LiteFold/InterPro · Datasets at Hugging Face

IPR006374

6,374

Variant surface antigen Stevor

VSA_Stevor

Family

802

false

Malaria is still a major cause of mortality in many areas of the world. Plasmodium falciparum causes the most severe human form of the disease and is responsible for most fatalities. Severe cases of malaria can occur when the parasite invades and then proliferates within red blood cell erythrocytes. The parasite produc...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF17410", "TIGR01478" ]

[ "Stevor", "STEVOR" ]

[ 801, 624 ]

2

[]

0

[]

0

[ "PUB00033900", "PUB00033906", "PUB00033907" ]

[ "10885986", "12368860", "14747138" ]

[ "Molecular aspects of severe malaria.", "The Plasmodium genome database.", "STEVOR--a multifunctional protein?" ]

[ 2000, 2002, 2004 ]

3

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 7, 795 ]

2

[]

0

true

Family

Variant surface antigen Stevor

VSA_Stevor

6

IPR006375

6,375

Mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase

Man1P_GuaTrfase/Man6P_Isoase

Family

11,989

false

This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase ( ) (PMI) and mannose-1-phosphate guanylyltransferase ( ) in Pseudomonas aeruginosa [ ], Xanthomonas campestris [ , ], and Acetobacter xylinus. The literature on the enzyme from Escherichia coli attributes mannose-6-phosphate isomerase activ...

[ "GO:0016779", "GO:0000271" ]

[ "nucleotidyltransferase activity", "polysaccharide biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01479" ]

[ "GMP_PMI" ]

[ 11989 ]

1

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

[ "2.7.7.13", "GenProp1017", "GenProp1648", "PWY-5659" ]

[ "EC:2.7.7.13", "GP:GenProp1017", "GP:GenProp1648", "METACYC:PWY-5659" ]

4

[]

0

[ "PUB00001448", "PUB00002165", "PUB00007419", "PUB00070196", "PUB00070197" ]

[ "8307007", "1370280", "11165500", "1846611", "8050998" ]

[ "Purification, cDNA cloning and heterologous expression of human phosphomannose isomerase.", "Genetics of xanthan production in Xanthomonas campestris: the xanA and xanB genes are involved in UDP-glucose and GDP-mannose biosynthesis.", "JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipa...

[ 1994, 1992, 2001, 1991, 1994 ]

5

[]

0

null

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

[ 185, 11654, 19, 1, 130 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase

Man1P_GuaTrfase/Man6P_Isoase

8

IPR006376

6,376

Copper-resistance protein CopA

Cu-R_CopA

Family

4,573

false

These sequences represent the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is ...

[ "GO:0005507", "GO:0042597" ]

[ "copper ion binding", "periplasmic space" ]

[ "molecular_function", "cellular_component" ]

2

[ "NCBIFAM" ]

[ "TIGR01480" ]

[ "copper_res_A" ]

[ 4573 ]

1

[]

0

[]

0

[]

0

[ "IPR045087" ]

[]

1

0

1

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

[ 4514, 13, 46 ]

3

[]

0

true

Family

Copper-resistance protein CopA

Cu-R_CopA

3

IPR006377

6,377

Catabolite control protein A

CcpA

Family

2,813

false

Catabolite control protein A is a LacI family global transcriptional regulator found in Gram-positive bacteria. CcpA is involved in repressing carbohydrate utilization genes (e.g. alpha-amylase [amyE], acetyl-coenzyme A synthase [acsA]) and in activating genes involved in transporting excess carbon from the cell (e.g. ...

[ "GO:0006355" ]

[ "regulation of DNA-templated transcription" ]

[ "biological_process" ]

1

[ "NCBIFAM" ]

[ "TIGR01481" ]

[ "ccpA" ]

[ 2813 ]

1

[]

0

[ "1rzr", "1zvv", "2hsg", "2jcg", "2o20", "3oqm", "3oqn", "3oqo", "7e5w" ]

9

[ "PUB00017688", "PUB00065438" ]

[ "10094627", "21106498" ]

[ "Transcriptional activation of the glycolytic las operon and catabolite repression of the gal operon in Lactococcus lactis are mediated by the catabolite control protein CcpA.", "Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-af...

[ 1998, 2011 ]

2

[]

0

null

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

[ 2810, 2, 1 ]

3

[]

0

true

Family

Catabolite control protein A

CcpA

5

IPR006379

6,379

HAD-superfamily hydrolase, subfamily IIB

HAD-SF_hydro_IIB

Family

95,565

false

This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterised by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily...

[]

0

[ "NCBIFAM" ]

[ "TIGR01484" ]

[ "HAD-SF-IIB" ]

[ 95565 ]

1

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

[ "GenProp1306", "GenProp1344", "GenProp1407", "GenProp1534", "GenProp1734", "R-BTA-446205", "R-CEL-446205", "R-DDI-446205", "R-DME-446205", "R-HSA-4043911", "R-HSA-446205", "R-MMU-446205", "R-MTU-868688", "R-PFA-446205", "R-SCE-446205", "R-SPO-446205" ]

[ "GP:GenProp1306", "GP:GenProp1344", "GP:GenProp1407", "GP:GenProp1534", "GP:GenProp1734", "REACTOME:R-BTA-446205", "REACTOME:R-CEL-446205", "REACTOME:R-DDI-446205", "REACTOME:R-DME-446205", "REACTOME:R-HSA-4043911", "REACTOME:R-HSA-446205", "REACTOME:R-MMU-446205", "REACTOME:R-MTU-868688", ...

16

[ "1nf2", "1nrw", "1rkq", "1rlm", "1rlo", "1rlt", "1s2o", "1tj3", "1tj4", "1tj5", "1u02", "1u2s", "1u2t", "1wzc", "1xvi", "1ymq", "2amy", "2b1q", "2b1r", "2b30", "2d2v", "2fuc", "2fue", "2hf2", "2i54", "2i55", "2pq0", "2q4r", "2qyh", "2rar", "2rav", "2rb5"...

88

[]

0

[]

[ "IPR000150", "IPR003337", "IPR005002", "IPR006381", "IPR006382" ]

0

5

0

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

[ 938, 72908, 21262, 25, 432 ]

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",...

[ 100, 1, 2, 26, 8, 10, 9, 3, 56, 7, 2, 5, 125 ]

13

true

Family

HAD-superfamily hydrolase, subfamily IIB

HAD-SF_hydro_IIB

1

IPR006380

6,380

Sucrose phosphatase-like domain

SPP-like_dom

Domain

8,104

false

This entry represents a conserved region of the sucrose phosphate phosphohydrolase (SPP) from plants [ , ]. SPP is a member of the Class IIB subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyses the final step in the biosynthesis of sucrose, a critically important m...

[]

0

[ "PFAM" ]

[ "PF05116" ]

[ "S6PP" ]

[ 8104 ]

1

[]

0

[ "1s2o", "1tj3", "1tj4", "1tj5", "1u2s", "1u2t", "2b1q", "2b1r", "2d2v", "3gyg" ]

10

[ "PUB00010220", "PUB00100837" ]

[ "11050182", "24670640" ]

[ "Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants.", "Nectar secretion requires sucrose phosphate synthases and the sugar transporter SWEET9." ]

[ 2000, 2014 ]

2

[]

[ "IPR012821", "IPR035659" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctHip2", "ecological metagenomes" ]

[ 3, 3593, 4468, 1, 39 ]

5

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

[ 39, 20, 70 ]

3

true

Domain

Sucrose phosphatase-like domain

SPP-like_dom

5

IPR006381

6,381

HAD-superfamily hydrolase, superfamily IIB, MPGP

HAD-SF-IIB-MPGP

Family

2,316

false

This group of proteins is a member of the IIB subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. It consists of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii [ ] and related proteins, including GpgP from Methanococcoides burtonii and Persephonella marina, ...

[ "GO:0050531", "GO:0051479", "GO:0005737" ]

[ "mannosyl-3-phosphoglycerate phosphatase activity", "mannosylglycerate biosynthetic process", "cytoplasm" ]

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

3

[ "SFLD", "NCBIFAM", "CDD" ]

[ "SFLDG01142", "TIGR01486", "cd07507" ]

[ "C2.B.2:_Mannosyl-3-phosphoglyc", "HAD-SF-IIB-MPGP", "HAD_Pase" ]

[ 2227, 2299, 986 ]

3

[ "EC", "METACYC" ]

[ "3.1.3.70", "PWY-5656" ]

[ "EC:3.1.3.70", "METACYC:PWY-5656" ]

2

[ "1wzc", "1xvi", "2zos", "3ztw", "3zty", "3zu6", "3zup", "3zw7", "3zwd", "3zwk", "3zx4", "3zx5" ]

12

[ "PUB00017808", "PUB00077965", "PUB00077966" ]

[ "11562374", "16428406", "17189358" ]

[ "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes.", "Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii.", "Glucosylglycerate biosynthesis in t...

[ 2001, 2006, 2007 ]

3

[ "IPR006379" ]

[ "IPR012815", "IPR033980" ]

1

2

0

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

[ 73, 2224, 2, 17 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

HAD-superfamily hydrolase, superfamily IIB, MPGP

HAD-SF-IIB-MPGP

3

IPR006382

6,382

Phosphoglycolate phosphatase

PGPase

Family

744

false

This group of archaeal sequences are phosphoglycolate phosphatases, which catalyse the dephosphorylation of 2-phosphoglycolate [ ].

[ "GO:0000287", "GO:0008967", "GO:0016311" ]

[ "magnesium ion binding", "phosphoglycolate phosphatase activity", "dephosphorylation" ]

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

3

[ "HAMAP" ]

[ "MF_01419" ]

[ "GPH_hydrolase_arch" ]

[ 744 ]

1

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

[ "3.1.3.18", "PWY-181", "PWY-8362", "PWY-8363" ]

[ "EC:3.1.3.18", "METACYC:PWY-181", "METACYC:PWY-8362", "METACYC:PWY-8363" ]

4

[ "1kyt", "1l6r", "1wr8" ]

3

[ "PUB00026943" ]

[ "14555659" ]

[ "Structure- and function-based characterization of a new phosphoglycolate phosphatase from Thermoplasma acidophilum." ]

[ 2004 ]

1

[ "IPR006379" ]

[]

1

0

1

[ "Archaea", "ecological metagenomes" ]

[ 736, 8 ]

2

[]

0

true

Family

Phosphoglycolate phosphatase

PGPase

9

IPR006384

6,384

HAD hydrolase, subfamily IA, Pyridoxal phosphate phosphatase-like

HAD_hydro_PyrdxlP_Pase-like

Family

9,183

false

The Haloacid Dehalogenase (HAD) superfamily is defined by the presence of three short catalytic motifs [ ]. The subfamilies are defined [ ] based on the location and the observed or predicted fold of a so-called capping domain [ ], or the absence of such a domain. Subfamily I consists of sequences in which the capping ...

[ "GO:0016791" ]

[ "phosphatase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR01489" ]

[ "DKMTPPase-SF" ]

[ 9183 ]

1

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

[ "3.1.3", "3.1.3.87", "GenProp1702", "PWY-4361", "R-DRE-1483191", "R-DRE-1483213", "R-HSA-1483191", "R-HSA-1483213", "R-MMU-1483191", "R-MMU-1483213" ]

[ "EC:3.1.3", "EC:3.1.3.87", "GP:GenProp1702", "METACYC:PWY-4361", "REACTOME:R-DRE-1483191", "REACTOME:R-DRE-1483213", "REACTOME:R-HSA-1483191", "REACTOME:R-HSA-1483213", "REACTOME:R-MMU-1483191", "REACTOME:R-MMU-1483213" ]

10

[ "2fea" ]

1

[ "PUB00003337", "PUB00009540", "PUB00009589" ]

[ "7966317", "10956028", "11601995" ]

[ "Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.", "The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and ca...

[ 1994, 2000, 2001 ]

3

[]

[ "IPR016965", "IPR017718" ]

0

2

0

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

[ 1886, 7261, 4, 32 ]

4

[ "Arabidopsis thaliana", "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 (strain ATCC 204508 / S288c)", "...

[ 15, 3, 4, 4, 3, 1, 9, 6, 1, 1, 23 ]

11

true

Family

HAD hydrolase, subfamily IA, Pyridoxal phosphate phosphatase-like

HAD_hydro_PyrdxlP_Pase-like

4

IPR006385

6,385

HAD-superfamily hydrolase, subfamily IB, SerB1-like

HAD_hydro_SerB1

Family

17,873

false

This group of proteins belong to the IB subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences are predominantly bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase SerB1 from Mycobacterium tuberculosis [ ]. This family includes Histidinol-phosp...

[]

0

[ "NCBIFAM" ]

[ "TIGR01490" ]

[ "HAD-SF-IB-hyp1" ]

[ 17873 ]

1

[]

0

[ "3fvv" ]

1

[ "PUB00082628", "PUB00100299" ]

[ "25037224", "31862725" ]

[ "High throughput screen identifies small molecule inhibitors specific for Mycobacterium tuberculosis phosphoserine phosphatase.", "PA0335, a Gene Encoding Histidinol Phosphate Phosphatase, Mediates Histidine Auxotrophy in <i>Pseudomonas aeruginosa</i>." ]

[ 2014, 2020 ]

2

[]

0

null

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

[ 17465, 1, 39, 1, 367 ]

5

[]

0

true

Family

HAD-superfamily hydrolase, subfamily IB, SerB1-like

HAD_hydro_SerB1

7

IPR006386

6,386

HAD-superfamily hydrolase, subfamily IB, PSPase-like, archaeal

HAD-SF_hydro_IB_PSP-like_arc

Family

80

false

This group of sequences belong to the IB subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences are all from archaeal species. The phylogenetically closest group of sequences to these are phosphoserine phosphatases. As there are no known archaeal phosphoserine phosph...

[]

0

[ "NCBIFAM" ]

[ "TIGR01491" ]

[ "HAD-SF-IB-PSPlk" ]

[ 80 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Archaea", "Bacteria", "mine drainage metagenome" ]

[ 76, 3, 1 ]

3

[]

0

true

Family

HAD-superfamily hydrolase, subfamily IB, PSPase-like, archaeal

HAD-SF_hydro_IB_PSP-like_arc

8

IPR006387

6,387

CPW-WPC domain

CPW_WPC_dom

Domain

931

false

This entry represents a domain of about 61 residues in length with six well-conserved cysteine residues and six well-conserved aromatic sites specific to proteins from Apicomplexa. The domain can be found in tandem repeats. It is named for motifs of CPxxW and (less well conserved) WPC. Its function is unknown.

[]

0

[ "PFAM", "SMART", "NCBIFAM" ]

[ "PF09717", "SM01099", "TIGR01492" ]

[ "CPW_WPC", "CPW_WPC", "CPW_WPC" ]

[ 931, 852, 822 ]

3

[]

0

[]

0

[]

0

[]

0

null

[ "Brevibacillus gelatini", "Eukaryota", "viral metagenome" ]

[ 1, 923, 7 ]

3

[]

0

true

Domain

CPW-WPC domain

CPW_WPC_dom

3

IPR006389

6,389

Early transcribed membrane protein, plasmodium

Early_transc_mb_plasmodium

Family

568

false

This entry represents a family of early transcribed membrane proteins from the malaria parasite Plasmodium falciparum and related species. Members of this entry have been shown to be expressed specifically in the ring stage as well as the rodent parasite Plasmodium yoelii [ ]. A homologue from Plasmodium chabaudi was l...

[]

0

[ "NCBIFAM" ]

[ "TIGR01495" ]

[ "ETRAMP" ]

[ 568 ]

1

[]

0

[]

0

[ "PUB00009604", "PUB00009605", "PUB00101909" ]

[ "11163452", "8139619", "34262880" ]

[ "Analysis of stage-specific transcription in plasmodium falciparum reveals a set of genes exclusively transcribed in ring stage parasites.", "A Plasmodium chabaudi antigen located in the parasitophorous vacuole membrane.", "Studies of the Parasite-Midgut Interaction Reveal <i>Plasmodium</i> Proteins Important f...

[ 2000, 1993, 2021 ]

3

[]

0

null

[ "Plasmodium" ]

[ 568 ]

1

[]

0

true

Family

Early transcribed membrane protein, plasmodium

Early_transc_mb_plasmodium

1

IPR006390

6,390

Dihydropteroate synthase domain

DHP_synth_dom

Domain

32,514

false

This domain is present in sequences representing dihydropteroate synthase, the enzyme that catalyses the second to last step in folic acid biosynthesis. Dihydropteroate synthase ( ) (DHPS), a functional homodimer, catalyses the condensation of 6-hydroxymethyl-7,8-dihydropteridine pyrophosphate to para-aminobenzoic acid...

