interpro_id
string
interpro_numeric_id
int64
name
string
short_name
string
entry_type
string
protein_count
int64
is_llm
bool
is_llm_reviewed
bool
abstract
string
go_ids
list
go_terms
list
go_categories
list
go_count
int64
member_databases
list
member_accessions
list
member_names
list
member_protein_counts
list
member_count
int64
external_databases
list
external_accessions
list
external_xrefs
list
external_xref_count
int64
pdb_ids
list
structure_count
int64
publication_ids
list
pubmed_ids
list
publication_titles
list
publication_years
list
publication_count
int64
parent_ids
list
child_ids
list
parent_count
int64
child_count
int64
tree_depth
float64
taxonomy_names
list
taxonomy_protein_counts
list
taxonomy_count
int64
key_species_names
list
key_species_protein_counts
list
key_species_count
int64
in_entry_list
bool
entry_list_type
string
entry_list_name
string
names_dat_name
string
short_names_dat_name
string
split_bucket
int64
IPR012812
12,812
Mannosyl-3-phosphoglycerate synthase
Osmo_MPG_synth
Family
348
false
false
This family consists of examples of mannosyl-3-phosphoglycerate synthase (MPGS), which together with mannosyl-3-phosphoglycerate phosphatase (MPGP), comprises a two-step pathway for mannosylglycerate biosynthesis. Mannosylglycerate is a compatible solute that tends to be restricted to extreme thermophiles of archaea an...
[ "GO:0050504", "GO:0051479", "GO:0005737" ]
[ "mannosyl-3-phosphoglycerate synthase activity", "mannosylglycerate biosynthetic process", "cytoplasm" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "NCBIFAM" ]
[ "PF09488", "TIGR02460" ]
[ "Osmo_MPGsynth", "osmo_MPGsynth" ]
[ 348, 178 ]
2
[ "EC", "GP", "METACYC" ]
[ "2.4.1.217", "GenProp0281", "PWY-5656" ]
[ "EC:2.4.1.217", "GP:GenProp0281", "METACYC:PWY-5656" ]
3
[ "2wvk", "2wvl", "2wvm", "2zu7", "2zu8", "2zu9" ]
6
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "ecological metagenomes", "leotiomyceta" ]
[ 75, 91, 13, 169 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Family
Mannosyl-3-phosphoglycerate synthase
Mannosyl-3-phosphoglycerate synthase
Osmo_MPG_synth
9
IPR012814
12,814
Pyranose 2-oxidase
P2OX
Family
253
false
false
Fungal pyranose 2-oxidase (P2OX) catalyses the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O2 to H2O2. Peroxide production is believed to be important to the wood rot fungi in which this enzyme is found for lignin degradation [ , ...
[ "GO:0050233", "GO:0050660" ]
[ "pyranose oxidase activity", "flavin adenine dinucleotide binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "NCBIFAM" ]
[ "TIGR02462" ]
[ "pyranose_ox" ]
[ 253 ]
1
[ "EC" ]
[ "1.1.3.10" ]
[ "EC:1.1.3.10" ]
1
[ "1tt0", "1tzl", "2f5v", "2f6c", "2igk", "2igm", "2ign", "2igo", "3bg6", "3bg7", "3bly", "3fdy", "3k4b", "3k4c", "3k4j", "3k4k", "3k4l", "3k4m", "3k4n", "3lsh", "3lsi", "3lsk", "3lsm", "3pl8", "4mif", "4mig", "4mih", "4moe", "4mof", "4mog", "4moh", "4moi"...
41
[ "PUB00077038", "PUB00077039" ]
[ "16349330", "8661938" ]
[ "Pyranose Oxidase, a Major Source of H(2)O(2) during Wood Degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida.", "Only C-2 specific glucose oxidase activity is expressed in ligninolytic cultures of the white rot fungus Phanerochaete chrysosporium." ]
[ 1994, 1996 ]
2
[ "IPR051473" ]
[]
1
0
1
[ "Bacteria", "Opisthokonta" ]
[ 20, 233 ]
2
[]
[]
0
true
Family
Pyranose 2-oxidase
Pyranose 2-oxidase
P2OX
8
IPR012815
12,815
Mannosyl-3-phosphoglycerate phosphatase
MPG_Pase
Family
446
false
false
Members of this family are mannosyl-3-phosphoglycerate phosphatase ( ). It acts sequentially after mannosyl-3-phosphoglycerate synthase ( ) in a two-step pathway of biosynthesis of the compatible solute mannosylglycerate, a typical osmolyte of thermophiles [ ].
[ "GO:0050531", "GO:0051479", "GO:0005737" ]
[ "mannosyl-3-phosphoglycerate phosphatase activity", "mannosylglycerate biosynthetic process", "cytoplasm" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP" ]
[ "MF_00617" ]
[ "MPGP_rel" ]
[ 446 ]
1
[ "EC", "METACYC" ]
[ "3.1.3.70", "PWY-5656" ]
[ "EC:3.1.3.70", "METACYC:PWY-5656" ]
2
[ "1wzc", "1xvi", "2zos" ]
3
[ "PUB00017808" ]
[ "11562374" ]
[ "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes." ]
[ 2001 ]
1
[ "IPR006381" ]
[]
1
0
1
[ "Archaea", "Enterobacteriaceae" ]
[ 14, 432 ]
2
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Mannosyl-3-phosphoglycerate phosphatase
Mannosyl-3-phosphoglycerate phosphatase
MPG_Pase
2
IPR012817
12,817
Chlorocatechol 1,2-dioxygenase
Chlorcchol_dOase
Family
107
false
false
Members of this protein family are chlorocatechol 1,2-dioxygenases. This enzyme is a homodimeric intradiol dioxygenase that degrade chlorocatechols via the addition of molecular oxygen and the subsequent cleavage between two adjacent hydroxyl groups. This reaction is part of the modified ortho-cleavage pathway which is...
[ "GO:0005506" ]
[ "iron ion binding" ]
[ "molecular_function" ]
1
[ "NCBIFAM", "CDD" ]
[ "TIGR02465", "cd03462" ]
[ "chlorocat_1_2", "1_2-CCD" ]
[ 85, 104 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...
[ "1.13.11.-", "PWY-181", "PWY-5163", "PWY-5642", "PWY-6068", "PWY-6069", "PWY-6084", "PWY-6087", "PWY-6089", "PWY-6093", "PWY-6094", "PWY-6102", "PWY-6107", "PWY-6178", "PWY-6190", "PWY-6193", "PWY-6336", "PWY-6339", "PWY-6667", "PWY-7006", "PWY-7009", "PWY-7010", "PWY-701...
[ "EC:1.13.11.-", "METACYC:PWY-181", "METACYC:PWY-5163", "METACYC:PWY-5642", "METACYC:PWY-6068", "METACYC:PWY-6069", "METACYC:PWY-6084", "METACYC:PWY-6087", "METACYC:PWY-6089", "METACYC:PWY-6093", "METACYC:PWY-6094", "METACYC:PWY-6102", "METACYC:PWY-6107", "METACYC:PWY-6178", "METACYC:PWY-...
38
[ "1s9a", "2boy", "3hgi", "3hhx", "3hhy", "3hj8", "3hjq", "3hjs", "3hkp", "3i4v", "3i4y", "3i51", "3o32", "3o5u", "3o6j", "3o6r", "3th1" ]
17
[ "PUB00015256", "PUB00080933" ]
[ "10730195", "16030237" ]
[ "Catechol dioxygenases.", "Amino acids in positions 48, 52, and 73 differentiate the substrate specificities of the highly homologous chlorocatechol 1,2-dioxygenases CbnA and TcbC." ]
[ 1999, 2005 ]
2
[]
[]
0
0
null
[ "Bacteria" ]
[ 107 ]
1
[]
[]
0
true
Family
Chlorocatechol 1,2-dioxygenase
Chlorocatechol 1,2-dioxygenase
Chlorcchol_dOase
6
IPR012818
12,818
Precorrin-6Y methyltransferase
CbiE
Domain
12,283
false
false
Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants...
