GO:0004674" ]

[ "protein serine/threonine kinase activity" ]

[ "molecular_function" ]

1

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.20.1480.20", "SSF140482" ]

[ "", "" ]

[ 8543, 8626 ]

2

[ "EC" ]

[ "2.7.11.1" ]

[ "EC:2.7.11.1" ]

1

[ "1v9v", "2m9x" ]

2

[]

0

[]

0

null

[ "Eukaryota" ]

[ 8676 ]

1

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

[ 9, 67, 5, 21, 18, 28 ]

6

true

Homologous_superfamily

Microtubule-associated serine/threonine-protein kinase, pre-PK domain superfamily

MAST_pre-PK_dom_sf

4

IPR023143

23,143

Mycolic acid cyclopropane synthase-like domain superfamily

Cyclopro_synthase-like_dom_sf

Homologous_superfamily

25

false

Some bacteria synthesise betaine from glycine by a three-step methylation process. The first enzyme, glycine/sarcosine N-methyltransferase, leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of sarcosine/dimethylglycine ...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.287.840" ]

[ "" ]

[ 25 ]

1

[]

0

[]

0

[ "PUB00054010" ]

[ "12466265" ]

[ "Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica." ]

[ 2003 ]

1

[]

0

null

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

[ 19, 5, 1 ]

3

[]

0

true

Homologous_superfamily

Mycolic acid cyclopropane synthase-like domain superfamily

Cyclopro_synthase-like_dom_sf

1

IPR023144

23,144

Phenylalanine ammonia-lyase, shielding domain superfamily

Phe_NH3-lyase_shielding_dom_sf

Homologous_superfamily

5,679

false

This superfamily represents the shielding domain at the C-terminal of PAL which is tightly connected to the core domain through the exceptionally long 55-residue helix α17. The shielding domain restricts the access to the active centre so that the risk of inactivation by nucleophiles in conjunction with dioxygen is min...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.274.20" ]

[ "" ]

[ 5679 ]

1

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

[ "4.3.1.24", "PWY-1121", "PWY-5048", "PWY-5883", "PWY-6444", "PWY-6457", "PWY-8157" ]

[ "EC:4.3.1.24", "METACYC:PWY-1121", "METACYC:PWY-5048", "METACYC:PWY-5883", "METACYC:PWY-6444", "METACYC:PWY-6457", "METACYC:PWY-8157" ]

7

[ "1t6j", "1t6p", "1w27", "1y2m", "2yii", "3nz4", "4baa", "4bab", "4c5r", "4c5s", "4c5u", "4c6g", "4cq5", "4v2q", "4v2r", "6at7", "6f6t", "6h2o", "6hqf", "6rgs" ]

20

[ "PUB00031359", "PUB00032159", "PUB00035855", "PUB00097889", "PUB00097890" ]

[ "15350127", "15548745", "16478474", "28605916", "33242032" ]

[ "Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis.", "Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase.", "The essential tyrosine-containing loop conformation and the role of the C-terminal multi-helix ...

[ 2004, 2004, 2006, 2017, 2021 ]

5

[]

0

null

[ "Ectobacillus ponti", "Eukaryota" ]

[ 1, 5678 ]

2

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

[ 13, 1, 33, 38 ]

4

true

Homologous_superfamily

Phenylalanine ammonia-lyase, shielding domain superfamily

Phe_NH3-lyase_shielding_dom_sf

6

IPR023145

23,145

YfbU, helix-hairpin domain superfamily

YfbU_helix-hairpin_sf

Homologous_superfamily

1,618

false

This superfamily represents a helix-hairpin domain found in a number of proteins of unknown function belonging to the UPF0304 family.

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.287.680" ]

[ "" ]

[ 1618 ]

1

[]

0

[ "1wpb", "4lr3" ]

2

[]

0

[]

0

null

[ "Bacteria", "Methanococcales", "Pezizomycotina", "ecological metagenomes" ]

[ 1611, 3, 2, 2 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Homologous_superfamily

YfbU, helix-hairpin domain superfamily

YfbU_helix-hairpin_sf

9

IPR023146

23,146

YfbU, alpha-helical bundle domain superfamily

YfbU_alpha-helical_sf

Homologous_superfamily

1,925

false

This superfamily represents a domain consisting of three α helices arranged in an orthogonal bundle, and found in a number of proteins of unknown function belonging to the UPF0304 family.