[ "GO:0004156", "GO:0009396" ]

[ "dihydropteroate synthase activity", "folic acid-containing compound biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM", "CDD" ]

[ "TIGR01496", "cd00739" ]

[ "DHPS", "DHPS" ]

[ 32392, 29322 ]

2

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

[ "2.5.1.15", "GenProp0038", "GenProp1332", "GenProp1616", "PWY-6614" ]

[ "EC:2.5.1.15", "GP:GenProp0038", "GP:GenProp1332", "GP:GenProp1616", "METACYC:PWY-6614" ]

5

[ "1ad1", "1ad4", "1aj0", "1aj2", "1ajz", "1eye", "1tws", "1tww", "1twz", "1tx0", "1tx2", "2bmb", "2dqw", "2dza", "2dzb", "2vef", "2veg", "2vp8", "2y5j", "2y5s", "3h21", "3h22", "3h23", "3h24", "3h26", "3h2a", "3h2c", "3h2e", "3h2f", "3h2m", "3h2n", "3h2o"...

109

[ "PUB00001816", "PUB00002127" ]

[ "1313386", "2123867" ]

[ "The multifunctional folic acid synthesis fas gene of Pneumocystis carinii appears to encode dihydropteroate synthase and hydroxymethyldihydropterin pyrophosphokinase.", "An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of pa...

[ 1992, 1990 ]

2

[ "IPR000489" ]

[]

1

0

1

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

[ 902, 28350, 2706, 4, 3, 549 ]

6

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

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

7

true

Domain

Dihydropteroate synthase domain

DHP_synth_dom

9

IPR006391

6,391

P-type ATPase, B chain, subfamily IA

P-type_ATPase_bsu_IA

Family

13,444

false

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

[ "GO:0005524", "GO:0008556", "GO:0006813", "GO:0016020" ]

[ "ATP binding", "P-type potassium transmembrane transporter activity", "potassium ion transport", "membrane" ]

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

4

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

[ "MF_00285", "PTHR43743", "TIGR01497", "cd02078" ]

[ "KdpB", "", "kdpB", "P-type_ATPase_K" ]

[ 12574, 13444, 12694, 10230 ]

4

[ "EC", "GP" ]

[ "7.2.2.6", "GenProp0172" ]

[ "EC:7.2.2.6", "GP:GenProp0172" ]

2

[ "1svj", "1u7q", "2a00", "2a29", "5mrw", "6hra", "6hrb", "7bgy", "7bh1", "7bh2", "7lc3", "7lc6", "7nnl", "7nnp", "7zrd", "7zre", "7zrg", "7zrh", "7zri", "7zrj", "7zrk", "7zrl", "7zrm", "9oc4" ]

24

[ "PUB00008269", "PUB00009606", "PUB00009616", "PUB00009724", "PUB00020603", "PUB00020604", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789", "PUB00160065", "PUB00160066" ]

[ "9858692", "1970651", "9419228", "10608856", "15473999", "15078220", "20450191", "18937357", "1385979", "9741106", "37264943", "37838176" ]

[ "Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli.", "The bacterial Kdp K(+)-ATPase and its relation to other transport ATPases, such as the Na+/K(+)- and Ca2(+)-ATPases in higher organisms.", "Evolution of substrate specificities in the P-type ATPase superfamily.", "The ...

[ 1998, 1990, 1998, 1999, 2004, 2004, 2010, 2008, 1992, 1998, 2023, 2023 ]

12

[ "IPR001757" ]

[]

1

0

1

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

[ 82, 13239, 14, 109 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

P-type ATPase, B chain, subfamily IA

P-type_ATPase_bsu_IA

6

IPR006394

6,394

Glutamate mutase sigma subunit

GlmS

Family

763

false

This entry represents the sigma subunit (GlmS) of glutamate mutase, a cobalamin-dependent enzyme that catalyses the first step in a pathway of glutamate fermentation [ ]. It catalyses the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate) [ ]. The rearrangement reactio...

[ "GO:0016866" ]

[ "intramolecular transferase activity" ]

[ "molecular_function" ]

1

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

[ "MF_00526", "TIGR01501", "cd02072" ]

[ "Me_Asp_mutase_S", "MthylAspMutase", "Glm_B12_BD" ]

[ 723, 763, 722 ]

3

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

[ "5.4.99.1", "PWY-5087", "PWY-5103", "PWY-6728" ]

[ "EC:5.4.99.1", "METACYC:PWY-5087", "METACYC:PWY-5103", "METACYC:PWY-6728" ]

4

[ "1b1a", "1be1", "1cb7", "1ccw", "1fmf", "1i9c", "1id8", "6h9e", "6h9f" ]

9

[ "PUB00009576", "PUB00019191", "PUB00068783", "PUB00080448" ]

[ "7880251", "9739092", "12413543", "10915555" ]

[ "Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli.", "How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum.", "Coenzyme B(12) dependent glutamate mutas...

[ 1994, 1998, 2002, 2000 ]

4

[]

0

null

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

[ 535, 214, 14 ]

3

[]

0

true

Family

Glutamate mutase sigma subunit

GlmS

6

IPR006395

6,395

Methylaspartate ammonia-lyase

Me_Asp_am_lyase

Family

901

false

Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. This reaction is part of the main catabolic pathway for glutamate. MAL belongs to the enolase supe...

[ "GO:0050096" ]

[ "methylaspartate ammonia-lyase activity" ]

[ "molecular_function" ]

1

[ "PIRSF", "SFLD", "NCBIFAM", "CDD" ]

[ "PIRSF017107", "SFLDF00007", "TIGR01502", "cd03314" ]

[ "MAL", "methylaspartate_ammonia-lyase", "B_methylAsp_ase", "MAL" ]

[ 866, 867, 897, 745 ]

4

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

[ "4.3.1.2", "PWY-5087", "PWY-6728" ]

[ "EC:4.3.1.2", "METACYC:PWY-5087", "METACYC:PWY-6728" ]

3

[ "1kcz", "1kd0", "1kko", "1kkr", "3zvh", "3zvi" ]

6

[ "PUB00014292", "PUB00019827", "PUB00080455" ]

[ "11748244", "11796115", "9385136" ]

[ "The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step.", "Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase.", "3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate ferme...

[ 2002, 2002, 1997 ]

3

[]

0

null

[ "Bacteria", "Fungi", "Halobacteriales", "metagenomes" ]

[ 667, 78, 143, 13 ]

4

[]

0

true

Family

Methylaspartate ammonia-lyase

Me_Asp_am_lyase

3

IPR006396

6,396

Glutamate mutase epsilon subunit

Glu_mut_E

Family

1,574

false

Glutamate mutase (methylaspartate mutase) catalyses the reversible interconversion of L-glutamate and L-threo-3-methylaspartate, the first step in the pathway of glutamate fermentation [ ]. Catalysis is initiated using the cobalamin cofactor. The E subunit is the catalytic subunit (MutE) [ ]. The first step in the cata...

[ "GO:0050097" ]

[ "methylaspartate mutase activity" ]

[ "molecular_function" ]

1

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

[ "MF_01923", "PF06368", "PIRSF001495", "TIGR01503", "cd00245" ]

[ "Me_Asp_mutase_E", "Met_asp_mut_E", "Met_asp_mut_epsi", "MthylAspMut_E", "Glm_e" ]

[ 696, 1574, 1392, 732, 763 ]

5

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

[ "5.4.99.1", "PWY-5087", "PWY-5103", "PWY-6728" ]

[ "EC:5.4.99.1", "METACYC:PWY-5087", "METACYC:PWY-5103", "METACYC:PWY-6728" ]

4

[ "1cb7", "1ccw", "1i9c", "6h9e", "6h9f" ]

5

[ "PUB00014831", "PUB00034444", "PUB00034445", "PUB00080451", "PUB00080454" ]

[ "9242908", "16285720", "14738967", "12543643", "11212921" ]

[ "Structure-based perspectives on B12-dependent enzymes.", "Electronic structure studies of the adenosylcobalamin cofactor in glutamate mutase.", "The role of the conserved histidine-aspartate pair in the 'base-off' binding of cobalamins.", "A glutamate mutase is involved in the biosynthesis of the lipopeptide...

[ 1997, 2005, 2004, 2003, 2001 ]

5

[]

0

null

[ "Aduncisulcus paluster", "Bacteria", "Stenosarchaea group", "ecological metagenomes" ]

[ 1, 1411, 140, 22 ]

4

[]

0

true

Family

Glutamate mutase epsilon subunit

Glu_mut_E

3

IPR006397

6,397

Glyoxylate carboligase

Glyox_carbo_lig

Family

3,823

false

Glyoxylate carboligase (Gcl), also called tartronate-semialdehyde synthase, releases CO2 while synthesizing a single molecule of tartronate semialdehyde from two molecules of glyoxylate. Its activity depends on the presence of thiamine diphosphate (ThDP), a derivative of vitamin B1 [ , ]. In the D-glycerate pathway, pa...

[ "GO:0009028", "GO:0009436" ]

[ "tartronate-semialdehyde synthase activity", "glyoxylate catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01504" ]

[ "glyox_carbo_lig" ]

[ 3823 ]

1

[ "GP", "GP" ]

[ "GenProp0689", "GenProp1374" ]

[ "GP:GenProp0689", "GP:GenProp1374" ]

2

[ "2pan", "7ct6", "8beo", "8i01", "8i05", "8i07", "8i08" ]

7

[ "PUB00048645", "PUB00101675" ]

[ "18176558", "22970650" ]

[ "Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes.", "Glyoxylate carboligase: a unique thiamin diphosphate-dependent enzyme that can cycle between the 4'-aminopyrimidinium and 1',4'-iminopyrimidine tautomeric forms in the absence of the conserved glutamate." ]

[ 2008, 2012 ]

2

[ "IPR045229" ]

[]

1

0

1

[ "Bacteria", "Steinernema glaseri", "mine drainage metagenome" ]

[ 3818, 1, 4 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glyoxylate carboligase

Glyox_carbo_lig

9

IPR006398

6,398

2-hydroxy-3-oxopropionate reductase

Tartro_sem_red

Family

6,637

false

These sequences represent 2-hydroxy-3-oxopropionate reductase ( ), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily me...

[ "GO:0008679", "GO:0046487" ]

[ "2-hydroxy-3-oxopropionate reductase activity", "glyoxylate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_02032", "TIGR01505" ]

[ "Tartronate_sem_reduc", "tartro_sem_red" ]

[ 977, 6637 ]

2

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

[ "1.1.1.60", "GenProp0689", "GenProp0714", "GenProp0716", "GenProp1225", "GenProp1374", "GenProp1514", "GenProp1675" ]

[ "EC:1.1.1.60", "GP:GenProp0689", "GP:GenProp0714", "GP:GenProp0716", "GP:GenProp1225", "GP:GenProp1374", "GP:GenProp1514", "GP:GenProp1675" ]

8

[ "1vpd", "1yb4" ]

2

[ "PUB00009608", "PUB00009609" ]

[ "10762278", "10601204" ]

[ "A common regulator for the operons encoding the enzymes involved in D-galactarate, D-glucarate, and D-glycerate utilization in Escherichia coli.", "Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli." ]

[ 2000, 1999 ]

2

[ "IPR015815" ]

[]

1

0

1

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

[ 6606, 8, 23 ]

3

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

2-hydroxy-3-oxopropionate reductase

Tartro_sem_red

7

IPR006399

6,399

Riboflavin synthase, archaeal

Ribfl_synth_arc

Family

383

false

These archaeal proteins, like the bacterial riboflavin biosynthesis alpha chain, catalyse the final step in riboflavin biosynthesis. However, shows closer similarity to 6,7-dimethyl-8-ribityllumazine synthase, which catalyses the previous reaction and which (in bacteria) is called the riboflavin synthase beta chain [ ]...

[ "GO:0004746", "GO:0009231" ]

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

[ "molecular_function", "biological_process" ]

2

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

[ "PIRSF015750", "TIGR01506", "cd09210" ]

[ "Ribfl_synth_arc", "ribC_arch", "Riboflavin_synthase_archaeal" ]

[ 324, 383, 343 ]

3

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

[ "2.5.1.9", "PWY-6167", "PWY-6168" ]

[ "EC:2.5.1.9", "METACYC:PWY-6167", "METACYC:PWY-6168" ]

3

[ "2b98", "2b99", "4y7j", "4y7k", "5im5" ]

5

[ "PUB00039571", "PUB00080559" ]

[ "16272154", "16042598" ]

[ "Crystal structure of an archaeal pentameric riboflavin synthase in complex with a substrate analog inhibitor: stereochemical implications.", "Structures and reaction mechanisms of riboflavin synthases of eubacterial and archaeal origin." ]

[ 2006, 2005 ]

2

[ "IPR002180" ]

[]

1

0

1

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

[ 356, 9, 18 ]

3

[]

0

true

Family

Riboflavin synthase, archaeal

Ribfl_synth_arc

7

IPR006400

6,400

Squalene hopene cyclase

Hopene-cyclase

Family

4,017

false

Hopanoids are planar, polycyclic hydrocarbons similar to eukaryotic sterols, containing five rings instead of the four rings in sterols, and they have a variety of polar and nonpolar side chains. Hopanoids and sterols share structural and functional similarities, for example, both lipid classes are able to modulate the...

[ "GO:0016866" ]

[ "intramolecular transferase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR01507" ]

[ "hopene_cyclase" ]

[ 4017 ]

1

[ "EC" ]

[ "5.4.99" ]

[ "EC:5.4.99" ]

1

[ "1gsz", "1h35", "1h36", "1h37", "1h39", "1h3a", "1h3b", "1h3c", "1o6h", "1o6q", "1o6r", "1o79", "1sqc", "1ump", "2sqc", "3sqc" ]

16

[ "PUB00005227", "PUB00098590", "PUB00100237" ]

[ "9295270", "29456243", "30051576" ]

[ "Structure and function of a squalene cyclase.", "Hopanoid lipids: from membranes to plant-bacteria interactions.", "Enfumafungin synthase represents a novel lineage of fungal triterpene cyclases." ]

[ 1997, 2018, 2018 ]

3

[ "IPR018333" ]

[]

1

0

1

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

[ 3613, 380, 24 ]

3

[]

0

true

Family

Squalene hopene cyclase

Hopene-cyclase

8

IPR006401

6,401

2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1-reductase, archaeal

Rib_reduct_arc

Family

820

false

These sequences represent a specific reductase of riboflavin biosynthesis in the archaea, diaminohydroxyphosphoribosylaminopyrimidine reductase. It should not be confused with bacterial 5-amino-6-(5-phosphoribosylamino)uracil reductase. The intermediate 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine in ribof...

[ "GO:0016491" ]

[ "oxidoreductase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR01508" ]

[ "rib_reduct_arch" ]

[ 820 ]

1

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

[ "1.1.1.302", "PWY-6167", "PWY-6168" ]

[ "EC:1.1.1.302", "METACYC:PWY-6167", "METACYC:PWY-6168" ]

3

[ "2azn", "5xux", "5xv0", "5xv2", "5xv5", "6p8c" ]

6

[]

0

[]

0

null

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

[ 734, 72, 14 ]

3

[]

0

true

Family

2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1-reductase, archaeal

Rib_reduct_arc

1

IPR006405

6,405

Nicotinate phosphoribosyltransferase pncB-type

Nic_PRibTrfase_pncB

Family

15,331

false

A deep split separates two related families of proteins, one of which includes experimentally characterised examples of nicotinate phosphoribosyltransferase ( ), the first enzyme of NAD salvage biosynthesis. This entry represents the other family. Members have a different (longer) spacing of several key motifs and have...

[ "GO:0004516", "GO:0009435" ]

[ "nicotinate phosphoribosyltransferase activity", "NAD+ biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01513" ]

[ "NAPRTase_put" ]

[ 15331 ]

1

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

[ "6.3.4.21", "PWY-5381", "R-CEL-196807", "R-CEL-6798695", "R-DDI-196807", "R-DDI-6798695", "R-DME-196807", "R-DME-6798695", "R-DRE-196807", "R-DRE-6798695", "R-HSA-196807", "R-HSA-6798695", "R-MMU-196807", "R-MMU-6798695", "R-RNO-196807", "R-RNO-6798695" ]

[ "EC:6.3.4.21", "METACYC:PWY-5381", "REACTOME:R-CEL-196807", "REACTOME:R-CEL-6798695", "REACTOME:R-DDI-196807", "REACTOME:R-DDI-6798695", "REACTOME:R-DME-196807", "REACTOME:R-DME-6798695", "REACTOME:R-DRE-196807", "REACTOME:R-DRE-6798695", "REACTOME:R-HSA-196807", "REACTOME:R-HSA-6798695", "R...

16

[ "2f7f", "4mzy", "4yub" ]

3

[ "PUB00067936" ]

[ "18490451" ]

[ "Biosynthesis and recycling of nicotinamide cofactors in mycobacterium tuberculosis. An essential role for NAD in nonreplicating bacilli." ]

[ 2008 ]

1

[ "IPR007229" ]

[]

1

0

1

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

[ 53, 12235, 2, 2972, 69 ]

5

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

[ 10, 1, 3, 4, 3, 2, 6, 6, 12 ]

9

true

Family

Nicotinate phosphoribosyltransferase pncB-type

Nic_PRibTrfase_pncB

1

IPR006406

6,406

Nicotinate phosphoribosyltransferase

Nic_PRibTrfase

Family

9,123

false

This family represents nicotinate phosphoribosyltransferase, the first enzyme in the salvage pathway of NAD biosynthesis from nicontinate (niacin). Members are primarily proteobacterial but also include yeasts and Methanosarcina acetivorans. A related family, apparently non-overlapping in species distribution, is . Mem...