[ "GO:0008276", "GO:0009236" ]
[ "protein methyltransferase activity", "cobalamin biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "NCBIFAM", "CDD" ]
[ "TIGR02467", "cd11644" ]
[ "CbiE", "Precorrin-6Y-MT" ]
[ 11955, 12234 ]
2
[ "EC", "GP" ]
[ "2.1.1", "GenProp0275" ]
[ "EC:2.1.1", "GP:GenProp0275" ]
2
[ "2bb3" ]
1
[ "PUB00009744", "PUB00014672", "PUB00014680", "PUB00014681", "PUB00015657", "PUB00035308", "PUB00035309", "PUB00035310", "PUB00070131" ]
[ "11215515", "11153269", "12429089", "1732195", "12869542", "17163662", "16042605", "12055304", "23922391" ]
[ "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Multiple biosynthetic pathways for vitamin B12: variations on a central theme.", "The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.", "Biosynthesis of vitamin B12 in Pseudomonas...
[ 2000, 2001, 2002, 1992, 2003, 2006, 2005, 2002, 2013 ]
9
[ "IPR000878" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 610, 11570, 11, 92 ]
4
[]
[]
0
true
Domain
Precorrin-6Y methyltransferase
Precorrin-6Y methyltransferase
CbiE
7
IPR012820
12,820
Sucrose synthase, plant/cyanobacteria
Sucrose_synthase_pln/cyn
Family
5,641
false
false
This entry represents sucrose synthase an enzyme that despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which ca...
[ "GO:0016157", "GO:0005985" ]
[ "sucrose synthase activity", "sucrose metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER", "NCBIFAM" ]
[ "PTHR45839", "TIGR02470" ]
[ "", "sucr_synth" ]
[ 5640, 4092 ]
2
[ "EC", "GP", "METACYC" ]
[ "2.4.1.13", "GenProp1639", "PWY-3801" ]
[ "EC:2.4.1.13", "GP:GenProp1639", "METACYC:PWY-3801" ]
3
[ "3s27", "3s28", "3s29", "4rbn" ]
4
[ "PUB00017811" ]
[ "11950997" ]
[ "Evolution of sucrose synthesis." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 393, 5238, 10 ]
3
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 40, 21, 113 ]
3
true
Family
Sucrose synthase, plant/cyanobacteria
Sucrose synthase, plant/cyanobacteria
Sucrose_synthase_pln/cyn
4
IPR012821
12,821
Sucrose phosphate synthase, sucrose phosphatase-like domain
Sucrose_P_synth_Pase-like_dom
Domain
486
false
false
Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic funct...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR02471" ]
[ "sucr_syn_bact_C" ]
[ 486 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[ "IPR006380" ]
[]
1
0
1
[ "Bacteria", "ecological metagenomes" ]
[ 472, 14 ]
2
[]
[]
0
true
Domain
Sucrose phosphate synthase, sucrose phosphatase-like domain
Sucrose phosphate synthase, sucrose phosphatase-like domain
Sucrose_P_synth_Pase-like_dom
7
IPR012822
12,822
Sucrose-phosphate synthase, glycosyltransferase domain
SucroseP_synth_GlycoTrfase_dom
Domain
474
false
false
This family consists of the N-terminal regions, or in some cases the entirety, of bacterial proteins closely related to plant sucrose-phosphate synthases (SPS). The C-terminal domain ( ), found with most members of this family, resembles both bona fide plant sucrose-phosphate phosphatases (SPP) and the SPP-like domain ...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR02472" ]
[ "sucr_P_syn_N" ]
[ 474 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "ecological metagenomes" ]
[ 463, 11 ]
2
[]
[]
0
true
Domain
Sucrose-phosphate synthase, glycosyltransferase domain
Sucrose-phosphate synthase, glycosyltransferase domain
SucroseP_synth_GlycoTrfase_dom
4
IPR012823
12,823
Flagellar export FliJ
Flagell_FliJ
Family
10,192
false
false
The bacterial flagellum consists of three major parts: the basal body (including the rod), the hook, and the filament. Outer components of the flagellum are transported to the assembly site by a specialised type III export apparatus, which is related to the type III secretion system (T3SS). FliJ is a soluble regulatory...
[ "GO:0071973", "GO:0009288" ]
[ "bacterial-type flagellum-dependent cell motility", "bacterial-type flagellum" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "NCBIFAM" ]
[ "PF02050", "TIGR02473" ]
[ "FliJ", "flagell_FliJ" ]
[ 10129, 8136 ]
2
[ "GP", "GP" ]
[ "GenProp0879", "GenProp0885" ]
[ "GP:GenProp0879", "GP:GenProp0885" ]
2
[ "3ajw", "8ftw", "8ftx" ]
3
[ "PUB00076721" ]
[ "25068520" ]
[ "Soluble components of the flagellar export apparatus, FliI, FliJ, and FliH, do not deliver flagellin, the major filament protein, from the cytosol to the export gate." ]
[ 2014 ]
1
[]
[ "IPR018006" ]
0
1
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 10049, 17, 126 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Flagellar export FliJ
Flagellar export FliJ
Flagell_FliJ
3
IPR012825
12,825
5,6-dimethylbenzimidazole synthase BluB
BluB
Family
6,980
false
false
A previously published hypothesis that BluB, involved in cobalamin biosynthesis [ , ], is cob(II)yrinic acid a,c-diamide reductase ( ) has now been contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis [ , ]. The BluB protein is related to the nitroreductase family.
[]
[]
[]
0
[ "NCBIFAM", "CDD" ]
[ "TIGR02476", "cd02145" ]
[ "BluB", "BluB" ]
[ 6980, 2449 ]
2
[ "EC", "METACYC" ]
[ "1.13.11.79", "PWY-5523" ]
[ "EC:1.13.11.79", "METACYC:PWY-5523" ]
2
[ "2isj", "2isk", "2isl" ]
3
[ "PUB00002275", "PUB00015657", "PUB00047736", "PUB00056791" ]
[ "7635831", "12869542", "17377583", "17301238" ]
[ "Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus.", "Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.", "BluB cannibalizes flavin to form the lower ligand of vitamin B12.", "Single-enzyme conve...
[ 1995, 2003, 2007, 2007 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 183, 6713, 20, 64 ]
4
[]
[]
0
true
Family
5,6-dimethylbenzimidazole synthase BluB
5,6-dimethylbenzimidazole synthase BluB
BluB
1
IPR012826
12,826
Flagellar motor switch FliN
FliN
Family
11,930
false
false
The flagellar motor switch in Escherichia coli and Salmonella typhimurium regulates the direction of flagellar rotation and hence controls swimming behaviour. The switch is a complex apparatus that responds to signals transduced by the chemotaxis sensory signalling system during chemotactic behaviour [ ]. The switch co...
[ "GO:0006935", "GO:0071973", "GO:0009288", "GO:0016020" ]
[ "chemotaxis", "bacterial-type flagellum-dependent cell motility", "bacterial-type flagellum", "membrane" ]
[ "biological_process", "biological_process", "cellular_component", "cellular_component" ]
4
[ "NCBIFAM" ]
[ "TIGR02480" ]
[ "fliN" ]
[ 11930 ]
1
[ "GP", "GP", "GP" ]
[ "GenProp0883", "GenProp1183", "GenProp1194" ]
[ "GP:GenProp0883", "GP:GenProp1183", "GP:GenProp1194" ]
3
[ "1o6a", "1yab", "4yxb", "4yxc", "5xrw", "8umd", "8umx", "8uox", "8upl", "8vib", "8vid", "8vkq", "8vkr", "8wiw", "8wo5", "8woe", "8xp0", "8xp1", "8yjt", "9n49", "9n4z" ]
21
[ "PUB00001834", "PUB00002083", "PUB00002290", "PUB00004790" ]
[ "8224881", "2656645", "8631704", "1631122" ]
[ "Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG.", "Flagellar switch of Salmonella typhimurium: gene sequences and deduced protein sequences.", "A mutational analysis of the interaction between FliG and FliM, two compone...