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.3190.10" ]

[ "" ]

[ 1925 ]

1

[]

0

[ "1wpb", "4lr3" ]

2

[]

0

[]

0

null

[ "Bacteria", "Methanococcales", "Pezizomycotina", "metagenomes" ]

[ 1913, 3, 4, 5 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Homologous_superfamily

YfbU, alpha-helical bundle domain superfamily

YfbU_alpha-helical_sf

7

IPR023148

23,148

tRNA (guanine-N(1)-)-methyltransferase, C-terminal domain superfamily

tRNA_m1G_MeTrfase_C_sf

Homologous_superfamily

25,755

false

In transfer RNA many different modified nucleosides are found, especially in the anticodon region. tRNA (guanine (N1))-methyltransferase TrmD is one of several nucleases operating together with the tRNA-modifying enzymes before the formation of the mature tRNA. It catalyses the reaction: S-adenosyl-L-methionine + guani...

[ "GO:0052906", "GO:0008033" ]

[ "tRNA (guanine(37)-N1)-methyltransferase activity", "tRNA processing" ]

[ "molecular_function", "biological_process" ]

2

[ "CATHGENE3D" ]

[ "G3DSA:1.10.1270.20" ]

[ "" ]

[ 25755 ]

1

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

[ "2.1.1.228", "PWY-6829", "PWY-7285", "PWY-7286" ]

[ "EC:2.1.1.228", "METACYC:PWY-6829", "METACYC:PWY-7285", "METACYC:PWY-7286" ]

4

[ "1oy5", "1p9p", "1uaj", "1uak", "1ual", "1uam", "3axz", "3ief", "3knu", "3ky7", "3quv", "4h3y", "4h3z", "4ig6", "4mcb", "4mcc", "4mcd", "4ypw", "4ypx", "4ypy", "4ypz", "4yq0", "4yq1", "4yq2", "4yq3", "4yq4", "4yq5", "4yq6", "4yq7", "4yq8", "4yq9", "4yqa"...

140

[ "PUB00006251" ]

[ "2207153" ]

[ "Role of tRNA modification in translational fidelity." ]

[ 1990 ]

1

[]

0

null

[ "Bacteria", "Caudoviricetes", "Eukaryota", "candidate division MSBL1 archaeon SCGC-AAA382N08", "unclassified sequences" ]

[ 25113, 2, 73, 1, 566 ]

5

[ "Escherichia coli (strain K12)", "Homo sapiens" ]

[ 1, 1 ]

2

true

Homologous_superfamily

tRNA (guanine-N(1)-)-methyltransferase, C-terminal domain superfamily

tRNA_m1G_MeTrfase_C_sf

2

IPR023149

23,149

Trans-aconitate 2-methyltransferase, C-terminal

Trans_acon_MeTrfase_C

Homologous_superfamily

7,137

false

This entry represents the C-terminal α-orthogonal bundle domain. Trans-aconitate methyltransferases in bacteria catalyse the monomethyl esterification of trans-aconitate. Trans-aconitate is an effective inhibitor of aconitase, with potentially toxic results, as aconitase plays an essential role in the conversion of cit...

[ "GO:0030798" ]

[ "trans-aconitate 2-methyltransferase activity" ]

[ "molecular_function" ]

1

[ "CATHGENE3D" ]

[ "G3DSA:1.10.150.290" ]

[ "" ]

[ 7137 ]

1

[ "EC" ]

[ "2.1.1.144" ]

[ "EC:2.1.1.144" ]

1

[ "2p35" ]

1

[ "PUB00054011" ]

[ "11329290" ]

[ "Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferases." ]

[ 2001 ]

1

[]

0

null

[ "Amsacta moorei entomopoxvirus", "Bacteria", "Eukaryota", "Methanobacteriota", "metagenomes" ]

[ 1, 6437, 636, 35, 28 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Homologous_superfamily

Trans-aconitate 2-methyltransferase, C-terminal

Trans_acon_MeTrfase_C

9

IPR023151

23,151

PEP-utilising enzyme, conserved site

PEP_util_CS

Conserved_site

42,309

false

A number of enzymes that catalyze the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) via a phospho-histidine intermediate have been shown to be structurally related [ , , , ]. These enzymes are: Pyruvate,orthophosphate dikinase ( ) (PPDK). PPDK catalyzes the reversible phosphorylation of pyruvate and pho...