[ "GO:0004516", "GO:0009435" ]

[ "nicotinate phosphoribosyltransferase activity", "NAD+ biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

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

[ "MF_00570", "NF003704", "TIGR01514", "cd01401" ]

[ "NAPRTase", "PRK05321.1", "NAPRTase", "PncB_like" ]

[ 8020, 8056, 8753, 4735 ]

4

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

[ "6.3.4.21", "PWY-5381", "R-SCE-196807", "R-SCE-6798695", "R-SPO-196807", "R-SPO-6798695" ]

[ "EC:6.3.4.21", "METACYC:PWY-5381", "REACTOME:R-SCE-196807", "REACTOME:R-SCE-6798695", "REACTOME:R-SPO-196807", "REACTOME:R-SPO-6798695" ]

6

[ "1vlp", "1ybe", "1yir", "2im5", "3os4", "4hl7" ]

6

[]

0

[ "IPR007229" ]

[]

1

0

1

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

[ 56, 7711, 1314, 8, 34 ]

5

[ "Escherichia coli (strain K12)", "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, 1 ]

4

true

Family

Nicotinate phosphoribosyltransferase

Nic_PRibTrfase

3

IPR006407

6,407

1,4-alpha-glucan-branching enzyme, GlgB

GlgB

Family

18,488

false

This entry represents the glycogen branching enzyme, GlgB, which is responsible for the transfer of chains of approximately seven alpha(1,4)-linked glucosyl residues to other similar chains (in new alpha-(1,6) linkages) in the biosynthesis of glycogen [ ]. The branching enzyme is responsible for the degree of alpha(1,6...

[ "GO:0003844", "GO:0005978" ]

[ "1,4-alpha-glucan branching enzyme activity", "glycogen biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_00685", "TIGR01515" ]

[ "GlgB", "branching_enzym" ]

[ 17317, 18487 ]

2

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

[ "2.4.1.18", "GenProp0168", "GenProp1247", "PWY-5067", "PWY-622", "PWY-7900" ]

[ "EC:2.4.1.18", "GP:GenProp0168", "GP:GenProp1247", "METACYC:PWY-5067", "METACYC:PWY-622", "METACYC:PWY-7900" ]

6

[ "1m7x", "3k1d", "4lpc", "4lq1", "5e6y", "5e6z", "5e70", "5gqu", "5gqv", "5gqw", "5gqx", "5gqy", "5gqz", "5gr0", "5gr1", "5gr2", "5gr3", "5gr4", "5gr5", "5gr6", "6joy", "6klf", "8sdb", "8zqa" ]

24

[ "PUB00027652", "PUB00027653" ]

[ "7862674", "2959476" ]

[ "Maize branching enzyme catalyzes synthesis of glycogen-like polysaccharide in glgB-deficient Escherichia coli.", "The degree of branching in (alpha 1,4)-(alpha 1,6)-linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes." ]

[ 1995, 1987 ]

2

[ "IPR037439" ]

[]

1

0

1

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

[ 39, 18201, 68, 180 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

1,4-alpha-glucan-branching enzyme, GlgB

GlgB

3

IPR006408

6,408

P-type ATPase, subfamily IIB

P-type_ATPase_IIB

Family

24,666

false

This family describes the P-type ATPase responsible for translocating calcium ions across the plasma membrane of eukaryotes [ ], out of the cell. In some organisms, this type of pump may also be found in vacuolar membranes [ ]. In humans and mice, at least, there are multiple isoforms of the PMCA pump with overlapping ...

[ "GO:0005388", "GO:0005524", "GO:0070588", "GO:0016020" ]

[ "P-type calcium transporter activity", "ATP binding", "calcium ion transmembrane transport", "membrane" ]

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

4

[ "NCBIFAM" ]

[ "TIGR01517" ]

[ "ATPase-IIB_Ca" ]

[ 24666 ]

1

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

[ "7.2.2.10", "R-BTA-418359", "R-BTA-5578775", "R-BTA-936837", "R-CEL-418359", "R-CEL-5578775", "R-CEL-936837", "R-DDI-418359", "R-DDI-5578775", "R-DDI-936837", "R-GGA-418359", "R-GGA-5578775", "R-GGA-936837", "R-HSA-418359", "R-HSA-5578775", "R-HSA-936837", "R-HSA-9662360", "R-HSA-9...

[ "EC:7.2.2.10", "REACTOME:R-BTA-418359", "REACTOME:R-BTA-5578775", "REACTOME:R-BTA-936837", "REACTOME:R-CEL-418359", "REACTOME:R-CEL-5578775", "REACTOME:R-CEL-936837", "REACTOME:R-DDI-418359", "REACTOME:R-DDI-5578775", "REACTOME:R-DDI-936837", "REACTOME:R-GGA-418359", "REACTOME:R-GGA-5578775", ...

30

[ "6a69", "8qmp", "9gsd", "9gse", "9gsf", "9gsg", "9gsh", "9gsi", "9gsy", "9gtb" ]

10

[ "PUB00009616", "PUB00009617", "PUB00009618", "PUB00009619", "PUB00020603", "PUB00020604", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789", "PUB00160065", "PUB00160066" ]

[ "9419228", "10434059", "10802325", "11779702", "15473999", "15078220", "20450191", "18937357", "1385979", "9741106", "37264943", "37838176" ]

[ "Evolution of substrate specificities in the P-type ATPase superfamily.", "Developmental expression of the four plasma membrane calcium ATPase (Pmca) genes in the mouse.", "Vacuolar localization of an Entamoeba histolytica homologue of the plasma membrane ATPase (PMCA).", "The role of plasma membrane Ca2+ pum...

[ 1998, 1999, 2000, 2002, 2004, 2004, 2010, 2008, 1992, 1998, 2023, 2023 ]

12

[ "IPR001757" ]

[]

1

0

1

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

[ 97, 2439, 22098, 4, 28 ]

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...

[ 49, 9, 74, 7, 18, 18, 2, 27, 25, 1, 1, 115 ]

12

true

Family

P-type ATPase, subfamily IIB

P-type_ATPase_IIB

9

IPR006409

6,409

Glycerol-3-phosphate cytidylyltransferase

G3P_cytidylTrfase

Family

1,914

false

This entry represents glycerol-3-phosphate cytidyltransferase, also called CDP-glycerol pyrophosphorylase. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase ( ). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynth...

[ "GO:0046872", "GO:0047348", "GO:0019350", "GO:0005737" ]

[ "metal ion binding", "glycerol-3-phosphate cytidylyltransferase activity", "teichoic acid biosynthetic process", "cytoplasm" ]

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

4

[ "NCBIFAM" ]

[ "TIGR01518" ]

[ "g3p_cytidyltrns" ]

[ 1914 ]

1

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

[ "2.7.7.39", "GenProp1398", "GenProp1756", "PWY-7815", "PWY-7816", "PWY-7819", "PWY-8248", "PWY-8429", "PWY-8430" ]

[ "EC:2.7.7.39", "GP:GenProp1398", "GP:GenProp1756", "METACYC:PWY-7815", "METACYC:PWY-7816", "METACYC:PWY-7819", "METACYC:PWY-8248", "METACYC:PWY-8429", "METACYC:PWY-8430" ]

9

[ "1coz", "1n1d", "2b7l" ]

3

[]

0

[]

0

null

[ "Bacteria", "Methanococcus maripaludis", "Phytophthora kernoviae 00238/432", "unclassified sequences" ]

[ 1907, 1, 1, 5 ]

4

[]

0

true

Family

Glycerol-3-phosphate cytidylyltransferase

G3P_cytidylTrfase

4

IPR006410

6,410

Conserved hypothetical protein CHP01519, Plasmodium falciparum (isolate 3D7)

CHP01519_PLAF7

Family

171

false

These sequences represent an uncharacterised family consisting of a small number of hypothetical proteins of the malaria parasite Plasmodium falciparum (isolate 3D7).

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09715", "TIGR01519" ]

[ "Plasmod_dom_1", "plasmod_dom_1" ]

[ 171, 152 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Plasmodium (Laverania)" ]

[ 171 ]

1

[]

0

true

Family

Conserved hypothetical protein CHP01519, Plasmodium falciparum (isolate 3D7)

CHP01519_PLAF7

6

IPR006411

6,411

Fructose-bisphosphate aldolase, class II, yeast/E. coli subtype

Fruct_bisP_bact

Family

12,014

false

Members of this family are class II examples of the glycolytic enzyme fructose-bisphosphate aldolase (FBA). They represent one of two deeply split, architecturally distinct clades of the family that includes class II fructose-bisphosphate aldolases, tagatose-bisphosphate aldolases, and related uncharacterised proteins....

[ "GO:0004332", "GO:0006096" ]

[ "fructose-bisphosphate aldolase activity", "glycolytic process" ]

[ "molecular_function", "biological_process" ]

2

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

[ "PTHR30559", "TIGR01520", "cd00946" ]

[ "", "FruBisAldo_II_A", "FBP_aldolase_IIA" ]

[ 12010, 11370, 6419 ]

3

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

[ "4.1.2.13", "GenProp0120", "GenProp0691", "GenProp1306", "GenProp1344", "GenProp1407", "GenProp1705", "PWY-1042", "PWY-1861", "PWY-5484", "PWY-6142", "PWY-7385", "PWY-8178", "PWY-8404" ]

[ "EC:4.1.2.13", "GP:GenProp0120", "GP:GenProp0691", "GP:GenProp1306", "GP:GenProp1344", "GP:GenProp1407", "GP:GenProp1705", "METACYC:PWY-1042", "METACYC:PWY-1861", "METACYC:PWY-5484", "METACYC:PWY-6142", "METACYC:PWY-7385", "METACYC:PWY-8178", "METACYC:PWY-8404" ]

14

[ "1b57", "1dos", "1gyn", "1zen", "3ekl", "3ekz", "3elf", "3qm3", "4a21", "4a22", "4def", "4del", "4lv4", "5gk3", "5gk4", "5gk5", "5gk6", "5gk7", "5gk8", "5vjd", "5vje", "6lnk", "7rgn", "7v6f", "7v6g", "7yva" ]

26

[ "PUB00005383" ]

[ "1412694" ]

[ "Fructose-bisphosphate aldolases: an evolutionary history." ]

[ 1992 ]

1

[ "IPR000771" ]

[]

1

0

1

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

[ 9225, 2570, 42, 177 ]

4

[ "Escherichia coli (strain K12)", "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, 1 ]

4

true

Family

Fructose-bisphosphate aldolase, class II, yeast/E. coli subtype

Fruct_bisP_bact

4

IPR006412

6,412

Fructose-bisphosphate aldolase, class II, Calvin cycle subtype

Fruct_bisP_Calv

Family

5,524

false

Members of this family are class II examples of the enzyme fructose-bisphosphate aldolase, an enzyme both of glycolysis and (in the opposite direction) of the Calvin cycle of CO2 fixation. A deep split separates the tightly conserved yeast/Escherichia coli/Mycobacterium subtype (all species lacking the Calvin cycle) re...

[ "GO:0004332", "GO:0006096" ]

[ "fructose-bisphosphate aldolase activity", "glycolytic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01521" ]

[ "FruBisAldo_II_B" ]

[ 5524 ]

1

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

[ "4.1.2.13", "GenProp0120", "PWY-1042", "PWY-1861", "PWY-5484", "PWY-6142", "PWY-7385", "PWY-8178", "PWY-8404" ]

[ "EC:4.1.2.13", "GP:GenProp0120", "METACYC:PWY-1042", "METACYC:PWY-1861", "METACYC:PWY-5484", "METACYC:PWY-6142", "METACYC:PWY-7385", "METACYC:PWY-8178", "METACYC:PWY-8404" ]

9

[ "5u4n", "5u7s" ]

2

[]

0

[ "IPR000771" ]

[]

1

0

1

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

[ 5439, 15, 70 ]

3

[]

0

true

Family

Fructose-bisphosphate aldolase, class II, Calvin cycle subtype

Fruct_bisP_Calv

2

IPR006413

6,413

P-type ATPase, subfamily IIA, PMR1-type

P-type_ATPase_IIA_PMR1

Family

4,131

false

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

[ "GO:0005388", "GO:0006816", "GO:0016020" ]

[ "P-type calcium transporter activity", "calcium ion transport", "membrane" ]

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

3

[ "NCBIFAM" ]

[ "TIGR01522" ]

[ "ATPase-IIA2_Ca" ]

[ 4131 ]

1

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

[ "7.2.2.10", "R-BTA-936837", "R-HSA-936837", "R-MMU-936837", "R-RNO-936837", "R-SCE-936837", "R-SPO-936837" ]

[ "EC:7.2.2.10", "REACTOME:R-BTA-936837", "REACTOME:R-HSA-936837", "REACTOME:R-MMU-936837", "REACTOME:R-RNO-936837", "REACTOME:R-SCE-936837", "REACTOME:R-SPO-936837" ]

7

[ "7yag", "7yah", "7yai", "7yaj", "7yam", "8iwp", "8iwr", "8iws", "8iwt", "8iwu", "8iww" ]

11

[ "PUB00009616", "PUB00009621", "PUB00009622", "PUB00020603", "PUB00020604", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789", "PUB00160065", "PUB00160066" ]

[ "9419228", "2526682", "10433975", "15473999", "15078220", "20450191", "18937357", "1385979", "9741106", "37264943", "37838176" ]

[ "Evolution of substrate specificities in the P-type ATPase superfamily.", "The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family.", "Two additional type IIA Ca(2+)-ATPases are expressed in Arabidopsis thaliana: evidence that type IIA sub-groups exist.", "The evolution...

[ 1998, 1989, 1999, 2004, 2004, 2010, 2008, 1992, 1998, 2023, 2023 ]

11

[ "IPR001757" ]

[]

1

0

1

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

[ 49, 217, 3862, 3 ]

4

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

[ 3, 4, 8, 8, 10, 1, 17, 1, 1 ]

9

true

Family

P-type ATPase, subfamily IIA, PMR1-type

P-type_ATPase_IIA_PMR1

2

IPR006414

6,414

P-type ATPase, subfamily IID

P-type_ATPase_IID

Family

3,751

false

This entry represents a group of ATPases has been classified by phylogentic analysis as type IID. They were initially described as a calcium efflux ATPases [ ], but more recent work has shown that the Schizosaccharomyces pombe (Fission yeast) CTA3 gene is in fact a potassium ion efflux pump [ ]. These sequences form th...

[ "GO:0019829", "GO:0006812", "GO:0016020" ]

[ "ATPase-coupled monoatomic cation transmembrane transporter activity", "monoatomic cation transport", "membrane" ]

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

3

[ "NCBIFAM", "CDD" ]

[ "TIGR01523", "cd02086" ]

[ "ATPase-IID_K-Na", "P-type_ATPase_Na_ENA" ]

[ 3750, 1257 ]

2

[ "EC" ]

[ "7.2.2.3" ]

[ "EC:7.2.2.3" ]

1

[]

0

[ "PUB00009616", "PUB00009624", "PUB00009625", "PUB00020603", "PUB00020604", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789", "PUB00160065", "PUB00160066" ]

[ "9419228", "1323458", "11932440", "15473999", "15078220", "20450191", "18937357", "1385979", "9741106", "37264943", "37838176" ]

[ "Evolution of substrate specificities in the P-type ATPase superfamily.", "An intracellular ATP-dependent calcium pump within the yeast Schizosaccharomyces pombe, encoded by the gene cta3.", "Potassium- or sodium-efflux ATPase, a key enzyme in the evolution of fungi.", "The evolution of A-, F-, and V-type ATP...

[ 1998, 1992, 2002, 2004, 2004, 2010, 2008, 1992, 1998, 2023, 2023 ]

11

[ "IPR001757" ]

[]

1

0

1

[ "Eukaryota" ]

[ 3751 ]

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)" ]

[ 3, 3, 1 ]

3

true

Family

P-type ATPase, subfamily IID

P-type_ATPase_IID

6

IPR006415

6,415

P-type ATPase, subfamily IIIB

P-type_ATPase_IIIB

Family

9,069

false

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

[ "GO:0015444", "GO:0015693", "GO:0016020" ]

[ "P-type magnesium transporter activity", "magnesium ion transport", "membrane" ]

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

3

[ "NCBIFAM", "PRINTS", "NCBIFAM", "CDD" ]

[ "NF011702", "PR01836", "TIGR01524", "cd02077" ]

[ "PRK15122.1", "MGATPASE", "ATPase-IIIB_Mg", "P-type_ATPase_Mg" ]

[ 5953, 8769, 8552, 6264 ]

4

[ "EC" ]

[ "7.2.2.14" ]

[ "EC:7.2.2.14" ]

1

[ "8uy7", "8uy8", "8uy9", "8uya", "8uyb", "8uyc", "9ejn" ]

7

[ "PUB00009616", "PUB00009627", "PUB00020603", "PUB00020604", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789", "PUB00160065", "PUB00160066" ]

[ "9419228", "1328179", "15473999", "15078220", "20450191", "18937357", "1385979", "9741106", "37264943", "37838176" ]

[ "Evolution of substrate specificities in the P-type ATPase superfamily.", "MgtA and MgtB: prokaryotic P-type ATPases that mediate Mg2+ influx.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-dis...