[ 1993, 1989, 1996, 1992 ]
4
[ "IPR001172" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 11761, 15, 154 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Flagellar motor switch FliN
Flagellar motor switch FliN
FliN
1
IPR012827
12,827
Hemerythrin, metal-binding domain
Hemerythrin_metal-bd
Domain
8,727
false
false
The hemerythrin family is composed of hemerythrin proteins found in invertebrates, and a broader collection of bacterial and archaeal homologues. Hemerythrin is an oxygen-binding protein found in the vascular system and coelomic fluid, or in muscles (myohemerythrin) in invertebrates [ ]. Many of the homologous proteins...
[ "GO:0046872" ]
[ "metal ion binding" ]
[ "molecular_function" ]
1
[ "NCBIFAM", "CDD" ]
[ "TIGR02481", "cd12107" ]
[ "hemeryth_dom", "Hemerythrin" ]
[ 8420, 8687 ]
2
[]
[]
[]
0
[ "1a7d", "1a7e", "1hmd", "1hmo", "1i4y", "2avk", "2awc", "2awy", "2hmq", "2hmz", "2mhr", "3agt", "3agu", "3waq", "3whn", "4xpw", "4xpx", "4xpy", "4xq1" ]
19
[ "PUB00001429", "PUB00001615", "PUB00003224", "PUB00004613", "PUB00005066" ]
[ "1425663", "2065779", "3681996", "3856224", "2362933" ]
[ "Ovohemerythrin, a major 14-kDa yolk protein distinct from vitellogenin in leech.", "Primary structure of myohemerythrin from the annelid Nereis diversicolor.", "Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution.", "Active site structures of deoxyhemerythrin and oxyhemerythrin.", "Th...
[ 1992, 1991, 1987, 1985, 1990 ]
5
[ "IPR012312" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 94, 7926, 512, 195 ]
4
[]
[]
0
true
Domain
Hemerythrin, metal-binding domain
Hemerythrin, metal-binding domain
Hemerythrin_metal-bd
7
IPR012828
12,828
ATP-dependent 6-phosphofructokinase, prokaryotic
PFKA_ATP_prok
Family
9,928
false
false
6-phosphofructokinase ( ), a key regulatory enzyme in glycolysis, catalyses the addition of phosphate from ATP to fructose 6-phosphate to give fructose 1,6-bisphosphate. This represents a key control step in glycolysis. This entry contains bacterial ATP-dependent 6-phosphofructokinases, which lack a β-hairpin loop pres...
[ "GO:0003872", "GO:0005524", "GO:0006002", "GO:0006096" ]
[ "6-phosphofructokinase activity", "ATP binding", "fructose 6-phosphate metabolic process", "glycolytic process" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]
4
[ "HAMAP", "NCBIFAM", "CDD" ]
[ "MF_00339", "TIGR02482", "cd00763" ]
[ "Phosphofructokinase_I_B1", "PFKA_ATP", "Bacterial_PFK" ]
[ 9891, 9741, 2741 ]
3
[ "EC", "GP", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.1.11", "GenProp0694", "GenProp1306", "GenProp1407", "GenProp1599", "GenProp1705", "PWY-1042", "PWY-1861", "PWY-5484", "PWY-7385" ]
[ "EC:2.7.1.11", "GP:GenProp0694", "GP:GenProp1306", "GP:GenProp1407", "GP:GenProp1599", "GP:GenProp1705", "METACYC:PWY-1042", "METACYC:PWY-1861", "METACYC:PWY-5484", "METACYC:PWY-7385" ]
10
[ "1mto", "1pfk", "1zxx", "2pfk", "3pfk", "3u39", "4a3s", "4i36", "4i4i", "4i7e", "4pfk", "5xoe", "5xz6", "5xz7", "5xz8", "5xz9", "5xza", "6pfk" ]
18
[]
[]
[]
[]
0
[ "IPR012003" ]
[]
1
0
1
[ "Bacteria", "Methanomicrobia", "Opisthokonta", "Siphoviridae sp. ctx254", "metagenomes" ]
[ 9829, 33, 12, 1, 53 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
ATP-dependent 6-phosphofructokinase, prokaryotic
ATP-dependent 6-phosphofructokinase, prokaryotic
PFKA_ATP_prok
6
IPR012829
12,829
Phosphofructokinase, mixed-substrate PFK group III
Phosphofructokinase_III
Family
8,419
false
false
This entry includes pyrophosphate--fructose 6-phosphate 1-phosphotransferase from Amycolatopsis methanolica [ ] and ATP-dependent 6-phosphofructokinase 2 from Streptomyces coelicolor [ ]. They catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis.
[ "GO:0047334", "GO:0006096" ]
[ "diphosphate-fructose-6-phosphate 1-phosphotransferase activity", "glycolytic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "NCBIFAM" ]
[ "MF_01976", "TIGR02483" ]
[ "Phosphofructokinase_III", "PFK_mixed" ]
[ 8409, 6027 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.1.11", "PWY-1042", "PWY-1861", "PWY-5484", "PWY-7385" ]
[ "EC:2.7.1.11", "METACYC:PWY-1042", "METACYC:PWY-1861", "METACYC:PWY-5484", "METACYC:PWY-7385" ]
5
[]
0
[ "PUB00014446", "PUB00017820" ]
[ "11717283", "9055413" ]
[ "Different physiological roles of ATP- and PP(i)-dependent phosphofructokinase isoenzymes in the methylotrophic actinomycete Amycolatopsis methanolica.", "Identification of ATP-dependent phosphofructokinase as a regulatory step in the glycolytic pathway of the actinomycete Streptomyces coelicolor A3(2)." ]
[ 2001, 1997 ]
2
[ "IPR012003" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 32, 8181, 10, 196 ]
4
[]
[]
0
true
Family
Phosphofructokinase, mixed-substrate PFK group III
Phosphofructokinase, mixed-substrate PFK group III
Phosphofructokinase_III
6
IPR012830
12,830
Citrate utilization protein B
CitB
Family
2,171
false
false
This entry identifies proteins that are decribed as citrate utilization protein B, restricted to the proteobacteria. CitB [ ] has been identified in Salmonella and Escherichia coli as the signal transduction component of a two-component system for citrate in which CitA acts as a citrate transporter. This domain is also...
[]
[]
[]
0
[ "PFAM", "NCBIFAM" ]
[ "PF27541", "TIGR02484" ]
[ "CitB", "CitB" ]
[ 2171, 1961 ]
2
[]
[]
[]
0
[]
0
[ "PUB00016702", "PUB00016912", "PUB00106878" ]
[ "15525640", "1718953", "30222098" ]
[ "Identification and characterization of a novel vitamin B12 (cobalamin) biosynthetic enzyme (CobZ) from Rhodobacter capsulatus, containing flavin, heme, and Fe-S cofactors.", "Cloning and nucleotide sequence of the gene (citA) encoding a citrate carrier from Salmonella typhimurium.", "The monofunctional cobalam...
[ 2005, 1991, 2018 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Opisthokonta", "ecological metagenomes" ]
[ 16, 2140, 2, 13 ]
4
[]
[]
0
true
Family
Citrate utilization protein B
Citrate utilization protein B
CitB
1
IPR012831
12,831
Precorrin 3B synthase CobZ
CobZ
Family
1,884
false
false
Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR02485" ]
[ "CobZ_N-term" ]
[ 1884 ]
1
[]
[]
[]
0
[]
0
[ "PUB00009744", "PUB00014672", "PUB00015657", "PUB00016702", "PUB00035308", "PUB00035309", "PUB00035310", "PUB00070131", "PUB00106694", "PUB00106878" ]
[ "11215515", "11153269", "12869542", "15525640", "17163662", "16042605", "12055304", "23922391", "17630784", "30222098" ]
[ "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Multiple biosynthetic pathways for vitamin B12: variations on a central theme.", "Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.", "Identification and characterization of a novel vitamin B12 (cobalamin) bios...