[ "GO:0016772" ]

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

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS00742" ]

[ "PEP_ENZYMES_2" ]

[ 42309 ]

1

[]

0

[ "1dik", "1ggo", "1jde", "1kbl", "1kc7", "1vbg", "1vbh", "2bg5", "2dik", "2hro", "2hwg", "2kx9", "2l5h", "2n5t", "2ols", "2r82", "2wqd", "2xdf", "2xz7", "2xz9", "5jvj", "5jvl", "5jvn", "5lu4", "6v9k", "6vbj", "6vu0", "8a8e", "9dae", "9pzl" ]

30

[ "PUB00000317", "PUB00001868", "PUB00005010", "PUB00017924" ]

[ "2176881", "8973315", "7686067", "1310524" ]

[ "Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs.", "Novel phosphotransferase-encoding genes revealed by a...

[ 1990, 1996, 1993, 1992 ]

4

[]

0

null

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

[ 806, 39377, 1594, 5, 527 ]

5

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

[ 6, 5, 6, 63 ]

4

true

Conserved_site

PEP-utilising enzyme, conserved site

PEP_util_CS

8

IPR023152

23,152

Ras GTPase-activating protein, conserved site

RasGAP_CS

Conserved_site

25,660

false

This entry represents a conserved site in the RasGAPs (Ras GTPase-activating proteins).

[ "GO:0043087" ]

[ "regulation of GTPase activity" ]

[ "biological_process" ]

1

[ "PROSITE" ]

[ "PS00509" ]

[ "RAS_GTPASE_ACTIV_1" ]

[ 25660 ]

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-DDI-5658442", "R-DME-5658442", "R-HSA-186763", "R-HSA-373753", "R-HSA-381676", "R-HSA-3928662", "R-HSA-5218921", "R-HSA-5626467", "R-HSA-5658442", "R-HSA-5674135", "R-HSA-6798695", "R-HSA-6802946", "R-HSA-6802948", "R-HSA-6802952", "R-HSA-6802953", "R-HSA-6802955", "R-HSA-8849471"...

[ "REACTOME:R-DDI-5658442", "REACTOME:R-DME-5658442", "REACTOME:R-HSA-186763", "REACTOME:R-HSA-373753", "REACTOME:R-HSA-381676", "REACTOME:R-HSA-3928662", "REACTOME:R-HSA-5218921", "REACTOME:R-HSA-5626467", "REACTOME:R-HSA-5658442", "REACTOME:R-HSA-5674135", "REACTOME:R-HSA-6798695", "REACTOME:R...

51

[ "1nf1", "1wer", "1wq1", "3bxj", "3fay", "5cjp", "6ob2", "6ob3", "6v65", "6v6f", "7moc", "7mp5", "7mp6", "7pgp", "7pgq", "7pgr", "7pgs", "7pgt", "7pgu", "7r03", "7r04", "8bos", "8e20", "8edl", "8edm", "8edn", "8edo", "9bz4" ]

28

[ "PUB00000726", "PUB00000983", "PUB00004087", "PUB00004162" ]

[ "7945277", "1883874", "1898771", "8259209" ]

[ "Regulation of the Ras signalling network.", "sar1, a gene from Schizosaccharomyces pombe encoding a protein that regulates ras1.", "The GTPase superfamily: conserved structure and molecular mechanism.", "Proteins regulating Ras and its relatives." ]

[ 1994, 1991, 1991, 1993 ]

4

[]

0

null

[ "Eukaryota", "mine drainage metagenome" ]

[ 25659, 1 ]