[ 1998, 1992, 2004, 2004, 2010, 2008, 1992, 1998, 2023, 2023 ]

10

[ "IPR001757" ]

[]

1

0

1

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

[ 37, 8303, 671, 58 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

P-type ATPase, subfamily IIIB

P-type_ATPase_IIIB

1

IPR006417

6,417

Nicotinamide-nucleotide adenylyltransferase

NadR_NMN_Atrans

Domain

1,543

false

The NadR protein of Escherichia coli and closely related bacteria is both enzyme and regulatory protein. The first 60 or so amino acids, N-terminal region is a DNA-binding helix-turn-helix domain ( ) responsible for repressing the nadAB genes of NAD de novo biosynthesis. The NadR homologues in Mycobacterium tuberculosi...

[ "GO:0000309", "GO:0009435" ]

[ "nicotinamide-nucleotide adenylyltransferase activity", "NAD+ biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01526" ]

[ "nadR_NMN_Atrans" ]

[ 1543 ]

1

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

[ "2.7.1.22", "2.7.7.1", "GenProp1658" ]

[ "EC:2.7.1.22", "EC:2.7.7.1", "GP:GenProp1658" ]

3

[ "1lw7", "6gye", "6gyf", "6gzo", "8x7f" ]

5

[]

0

[]

0

null

[ "Bacteria", "Herelleviridae" ]

[ 1519, 24 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Nicotinamide-nucleotide adenylyltransferase

NadR_NMN_Atrans

3

IPR006418

6,418

Nicotinamide-nucleotide adenylyltransferase, archaea

NMN_Atrans_arc

Family

1,053

false

This family of archaeal proteins exhibits NAD salvage biosynthesis enzyme nicotinamide-nucleotide adenylyltransferase ( ) activity. In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase ( ), an enzyme of NAD de novo biosynthesis, although with a higher Km....

[ "GO:0000309", "GO:0009435", "GO:0005737" ]

[ "nicotinamide-nucleotide adenylyltransferase activity", "NAD+ biosynthetic process", "cytoplasm" ]

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

3

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

[ "MF_00243", "NF002243", "TIGR01527", "cd02166" ]

[ "NMN_adenylyltr", "PRK01153.1", "arch_NMN_Atrans", "NMNAT_Archaea" ]

[ 1046, 1039, 813, 577 ]

4

[ "EC", "GP" ]

[ "2.7.7.1", "GenProp0057" ]

[ "EC:2.7.7.1", "GP:GenProp0057" ]

2

[ "1ej2", "1f9a", "1hyb", "1m8f", "1m8g", "1m8j", "1m8k", "4yp5", "4yp6", "4yp7" ]

10

[]

0

[]

0

null

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

[ 995, 31, 27 ]

3

[]

0

true

Family

Nicotinamide-nucleotide adenylyltransferase, archaea

NMN_Atrans_arc

6

IPR006419

6,419

Nicotinamide mononucleotide transporter PnuC

NMN_transpt_PnuC

Family

14,751

false

PnuC is a membrane protein responsible for nicotinamide mononucleotide transport [ , ], subject to regulation by interaction with the NadR (also called NadI) protein (see ). The extreme N- and C-terminal regions are poorly conserved.

[ "GO:0034257", "GO:0034258", "GO:0016020" ]

[ "nicotinamide riboside transmembrane transporter activity", "nicotinamide riboside transport", "membrane" ]

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

3

[ "PFAM", "PANTHER", "NCBIFAM" ]

[ "PF04973", "PTHR36122", "TIGR01528" ]

[ "NMN_transporter", "", "NMN_trans_PnuC" ]

[ 14750, 13937, 12817 ]

3

[]

0

[ "4qtn" ]

1

[ "PUB00008726", "PUB00061685", "PUB00088390", "PUB00088391" ]

[ "2546921", "15561822", "22136195", "28406895" ]

[ "Genetic characterization of the pnuC gene, which encodes a component of the nicotinamide mononucleotide transport system in Salmonella typhimurium.", "PnuC and the utilization of the nicotinamide riboside analog 3-aminopyridine in Haemophilus influenzae.", "RibM from Streptomyces davawensis is a riboflavin/ros...

[ 1989, 2004, 2011, 2017 ]

4

[]

0

null

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

[ 14099, 77, 3, 295, 277 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Nicotinamide mononucleotide transporter PnuC

NMN_transpt_PnuC

5

IPR006421

6,421

Glycogen debranching enzyme, metazoa

Glycogen_debranch_met

Family

2,863

false

Glycogen debranching enzyme possesses two different catalytic activities; oligo-1,4-->1,4-glucantransferase ( ) and amylo-1,6-glucosidase ( ). Site-directed mutagenesis studies in Saccharomyces cerevisiae (Baker's yeast) [ ] indicate that the transferase and glucosidase activities are independent and located in differe...

[ "GO:0004134", "GO:0004135", "GO:0005978" ]

[ "4-alpha-glucanotransferase activity", "amylo-alpha-1,6-glucosidase activity", "glycogen biosynthetic process" ]

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

3

[ "NCBIFAM" ]

[ "TIGR01531" ]

[ "glyc_debranch" ]

[ 2863 ]

1

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

[ "2.4.1.25", "3.2.1.33", "GenProp0168", "GenProp1259", "PWY-5941", "PWY-6724", "PWY-6737", "PWY-7238", "R-HSA-6798695", "R-HSA-70221", "R-SCE-6798695", "R-SCE-70221" ]

[ "EC:2.4.1.25", "EC:3.2.1.33", "GP:GenProp0168", "GP:GenProp1259", "METACYC:PWY-5941", "METACYC:PWY-6724", "METACYC:PWY-6737", "METACYC:PWY-7238", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-70221", "REACTOME:R-SCE-6798695", "REACTOME:R-SCE-70221" ]

12

[ "5d06", "5d0f", "7eim", "7ejp", "7ejt", "7eku", "7ekw", "7ekx", "8zeq" ]

9

[ "PUB00009629" ]

[ "11375985" ]

[ "Identification of the catalytic residues of bifunctional glycogen debranching enzyme." ]

[ 2001 ]

1

[ "IPR010401" ]

[]

1

0

1

[ "Eukaryota" ]

[ 2863 ]

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)" ]

[ 1, 14, 7, 4, 2, 1, 2, 1 ]

8

true

Family

Glycogen debranching enzyme, metazoa

Glycogen_debranch_met

9

IPR006422

6,422

D-erythrose-4-phosphate dehydrogenase

E4P_DH_bac

Family

2,847

false

This entry contains a small clade of dehydrogenases in gammaproteobacteria which utilise NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose [ ]. This enzyme activity appears to have evolved from glycerald...

[ "GO:0048001", "GO:0051287", "GO:0042823", "GO:0005737" ]

[ "erythrose-4-phosphate dehydrogenase activity", "NAD binding", "pyridoxal phosphate biosynthetic process", "cytoplasm" ]

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

4

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

[ "MF_01640", "NF010058", "TIGR01532" ]

[ "E4P_dehydrog", "PRK13535.1", "E4PD_g-proteo" ]

[ 1910, 2031, 2772 ]

3

[ "EC", "GP" ]

[ "1.2.1.72", "GenProp1633" ]

[ "EC:1.2.1.72", "GP:GenProp1633" ]

2

[ "2x5j", "2x5k", "2xf8" ]

3

[ "PUB00002270" ]

[ "7751290" ]

[ "Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis." ]

[ 1995 ]

1

[ "IPR020831" ]

[]

1

0

1

[ "Bacteria", "Nematoda", "metagenomes" ]

[ 2841, 2, 4 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-erythrose-4-phosphate dehydrogenase

E4P_DH_bac

9

IPR006423

6,423

5-nucleotidase lipoprotein e(P4)

Lipo_e_P4

Family

2,913

false

This entry represents a set of bacterial lipoproteins belonging to a larger acid phosphatase family ( ), which in turn belongs to the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases. Members are found on the outer membrane of Gram-negative bacteria and the cytoplasmic membrane of Gram-positive...

[ "GO:0009279" ]

[ "cell outer membrane" ]

[ "cellular_component" ]

1

[ "PIRSF", "SFLD", "NCBIFAM", "CDD" ]

[ "PIRSF019271", "SFLDG01125", "TIGR01533", "cd07534" ]

[ "Acid_Ptase_C", "C1.1:_Acid_Phosphatase_Like", "lipo_e_P4", "HAD_CAP" ]

[ 2573, 2825, 1977, 1817 ]

4

[ "GP" ]

[ "GenProp1658" ]

[ "GP:GenProp1658" ]

1

[ "2i33", "2i34", "3et4", "3et5", "3ocu", "3ocv", "3ocw", "3ocx", "3ocy", "3ocz", "3pct", "3sf0", "7cle", "7f7a", "7f7b", "7f7c", "7f7d" ]

17

[ "PUB00017708" ]

[ "11395461" ]

[ "NadN and e (P4) are essential for utilization of NAD and nicotinamide mononucleotide but not nicotinamide riboside in Haemophilus influenzae." ]

[ 2001 ]

1

[ "IPR005519" ]

[]

1

0

1

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

[ 2898, 5, 10 ]

3

[]

0

true

Family

5-nucleotidase lipoprotein e(P4)

Lipo_e_P4

7

IPR006424

6,424

Glyceraldehyde-3-phosphate dehydrogenase, type I

Glyceraldehyde-3-P_DH_1

Family

50,345

false

This group of sequences represent glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilise NAD ( ), NADP ( ) or either ( ). In some species, NAD- ...

[ "GO:0016620", "GO:0050661", "GO:0051287", "GO:0006006" ]

[ "oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor", "NADP binding", "NAD binding", "glucose metabolic process" ]

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

4

[ "NCBIFAM" ]

[ "TIGR01534" ]

[ "GAPDH-I" ]

[ 50345 ]

1

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

[ "1.2.1", "1.2.1.12", "GenProp0691", "GenProp1306", "GenProp1344", "GenProp1407", "GenProp1599", "GenProp1612", "GenProp1691", "GenProp1736", "PWY-1042", "PWY-5484", "PWY-6901", "PWY-7003", "PWY-8004", "PWY-8404", "R-BTA-70171", "R-BTA-70263", "R-CEL-70171", "R-CEL-70263", "R-...

[ "EC:1.2.1", "EC:1.2.1.12", "GP:GenProp0691", "GP:GenProp1306", "GP:GenProp1344", "GP:GenProp1407", "GP:GenProp1599", "GP:GenProp1612", "GP:GenProp1691", "GP:GenProp1736", "METACYC:PWY-1042", "METACYC:PWY-5484", "METACYC:PWY-6901", "METACYC:PWY-7003", "METACYC:PWY-8004", "METACYC:PWY-84...

43

[ "1a7k", "1cer", "1crw", "1dbv", "1dc3", "1dc4", "1dc5", "1dc6", "1dss", "1gad", "1gae", "1gd1", "1gpd", "1gyp", "1gyq", "1hdg", "1i32", "1i33", "1ihx", "1ihy", "1j0x", "1jn0", "1k3t", "1ml3", "1nbo", "1npt", "1nq5", "1nqa", "1nqo", "1obf", "1qxs", "1rm3"...

243

[ "PUB00002270", "PUB00009631", "PUB00009725", "PUB00009726" ]

[ "7751290", "10799476", "11200221", "9182530" ]

[ "Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis.", "Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium.", "Phylogenetic analyses a...

[ 1995, 2000, 2001, 1997 ]

4

[ "IPR020831" ]

[]

1

0

1

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

[ 291, 37170, 12367, 517 ]

4

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

[ 27, 4, 3, 4, 1, 5, 9, 1, 16, 16, 3, 2, 52 ]

13

true

Family

Glyceraldehyde-3-phosphate dehydrogenase, type I

Glyceraldehyde-3-P_DH_1

1

IPR006425

6,425

Glucoamylase, bacterial

Glucoamylase_bac

Family

396

false

Glucoamylase (GA), also known as glucan 1,4-alpha-glucosidase, which belongs to family 15 ( ) in the classification of glycosyl hydrolases. GA catalyses the release of D-glucose from the non-reducing ends of starch and other oligo- or poly-saccharides. Studies of fungal GA have indicated 3 closely-clustered acidic resi...

[]

0

[ "NCBIFAM" ]

[ "TIGR01535" ]

[ "glucan_glucosid" ]

[ 396 ]

1

[]

0

[ "1lf6", "1lf9", "1ug9", "1ulv" ]

4

[ "PUB00001422", "PUB00004952" ]

[ "1633799", "1970434" ]

[ "Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme.", "Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori." ]

[ 1992, 1990 ]

2

[ "IPR000165" ]

[]

1

0

1

[ "Bacteria", "Symbiodiniaceae" ]

[ 394, 2 ]

2

[]

0

true

Family

Glucoamylase, bacterial

Glucoamylase_bac

2

IPR006426

6,426

Asparagine synthase, glutamine-hydrolyzing

Asn_synth_AEB

Family

36,990

false

These sequences represent glutamine-hydrolysing asparagine synthase. The group have a poorly conserved C-terminal extension while bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus sub...

[ "GO:0004066", "GO:0070981" ]

[ "asparagine synthase (glutamine-hydrolyzing) activity", "L-asparagine biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF", "NCBIFAM" ]

[ "PIRSF001589", "TIGR01536" ]

[ "Asn_synthetase_glu-h", "asn_synth_AEB" ]

[ 36240, 32285 ]

2

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

[ "6.3.5.4", "GenProp0259", "GenProp0652", "GenProp1404", "R-BTA-8963693", "R-DDI-8963693", "R-HSA-380994", "R-HSA-8963693", "R-HSA-9633012", "R-HSA-9648895", "R-MMU-8963693", "R-RNO-8963693", "R-SCE-8963693", "R-SPO-8963693" ]

[ "EC:6.3.5.4", "GP:GenProp0259", "GP:GenProp0652", "GP:GenProp1404", "REACTOME:R-BTA-8963693", "REACTOME:R-DDI-8963693", "REACTOME:R-HSA-380994", "REACTOME:R-HSA-8963693", "REACTOME:R-HSA-9633012", "REACTOME:R-HSA-9648895", "REACTOME:R-MMU-8963693", "REACTOME:R-RNO-8963693", "REACTOME:R-SCE-8...

14

[ "1ct9", "6gq3", "7ylz", "8sue", "9b6c" ]

5

[ "PUB00015572" ]

[ "10498721" ]

[ "Three asparagine synthetase genes of Bacillus subtilis." ]

[ 1999 ]

1

[]

[ "IPR017535", "IPR017539" ]

0

2

0

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

[ 412, 29498, 6516, 58, 506 ]

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",...

[ 14, 2, 1, 1, 1, 3, 3, 1, 4, 4, 2, 1, 23 ]

13

true

Family

Asparagine synthase, glutamine-hydrolyzing

Asn_synth_AEB

9

IPR006427

6,427

Phage portal protein, HK97

Portal_HK97

Family

10,862

false

This entry represents one of several distantly related families of phage portal proteins. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of...

[]

0

[ "NCBIFAM" ]

[ "TIGR01537" ]

[ "portal_HK97" ]

[ 10862 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "6tba", "6te8", "6te9", "6to8", "6toa", "6tui", "8cez", "8fql", "9lbn" ]

9

[ "PUB00017711" ]

[ "7723020" ]

[ "Genetic basis of bacteriophage HK97 prohead assembly." ]

[ 1995 ]

1

[ "IPR006944" ]

[]

1

0

1

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

[ 9637, 21, 2, 1033, 169 ]

5

[]

0

true

Family

Phage portal protein, HK97

Portal_HK97

1

IPR006428

6,428

Portal protein, SPP1-type

Portal_SPP1-type

Family

1,790

false

The portal protein is a bacteriophage component that forms a hole, or portal, enabling DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins [ ]. This entry represents one particular subfamily of portal proteins consisting of the Bacillus phage SPP1 ...

[]

0

[ "NCBIFAM" ]

[ "TIGR01538" ]

[ "portal_SPP1" ]

[ 1790 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "2jes", "5a20", "5a21", "7z4w", "8v8b", "8vd8", "8vdc", "8vde" ]

8

[ "PUB00020097" ]

[ "11501993" ]

[ "Structural organisation of the head-to-tail interface of a bacterial virus." ]

[ 2001 ]

1

[ "IPR021145" ]

[]

1

0

1

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

[ 1460, 4, 322, 4 ]

4

[]

0

true

Family

Portal protein, SPP1-type

Portal_SPP1-type

6

IPR006429

6,429

Phage portal protein, lambda family

Phage_lambda_portal

Family

5,573

false

This entry represents one of several distantly related families of phage portal protein. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of ...