[ 2000, 2001, 2003, 2005, 2006, 2005, 2002, 2013, 2007, 2018 ]
10
[ "IPR050315" ]
[]
1
0
1
[ "Archaea", "Bacteria", "ecological metagenomes" ]
[ 7, 1871, 6 ]
3
[]
[]
0
true
Family
Precorrin 3B synthase CobZ
Precorrin 3B synthase CobZ
CobZ
2
IPR012832
12,832
Reductive dehalogenase
RDH
Domain
1,062
false
false
This entry represents the C-terminal domain in corrin and 8-iron Fe-S cluster-containing reductive dehalogenase [ ] found primarily in halorespiring microorganisms such as Dehalococcoides ethenogenes which contains as many as 17 enzymes of this type with varying substrate ranges. One example of a characterised enzyme i...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR02486" ]
[ "RDH" ]
[ 1062 ]
1
[ "EC" ]
[ "1.21.99.5" ]
[ "EC:1.21.99.5" ]
1
[ "4uqu", "4ur0", "4ur1", "4ur2", "4ur3", "5m2g", "5m8u", "5m8w", "5m8x", "5m8y", "5m8z", "5m90", "5m91", "5m92", "5ma0", "5ma1", "5ma2", "5maa", "5obi", "5obp", "8q4h" ]
21
[ "PUB00016698", "PUB00016713" ]
[ "11097881", "9224702" ]
[ "Trichloroethene reductive dehalogenase from Dehalococcoides ethenogenes: sequence of tceA and substrate range characterization.", "Redox chemistry of cobalamin and iron-sulfur cofactors in the tetrachloroethene reductase of Dehalobacter restrictus." ]
[ 2000, 1997 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "unclassified sequences" ]
[ 5, 1008, 49 ]
3
[]
[]
0
true
Domain
Reductive dehalogenase
Reductive dehalogenase
RDH
6
IPR012833
12,833
Ribonucleoside-triphosphate reductase, anaerobic
NrdD
Family
15,065
false
false
This entry represents anaerobic, class III ribonucleotide reductase. The mechanism of the enzyme involves a glycine-centred radical [ ], a C-terminal zinc binding site [ ], and a set of conserved active site cysteines and asparagines [ ]. This enzyme requires an activating component, NrdG, a radical-SAM domain containi...
[ "GO:0008998", "GO:0016491", "GO:0006260" ]
[ "ribonucleoside-triphosphate reductase (thioredoxin) activity", "oxidoreductase activity", "DNA replication" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "NCBIFAM", "NCBIFAM", "CDD" ]
[ "PF13597", "TIGR02487", "TIGR02827", "cd01675" ]
[ "NRDD", "NrdD", "RNR_anaer_Bdell", "RNR_III" ]
[ 15065, 11333, 534, 8977 ]
4
[ "EC", "GP", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC" ]
[ "1.1.98.6", "GenProp0291", "GenProp1343", "GenProp1446", "GenProp1484", "GenProp1621", "PWY-7187", "PWY-7220", "PWY-7222" ]
[ "EC:1.1.98.6", "GP:GenProp0291", "GP:GenProp1343", "GP:GenProp1446", "GP:GenProp1484", "GP:GenProp1621", "METACYC:PWY-7187", "METACYC:PWY-7220", "METACYC:PWY-7222" ]
9
[ "1h78", "1h79", "1h7a", "1h7b", "1hk8", "4coi", "4coj", "4col", "4com", "4con", "4u3e", "8p23", "8p27", "8p28", "8p2c", "8p2d", "8p2s", "8p39" ]
18
[ "PUB00016693", "PUB00016704", "PUB00016706", "PUB00033790", "PUB00060768" ]
[ "11526118", "10066165", "12655046", "10574800", "15158709" ]
[ "Two active site asparagines are essential for the reaction mechanism of the class III anaerobic ribonucleotide reductase from bacteriophage T4.", "A glycyl radical site in the crystal structure of a class III ribonucleotide reductase.", "A metal-binding site in the catalytic subunit of anaerobic ribonucleotide...
[ 2001, 1999, 2003, 1999, 2004 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 553, 12884, 198, 1041, 389 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Ribonucleoside-triphosphate reductase, anaerobic
Ribonucleoside-triphosphate reductase, anaerobic
NrdD
7
IPR012834
12,834
Flagellar basal-body rod FlgG
FlgG_G_neg
Family
9,799
false
false
This family consists of the FlgG protein of the flagellar apparatus in bacteria. The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod [ ]. The rod consists of about 26 subunits of flgG in the distal portion, and flgB, flgC and flgF are ...
[ "GO:0071973", "GO:0009426" ]
[ "bacterial-type flagellum-dependent cell motility", "bacterial-type flagellum basal body, distal rod" ]
[ "biological_process", "cellular_component" ]
2
[ "NCBIFAM" ]
[ "TIGR02488" ]
[ "flgG_G_neg" ]
[ 9799 ]
1
[ "GP" ]
[ "GenProp0880" ]
[ "GP:GenProp0880" ]
1
[ "5wrh", "6jzr", "7bin", "7cbm", "7cgo", "7e80", "7e82", "7nvg", "8wki", "8wkk", "8wl2", "8wlp", "8wlq", "8wlt", "8wo5", "8woe", "8z5u", "8z5w", "8z60" ]
19
[ "PUB00033604" ]
[ "15136044" ]
[ "In vitro characterization of FlgB, FlgC, FlgF, FlgG, and FliE, flagellar basal body proteins of Salmonella." ]
[ 2004 ]
1
[ "IPR020013" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 9664, 24, 111 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Flagellar basal-body rod FlgG
Flagellar basal-body rod FlgG
FlgG_G_neg
2
IPR012835
12,835
Flagellar hook FlgE
FlgE_epsilon
Family
449
false
false
Members of this family are flagellar hook proteins, designated FlgE, as found in the epsilon subdivision of the proteobacteria (Helicobacter, Wolinella, and Campylobacter). These proteins differ significantly in architecture from proteins designated FlgE in other lineages; the N-terminal and C-terminal domains are homo...
[ "GO:0044781", "GO:0009288" ]
[ "bacterial-type flagellum organization", "bacterial-type flagellum" ]
[ "biological_process", "cellular_component" ]
2
[ "NCBIFAM" ]
[ "TIGR02489" ]
[ "flgE_epsilon" ]
[ 449 ]
1
[]
[]
[]
0
[ "5az4", "5jxl" ]
2
[ "PUB00017823" ]
[ "9658019" ]
[ "The central, surface-exposed region of the flagellar hook protein FlgE of Campylobacter jejuni shows hypervariability among strains." ]
[ 1998 ]
1
[ "IPR020013" ]
[]
1
0
1
[ "Campylobacterota", "hydrothermal vent metagenome" ]
[ 445, 4 ]
2
[]
[]
0
true
Family
Flagellar hook FlgE
Flagellar hook FlgE
FlgE_epsilon
8
IPR012836
12,836
Flagellar basal-body rod FlgF
FlgF
Family
6,129
false
false
FlgF is a flagellar basal-body protein that along with FlgBCG composes the rod of bacterial flagellin [ ]. This entry contains proteins only from the proteobacteria, and not in the epsilon subdivision (where the architecture of the related FlgE protein differs substantially from other lineages).