2

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

[ 3, 141, 13, 56, 48, 3, 74, 3, 1 ]

9

true

Conserved_site

Ras GTPase-activating protein, conserved site

RasGAP_CS

2

IPR023153

23,153

Dual-action ribosomal maturation protein DarP superfamily

DarP_sf

Homologous_superfamily

6,886

false

This superfamily includes Dual-action ribosomal maturation protein DarP from Pseudomonas syringae and similar sequences from bacteria and some plant species. DarP is a member of a network of 50S ribosomal subunit biogenesis factors which assembles along the 30S-50S interface, preventing incorrect 23S rRNA structures fr...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.10.60.30", "SSF158710" ]

[ "", "" ]

[ 6845, 6883 ]

2

[]

0

[ "2p0t", "7bl5", "9h3q", "9h3r", "9h3s" ]

5

[]

0

[]

0

null

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

[ 6132, 691, 63 ]

3

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

[ 4, 1, 4, 3 ]

4

true

Homologous_superfamily

Dual-action ribosomal maturation protein DarP superfamily

DarP_sf

7

IPR023155

23,155

Cytochrome c-552/4

Cyt_c-552/4

Domain

5,780

false

This domain contains a di-heme elbow motif. It is found among others in cytochrome c-554 and c-552. Cytochrome c554 is a tetra-heme cytochrome involved in the oxidation of NH3 by Nitrosomonas europaea [ ].

[]

0

[ "PFAM" ]

[ "PF13435" ]

[ "Cytochrome_C554" ]

[ 5780 ]

1

[]

0

[ "1bvb", "1ft5", "1ft6", "1sp3", "4qo5", "5ze8", "6i5b", "6qvm" ]

8

[ "PUB00025023" ]

[ "11372197" ]

[ "High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea." ]

[ 2001 ]

1

[]

0

null

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

[ 97, 5432, 1, 250 ]

4

[]

0

true

Domain

Cytochrome c-552/4

Cyt_c-552/4

9

IPR023157

23,157

AGR-C-984p-like superfamily

AGR-C-984p-like_sf

Homologous_superfamily

1,944

false

This domain superfamily is found in a family of conserved proteins of unknown function, DUF1217. Some members contain multiple copies of the domain.

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.10.3700.10", "SSF158837" ]

[ "", "" ]

[ 1938, 1944 ]

2

[]

0

[ "2o8s" ]

1

[]

0

[]

0

null

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

[ 1931, 4, 9 ]

3

[]

0

true

Homologous_superfamily

AGR-C-984p-like superfamily

AGR-C-984p-like_sf

9

IPR023159

23,159

SO1590-like superfamily

SO1590-like_sf

Homologous_superfamily

2,887

false

This superfamily represents a β-barrel domain that is found in a family of bacterial proteins of unknown function. The crystal structure of such an uncharacterised protein (YP563039) from Shewanella denitrificans (strain OS217/ATCC BAA-1090/DSM 15013) at 1.80A resolution and of a protein with unknown function (SO1590) ...

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:2.40.350.10", "SSF159238" ]

[ "", "" ]

[ 2872, 2880 ]

2

[]

0

[ "2ooj", "2q03" ]

2

[]

0

[]

0

null

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

[ 2769, 105, 4, 9 ]

4

[]

0

true

Homologous_superfamily

SO1590-like superfamily

SO1590-like_sf

1

IPR023160

23,160

Ribonuclease HII, helix-loop-helix cap domain superfamily

RNase_HII_hlx-loop-hlx_cap_dom

Homologous_superfamily

4,929

false

This superfamily represents the helix-loop-helix cap domain of ribonuclease HII. This C-terminal domain forms a compact structure consisting of two α-helices: α8 and α9. Unlike the N-terminal domain, bacterial RNases HI do not possess this domain. In the full-length enzyme, the α9 helix is followed by 15 amino acid res...