[ "GO:0005198", "GO:0019068" ]

[ "structural molecule activity", "virion assembly" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "PFAM", "NCBIFAM" ]

[ "MF_04135", "PF05136", "TIGR01539" ]

[ "PORTAL_LAMBDA", "Phage_portal_2", "portal_lambda" ]

[ 427, 5566, 4802 ]

3

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "8gtd", "8k38", "8k39", "8vhx", "8xot", "8xou", "8xow", "8xpm", "8xqb" ]

9

[]

0

[]

0

null

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

[ 5220, 35, 234, 84 ]

4

[]

0

true

Family

Phage portal protein, lambda family

Phage_lambda_portal

7

IPR006430

6,430

Phage portal protein PBSX family

Phage_portal_PBSX

Family

3,887

false

This entry represents one of several distantly related families of phage portal protein. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of ...

[]

0

[ "NCBIFAM" ]

[ "TIGR01540" ]

[ "portal_PBSX" ]

[ 3887 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[]

0

[]

0

[ "IPR006944" ]

[ "IPR016753", "IPR030935" ]

1

2

0

[ "Bacteria", "Methanothermobacter wolfeii", "Protostomia", "Viruses", "metagenomes" ]

[ 3718, 1, 5, 153, 10 ]

5

[]

0

true

Family

Phage portal protein PBSX family

Phage_portal_PBSX

4

IPR006431

6,431

Bacteriophage tail tape measure, C-terminal

Phage_tape_meas_C

Domain

5,010

false

This entry represents a domain found near the C terminus of bacteriophage tape measure proteins. Long-tailed bacteriophages possess a large gene encoding a tape measure protein (TMP) [ ]. TMP is important for assembly of phage tails and involved in tail length determination [ , ]. Mutated forms of TMP cause tail fibres...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09718", "TIGR01541" ]

[ "Tape_meas_lam_C", "tape_meas_lam_C" ]

[ 4908, 3748 ]

2

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "8iyk", "8iyl", "8k35", "9l9p" ]

4

[ "PUB00010241", "PUB00048232" ]

[ "11040123", "19251647" ]

[ "Mutational analysis of two structural genes of the temperate lactococcal bacteriophage TP901-1 involved in tail length determination and baseplate assembly.", "The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system." ]

[ 2000, 2009 ]

2

[]

0

null

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

[ 4463, 6, 510, 31 ]

4

[]

0

true

Domain

Bacteriophage tail tape measure, C-terminal

Phage_tape_meas_C

5

IPR006432

6,432

Phage portal protein, A118-type

Phage_portal_A118-type

Family

504

false

These entry represents a family of phage minor structural proteins. They are proposed to be portal proteins on the basis of their gene positions within the phage gene order, presence in mature phage, size, and conservation across a number of complete genomes of tailed phage that lack other candidate portal proteins [ ]...

[]

0

[ "PIRSF", "NCBIFAM" ]

[ "PIRSF011911", "TIGR01542" ]

[ "A118_put_portal", "A118_put_portal" ]

[ 470, 477 ]

2

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[]

0

[ "PUB00009633", "PUB00020097" ]

[ "10652093", "11501993" ]

[ "Complete nucleotide sequence, molecular analysis and genome structure of bacteriophage A118 of Listeria monocytogenes: implications for phage evolution.", "Structural organisation of the head-to-tail interface of a bacterial virus." ]

[ 2000, 2001 ]

2

[ "IPR021145" ]

[]

1

0

1

[ "Bacteria", "Viruses" ]

[ 444, 60 ]

2

[]

0

true

Family

Phage portal protein, A118-type

Phage_portal_A118-type

7

IPR006433

6,433

Prohead protease

Prohead_protease

Family

7,098

false

This entry represents the prohead protease from bacteriophage HK97 and related phages [ ]. It is generally encoded next to the gene for the capsid protein that it processes, and in some cases may be fused to it. It is also found in a number of bacteria, possibly as the result of horizontal transfer.

[]

0

[ "NCBIFAM" ]

[ "TIGR01543" ]

[ "proheadase_HK97" ]

[ 7098 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[]

0

[ "PUB00017711" ]

[ "7723020" ]

[ "Genetic basis of bacteriophage HK97 prohead assembly." ]

[ 1995 ]

1

[]

0

null

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

[ 6175, 10, 1, 805, 107 ]

5

[]

0

true

Family

Prohead protease

Prohead_protease

7

IPR006434

6,434

Pyrimidine 5'-nucleotidase, eukaryotic

Pyrimidine_nucleotidase_eu

Family

4,956

false

This family is a small group of metazoan sequences with sequences from Arabidopsis thaliana (Mouse-ear cress) and rice. The sequences represent pyrimidine 5-nucleotidases, apparently in reference to HSPC233, the Homo sapiens (Human) homologue [ ]. The structure of mouse sequence has been reported [ ]. This group of seq...

[ "GO:0000287", "GO:0008253", "GO:0005737" ]

[ "magnesium ion binding", "5'-nucleotidase activity", "cytoplasm" ]

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

3

[ "PFAM", "SFLD", "NCBIFAM", "CDD" ]

[ "PF05822", "SFLDG01128", "TIGR01544", "cd07504" ]

[ "UMPH-1", "C1.4:_5'-Nucleotidase_Like", "HAD-SF-IE", "HAD_5NT" ]

[ 4954, 3752, 3124, 2220 ]

4

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

[ "3.1.3.5", "3.1.3.91", "PWY-5381", "PWY-5695", "PWY-6596", "PWY-6606", "PWY-6607", "PWY-6608", "PWY-7185", "PWY-7821", "R-CEL-429958", "R-CEL-73621", "R-DME-429958", "R-DME-73621", "R-DRE-73621", "R-GGA-429958", "R-GGA-73621", "R-HSA-429958", "R-HSA-73621", "R-MMU-429958", "R...

[ "EC:3.1.3.5", "EC:3.1.3.91", "METACYC:PWY-5381", "METACYC:PWY-5695", "METACYC:PWY-6596", "METACYC:PWY-6606", "METACYC:PWY-6607", "METACYC:PWY-6608", "METACYC:PWY-7185", "METACYC:PWY-7821", "REACTOME:R-CEL-429958", "REACTOME:R-CEL-73621", "REACTOME:R-DME-429958", "REACTOME:R-DME-73621", "...

22

[ "2bdu", "2cn1", "2g06", "2g07", "2g08", "2g09", "2g0a", "2jga", "2q4t", "2vkq", "4fe3", "4kx3", "4kx5", "4nv0", "4nwi", "7zee", "7zeg", "7zeh" ]

18

[ "PUB00003337", "PUB00039616", "PUB00055591" ]

[ "7966317", "16672222", "10942414" ]

[ "Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.", "Structure of pyrimidine 5'-nucleotidase type 1. Insight into mechanism of action and inhibition during lead poisoning.", "Human e...

[ 1994, 2006, 2000 ]

3

[]

0

null

[ "Bacteria", "Candidatus Iainarchaeum sp.", "Eukaryota", "bioreactor metagenome" ]

[ 41, 1, 4913, 1 ]

4

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

[ 4, 4, 2, 1, 8, 4, 5, 6, 10 ]

9

true

Family

Pyrimidine 5'-nucleotidase, eukaryotic

Pyrimidine_nucleotidase_eu

5

IPR006435

6,435

HAD-superfamily hydrolase, subfamily IF, YfhB

HAD-SF_hydro_IF_YfhB

Family

1,088

false

This entry represents of sequences limited to the gamma proteobacteria, including Phosphatidylglycerophosphatase C (PgpC, previously known as YfhB) from Escherichia coli [ ]. This group is a member of the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases and all of the conserved catalytic motifs...

[]

0

[ "NCBIFAM" ]

[ "TIGR01545" ]

[ "YfhB_g-proteo" ]

[ 1088 ]

1

[ "GP", "GP" ]

[ "GenProp1252", "GenProp1627" ]

[ "GP:GenProp1252", "GP:GenProp1627" ]

2

[]

0

[ "PUB00003337", "PUB00106620" ]

[ "7966317", "21148555" ]

[ "Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.", "Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli." ]

[ 1994, 2011 ]

2

[]

0

null

[ "Pseudomonadota", "bioreactor metagenome" ]

[ 1087, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

HAD-superfamily hydrolase, subfamily IF, YfhB

HAD-SF_hydro_IF_YfhB

1

IPR006436

6,436

Glyceraldehyde-3-phosphate dehydrogenase, type II

Glyceraldehyde-3-P_DH_2_arc

Family

1,272

false

This family describes the type II glyceraldehyde-3-phosphate dehydrogenases. These enzymes catalyse the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. In archaea, either NAD or NADP may be utilised as the cofactor.

[ "GO:0016620", "GO:0050661", "GO:0051287", "GO:0006096", "GO:0005737" ]

[ "oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor", "NADP binding", "NAD binding", "glycolytic process", "cytoplasm" ]

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

5

[ "HAMAP", "NCBIFAM" ]

[ "MF_00559", "TIGR01546" ]

[ "G3P_dehdrog_arch", "GAPDH-II_archae" ]

[ 1262, 1272 ]

2

[ "EC", "GP" ]

[ "1.2.1.59", "GenProp0691" ]

[ "EC:1.2.1.59", "GP:GenProp0691" ]

2

[ "1b7g", "1cf2", "2czc", "2yyy" ]

4

[]

0

[ "IPR020831" ]

[]

1

0

1

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

[ 808, 439, 1, 24 ]

4

[]

0

true

Family

Glyceraldehyde-3-phosphate dehydrogenase, type II

Glyceraldehyde-3-P_DH_2_arc

6

IPR006437

6,437

Bacteriophage terminase, large subunit

Phage_terminase_lsu

Family

5,148

false

This group of sequences represent a highly divergent family of the large subunit of phage terminase. All members are encoded by phage genomes or within prophage regions of bacterial genomes. This is a distinct family from the phage terminase family represented by . Initiation of packaging of double-stranded viral DNA i...

[]

0

[ "NCBIFAM" ]

[ "TIGR01547" ]

[ "phage_term_2" ]

[ 5148 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "4idh", "4iee", "4iei", "4ife", "5c10", "5c12", "5c15", "5c2d", "5c2f", "5oe8", "5oe9", "5oea", "5oeb", "5oee" ]

14

[ "PUB00008493", "PUB00008494", "PUB00085647" ]

[ "10930407", "1548711", "12697751" ]

[ "Functional analysis of the terminase large subunit, G2P, of Bacillus subtilis bacteriophage SPP1.", "Molecular analysis of the Bacillus subtilis bacteriophage SPP1 region encompassing genes 1 to 6. The products of gene 1 and gene 2 are required for pac cleavage.", "Bacillus subtilis bacteriophage SPP1 DNA pack...

[ 2000, 1992, 2003 ]

3

[]

[ "IPR044269" ]

0

1

0

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

[ 4185, 9, 8, 880, 66 ]

5

[]

0

true

Family

Bacteriophage terminase, large subunit

Phage_terminase_lsu

9

IPR006438

6,438

HAD hydrolase, TIGR01548 family

HAD-SF_TIGR01548

Family

717

false

This entry represents a small and phylogenetically curious clade of sequences. Sequences are found from Halobacterium (an archaeon), Nostoc and Synechococcus (cyanobacteria) and Phytophthora (a stramenophile eukaryote). These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile h...

[]

0

[ "NCBIFAM" ]

[ "TIGR01548" ]

[ "HAD-SF-IA-hyp1" ]

[ 717 ]

1

[]

0

[]

0

[ "PUB00003337" ]

[ "7966317" ]

[ "Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search." ]

[ 1994 ]

1

[]

0

null

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

[ 280, 106, 330, 1 ]

4

[]

0

true

Family

HAD hydrolase, TIGR01548 family

HAD-SF_TIGR01548

7

IPR006439

6,439

HAD hydrolase, subfamily IA

HAD-SF_hydro_IA

Family

218,513

false

The Haloacid Dehalogenase (HAD) superfamily is defined by the presence of three short catalytic motifs [ ]. The subfamilies are defined [ ] based on the location and the observed or predicted fold of a so-called capping domain [ ], or the absence of such a domain. Subfamily I consists of sequences in which the capping ...

[]

0

[ "PRINTS", "NCBIFAM", "NCBIFAM", "NCBIFAM" ]

[ "PR00413", "TIGR01493", "TIGR01509", "TIGR01549" ]

[ "HADHALOGNASE", "HAD-SF-IA-v2", "HAD-SF-IA-v3", "HAD-SF-IA-v1" ]

[ 94703, 13880, 147003, 105588 ]

4

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

[ "3.1.3", "GenProp1469", "GenProp1734", "GenProp1737", "R-BTA-1237112", "R-CEL-1237112", "R-DME-1237112", "R-DME-73614", "R-DRE-1237112", "R-DRE-71737", "R-HSA-1237112", "R-HSA-2142670", "R-HSA-4085001", "R-HSA-73614", "R-HSA-77289", "R-HSA-9018682", "R-HSA-9033241", "R-MMU-1237112"...

[ "EC:3.1.3", "GP:GenProp1469", "GP:GenProp1734", "GP:GenProp1737", "REACTOME:R-BTA-1237112", "REACTOME:R-CEL-1237112", "REACTOME:R-DME-1237112", "REACTOME:R-DME-73614", "REACTOME:R-DRE-1237112", "REACTOME:R-DRE-71737", "REACTOME:R-HSA-1237112", "REACTOME:R-HSA-2142670", "REACTOME:R-HSA-408500...

36

[ "1aq6", "1cqz", "1cr6", "1ek1", "1ek2", "1fez", "1jud", "1lvh", "1o03", "1o08", "1qh9", "1qq5", "1qq6", "1qq7", "1rdf", "1rql", "1rqn", "1s8o", "1swv", "1sww", "1te2", "1vj5", "1x42", "1yns", "1z4n", "1z4o", "1zd2", "1zd3", "1zd4", "1zd5", "1zol", "1zrm"...

336

[ "PUB00003337", "PUB00009540", "PUB00009589" ]

[ "7966317", "10956028", "11601995" ]

[ "Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.", "The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and ca...

[ 1994, 2000, 2001 ]

3

[]

[ "IPR006323", "IPR006328", "IPR006351", "IPR010237", "IPR010972", "IPR011949", "IPR011950", "IPR011951", "IPR023733", "IPR037512", "IPR044266", "IPR044999", "IPR045228", "IPR051540" ]

0

14

0

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

[ 4497, 174806, 36889, 26, 2295 ]

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",...

[ 94, 9, 8, 24, 10, 15, 9, 7, 67, 25, 9, 5, 128 ]

13

true

Family

HAD hydrolase, subfamily IA

HAD-SF_hydro_IA

4

IPR006440

6,440

Death on curing protein

Doc

Family

7,974

false

This entry represents death-on-curing (Doc) proteins mostly from bacteria and archaea. Bacterial toxin-antitoxin (TA) system (or "addiction module") composed of closely linked genes encoding a stable toxin that can harm the host cell and its cognate labile antitoxin, which protects the host from the toxin's deleterious...

[ "GO:0016301" ]

[ "kinase activity" ]

[ "molecular_function" ]

1

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

[ "PIRSF018297", "PTHR39426", "TIGR01550" ]

[ "Doc", "", "DOC_P1" ]

[ 3312, 7497, 7215 ]

3

[ "GP" ]

[ "GenProp0321" ]

[ "GP:GenProp0321" ]

1

[ "3dd7", "3dd9", "3k33", "3kh2" ]

4

[ "PUB00009637", "PUB00051349", "PUB00074261", "PUB00074262", "PUB00074263" ]

[ "8411153", "18757857", "19325885", "24141193", "24448800" ]

[ "Plasmid addiction genes of bacteriophage P1: doc, which causes cell death on curing of prophage, and phd, which prevents host death when prophage is retained.", "Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation.", "Bacterial toxin-antitoxin systems: more than selfish en...

[ 1993, 2008, 2009, 2013, 2014 ]

5

[]

0

null

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

[ 283, 7264, 11, 299, 117 ]

5

[]

0

true

Family

Death on curing protein

Doc

9

IPR006441

6,441

Bacteriophage P2, capsid

Phage_P2_GpN

Family

3,965

false

This entry represents Capsid proteins from Bacteriophage P2 (GpN) and similar proteins from tailed bacteriophages and bacterial prophages mainly among Proteobacteria. GpN undergoes proteolytic cleavage into three products: Minor capsid protein H1, a 39 kDa protein Minor capsid protein H2, 38.6 kDa Major capsid protein ...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF05125", "TIGR01551" ]

[ "Phage_cap_P2", "major_capsid_P2" ]

[ 3965, 3391 ]

2

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "7jw1", "7oz4" ]

2

[ "PUB00100003", "PUB00100004", "PUB00100005" ]

[ "22508104", "32867300", "8874520" ]

[ "Structure and size determination of bacteriophage P2 and P4 procapsids: function of size responsiveness mutations.", "Structure of the Capsid Size-Determining Scaffold of \"Satellite\" Bacteriophage P4.", "The N-terminal part of bacteriophage P2 capsid protein is essential for postassembly maturation of P2 and...