[ "GO:0071973", "GO:0030694" ]
[ "bacterial-type flagellum-dependent cell motility", "bacterial-type flagellum basal body, rod" ]
[ "biological_process", "cellular_component" ]
2
[ "NCBIFAM" ]
[ "TIGR02490" ]
[ "flgF" ]
[ 6129 ]
1
[ "GP" ]
[ "GenProp0880" ]
[ "GP:GenProp0880" ]
1
[ "8z5s", "8z5u", "8z5w", "8z60" ]
4
[ "PUB00033604" ]
[ "15136044" ]
[ "In vitro characterization of FlgB, FlgC, FlgF, FlgG, and FliE, flagellar basal body proteins of Salmonella." ]
[ 2004 ]
1
[ "IPR020013" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 6048, 4, 77 ]
3
[]
[]
0
true
Family
Flagellar basal-body rod FlgF
Flagellar basal-body rod FlgF
FlgF
8
IPR012837
12,837
Ribonucleoside-triphosphate reductase activating, anaerobic
NrdG
Family
8,573
false
false
This enzyme [ ] is a member of the radical-SAM protein and utilises S-adenosyl methionine, an iron-sulphur cluster and a reductant (dihydroflavodoxin [ ]) to produce a glycine-centred radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, ). The two components form an alpha-2/beta-2 heterodim...
[ "GO:0043365", "GO:0051539" ]
[ "[formate-C-acetyltransferase]-activating enzyme activity", "4 iron, 4 sulfur cluster binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PIRSF", "SFLD", "NCBIFAM" ]
[ "PIRSF000368", "SFLDF00299", "TIGR02491" ]
[ "NrdG", "anaerobic_ribonucleoside-triph", "NrdG" ]
[ 7501, 8422, 7430 ]
3
[ "EC", "GP", "METACYC" ]
[ "1.97.1.-", "GenProp0291", "PWY-6530" ]
[ "EC:1.97.1.-", "GP:GenProp0291", "METACYC:PWY-6530" ]
3
[]
0
[ "PUB00016703", "PUB00016711" ]
[ "11389585", "11297442" ]
[ "Activation of class III ribonucleotide reductase from E. coli. The electron transfer from the iron-sulfur center to S-adenosylmethionine.", "Activation of class III ribonucleotide reductase by flavodoxin: a protein radical-driven electron transfer to the iron-sulfur center." ]
[ 2001, 2001 ]
2
[ "IPR034457" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "Methanobacteriati", "Viruses", "unclassified sequences" ]
[ 7925, 7, 13, 571, 57 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Ribonucleoside-triphosphate reductase activating, anaerobic
Ribonucleoside-triphosphate reductase activating, anaerobic
NrdG
2
IPR012838
12,838
Pyruvate formate-lyase 1 activating enzyme
PFL1_activating
Family
7,577
false
false
Pyruvate formate lyase-activating enzyme is a 28kDa monomeric protein which is involved in the anerobic glucose metabolism pathway. It is a member of the radical S-adenosylmethionine family of enzymes which initiate radical catalysis. It is necessary to activate pyruvate formate lyase (PFL), which catalyses the convers...
[ "GO:0043365" ]
[ "[formate-C-acetyltransferase]-activating enzyme activity" ]
[ "molecular_function" ]
1
[ "NCBIFAM" ]
[ "TIGR02493" ]
[ "PFLA" ]
[ 7577 ]
1
[ "EC", "GP" ]
[ "1.97.1.4", "GenProp0943" ]
[ "EC:1.97.1.4", "GP:GenProp0943" ]
2
[ "3c8f", "3cb8", "8fo0", "8fol", "8fsi" ]
5
[ "PUB00044952" ]
[ "15581584" ]
[ "Pyruvate formate-lyase activating enzyme: elucidation of a novel mechanism for glycyl radical formation." ]
[ 2005 ]
1
[ "IPR012839" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "metagenomes", "unclassified Caudoviricetes" ]
[ 7504, 48, 23, 2 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Pyruvate formate-lyase 1 activating enzyme
Pyruvate formate-lyase 1 activating enzyme
PFL1_activating
9
IPR012839
12,839
Organic radical enzyme activase
Organic_radical_activase
Family
11,931
false
false
This subset of the radical-SAM domain includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centred radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, , ) and the anaerobic ribonucleotide reductase activating enzyme (...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PIRSF" ]
[ "PIRSF000371" ]
[ "PFL_act_enz" ]
[ 11931 ]
1
[ "EC" ]
[ "1.97.1" ]
[ "EC:1.97.1" ]
1
[ "3c8f", "3cb8", "8fo0", "8fol", "8fsi" ]
5
[ "PUB00016705", "PUB00016707", "PUB00016708", "PUB00090957" ]
[ "15153112", "12704244", "14735297", "28183913" ]
[ "Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity.", "Molecular characterization of the 1,3-propanediol (1,3-PD) operon of Clostridium butyricum.", "Genes involved in the anaerobic degradation of toluene in a denitr...
[ 2004, 2003, 2004, 2017 ]
4
[ "IPR034457" ]
[ "IPR012838", "IPR033974", "IPR040074" ]
1
3
0
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes", "unclassified Caudoviricetes" ]
[ 33, 11824, 3, 69, 2 ]
5
[ "Escherichia coli (strain K12)" ]
[ 4 ]
1
true
Family
Organic radical enzyme activase
Organic radical enzyme activase
Organic_radical_activase
9
IPR012840
12,840
Anaerobic ribonucleoside-triphosphate reductase activating protein
NrdG2
Family
3,491
false
false
This enzyme is a member of the radical-SAM family. It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, ) and presumably fulfils the identical function as NrdG [ , ], which utilises S-adenosyl methionine, an iron-sulphur cluster and a reductant (dihydroflavodoxin) to pr...
[]
[]
[]
0
[ "SFLD", "NCBIFAM" ]
[ "SFLDG01094", "TIGR02495" ]
[ "Uncharacterised_Radical_SAM_Su", "NrdG2" ]
[ 3452, 3431 ]
2
[ "GP" ]
[ "GenProp0291" ]
[ "GP:GenProp0291" ]
1
[]
0
[ "PUB00016703", "PUB00016711", "PUB00093688" ]
[ "11389585", "11297442", "26536144" ]
[ "Activation of class III ribonucleotide reductase from E. coli. The electron transfer from the iron-sulfur center to S-adenosylmethionine.", "Activation of class III ribonucleotide reductase by flavodoxin: a protein radical-driven electron transfer to the iron-sulfur center.", "A Ferredoxin Disulfide Reductase ...
[ 2001, 2001, 2015 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 339, 2896, 3, 159, 94 ]
5
[]
[]
0
true
Family
Anaerobic ribonucleoside-triphosphate reductase activating protein
Anaerobic ribonucleoside-triphosphate reductase activating protein
NrdG2
8
IPR012842
12,842
Type 3 secretion system stator protein SctL/SctL2
T3SS_SctL/SctL2
Family
2,131
false
false
This entry represents Type 3 secretion system stator proteins (also referred to HrpE-like proteins), which are the cytoplasmic components of bacterial type III secretion systems [ ]. Type 3 secretion systems (T3SSs) are used by many different Gram-negative pathogens and symbionts to inject bacterial effector proteins i...
[ "GO:0030254" ]
[ "protein secretion by the type III secretion system" ]
[ "biological_process" ]
1
[ "NCBIFAM" ]
[ "TIGR02499" ]
[ "HrpE_YscL_not" ]
[ 2131 ]
1
[ "GP" ]
[ "GenProp0052" ]
[ "GP:GenProp0052" ]
1
[]
0
[ "PUB00034695", "PUB00097915", "PUB00097916", "PUB00097917" ]
[ "16672607", "20453832", "24722491", "30107569" ]
[ "Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL.", "Deciphering the assembly of the Yersinia type III secretion injectisome.", "Functional characterization of the type III secretion ATPase SsaN encoded by Salmonella pathogenicity island 2.", "Bacterial t...