[ "GO:0004523" ]

[ "RNA-DNA hybrid ribonuclease activity" ]

[ "molecular_function" ]

1

[ "CATHGENE3D" ]

[ "G3DSA:1.10.10.460" ]

[ "" ]

[ 4929 ]

1

[ "EC" ]

[ "3.1.26.4" ]

[ "EC:3.1.26.4" ]

1

[ "1eke", "1i39", "1i3a", "1io2", "1x1p", "2dfe", "2dff", "2dfh", "3kio", "3p56", "3p5j", "3p83", "3puf", "8yjz" ]

14

[ "PUB00021793", "PUB00026076" ]

[ "11254381", "11274461" ]

[ "Structural biochemistry of a type 2 RNase H: RNA primer recognition and removal during DNA replication.", "Catalytic center of an archaeal type 2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses." ]

[ 2001, 2001 ]

2

[]

0

null

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

[ 907, 23, 3948, 3, 48 ]

5

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

[ 5, 1, 2, 11, 3, 3, 1, 2, 4, 1, 1, 6 ]

12

true

Homologous_superfamily

Ribonuclease HII, helix-loop-helix cap domain superfamily

RNase_HII_hlx-loop-hlx_cap_dom

8

IPR023162

23,162

Apc36109-like domain superfamily

Apc36109-like_dom_sf

Homologous_superfamily

1,200

false

This domain superfamily was determined from the crystal structure of APC36109 from Bacillus stearothermophilus (Geobacillus stearothermophilus). It is found in a family of proteins of unknown function.

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.10.340.20", "SSF116922" ]

[ "", "" ]

[ 1157, 1075 ]

2

[]

0

[ "1u84", "3r2x" ]

2

[]

0

[]

0

null

[ "Bacteria", "Rhizophagus irregularis", "ecological metagenomes" ]

[ 1195, 1, 4 ]

3

[]

0

true

Homologous_superfamily

Apc36109-like domain superfamily

Apc36109-like_dom_sf

3

IPR023163

23,163

SMc04008-like domain

SMc04008-like_domain

Domain

4,121

false

This domain was determined from the crystal structures of the proteins of unknown function from Rhizobium meliloti (Sinorhizobium meliloti) and Alcanivorax borkumensis . The domain is found in a family, which consists of several short bacterial proteins of around 100 residues in length. The function of this domain is u...

[]

0

[ "PFAM" ]

[ "PF06844" ]

[ "DUF1244" ]

[ 4121 ]

1

[]

0

[ "2o35", "3fyb" ]

2

[]

0

[]

0

null

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

[ 3984, 80, 57 ]

3

[]

0

true

Domain

SMc04008-like domain

SMc04008-like_domain

2

IPR023164

23,164

YqgQ-like superfamily

YqgQ-like_sf

Homologous_superfamily

2,358

false

This domain superfamily was determined from the crystal structure of a protein of unknown fuction from Bacillus subtilis. The domain is found in a family of proteins whose function is unknown; however it is found in the family represented by .

[]

0

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.10.287.760", "SSF158379" ]

[ "", "" ]

[ 2357, 2356 ]

2

[]

0

[ "2nn4" ]

1

[]

0

[]

0

null

[ "Bacteria" ]

[ 2358 ]

1

[]

0

true

Homologous_superfamily

YqgQ-like superfamily

YqgQ-like_sf

6

IPR023165

23,165

rRNA adenine dimethylase-like, C-terminal

rRNA_Ade_diMease-like_C

Homologous_superfamily

32,372

false

KsgA is a universally conserved rRNA adenine dimethyltransferase that 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 conserved in all species of eubacteria, e...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.8.100" ]

[ "" ]

[ 32372 ]

1

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

[ "2.1.1", "2.1.1.182", "R-HSA-2151201", "R-HSA-6793080", "R-SCE-163282", "R-SPO-163282" ]

[ "EC:2.1.1", "EC:2.1.1.182", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-6793080", "REACTOME:R-SCE-163282", "REACTOME:R-SPO-163282" ]

6

[ "1i4w", "1qam", "1qan", "1qao", "1qaq", "1qyr", "1yub", "2erc", "3ftc", "3ftd", "3fte", "3ftf", "3fut", "3fuu", "3fuv", "3fuw", "3fux", "3fyc", "3fyd", "3grr", "3gru", "3grv", "3gry", "3r9x", "3tpz", "3tqs", "3uzu", "4adv", "4gc5", "4gc9", "4jxj", "6aax"...