[ 2012, 2020, 1996 ]

3

[]

0

null

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

[ 3784, 5, 167, 9 ]

4

[]

0

true

Family

Bacteriophage P2, capsid

Phage_P2_GpN

2

IPR006443

6,443

Formate dehydrogenase-N, alpha subunit

Formate-DH-alph_fdnG

Family

5,433

false

This family of sequences describe a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex aeolicus. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase. The holo-enzyme also contains beta and gamma subunits of 32 and 20kDa. T...

[ "GO:0008863", "GO:0009055", "GO:0043546", "GO:0047111", "GO:0045333" ]

[ "formate dehydrogenase (NAD+) activity", "electron transfer activity", "molybdopterin cofactor binding", "formate dehydrogenase (cytochrome-c-553) activity", "cellular respiration" ]

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

5

[ "NCBIFAM" ]

[ "TIGR01553" ]

[ "formate-DH-alph" ]

[ 5433 ]

1

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

[ "1.17.1.9", "GenProp1135", "GenProp1329", "GenProp1535", "PWY-1881", "PWY-5497", "PWY-6696", "PWY-7985" ]

[ "EC:1.17.1.9", "GP:GenProp1135", "GP:GenProp1329", "GP:GenProp1535", "METACYC:PWY-1881", "METACYC:PWY-5497", "METACYC:PWY-6696", "METACYC:PWY-7985" ]

8

[ "1h0h", "1kqf", "1kqg", "6sdr", "6sdv", "7z5o", "8bqg", "8bqh", "8bqi", "8bqj", "8bqk", "8bql", "8cm4", "8cm5", "8cm6", "8cm7", "8rc8", "8rc9", "8rca", "8rcb", "8rcc", "8rcg", "9qm0", "9qm1" ]

24

[ "PUB00009638", "PUB00009639" ]

[ "3045516", "1834669" ]

[ "Nitrate respiration in relation to facultative metabolism in enterobacteria.", "Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine." ]

[ 1988, 1991 ]

2

[]

0

null

[ "Bacteria", "Conexivisphaera calida", "Eukaryota", "metagenomes" ]

[ 5406, 1, 5, 21 ]

4

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Formate dehydrogenase-N, alpha subunit

Formate-DH-alph_fdnG

8

IPR006445

6,445

Phage-associated protein HI1409

Phage-assoc_HI1409

Family

1,080

false

This family of uncharacterised proteins is found in prophage regions of a number of bacterial genomes, including Haemophilus influenzae, Xylella fastidiosa, Salmonella typhi, and Enterococcus faecalis. This family includes sequences mainly from proteobacteria and firmicutes, such as Abc1, a protein that counteracts or ...

[]

0

[ "NCBIFAM" ]

[ "TIGR01555" ]

[ "phge_rel_HI1409" ]

[ 1080 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "8hds" ]

1

[ "PUB00101341" ]

[ "35395152" ]

[ "Phage anti-CBASS and anti-Pycsar nucleases subvert bacterial immunity." ]

[ 2022 ]

1

[]

0

null

[ "Bacteria", "Caudoviricetes", "Linnemannia", "metagenomes" ]

[ 1000, 69, 4, 7 ]

4

[]

0

true

Family

Phage-associated protein HI1409

Phage-assoc_HI1409

7

IPR006446

6,446

Rhamnosyltransferase

RhaTrfase

Family

594

false

This subfamily is composed of sequences from the gammaproteobacteria that function as L-rhamnosyltransferases in the synthesis of their respective surface polysaccharides. Rhamnolipids are glycolipids containing mono- or di- L-rhamnose molecules. Rhamnolipid synthesis occurs by sequential glycosyltransferase reactions ...

[]

0

[ "NCBIFAM" ]

[ "TIGR01556" ]

[ "rhamnosyltran" ]

[ 594 ]

1

[ "CAZY" ]

[ "GT2" ]

[ "CAZY:GT2" ]

1

[]

0

[ "PUB00009640" ]

[ "11359576" ]

[ "Cloning and functional characterization of the Pseudomonas aeruginosa rhlC gene that encodes rhamnosyltransferase 2, an enzyme responsible for di-rhamnolipid biosynthesis." ]

[ 2001 ]

1

[]

0

null

[ "Bacteria", "Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)", "ecological metagenomes" ]

[ 588, 1, 5 ]

3

[]

0

true

Family

Rhamnosyltransferase

RhaTrfase

3

IPR006447

6,447

Myb domain, plants

Myb_dom_plants

Domain

52,888

false

This DNA-binding domain is restricted to (but common in) plant proteins, many of which also contain a response regulator domain. The domain appears related to the Myb-like DNA-binding domain [ , ].

[ "GO:0003677" ]

[ "DNA binding" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR01557" ]

[ "myb_SHAQKYF" ]

[ 52888 ]

1

[ "REACTOME" ]

[ "R-DDI-5689901" ]

[ "REACTOME:R-DDI-5689901" ]

1

[ "1irz", "5lxu", "6j4k", "6j4r", "6j5b", "6nvz", "6qec", "7d3t", "7d3y", "7e40", "8xas", "8xat", "9h6e" ]

13

[ "PUB00009641", "PUB00009642" ]

[ "10652136", "7957104" ]

[ "The tomato I-box binding factor LeMYBI is a member of a novel class of myb-like proteins.", "A novel DNA binding protein with homology to Myb oncoproteins containing only one repeat can function as a transcriptional activator." ]

[ 1999, 1994 ]

2

[ "IPR017930" ]

[]

1

0

1

[ "Eukaryota", "Viruses" ]

[ 52886, 2 ]

2

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

[ 386, 243, 474 ]

3

true

Domain

Myb domain, plants

Myb_dom_plants

6

IPR006449

6,449

Squalene synthase-like

Squal_synth-like

Family

4,567

false

This family of sequences describe farnesyl-diphosphate farnesyltransferase, also known as squalene synthase, as found in eukaryotes. This family is related to phytoene synthases. Tentatively identified archaeal homologues lack the C-terminal predicted transmembrane region universally conserved among members of this fam...

[ "GO:0051996", "GO:0008610" ]

[ "squalene synthase [NAD(P)H] activity", "lipid biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01559" ]

[ "squal_synth" ]

[ 4567 ]

1

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

[ "2.5.1.21", "GenProp1530", "GenProp1594", "GenProp1683", "R-DDI-191273", "R-HSA-191273", "R-HSA-1989781", "R-HSA-2426168", "R-MMU-191273", "R-RNO-191273", "R-SCE-191273", "R-SPO-191273" ]

[ "EC:2.5.1.21", "GP:GenProp1530", "GP:GenProp1594", "GP:GenProp1683", "REACTOME:R-DDI-191273", "REACTOME:R-HSA-191273", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-2426168", "REACTOME:R-MMU-191273", "REACTOME:R-RNO-191273", "REACTOME:R-SCE-191273", "REACTOME:R-SPO-191273" ]

12

[ "1ezf", "3asx", "3lee", "3q2z", "3q30", "3v66", "3vj8", "3vj9", "3vja", "3vjb", "3vjc", "3wc9", "3wca", "3wcb", "3wcc", "3wcd", "3wce", "3wcf", "3wcg", "3wch", "3wci", "3wcj", "3wcl", "3wcm", "3wef", "3weg", "3weh", "3wei", "3wej", "3wek", "3wsa", "3wsb"...

36

[ "PUB00017047", "PUB00086654" ]

[ "10896663", "21746901" ]

[ "Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis.", "Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii." ]

[ 2000, 2011 ]

2

[ "IPR044844" ]

[]

1

0

1

[ "Crocinitomicaceae", "Eukaryota", "hydrothermal vent metagenome" ]

[ 4, 4562, 1 ]

3

[ "Arabidopsis thaliana", "Danio rerio", "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 (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (st...

[ 10, 2, 10, 4, 2, 5, 3, 1, 1, 20 ]

10

true

Family

Squalene synthase-like

Squal_synth-like

9

IPR006450

6,450

Phage HK97 gp6-like

Phage_HK97_gp6-like

Family

6,987

false

This group of sequences represents small (~100 amino acids) hypothetical proteins found in phage (such as gp6 from phage HK97) and in putative prophage regions of a number of bacterial genomes. Gp6 from HK97 is a protein the crystallizes into an oligomeric ring, consistent with its role as a phage head-tail connector p...

[]

0

[ "NCBIFAM" ]

[ "TIGR01560" ]

[ "put_DNA_pack" ]

[ 6987 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "3jvo" ]

1

[]

0

[ "IPR021146" ]

[]

1

0

1

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

[ 6366, 12, 1, 526, 82 ]

5

[]

0

true

Family

Phage HK97 gp6-like

Phage_HK97_gp6-like

6

IPR006451

6,451

Glycogen debranching enzyme, archaeal type

Glycogen_debranch_arc

Family

1,102

false

These sequences are largely uncharacterised archaeal proteins which include those from Methanosarcina acetivorans and Sulfolobus solfataricus. The group also contains sequences from the Gram-positive bacterium Clostridium perfringens and from cyanobacterial species. All the sequences display weak relatedness to the cha...

[]

0

[ "NCBIFAM" ]

[ "TIGR01561" ]

[ "gde_arch" ]

[ 1102 ]

1

[ "GP" ]

[ "GenProp0168" ]

[ "GP:GenProp0168" ]

1

[]

0

[]

0

[ "IPR010401" ]

[]

1

0

1

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

[ 161, 934, 1, 6 ]

4

[]

0

true

Family

Glycogen debranching enzyme, archaeal type

Glycogen_debranch_arc

1

IPR006452

6,452

Formate dehydrogenase accessory protein

Formate_DH_accessory

Family

4,046

false

This entry contains formate dehydrogenase accessory protein FdhE and its homologues, found largely in proteobacteria, where the fdhE genes are almost always genetically-linked to the structural genes for formate dehydrogenases [ ]. FdhE is required for the assembly of formate dehydrogenase although not present in the f...

[ "GO:0005737" ]

[ "cytoplasm" ]

[ "cellular_component" ]

1

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

[ "MF_00611", "PIRSF018296", "PTHR37689", "TIGR01562", "cd16341" ]

[ "FdeH", "Format_dh_formtn", "", "FdhE", "FdhE" ]

[ 2974, 3244, 4044, 3271, 3871 ]

5

[]

0

[ "2fiy" ]

1

[ "PUB00009643", "PUB00013624", "PUB00104131", "PUB00106621" ]

[ "2170340", "8522521", "9274019", "18716757" ]

[ "Identification and expression of the Escherichia coli fdhD and fdhE genes, which are involved in the formation of respiratory formate dehydrogenase.", "Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase.", "Suppression of Escher...

[ 1990, 1995, 1997, 2008 ]

4

[]

0

null

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

[ 3976, 7, 24, 39 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Formate dehydrogenase accessory protein

Formate_DH_accessory

5

IPR006454

6,454

S-layer protein

S_layer_MJ

Family

234

false

These sequences represent one of several families of proteins associated with the formation of prokaryotic S-layers. Members of this family are found in archaeal species, including Pyrococcus horikoshii (split into two tandem reading frames), Methanocaldococcus jannaschii (Methanococcus jannaschii), and related species...

[ "GO:0005618" ]

[ "cell wall" ]

[ "cellular_component" ]

1

[ "NCBIFAM" ]

[ "TIGR01564" ]

[ "S_layer_MJ" ]

[ 234 ]

1

[]

0

[ "9fsa" ]

1

[]

0

[]

0

null

[ "Archaea", "Mobilitalea sibirica", "ecological metagenomes" ]

[ 230, 1, 3 ]

3

[]

0

true

Family

S-layer protein

S_layer_MJ

2

IPR006456

6,456

ZF-HD homeobox protein, Cys/His-rich dimerisation domain

ZF_HD_homeobox_Cys/His_dimer

Domain

7,845

false

The homeodomain (HD) is a 60-amino acid DNA-binding domain found in many transcription factors. HD-containing proteins are found in diverse organisms such as humans, Drosophila, nematode worms, and plants, where they play important roles in development. Zinc-finger-homeodomain (ZF- HD) subfamily proteins have only been...

[]

0

[ "PFAM", "PROFILE", "NCBIFAM" ]

[ "PF04770", "PS51523", "TIGR01566" ]

[ "ZF-HD_dimer", "ZF_HD_DIMER", "ZF_HD_prot_N" ]

[ 7828, 7758, 7410 ]

3

[]

0

[]

0

[ "PUB00008620", "PUB00055518", "PUB00055519" ]

[ "11289511", "16428600", "17485478" ]

[ "Characterization of a novel class of plant homeodomain proteins that bind to the C4 phosphoenolpyruvate carboxylase gene of Flaveria trinervia.", "The Arabidopsis zinc finger-homeodomain genes encode proteins with unique biochemical properties that are coordinately expressed during floral development.", "Patho...

[ 2001, 2006, 2007 ]

3

[]

0

null

[ "Eukaryota", "Reyranella humidisoli" ]

[ 7844, 1 ]

2

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

[ 54, 29, 75 ]

3

true

Domain

ZF-HD homeobox protein, Cys/His-rich dimerisation domain

ZF_HD_homeobox_Cys/His_dimer

3

IPR006457

6,457

S-layer family duplication domain

S_layer-rel_Mac

Domain

654

false

This entry represents a domain found tandemly duplicated in two proven archaeal S-layer glycoproteins, MA0829 from Methanosarcina acetivorans C2A and MM1976 from Methanosarcina mazei Go1 [ ], as well as in several paralogues of those L-layer proteins from both species. Members of the family show regions of local simila...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF07752", "TIGR01567" ]

[ "S-layer", "S_layer_rel_Mac" ]

[ 654, 477 ]

2

[]

0

[ "3u2g", "3u2h" ]

2

[ "PUB00060425" ]

[ "19228054" ]

[ "S-layer, surface-accessible, and concanavalin A binding proteins of Methanosarcina acetivorans and Methanosarcina mazei." ]

[ 2009 ]

1

[]

0

null

[ "Methanomicrobia", "unclassified sequences" ]

[ 645, 9 ]

2

[]

0

true

Domain

S-layer family duplication domain

S_layer-rel_Mac

4

IPR006458

6,458

Ovate protein family, C-terminal

Ovate_C

Domain

10,995

false

This domain in found towards the C terminus in the Oval family of transcriptional repressors. These proteins are important regulators of growth and development in plants [ , , ].

[]

0

[ "PFAM", "PROFILE", "NCBIFAM" ]

[ "PF04844", "PS51754", "TIGR01568" ]

[ "Ovate", "OVATE", "A_thal_3678" ]

[ 10381, 10899, 9995 ]

3

[]

0

[]

0

[ "PUB00057482", "PUB00057483", "PUB00057484" ]

[ "12242331", "17461792", "21886836" ]

[ "A new class of regulatory genes underlying the cause of pear-shaped tomato fruit.", "Arabidopsis Ovate Family Protein 1 is a transcriptional repressor that suppresses cell elongation.", "Arabidopsis ovate family proteins, a novel transcriptional repressor family, control multiple aspects of plant growth and de...

[ 2002, 2007, 2011 ]

3

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 2, 10993 ]

2

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

[ 72, 89, 112 ]

3

true

Domain

Ovate protein family, C-terminal

Ovate_C

7

IPR006459

6,459

Casparian strip membrane protein

CASP/CASPL

Family

10,106

false

This family consists of CASP and CASP-like proteins. In vascular plants Casparian strips span the cell wall of adjacent endodermal cells to form a tight junction that blocks extracellular diffusion [ ]. Casparian Strip Membrane Domain Proteins (CASPs) are four-membrane-span proteins that recruit the lignin polymerisati...

[]

0

[ "NCBIFAM" ]

[ "TIGR01569" ]

[ "A_tha_TIGR01569" ]

[ 10106 ]

1

[]

0

[]

0

[ "PUB00072979", "PUB00072980" ]

[ "24920445", "23940370" ]

[ "Functional and evolutionary analysis of the CASPARIAN STRIP MEMBRANE DOMAIN PROTEIN family.", "Dirigent domain-containing protein is part of the machinery required for formation of the lignin-based Casparian strip in the root." ]

[ 2014, 2013 ]

2

[]

[ "IPR044173" ]

0

1

0

[ "Embryophyta" ]

[ 10106 ]

1

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

[ 77, 32, 65 ]

3

true

Family

Casparian strip membrane protein

CASP/CASPL

1

IPR006460

6,460

Protein MIZU-KUSSEI 1-like, plant

MIZ1-like_pln

Family

5,482

false

This entry includes Arabidopsis MIZU-KUSSEI 1 (MIZ1), which is an essential protein for hydrotropism in roots. It can be regulated by light signal and ABA signalling [ , ].