[ 2006, 2010, 2014, 2018 ]
4
[]
[ "IPR010586" ]
0
1
0
[ "Bacteria", "metagenomes" ]
[ 2124, 7 ]
2
[]
[]
0
true
Family
Type 3 secretion system stator protein SctL/SctL2
Type 3 secretion system stator protein SctL/SctL2
T3SS_SctL/SctL2
6
IPR012843
12,843
YscD
YscD
Family
1,497
false
false
This family represents YscD from proteobacteria and similar putative type III secretion system bacteria such as HrpQ in Pseudomonas syringae, and EscD in enteropathogenic Escherichia coli. In the Chlamydiae, this entry describes the C-terminal 400 residues of a longer protein. YscD is a single-pass inner membrane prote...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR02500" ]
[ "type_III_yscD" ]
[ 1497 ]
1
[ "GP" ]
[ "GenProp0052" ]
[ "GP:GenProp0052" ]
1
[ "4a0e", "4alz", "4d9v" ]
3
[ "PUB00020581", "PUB00076172" ]
[ "1860816", "23908767" ]
[ "Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica.", "In situ structural analysis of the Yersinia enterocolitica injectisome." ]
[ 1991, 2013 ]
2
[]
[]
0
0
null
[ "Bacteria", "Bracon brevicornis", "metagenomes" ]
[ 1494, 1, 2 ]
3
[]
[]
0
true
Family
YscD
YscD
YscD
8
IPR012844
12,844
Dihydroxyacetone kinase phosphotransferase subunit, N-terminal domain
DhaM_N
Domain
4,815
false
false
In Escherichia coli and many other bacteria, unlike the yeasts and a few bacteria such as Citrobacter freundii, the dihydroxyacetone kinase (also called glycerone kinase) transfers a phosphate from a phosphoprotein rather than from ATP. The dihydroxyacetone kinase of Escherichia coli consists of three subunits: DhaK, D...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR02364" ]
[ "dha_pts" ]
[ 4815 ]
1
[ "EC", "GP", "GP" ]
[ "2.7.1.121", "GenProp1146", "GenProp1324" ]
[ "EC:2.7.1.121", "GP:GenProp1146", "GP:GenProp1324" ]
3
[ "3b48", "3cr3", "3ct6" ]
3
[ "PUB00033180" ]
[ "11350937" ]
[ "The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor." ]
[ 2001 ]
1
[ "IPR004701" ]
[]
1
0
1
[ "Bacteria", "Ecdysozoa", "Methanobacteriota", "metagenomes" ]
[ 4702, 3, 100, 10 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Dihydroxyacetone kinase phosphotransferase subunit, N-terminal domain
Dihydroxyacetone kinase phosphotransferase subunit, N-terminal domain
DhaM_N
8
IPR012845
12,845
RNA polymerase sigma factor, FliA/WhiG
RNA_pol_sigma_FliA_WhiG
Family
10,988
false
false
Most members of this family are the flagellar operon sigma factor FliA, controlling transcription of bacterial flagellar genes by RNA polymerase. An exception is the sigma factor WhiG in the genus Streptomyces, involved in the production of sporulating aerial mycelium. The bacterial core RNA polymerase complex, which c...
[ "GO:0003677", "GO:0003899", "GO:0016987", "GO:0006352", "GO:0006355" ]
[ "DNA binding", "DNA-directed RNA polymerase activity", "sigma factor activity", "DNA-templated transcription initiation", "regulation of DNA-templated transcription" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "biological_process" ]
5
[ "NCBIFAM" ]
[ "TIGR02479" ]
[ "FliA_WhiG" ]
[ 10988 ]
1
[]
[]
[]
0
[ "1rp3", "1sc5", "6pfj", "6pfv", "6pmi", "6pmj" ]
6
[ "PUB00000061", "PUB00002181", "PUB00004340", "PUB00088319" ]
[ "3052291", "1597408", "3092189", "25596450" ]
[ "Structure and function of bacterial sigma factors.", "The sigma 70 family: sequence conservation and evolutionary relationships.", "Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.", "Plastid sigma factors: Their individual functions and regulation in transcription."...
[ 1988, 1992, 1986, 2015 ]
4
[]
[ "IPR028617" ]
0
1
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 10807, 12, 169 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
RNA polymerase sigma factor, FliA/WhiG
RNA polymerase sigma factor, FliA/WhiG
RNA_pol_sigma_FliA_WhiG
4
IPR012846
12,846
Acetolactate synthase, large subunit, biosynthetic
Acetolactate_synth_lsu
Family
32,325
false
false
Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this entry also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyac...
[ "GO:0000287", "GO:0003984", "GO:0030976", "GO:0050660", "GO:0009082" ]
[ "magnesium ion binding", "acetolactate synthase activity", "thiamine pyrophosphate binding", "flavin adenine dinucleotide binding", "branched-chain amino acid biosynthetic process" ]
[ "molecular_function", "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
5
[ "NCBIFAM" ]
[ "TIGR00118" ]
[ "acolac_lg" ]
[ 32325 ]
1
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.2.1.6", "GenProp0162", "GenProp0163", "GenProp0164", "GenProp1342", "PWY-5101", "PWY-5103", "PWY-5104", "PWY-5938", "PWY-5939", "PWY-6389", "PWY-7111" ]
[ "EC:2.2.1.6", "GP:GenProp0162", "GP:GenProp0163", "GP:GenProp0164", "GP:GenProp1342", "METACYC:PWY-5101", "METACYC:PWY-5103", "METACYC:PWY-5104", "METACYC:PWY-5938", "METACYC:PWY-5939", "METACYC:PWY-6389", "METACYC:PWY-7111" ]
12
[ "1jsc", "1n0h", "1t9a", "1t9b", "1t9c", "1t9d", "1ybh", "1yhy", "1yhz", "1yi0", "1yi1", "1z8n", "3e9y", "3ea4", "5fem", "5ims", "5k2o", "5k3s", "5k6q", "5k6r", "5k6t", "5wj1", "5wkc", "6bd3", "6bd9", "6dek", "6del", "6dem", "6den", "6deo", "6dep", "6deq"...
52
[]
[]
[]
[]
0
[ "IPR045229" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 796, 27530, 3606, 393 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 4, 3, 1, 5, 1, 1, 8 ]
7
true
Family
Acetolactate synthase, large subunit, biosynthetic
Acetolactate synthase, large subunit, biosynthetic
Acetolactate_synth_lsu
7
IPR012847
12,847
Sucrose phosphatase, plant/cyanobacteria
Sucrose_phosphatase_pln/cyn
Family
1,647
false
false
This entry describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). However, a closely related group of sequences from bacteria and archaea may prove to catalyze the same reaction. SPP is a member of the Class IIB subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleop...
[ "GO:0000287", "GO:0050307", "GO:0005986" ]
[ "magnesium ion binding", "sucrose-phosphate phosphatase activity", "sucrose biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "NCBIFAM" ]
[ "TIGR01485" ]
[ "SPP_plant-cyano" ]
[ 1647 ]
1
[ "EC", "METACYC", "METACYC" ]
[ "3.1.3.24", "PWY-7238", "PWY-7347" ]
[ "EC:3.1.3.24", "METACYC:PWY-7238", "METACYC:PWY-7347" ]
3
[ "1s2o", "1tj3", "1tj4", "1tj5", "1u2s", "1u2t", "2b1q", "2b1r", "2d2v" ]
9
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 222, 1425 ]
2
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 18, 6, 24 ]
3
true
Family
Sucrose phosphatase, plant/cyanobacteria
Sucrose phosphatase, plant/cyanobacteria
Sucrose_phosphatase_pln/cyn
2
IPR012848
12,848
Aspartic peptidase, N-terminal
Aspartic_peptidase_N
Domain
6,409
false
false
This entry represents the N-terminal domain of the aspartic peptidases.
[ "GO:0004190", "GO:0006508" ]
[ "aspartic-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF07966" ]
[ "A1_Propeptide" ]
[ 6409 ]
1
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "3.4.23", "GenProp1728", "R-CEL-2022377", "R-CFA-1442490", "R-CFA-2022377", "R-CFA-2132295", "R-CFA-5683826", "R-CFA-6798695", "R-CFA-77387", "R-HSA-1442490", "R-HSA-2022377", "R-HSA-2132295", "R-HSA-5683826", "R-HSA-6798695", "R-HSA-77387", "R-HSA-9018519", "R-MMU-1442490", "R-MMU...