76

[ "PUB00014820", "PUB00052052", "PUB00072555" ]

[ "15136037", "19285505", "23804760" ]

[ "Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli.", "Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine.", "Structural basis for S-adenosylmethionine bind...

[ 2004, 2009, 2013 ]

3

[]

0

null

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

[ 731, 27298, 3730, 2, 2, 609 ]

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

[ 10, 1, 8, 1, 1, 3, 1, 1, 3, 1, 1, 12 ]

12

true

Homologous_superfamily

rRNA adenine dimethylase-like, C-terminal

rRNA_Ade_diMease-like_C

8

IPR023166

23,166

BaiN-like, insert domain superfamily

BaiN-like_dom_sf

Homologous_superfamily

24,035

false

This entry represents two structural (β-barrel and H2TH α-helical) domains that are found inserted within a Rossmann fold-like domain. This domain is found in 3-dehydro-bile acid delta(4,6)-reductase from Clostridium scindens (BaiN), Ribosomal RNA dihydrouridine synthase (rdsA) from Escherichia coli and Aminoacetone ox...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.8.260" ]

[ "" ]

[ 24035 ]

1

[]

0

[ "2gqf", "2i0z", "3v76", "4cnj", "4cnk" ]

5

[ "PUB00090979", "PUB00106457", "PUB00160761", "PUB00160762", "PUB00160763" ]

[ "29217478", "25269103", "18469105", "22666463", "39078675" ]

[ "Identification of a gene encoding a flavoprotein involved in bile acid metabolism by the human gut bacterium Clostridium scindens ATCC 35704.", "Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new three-domain family of bacterial flavoproteins.", "SO-LAAO, a novel L-amino acid oxidase that...

[ 2018, 2014, 2008, 2012, 2024 ]

5

[]

0

null

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

[ 23044, 682, 92, 217 ]

4

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

[ 9, 1, 4, 5 ]

4

true

Homologous_superfamily

BaiN-like, insert domain superfamily

BaiN-like_dom_sf

1

IPR023167

23,167

Yap1 redox domain superfamily

Yap1_redox_dom_sf

Homologous_superfamily

2,298

false

The transcription factor Yap1 is a central regulator of the response to oxidative stress in Saccharomyces cerevisiae. In the active oxidized form, a nuclear export signal (NES) in the carboxy-terminal cysteine-rich domain is masked by disulphide-bond-mediated interactions with a conserved amino-terminal α-helix. Upon r...

[]

0

[ "SSF" ]

[ "SSF111430" ]

[ "" ]

[ 2298 ]

1

[]

0

[ "1sse" ]

1

[ "PUB00031186" ]

[ "15318225" ]

[ "Structural basis for redox regulation of Yap1 transcription factor localization." ]

[ 2004 ]

1

[]

0

null

[ "Eukaryota" ]

[ 2298 ]

1

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

[ 1, 3, 1 ]

3

true

Homologous_superfamily

Yap1 redox domain superfamily

Yap1_redox_dom_sf

4

IPR023168

23,168

Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C-terminal, domain 2

GatB_Yqey_C_2

Homologous_superfamily

45,096

false

Glutamyl-tRNA(Gln) amidotransferase (Gat; ) provides a means of producing correctly charged Gln-tRNA(Gln) through the transamidation of mis-acylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase [ , ]. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Gl...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.10.410" ]

[ "" ]

[ 45096 ]

1

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

[ "6.3.5.-", "PWY-5297", "PWY-7811", "PWY-8229" ]

[ "EC:6.3.5.-", "METACYC:PWY-5297", "METACYC:PWY-7811", "METACYC:PWY-8229" ]

4

[ "1ng6", "1zq1", "2d6f", "2df4", "2dqn", "2f2a", "2g5h", "2g5i", "2hz7", "3al0", "3h0l", "3h0m", "3h0r", "3ip4", "8xje", "8xjg" ]

16

[ "PUB00007932", "PUB00038985" ]

[ "9342321", "16216574" ]