[ "GO:0010274" ]

[ "hydrotropism" ]

[ "biological_process" ]

1

[ "PFAM", "PANTHER", "NCBIFAM" ]

[ "PF04759", "PTHR31696", "TIGR01570" ]

[ "DUF617", "", "A_thal_3588" ]

[ 5480, 4195, 5086 ]

3

[]

0

[]

0

[ "PUB00083346", "PUB00083347" ]

[ "22321255", "23012350" ]

[ "Light and abscisic acid signalling are integrated by MIZ1 gene expression and regulate hydrotropic response in roots of Arabidopsis thaliana.", "Overexpression of MIZU-KUSSEI1 enhances the root hydrotropic response by retaining cell viability under hydrostimulated conditions in Arabidopsis thaliana." ]

[ 2012, 2012 ]

2

[]

0

null

[ "Eukaryota" ]

[ 5482 ]

1

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

[ 49, 42, 42 ]

3

true

Family

Protein MIZU-KUSSEI 1-like, plant

MIZ1-like_pln

3

IPR006461

6,461

PLAC8 motif-containing protein

PLAC_motif_containing

Family

20,503

false

This entry represents a group of cys-rich proteins, including cornifelin and PLAC8 from animals, MCA (MID1-COMPLEMENTING ACTIVITY) and PCR (PLANT CADMIUM RESISTANCE) from Arabidopsis and cell number regulators from maize [ , ]. Cornifelin is part of the insoluble cornified cell envelope (CE) of stratified squamous epit...

[]

0

[ "PFAM", "PANTHER", "NCBIFAM" ]

[ "PF04749", "PTHR15907", "TIGR01571" ]

[ "PLAC8", "", "A_thal_Cys_rich" ]

[ 20088, 16669, 19376 ]

3

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

[ "R-BTA-6798695", "R-HSA-6798695", "R-HSA-9830364", "R-MMU-6798695" ]

[ "REACTOME:R-BTA-6798695", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-9830364", "REACTOME:R-MMU-6798695" ]

4

[]

0

[ "PUB00074698", "PUB00074699", "PUB00074700", "PUB00074702", "PUB00074703", "PUB00074704", "PUB00074705", "PUB00074706", "PUB00074707" ]

[ "15147942", "20097794", "20647347", "25377654", "24475319", "20400678", "23155406", "21949028", "21347707" ]

[ "Identification and characterization of a novel component of the cornified envelope, cornifelin.", "MCA1 and MCA2 that mediate Ca2+ uptake have distinct and overlapping roles in Arabidopsis.", "Arabidopsis PCR2 is a zinc exporter involved in both zinc extrusion and long-distance zinc transport.", "Identificat...

[ 2004, 2010, 2010, 2014, 2014, 2010, 2012, 2011, 2011 ]

9

[]

0

null

[ "Cyvirus", "Eukaryota", "viral metagenome" ]

[ 3, 20494, 6 ]

3

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

[ 74, 29, 6, 4, 1, 77, 9, 68 ]

8

true

Family

PLAC8 motif-containing protein

PLAC_motif_containing

4

IPR006462

6,462

Protein MS5

MS5

Family

2,774

false

These sequences comprise a paralogous family of proteins predominantly found in Brassicaceae. Length heterogeneity within the family is attributable partly to a 21-residue repeat present in from zero to three tandem copies. One member of the family, protein MS5, has been shown to be important for progression of meiosis...

[]

0

[ "PFAM", "PANTHER", "NCBIFAM" ]

[ "PF04776", "PTHR31260", "TIGR01572" ]

[ "protein_MS5", "", "A_thl_para_3677" ]

[ 1549, 2415, 1052 ]

3

[]

0

[ "6l77" ]

1

[ "PUB00080256", "PUB00106857" ]

[ "27194707", "32415887" ]

[ "MS5 mediates early meiotic progression and its natural variants may have applications for hybrid production in Brassica napus.", "Structural analysis of the meiosis-related protein MS5 reveals non-canonical papain enhancement by cystatin-like folds." ]

[ 2016, 2020 ]

2

[]

0

null

[ "Mesangiospermae" ]

[ 2774 ]

1

[ "Arabidopsis thaliana" ]

[ 124 ]

1

true

Family

Protein MS5

MS5

1

IPR006463

6,463

tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase MiaB

MiaB_methiolase

Family

24,755

false

This entry represents the MiaB enzyme and homologues that are responsible for the modification of the isopentenylated adenine-37 base of most bacterial and eukaryotic tRNAs that read codons beginning with uracil (all except tRNA(I,V) Ser). Adenine-37 is next to the anticodon on the 3' side in these tRNA's, and lack of ...

[ "GO:0016740", "GO:0051539", "GO:0006400" ]

[ "transferase activity", "4 iron, 4 sulfur cluster binding", "tRNA modification" ]

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

3

[ "HAMAP", "SFLD" ]

[ "MF_01864", "SFLDF00273" ]

[ "tRNA_metthiotr_MiaB", "(dimethylallyl)adenosine_tRNA_" ]

[ 23232, 23955 ]

2

[ "EC" ]

[ "2.8.4.3" ]

[ "EC:2.8.4.3" ]

1

[ "7mjv", "7mjw", "7mjx", "7mjy", "7mjz" ]

5

[ "PUB00009727", "PUB00009728", "PUB00009729", "PUB00017717", "PUB00083446", "PUB00083447", "PUB00083448" ]

[ "10572129", "11882645", "11313137", "12766153", "15339930", "17407324", "23991893" ]

[ "Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli.", "Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein.", "TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine...

[ 1999, 2002, 2001, 2003, 2004, 2007, 2013 ]

7

[ "IPR005839" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Podoviridae sp. ctIpM11", "environmental samples", "unclassified sequences" ]

[ 22105, 2255, 1, 2, 392 ]

5

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

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

10

true

Family

tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase MiaB

MiaB_methiolase

3

IPR006464

6,464

N-acetyltransferase RimI/Ard1

AcTrfase_RimI/Ard1

Family

19,424

false

Members of this entry belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This entry covers prokaryotes and the archaea. It contains RimI, which catalyses the acetylation of the N-terminal alanine of ribosomal protein bS18 [ ] and Ard1, an N-terminal protein acetyltransferase from Sulfolobus that has rel...

[ "GO:0008080", "GO:0006474" ]

[ "N-acetyltransferase activity", "N-terminal protein amino acid acetylation" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01575" ]

[ "rimI" ]

[ 19424 ]

1

[ "EC" ]

[ "2.3.1" ]

[ "EC:2.3.1" ]

1

[ "2cnm", "2cns", "2cnt", "2x7b", "4lx9", "4pv6", "4r3k", "4r3l", "5c88", "5isv", "6ag5", "9mto" ]

12

[ "PUB00014765", "PUB00085016" ]

[ "2828880", "17511810" ]

[ "Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12.", "An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus." ]

[ 1987, 2007 ]

2

[]

[ "IPR043690" ]

0

1

0

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

[ 905, 18032, 73, 414 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

N-acetyltransferase RimI/Ard1

AcTrfase_RimI/Ard1

3

IPR006465

6,465

Oligosaccharide amylase

Oligosac_amylase

Family

34

false

The name of this type of amylase is based on the characterisation of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterised glucoamylases, this T. vulga...

[]

0

[ "NCBIFAM" ]

[ "TIGR01577" ]

[ "oligosac_amyl" ]

[ 34 ]

1

[]

0

[]

0

[ "PUB00009730" ]

[ "11549021" ]

[ "Novel glucoamylase-type enzymes from Thermoactinomyces vulgaris and Methanococcus jannaschii whose genes are found in the flanking region of the alpha-amylase genes." ]

[ 2001 ]

1

[ "IPR000165" ]

[]

1

0

1

[ "Methanobacteriota", "Thermoactinomyces vulgaris" ]

[ 33, 1 ]

2

[]

0

true

Family

Oligosaccharide amylase

Oligosac_amylase

2

IPR006466

6,466

MiaB-like tRNA modifying enzyme, archaea/eukaryota

MiaB-like_arc_euk

Family

3,451

false

This clade of sequences is closely related to MiaB, a modifier of isopentenylated adenosine-37 of certain eukaryotic and bacterial tRNAs (see ). Sequence alignments suggest that this family of sequences perform the same chemical transformation as MiaB, perhaps on a different (or differently modified) tRNA base substrat...

[ "GO:0035598", "GO:0035600" ]

[ "tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase activity", "tRNA methylthiolation" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01578" ]

[ "MiaB-like-B" ]

[ 3451 ]

1

[ "EC", "REACTOME" ]

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

[ "EC:2.8.4.5", "REACTOME:R-HSA-6782315" ]

2

[]

0

[ "PUB00009727", "PUB00009728", "PUB00009729" ]

[ "10572129", "11882645", "11313137" ]

[ "Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli.", "Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein.", "TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine...

[ 1999, 2002, 2001 ]

3

[ "IPR005839" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Megaviridae environmental sample", "ecological metagenomes" ]

[ 871, 8, 2558, 1, 13 ]

5

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

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

9

true

Family

MiaB-like tRNA modifying enzyme, archaea/eukaryota

MiaB-like_arc_euk

5

IPR006467

6,467

MiaB-like tRNA modifying enzyme, bacteria

MiaB-like_bact

Family

10,172

false

This entry represents a group of bacterial tRNA modifying enzymes, including tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase from Natranaerobius thermophilus (MiaB) and Threonylcarbamoyladenosine tRNA methylthiotransferase MtaB from Bacillus subtilis. Members of this family are closely related to MiaB, a modifie...

[ "GO:0016740" ]

[ "transferase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR01579" ]

[ "MiaB-like-C" ]

[ 10172 ]

1

[ "EC" ]

[ "2.8.4.5" ]

[ "EC:2.8.4.5" ]

1

[]

0

[ "PUB00009728", "PUB00009729", "PUB00009731" ]

[ "11882645", "11313137", "572129" ]

[ "Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein.", "TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes.", "Corneal endothelial cell density in iridocyclitis." ]

[ 2002, 2001, 1979 ]

3

[ "IPR005839" ]

[ "IPR034557" ]

1

0

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

[ 10020, 16, 136 ]

3

[]

0

true

Family

MiaB-like tRNA modifying enzyme, bacteria

MiaB-like_bact

2

IPR006468

6,468

Nitrate reductase alpha subunit

NarG

Family

8,432

false

The nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex is a heterotrimer consisting of alpha, beta and gamma subunits [ ]. The alpha subunit contains a molybdenum cofactor, the beta subunit contains [Fe-S] clusters while the gamma subunit ...

[ "GO:0008940", "GO:0042126", "GO:0009325" ]

[ "nitrate reductase activity", "nitrate metabolic process", "nitrate reductase complex" ]

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

3

[ "NCBIFAM" ]

[ "TIGR01580" ]

[ "narG" ]

[ 8432 ]

1

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

[ "1.7.5.1", "GenProp0636", "GenProp1122", "GenProp1329", "GenProp1474", "GenProp1583", "GenProp1676", "PWY-6748" ]

[ "EC:1.7.5.1", "GP:GenProp0636", "GP:GenProp1122", "GP:GenProp1329", "GP:GenProp1474", "GP:GenProp1583", "GP:GenProp1676", "METACYC:PWY-6748" ]

8

[ "1q16", "1r27", "1siw", "1y4z", "1y5i", "1y5l", "1y5n", "3egw", "3ir5", "3ir6", "3ir7" ]

11

[ "PUB00017048", "PUB00017049" ]

[ "11289300", "12910261" ]

[ "The coordination and function of the redox centres of the membrane-bound nitrate reductases.", "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A." ]

[ 2001, 2003 ]

2

[]

0

null

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

[ 26, 8331, 2, 73 ]

4

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Nitrate reductase alpha subunit

NarG

7

IPR006469

6,469

NifC-like ABC-type porter

NifC_ABC_porter

Family

4,469

false

This entry represents a clade of ABC porter genes with relatively weak homology compared to its neighbour clades, the molybdate and sulphate porters. Neighbour-Joining, PAM-distance phylogenetic trees support the separation of these clades in this way. Included in this group are the NifC genes of Clostridium pasteurian...

[ "GO:0022857", "GO:0055085", "GO:0016020" ]

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

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

3

[ "NCBIFAM" ]

[ "TIGR01581" ]

[ "Mo_ABC_porter" ]

[ 4469 ]

1

[]

0

[]

0

[ "PUB00004290", "PUB00009732", "PUB00014769", "PUB00017894", "PUB00017895", "PUB00017896", "PUB00017897", "PUB00017898", "PUB00017899", "PUB00025109", "PUB00026406", "PUB00043654" ]

[ "9872322", "2194453", "9873074", "11421269", "1282354", "9640644", "11988180", "11470432", "11402022", "11080142", "11532960", "11421270" ]

[ "Crystal structure of the ATP-binding subunit of an ABC transporter.", "A nitrogen-fixation gene (nifC) in Clostridium pasteurianum with sequence similarity to chlJ of Escherichia coli.", "Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transpo...

[ 1998, 1990, 1999, 2001, 1992, 1998, 2002, 2001, 2001, 2000, 2001, 2001 ]

12

[]

0

null

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

[ 4091, 300, 4, 74 ]

4

[]

0

true

Family

NifC-like ABC-type porter

NifC_ABC_porter

3

IPR006471

6,471

Formate dehydrogenase, gamma subunit

Formate_DH_gsu

Family

6,183

false

These sequences represent the gamma chain of the gammaproteobacteria (and Aquifex aeolicus) formate dehydrogenase. This subunit is integral to the cytoplasmic membrane, consisting of 4 transmembrane helices, and receives electrons from the beta subunit. The entire Escherichia coli formate dehydrogenase N (nitrate-induc...

[ "GO:0008863", "GO:0045333", "GO:0009326", "GO:0016020" ]

[ "formate dehydrogenase (NAD+) activity", "cellular respiration", "formate dehydrogenase complex", "membrane" ]

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

4

[ "NCBIFAM" ]

[ "TIGR01583" ]

[ "formate-DH-gamm" ]

[ 6183 ]

1

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

[ "GenProp1135", "GenProp1329", "GenProp1535" ]

[ "GP:GenProp1135", "GP:GenProp1329", "GP:GenProp1535" ]

3

[ "1kqf", "1kqg" ]

2

[ "PUB00009871" ]

[ "11884747" ]

[ "Molecular basis of proton motive force generation: structure of formate dehydrogenase-N." ]

[ 2002 ]

1

[]

0

null

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

[ 6143, 4, 36 ]

3

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Formate dehydrogenase, gamma subunit

Formate_DH_gsu

7

IPR006472

6,472

Citrate lyase, alpha subunit

Citrate_lyase_asu

Family

3,826

false

These sequences, from both Gram-positive and Gram-negative bacteria, represent the alpha subunit of the holoenzyme citrate lyase composed of alpha ( ), beta, and acyl carrier protein subunits in a stoichiometric relationship of 6:6:6. Citrate lyase is an enzyme which converts citrate to oxaloacetate. In bacteria, this ...

[ "GO:0008814", "GO:0006084", "GO:0005737", "GO:0009346" ]

[ "citrate CoA-transferase activity", "acetyl-CoA metabolic process", "cytoplasm", "ATP-independent citrate lyase complex" ]

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

4

[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM" ]

[ "PF04223", "PIRSF009451", "PTHR40596", "TIGR01584" ]

[ "CitF", "Citrt_lyas_alpha", "", "citF" ]

[ 3825, 3466, 3820, 3513 ]

4

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

[ "2.8.3.10", "4.1.3.6", "GenProp0672", "PWY-6038" ]

[ "EC:2.8.3.10", "EC:4.1.3.6", "GP:GenProp0672", "METACYC:PWY-6038" ]

4

[ "1xr4", "2hj0" ]

2

[ "PUB00009735", "PUB00014613" ]

[ "1115558", "7830578" ]

[ "Citrate lyase from Streptococcus diacetilactis. Association with its acetylating enzyme.", "Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: localization, sequencing, and expression." ]

[ 1975, 1994 ]

2

[]

0

null

[ "Aciduliprofundum boonei (strain DSM 19572 / T469)", "Bacteria", "Eukaryota", "metagenomes" ]

[ 1, 3753, 17, 55 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Citrate lyase, alpha subunit

Citrate_lyase_asu

7

IPR006473

6,473

Peptidase C58, YopT-type domain

Peptidase_C58_Yopt

Domain

1,030

false

This group of sequences are characterised by a cysteine protease domain, corresponding to MEROPS peptidase family C58 (clan CA), found in proteins of bacteria that include plant pathogens (Pseudomonas syringae), root nodule bacteria, and intracellular pathogens (e.g. Yersinia pestis, Haemophilus ducreyi, Pasteurella mu...

[ "GO:0004197" ]

[ "cysteine-type endopeptidase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "NCBIFAM" ]

[ "PF03543", "TIGR01586" ]

[ "Peptidase_C58", "yopT_cys_prot" ]

[ 886, 534 ]

2

[ "EC" ]

[ "3.4.22.-" ]

[ "EC:3.4.22.-" ]

1

[ "1ukf", "6ii0", "6ii2", "6ii6", "6u8t", "8sfg", "9euv", "9euw", "9qb8", "9qbb", "9qhh" ]

11

[ "PUB00009736" ]

[ "12062101" ]

[ "A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis." ]

[ 2002 ]

1

[]

0

null

[ "Bacteria", "viral metagenome" ]

[ 1029, 1 ]

2

[]

0

true

Domain

Peptidase C58, YopT-type domain

Peptidase_C58_Yopt

6

IPR006474

6,474

Helicase Cas3, CRISPR-associated, core

Helicase_Cas3_CRISPR-ass_core

Domain

7,667

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 entry represents a highly conserved core region found in the Cas3 family of proteins. These proteins are found in association with CRISPR repea...