[ "EC:3.4.23", "GP:GenProp1728", "REACTOME:R-CEL-2022377", "REACTOME:R-CFA-1442490", "REACTOME:R-CFA-2022377", "REACTOME:R-CFA-2132295", "REACTOME:R-CFA-5683826", "REACTOME:R-CFA-6798695", "REACTOME:R-CFA-77387", "REACTOME:R-HSA-1442490", "REACTOME:R-HSA-2022377", "REACTOME:R-HSA-2132295", "RE...
27
[ "1avf", "1htr", "1tzs", "2psg", "2x0b", "3psg", "3vcm", "4amt", "5mkt", "5ux4" ]
10
[ "PUB00000093", "PUB00000349", "PUB00001330" ]
[ "2194475", "1851433", "6795036" ]
[ "The structure and function of the aspartic proteinases.", "Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.", "Gastric proteinases--structure, function, evolution and mechanism of action." ]
[ 1990, 1991, 1981 ]
3
[]
[]
0
0
null
[ "Eumetazoa", "Nocardioides humilatus" ]
[ 6408, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 1, 1, 34, 26, 17 ]
6
true
Domain
Aspartic peptidase, N-terminal
Aspartic peptidase, N-terminal
Aspartic_peptidase_N
3
IPR012849
12,849
Abl-interactor, homeo-domain homologous domain
Abl-interactor_HHR_dom
Domain
8,173
false
false
The region is found towards the N terminus of a number of adaptor proteins that interact with Abl-family tyrosine kinases [ ]. More specifically, it is termed the homeo-domain homologous region (HHR), as it is similar to the DNA-binding region of homeo-domain proteins [ ]. Other homeo-domain proteins have been implicat...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07815" ]
[ "Abi_HHR" ]
[ 8173 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-2029482", "R-HSA-4420097", "R-HSA-5663213", "R-HSA-9013149", "R-HSA-9013404", "R-HSA-9013423", "R-HSA-9664422", "R-MMU-2029482", "R-MMU-4420097", "R-MMU-5663213", "R-MMU-9013149", "R-MMU-9013404", "R-MMU-9013423", "R-RNO-2029482", "R-RNO-4420097", "R-RNO-5663213", "R-RNO-90131...
[ "REACTOME:R-HSA-2029482", "REACTOME:R-HSA-4420097", "REACTOME:R-HSA-5663213", "REACTOME:R-HSA-9013149", "REACTOME:R-HSA-9013404", "REACTOME:R-HSA-9013423", "REACTOME:R-HSA-9664422", "REACTOME:R-MMU-2029482", "REACTOME:R-MMU-4420097", "REACTOME:R-MMU-5663213", "REACTOME:R-MMU-9013149", "REACTOM...
18
[ "3p8c", "4n78", "7usc", "7usd", "7use" ]
5
[ "PUB00016372", "PUB00016604" ]
[ "7590236", "12011975" ]
[ "Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity.", "In search of a function for the E3B1/Abi2/Argbp1/NESH family (Review)." ]
[ 1995, 2002 ]
2
[]
[]
0
0
null
[ "Metazoa" ]
[ 8173 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 52, 3, 18, 25, 25 ]
6
true
Domain
Abl-interactor, homeo-domain homologous domain
Abl-interactor, homeo-domain homologous domain
Abl-interactor_HHR_dom
6
IPR012850
12,850
Alpha-amylase, C-terminal beta-sheet
A-amylase_bs_C
Domain
3,672
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0004556", "GO:0005509", "GO:0005975" ]
[ "alpha-amylase activity", "calcium ion binding", "carbohydrate metabolic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "SMART" ]
[ "PF07821", "SM00810" ]
[ "Alpha-amyl_C2", "Alpha-amyl_C2" ]
[ 3669, 3620 ]
2
[ "EC" ]
[ "3.2.1.1" ]
[ "EC:3.2.1.1" ]
1
[ "1amy", "1ava", "1bg9", "1ht6", "1p6w", "1rp8", "1rp9", "1rpk", "2qps", "2qpu", "3bsg", "3bsh", "3wn6" ]
13
[ "PUB00004870", "PUB00005266", "PUB00016439", "PUB00016510", "PUB00027666" ]
[ "7624375", "8535779", "9571044", "8196040", "11141191" ]
[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis.", "Crystal and molecular struc...
[ 1995, 1995, 1998, 1994, 2001 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 173, 3497, 2 ]
3
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 10, 28, 24 ]
3
true
Domain
Alpha-amylase, C-terminal beta-sheet
Alpha-amylase, C-terminal beta-sheet
A-amylase_bs_C
8
IPR012851
12,851
Spore coat protein CotF-like
Spore_coat_CotF-like
Family
5,847
false
false
The Coat F proteins contribute to the Bacillales spore coat. They occur multiple times in the genomes in which they are found. Bacillus subtilis endospore protein coats protect them and may play a role in their germination [ ]. Spore coat protein F, on the outer surface of the endospore, is one of a suite of proteins t...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF07875", "PTHR39183" ]
[ "Coat_F", "" ]
[ 5430, 2943 ]
2
[]
[]
[]
0
[]
0
[ "PUB00044606", "PUB00044607" ]
[ "18723620", "14711677" ]
[ "Characterization of spores of Bacillus subtilis that lack most coat layers.", "Species differentiation of a diverse suite of Bacillus spores by mass spectrometry-based protein profiling." ]
[ 2008, 2004 ]
2
[]
[ "IPR016493", "IPR017022" ]
0
2
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 5808, 5, 34 ]
3
[ "Arabidopsis thaliana" ]
[ 1 ]
1
true
Family
Spore coat protein CotF-like
Spore coat protein CotF-like
Spore_coat_CotF-like
4
IPR012852
12,852
Calcium binding and coiled-coil domain-like
CALCOCO1-like
Domain
2,561
false
false
Calcium-binding and coiled-coil domain-containing protein 1 (Calcoco1) from Mus musculus ( ) binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1 ( ), and thus enhances transcriptional activation by a number of nuclear receptors. Calcoco1 has a central coiled-coil region with three leucine ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07888" ]
[ "CALCOCO1" ]
[ 2561 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-5357905", "R-BTA-936440", "R-HSA-5357905", "R-HSA-936440", "R-MMU-5357905", "R-MMU-936440", "R-RNO-5357905", "R-RNO-936440" ]
[ "REACTOME:R-BTA-5357905", "REACTOME:R-BTA-936440", "REACTOME:R-HSA-5357905", "REACTOME:R-HSA-936440", "REACTOME:R-MMU-5357905", "REACTOME:R-MMU-936440", "REACTOME:R-RNO-5357905", "REACTOME:R-RNO-936440" ]
8
[]
0
[ "PUB00016596" ]
[ "14690606" ]
[ "CoCoA, a nuclear receptor coactivator which acts through an N-terminal activation domain of p160 coactivators." ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Bacillati", "Opisthokonta" ]
[ 36, 2525 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 29, 12, 6, 10 ]
4
true
Domain
Calcium binding and coiled-coil domain-like
Calcium binding and coiled-coil domain-like
CALCOCO1-like
6
IPR012853
12,853
Chloramphenicol phosphotransferase-like
CPT
Family
2,762
false
false
The members of this family are all similar to chloramphenicol 3-O phosphotransferase (CPT, ) expressed by Streptomyces venezuelae. Chloramphenicol (Cm) is a metabolite produced by this bacterium that can inhibit ribosomal peptidyl transferase activity and therefore protein production. By transferring a phosphate group ...