[ "Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation.", "Structural basis for tRNA-dependent amidotransferase function." ]

[ 1997, 2005 ]

2

[]

0

null

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

[ 1668, 38243, 4155, 61, 969 ]

5

[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

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

10

true

Homologous_superfamily

Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C-terminal, domain 2

GatB_Yqey_C_2

3

IPR023170

23,170

Helix-hairpin-helix, base-excision DNA repair, C-terminal

HhH_base_excis_C

Homologous_superfamily

84,476

false

This entry represents the extreme C terminus of the helix-hairpin-helix base-excision DNA repair enzyme family, including the DNA glycosylases and lyases [ , , ].

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.10.1670.10" ]

[ "" ]

[ 84476 ]

1

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

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

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

39

[ "1diz", "1ebm", "1fn7", "1hu0", "1kea", "1kg2", "1kg3", "1kg4", "1kg5", "1kg6", "1kg7", "1ko9", "1kqj", "1lwv", "1lww", "1lwy", "1m3h", "1m3q", "1mpg", "1mud", "1mun", "1muy", "1n39", "1n3a", "1n3c", "1orn", "1orp", "1p59", "1pu6", "1pu7", "1pu8", "1pvs"...

151

[ "PUB00006161", "PUB00027216", "PUB00097366" ]

[ "7664751", "15610848", "30442810" ]

[ "Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure.", "Structures of end products resulting from lesion processing by a DNA glycosylase/lyase.", "Small-molecule inhibitor of OGG1 suppresses proinflammatory gene expression and inflammation." ]

[ 1995, 2004, 2018 ]

3

[]

0

null

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

[ 3177, 62863, 17147, 19, 1270 ]

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",...

[ 44, 1, 6, 5, 3, 45, 12, 5, 27, 14, 3, 2, 100 ]

13

true

Homologous_superfamily

Helix-hairpin-helix, base-excision DNA repair, C-terminal

HhH_base_excis_C

2

IPR023171

23,171

Na+/H+ antiporter domain superfamily

Na/H_antiporter_dom_sf

Homologous_superfamily

17,030

false

NhaA is a sodium ion/proton antiporter that uses the proton electrochemical gradient to expel sodium ions from the cytoplasm and functions primarily in the adaptation to high salinity at alkaline pH. NhaA is also believed to be responsible for adaptation to alkaline pH when sodium is available. NhaA is one of the three...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.20.1530.10" ]

[ "" ]

[ 17030 ]

1

[]

0

[ "1zcd", "3fi1", "4atv", "4au5", "7a0w", "7a0x", "7a0y", "7s24", "8ps0" ]

9

[ "PUB00054014" ]

[ "19448069" ]

[ "NhaA crystal structure: functional-structural insights." ]

[ 2009 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Odinarchaeota yellowstonii (strain LCB_4)", "metagenomes", "uncultured Caudovirales phage" ]

[ 16535, 162, 1, 331, 1 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Homologous_superfamily

Na+/H+ antiporter domain superfamily

Na/H_antiporter_dom_sf

4

IPR023172

23,172

Peptidase S51, dipeptidase E

Peptidase_S51_dipeptidase-E

Family

878

false

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

[ "GO:0016805" ]

[ "dipeptidase activity" ]

[ "molecular_function" ]

1

[ "HAMAP" ]

[ "MF_00510" ]

[ "Peptidase_E" ]

[ 878 ]

1

[ "EC" ]

[ "3.4.13.21" ]

[ "EC:3.4.13.21" ]

1

[ "1fy2", "1fye", "6a4r", "6a4s" ]

4

[ "PUB00000522", "PUB00003576", "PUB00011861", "PUB00054015" ]

[ "8439290", "7845208", "11106384", "9928148" ]

[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad.", "Biochemical characterization of alpha-aspartyl dipeptidase. Cloning and expression of its gene." ]

[ 1993, 1994, 2000, 1998 ]

4

[ "IPR005320" ]

[]

1

0

1

[ "Bacteria" ]

[ 878 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Peptidase S51, dipeptidase E

Peptidase_S51_dipeptidase-E

7