[]

0

[ "NCBIFAM" ]

[ "TIGR01587" ]

[ "cas3_core" ]

[ 7667 ]

1

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

[ "3.6.4.-", "GenProp0021", "GenProp0313", "GenProp0315", "GenProp0317", "GenProp0319", "GenProp0320", "GenProp0768", "GenProp0922", "PWY-7250" ]

[ "EC:3.6.4.-", "GP:GenProp0021", "GP:GenProp0313", "GP:GenProp0315", "GP:GenProp0317", "GP:GenProp0319", "GP:GenProp0320", "GP:GenProp0768", "GP:GenProp0922", "METACYC:PWY-7250" ]

10

[ "4q2c", "4q2d", "4qqw", "4qqx", "4qqy", "4qqz", "6c66", "7r2k", "7tr8", "7tr9", "7tra", "8g9u", "8wtk", "8wtl", "8zns" ]

15

[ "PUB00009737", "PUB00043286", "PUB00043287", "PUB00043288", "PUB00060621", "PUB00071890" ]

[ "11952905", "17442114", "17379808", "16545108", "21699496", "24459147" ]

[ "Identification of genes that are associated with DNA repeats in prokaryotes.", "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: computati...

[ 2002, 2007, 2007, 2006, 2011, 2014 ]

6

[]

0

null

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

[ 441, 7157, 5, 64 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Helicase Cas3, CRISPR-associated, core

Helicase_Cas3_CRISPR-ass_core

6

IPR006475

6,475

Citrate lyase, beta subunit, bacteria

Citrate_lyase_beta_bac

Family

2,053

false

This group of sequences represent the beta subunit of the holoenzyme citrate lyase ( ) composed of alpha ( ), beta, and acyl carrier protein subunits in a stoichiometric relationship of 6:6:6. Citrate lyase is an enzyme which converts citrate to oxaloacetate. In bacteria, this reaction is involved in citrate fermentati...

[ "GO:0008816", "GO:0006084", "GO:0005737", "GO:0009346" ]

[ "citryl-CoA lyase activity", "acetyl-CoA metabolic process", "cytoplasm", "ATP-independent citrate lyase complex" ]

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

4

[ "NCBIFAM" ]

[ "TIGR01588" ]

[ "citE" ]

[ 2053 ]

1

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

[ "4.1.3.34", "4.1.3.6", "GenProp0672", "PWY-5392", "PWY-6038" ]

[ "EC:4.1.3.34", "EC:4.1.3.6", "GP:GenProp0672", "METACYC:PWY-5392", "METACYC:PWY-6038" ]

5

[]

0

[ "PUB00005807" ]

[ "9457870" ]

[ "Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster." ]

[ 1998 ]

1

[ "IPR011206" ]

[]

1

0

1

[ "Bacteria", "Spodoptera exigua", "bioreactor metagenome" ]

[ 2048, 1, 4 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Citrate lyase, beta subunit, bacteria

Citrate_lyase_beta_bac

9

IPR006476

6,476

Conserved hypothetical protein CHP01589, plant

CHP01589_pln

Family

4,949

false

This plant-specific family of proteins are defined by an uncharacterised region 57 residues in length. It is found toward the N terminus of most proteins that contain it. Examples include at least several proteins from Arabidopsis thaliana (Mouse-ear cress) and Oryza sativa (Rice). The function of the proteins are unkn...

[]

0

[ "PFAM", "PANTHER", "NCBIFAM" ]

[ "PF09713", "PTHR31871", "TIGR01589" ]

[ "A_thal_3526", "", "A_thal_3526" ]

[ 4870, 4692, 4668 ]

3

[]

0

[]

0

[]

0

[]

0

null

[ "Eukaryota" ]

[ 4949 ]

1

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

[ 79, 21, 62 ]

3

true

Family

Conserved hypothetical protein CHP01589, plant

CHP01589_pln

5

IPR006477

6,477

Variant antigen yir/bir/cir

Yir_bir_cir

Family

6,899

false

This group of sequences identifies a large paralogous family of variant antigens from several Plasmodium species (Plasmodium yoelii, Plasmodium berghei and Plasmodium chabaudi). It is not believed that there are any orthologs of this family in Plasmodium falciparum.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF06022", "TIGR01590" ]

[ "Cir_Bir_Yir", "yir-bir-cir_Pla" ]

[ 6899, 5306 ]

2

[]

0

[ "6zyv" ]

1

[]

0

[]

0

null

[ "Eukaryota" ]

[ 6899 ]

1

[]

0

true

Family

Variant antigen yir/bir/cir

Yir_bir_cir

3

IPR006478

6,478

Formate dehydrogenase, alpha subunit

Formate_DH_asu

Family

10,811

false

This group of sequences describe a subset of formate dehydrogenase alpha chains found mainly in the archaea but also in alpha and gamma proteobacteria and a small number of Gram-positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase. The holo-enzyme a...

[ "GO:0008863", "GO:0015942" ]

[ "formate dehydrogenase (NAD+) activity", "formate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR01591" ]

[ "Fdh-alpha" ]

[ 10811 ]

1

[ "GP", "GP" ]

[ "GenProp1267", "GenProp1496" ]

[ "GP:GenProp1267", "GP:GenProp1496" ]

2

[ "1aa6", "1fdi", "1fdo", "2iv2", "6tg9", "6tga", "7bkb", "7bkc", "7bkd", "7bke", "7e5z", "7qv7", "7vw6", "7xqw", "7z0t", "8j83", "8rqz", "8rr0", "9gzq", "9ktl", "9ktr" ]

21

[ "PUB00009738", "PUB00009739" ]

[ "3531194", "9036855" ]

[ "Cloning, expression, and nucleotide sequence of the formate dehydrogenase genes from Methanobacterium formicicum.", "Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster." ]

[ 1986, 1997 ]

2

[]

0

null

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

[ 852, 9617, 8, 334 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Formate dehydrogenase, alpha subunit

Formate_DH_asu

8

IPR006480

6,480

Bacteriophage holin family

Phage_holin_4_1

Family

5,125

false

Phage holins and lytic enzymes are both necessary for bacterial lysis and virus dissemination. This family also includes TcdE/UtxA involved in toxin secretion in Clostridium difficile [ ]. The 1.E.10 family is represented by Bacillus subtilis phi29 holin [ , ]; 1.E.16 represents the Cph1 holin[ ]; and the 1.E.19 family...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF05105", "TIGR01593" ]

[ "Phage_holin_4_1", "holin_tox_secr" ]

[ 5123, 4149 ]

2

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[]

0

[ "PUB00009740", "PUB00075698", "PUB00075699", "PUB00075700" ]

[ "11444771", "8432697", "22436471", "9440507" ]

[ "Evidence for holin function of tcdE gene in the pathogenicity of Clostridium difficile.", "The missing link in phage lysis of gram-positive bacteria: gene 14 of Bacillus subtilis phage phi 29 encodes the functional homolog of lambda S protein.", "Characterization and determination of holin protein of Streptoco...

[ 2001, 1993, 2012, 1998 ]

4

[]

0

null

[ "Bacteria", "Methanolapillus millepedarum", "Phytophthora kernoviae 00238/432", "Viruses", "metagenomes" ]

[ 4604, 1, 2, 477, 41 ]

5

[]

0

true

Family

Bacteriophage holin family

Phage_holin_4_1

7

IPR006481

6,481

Bacteriophage lambda, GpS, holin

Phage_lambda_GpS_holin

Family

2,702

false

This protein family represent one of a large number of mutually dissimilar families of phage holins. Holins act against the host cell membrane to allow lytic enzymes of the phage to reach the bacterial cell wall. This family includes the product of the S gene of phage lambda.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF05106", "TIGR01594" ]

[ "Phage_holin_3_1", "holin_lambda" ]

[ 2702, 2312 ]

2

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobrevibacter smithii DSM 2374", "Viruses", "metagenomes" ]

[ 2590, 7, 1, 101, 3 ]

5

[]

0

true

Family

Bacteriophage lambda, GpS, holin

Phage_lambda_GpS_holin

7

IPR006482

6,482

CRISPR-associated protein Cas7, subtype I-B/I-C

Cas7_Csh2/Csh2

Family

3,349

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 entry represents Cas7 from the I-B (Csh2) and I-C (Csd2) subtypes. The Cascade I-B complex requires Cas5, Cas6, and Cas7 for maintaining a stab...

[ "GO:0043571" ]

[ "maintenance of CRISPR repeat elements" ]

[ "biological_process" ]

1

[ "PFAM", "NCBIFAM" ]

[ "PF05107", "TIGR01595" ]

[ "Cas_Cas7", "cas_CT1132" ]

[ 3349, 2784 ]

2

[]

0

[ "7kha", "7xz3", "8dej", "8dex", "8dfa", "8dfo", "8dfs", "8g9s", "8g9t", "8g9u", "8gaf", "8gam", "8gan" ]

13

[ "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

[]

[ "IPR013418", "IPR013419" ]

0

2

0

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

[ 240, 3053, 2, 54 ]

4

[]

0

true

Family

CRISPR-associated protein Cas7, subtype I-B/I-C

Cas7_Csh2/Csh2

2

IPR006483

6,483

CRISPR-associated Cas3-type, HD domain

CRISPR-assoc_Cas3_HD

Domain

10,128

false

This entry represents the HD domain, which is found in a number of Cas proteins that tend to be found near CRISPR repeats. These domains can be found either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein. CRISPR loci appear to be mobile elements with a wide host range....

[]

0

[ "PFAM", "PROFILE", "NCBIFAM" ]

[ "PF18019", "PS51643", "TIGR01596" ]

[ "Cas3_HD", "HD_CAS3", "cas3_HD" ]

[ 6048, 9922, 8254 ]

3

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

[ "3.6.4.-", "GenProp0021", "GenProp0317", "GenProp0319", "PWY-7250" ]

[ "EC:3.6.4.-", "GP:GenProp0021", "GP:GenProp0317", "GP:GenProp0319", "METACYC:PWY-7250" ]

5

[ "3s4l", "3sk9", "3skd", "4q2c", "4q2d", "4qqw", "4qqx", "4qqy", "4qqz", "5b7i", "5gqh", "6c66", "7r2k", "7tr8", "7tr9", "7tra", "8flj", "8g9u", "8k22", "8k23", "8k24", "8wth", "8zns", "9p11", "9p1d" ]

25

[ "PUB00043286", "PUB00043287", "PUB00043288", "PUB00060516", "PUB00060517", "PUB00060621", "PUB00071890" ]

[ "17442114", "17379808", "16545108", "21343909", "22009198", "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, 2011, 2011, 2014 ]

7

[]

0

null

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

[ 523, 9513, 2, 7, 83 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

CRISPR-associated Cas3-type, HD domain

CRISPR-assoc_Cas3_HD

9

IPR006484

6,484

Plasmodium yoelii subtelomeric PYST-B

PYST_B

Family

840

false

The sequences in this group represent a paralogous family of Plasmodium yoelii genes preferentially located in the subtelomeric regions of the chromosomes [ ]. There are no obvious homologues to these genes in any other organism.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09592", "TIGR01597" ]

[ "DUF2031", "PYST-B" ]

[ 840, 662 ]

2

[]

0

[]

0

[ "PUB00044233" ]

[ "12368865" ]

[ "Genome sequence and comparative analysis of the model rodent malaria parasite Plasmodium yoelii yoelii." ]

[ 2002 ]

1

[]

0

null

[ "Oceanimonas smirnovii", "Plasmodium (Vinckeia)" ]

[ 1, 839 ]

2

[]

0

true

Family

Plasmodium yoelii subtelomeric PYST-B

PYST_B

2

IPR006485

6,485

Bacteriophage-like holin

Phage-like_holin

Family

1,721

false

This family of holins is found in tailed bacteriophages, antinobacteria and firmicutes. Phage proteins for bacterial lysis typically include a membrane-disrupting protein, or holin, and one or more cell wall degrading enzymes that reach the cell wall because of holin action. Holins are found in a large number of mutual...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF04531", "TIGR01598" ]

[ "Phage_holin_1", "holin_phiLC3" ]

[ 1721, 1285 ]

2

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[]

0

[ "PUB00010120", "PUB00105459" ]

[ "11459934", "25157079" ]

[ "Holins kill without warning.", "Holins in bacteria, eukaryotes, and archaea: multifunctional xenologues with potential biotechnological and biomedical applications." ]

[ 2001, 2015 ]

2

[]

0

null

[ "Bacteria", "Halobaculum halobium", "Viruses", "metagenomes" ]

[ 1293, 1, 424, 3 ]

4

[]

0

true

Family

Bacteriophage-like holin

Phage-like_holin

8

IPR006486

6,486

Plasmodium yoelii subtelomeric PYST-A

PYST_A

Family

2,302

false

A single high-scoring gene was identified in the complete genome of P. falciparum as well as a single gene from Plasmodium chabaudi. There are no obvious homologues to these genes in any non-Plasmodium organism. These observations suggest an expansion of this family in Plasmodium yoelii from a common Plasmodium ancesto...

[]

0

[ "NCBIFAM" ]

[ "TIGR01599" ]

[ "PYST-A" ]

[ 2302 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Plasmodium" ]

[ 2302 ]

1

[]

0

true

Family

Plasmodium yoelii subtelomeric PYST-A

PYST_A

7

IPR006487

6,487

Bacteriophage lambda, Tail tip protein L

Phage_lambda_L

Family

3,875

false

This entry represents Tail tip protein (L) from Bacteriophage lambda and similar proteins found in tailed bacteriophages (Caudovirales) and prophages mostly from Proteobacteria. L is part of the distal tail tip complex which plays a role in DNA ejection during entry, and in tail assembly initiation during exit. The tai...

[ "GO:0051536", "GO:0046718", "GO:0030430" ]

[ "iron-sulfur cluster binding", "symbiont entry into host cell", "host cell cytoplasm" ]

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

3

[ "PFAM", "NCBIFAM" ]

[ "PF05100", "TIGR01600" ]

[ "Phage_tail_L", "phage_tail_L" ]

[ 3875, 3704 ]

2

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "8iyk", "8iyl", "8k35", "8xcg", "9e7m", "9l9p" ]

6

[ "PUB00075672", "PUB00077057" ]

[ "23542343", "1003470" ]

[ "Tail tip proteins related to bacteriophage λ gpL coordinate an iron-sulfur cluster.", "Morphogenesis of bacteriophage lambda tail. Polymorphism in the assembly of the major tail protein." ]

[ 2013, 1976 ]

2

[]

0

null

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

[ 3412, 10, 432, 21 ]

4

[]

0

true

Family

Bacteriophage lambda, Tail tip protein L

Phage_lambda_L

3

IPR006488

6,488

PYST-C1-like, N-terminal

PYST-C1_N

Domain

438

false

This entry represents the N-terminal domain of a paralogous family of Plasmodium yoelii proteins that are preferentially encoded in the subtelomeric regions of the chromosomes. There are no obvious homologues to these proteins in other organisms. The C-terminal portions of the proteins are divergent and some contain ot...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09690", "TIGR01601" ]

[ "PYST-C1", "PYST-C1" ]

[ 399, 415 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Plasmodium (Vinckeia)" ]

[ 438 ]

1

[]

0

true

Domain

PYST-C1-like, N-terminal

PYST-C1_N

7

IPR006490

6,490

Phage major tail protein, phi13 family

Maj_tail_phi13

Family

2,856

false

This is a set of proteins that share low levels of sequence similarity but similar lengths and similar patterns of charged, hydrophobic, and Gly/Pro residues. Most members belong to phage of Gram-positive bacteria. Several are identified as phage major tail proteins.

[]

0

[ "NCBIFAM" ]

[ "TIGR01603" ]

[ "maj_tail_phi13" ]

[ 2856 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[]

0

[]

0

[]

[ "IPR006724" ]

0

1

0

[ "Bacteria", "Ecdysozoa", "Halobaculum halobium", "Viruses", "metagenomes" ]

[ 2395, 4, 1, 440, 16 ]

5

[]

0

true

Family

Phage major tail protein, phi13 family

Maj_tail_phi13

7

IPR006491

6,491

Plasmodium yoelii subtelomeric PYST-C2

PYST_C2

Domain

93

false

These sequences represent a domain found in a paralogous gene family of Plasmodium yoelii preferentially located in the subtelomeric regions of the chromosomes. There are no obvious homologues to these genes in any other organism. The proteins often contain an N-terminal yoelii-specific domain such as PYST-C1 ( ).

[]

0

[ "NCBIFAM" ]

[ "TIGR01604" ]

[ "PYST-C2" ]

[ 93 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Plasmodium (Vinckeia)" ]

[ 93 ]

1

[]

0

true

Domain

Plasmodium yoelii subtelomeric PYST-C2

PYST_C2

1