[ "GO:0005524", "GO:0016740" ]
[ "ATP binding", "transferase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "PIRSF", "CDD" ]
[ "PF07931", "PIRSF007531", "cd00227" ]
[ "CPT", "CPT", "CPT" ]
[ 2762, 2059, 37 ]
3
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.1.-", "PWY-5129", "PWY-6322", "PWY-6369", "PWY-6626", "PWY-6682", "PWY-6955", "PWY-7077", "PWY-7321", "PWY-7740", "PWY-7769", "PWY-7886", "PWY-7948", "PWY-7975", "PWY-8129", "PWY-8324", "PWY-8367", "PWY-8392", "PWY-8393", "PWY-8394", "PWY-8402" ]
[ "EC:2.7.1.-", "METACYC:PWY-5129", "METACYC:PWY-6322", "METACYC:PWY-6369", "METACYC:PWY-6626", "METACYC:PWY-6682", "METACYC:PWY-6955", "METACYC:PWY-7077", "METACYC:PWY-7321", "METACYC:PWY-7740", "METACYC:PWY-7769", "METACYC:PWY-7886", "METACYC:PWY-7948", "METACYC:PWY-7975", "METACYC:PWY-8...
21
[ "1grq", "1grr", "1qhn", "1qhs", "1qhx", "1qhy" ]
6
[ "PUB00016586", "PUB00027902" ]
[ "11468347", "10835366" ]
[ "Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity.", "The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism." ]
[ 2001, 2000 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "metagenomes", "uncultured Caudovirales phage" ]
[ 2646, 100, 2, 13, 1 ]
5
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Chloramphenicol phosphotransferase-like
Chloramphenicol phosphotransferase-like
CPT
3
IPR012854
12,854
Copper amine oxidase-like, N-terminal
Cu_amine_oxidase-like_N
Domain
21,514
false
false
Amine oxidases (AO) are enzymes that catalyse the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing ( ) and copper-containing ( ). Copper-containing AO act as a disulphide-linked homodimer. They cata...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07833" ]
[ "Cu_amine_oxidN1" ]
[ 21514 ]
1
[ "EC", "GP" ]
[ "1.4.3.21", "GenProp1402" ]
[ "EC:1.4.3.21", "GP:GenProp1402" ]
2
[ "1d6u", "1d6y", "1d6z", "1dyu", "1jrq", "1lvn", "1oac", "1qaf", "1qak", "1qal", "1spu", "2w0q", "2wgq", "2wo0", "2wof", "2woh", "6ezz", "6grr", "8imd" ]
19
[ "PUB00005251", "PUB00010699", "PUB00010700", "PUB00010701", "PUB00016565" ]
[ "8591028", "9048544", "9405045", "8805580", "10576737" ]
[ "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.", "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.", "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the...
[ 1995, 1997, 1997, 1996, 1999 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 2, 21351, 15, 7, 139 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 2, 1 ]
2
true
Domain
Copper amine oxidase-like, N-terminal
Copper amine oxidase-like, N-terminal
Cu_amine_oxidase-like_N
3
IPR012856
12,856
D-aminopeptidase, domain B
DAP_B_dom
Domain
674
false
false
D-aminopeptidase ( ) is a dimeric enzyme with each monomer being composed of three domains. Domain B is organised to form a β barrel made up of eight antiparallel β strands. It is connected to domain A, the catalytic domain, by an eight-residue sequence, and also interacts with both domains A and C via non-covalent bon...
[ "GO:0004177" ]
[ "aminopeptidase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF07930" ]
[ "DAP_B" ]
[ 674 ]
1
[ "EC" ]
[ "3.4.11.19" ]
[ "EC:3.4.11.19" ]
1
[ "1ei5" ]
1
[ "PUB00013322" ]
[ "10986464" ]
[ "Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Pseudomonadota", "bioreactor metagenome", "leotiomyceta" ]
[ 281, 1, 392 ]
3
[]
[]
0
true
Domain
D-aminopeptidase, domain B
D-aminopeptidase, domain B
DAP_B_dom
1
IPR012858
12,858
Dendritic cell-specific transmembrane protein-like
DC_STAMP-like
Domain
4,592
false
false
This group of sequences is similar to a region of the dendritic cell-specific transmembrane protein (DC-STAMP, ). This is thought to be a novel receptor protein that shares no identity with other multimembrane-spanning proteins [ ]. It is thought to have seven putative transmembrane regions [ ], two of which are found ...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF07782" ]
[ "DC_STAMP" ]
[ 4592 ]
1
[ "REACTOME" ]
[ "R-HSA-8874211" ]
[ "REACTOME:R-HSA-8874211" ]
1
[]
0
[ "PUB00016463" ]
[ "11169400" ]
[ "DC-STAMP, a novel multimembrane-spanning molecule preferentially expressed by dendritic cells." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Eumetazoa", "Nocardioides malaquae" ]
[ 4591, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 52, 5, 9, 7, 10 ]
6
true
Domain
Dendritic cell-specific transmembrane protein-like
Dendritic cell-specific transmembrane protein-like
DC_STAMP-like
2
IPR012859
12,859
Archaeal Type IV pilin, N-terminal
Pilin_N_archaeal
Domain
2,821
false
false
This entry represents the N-terminal domain of archaeal pilins, which play important roles in surface adhesion. Sequences covered by this domain are not mixed up with sequences having such an extremely high sequence conservation as described in [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF07790" ]
[ "Pilin_N" ]
[ 2821 ]
1
[]
[]
[]
0
[ "8fj5", "8gi2", "8rey" ]
3
[ "PUB00069628" ]
[ "23794623" ]
[ "Novel archaeal adhesion pilins with a conserved N terminus." ]
[ 2013 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Saline Natrinema sp. J7-1 virus 2", "unclassified sequences" ]
[ 2773, 2, 1, 45 ]
4
[]
[]
0
true
Domain
Archaeal Type IV pilin, N-terminal
Archaeal Type IV pilin, N-terminal
Pilin_N_archaeal
2
IPR012860
12,860
Arf3-interacting protein 1, N-terminal domain
Afi1_N
Domain
1,871
false
false
This domain occurs at the N terminus of Afi1 (Arf3-interacting protein 1), a protein necessary for vesicle trafficking in yeast. This domain is the interacting region of the protein which binds to Arf3. Afi1 is distributed asymmetrically at the plasma membrane and is required for polarized distribution of Arf3 but not ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07792" ]
[ "Afi1" ]
[ 1871 ]
1
[]
[]
[]
0
[]
0
[ "PUB00057274" ]
[ "18397879" ]
[ "Afi1p functions as an Arf3p polarization-specific docking factor for development of polarity." ]
[ 2008 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1871 ]
1
[ "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 (strain 972 / ATCC 24843)" ]
[ 1, 1, 1, 1 ]
4
true
Domain
Arf3-interacting protein 1, N-terminal domain
Arf3-interacting protein 1, N-terminal domain
Afi1_N
7
IPR012861
12,861
Protein of unknown function DUF1634
DUF1634
Family
1,945
false
false
This family contains many hypothetical bacterial and archaeal proteins. A few members of this family are annotated as being putative transmembrane proteins, and the region in question in fact contains many hydrophobic residues.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07843" ]
[ "DUF1634" ]
[ 1945 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "metagenomes" ]
[ 126, 1806, 13 ]
3
[]
[]
0
true
Family
Protein of unknown function DUF1634
Protein of unknown function DUF1634
DUF1634
9
IPR012862
12,862
Protein of unknown function DUF1635
DUF1635
Family
2,544
false
false
The members of this family include sequences that are parts of hypothetical proteins expressed by plant species. The region in question is about 170 amino acids long.
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF07795", "PTHR33431" ]
[ "DUF1635", "" ]
[ 2541, 2469 ]
2
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Embryophyta" ]
[ 2544 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 23, 5, 11 ]
3
true
Family
Protein of unknown function DUF1635
Protein of unknown function DUF1635
DUF1635
4
IPR012864
12,864
Cysteine oxygenase/2-aminoethanethiol dioxygenase
PCO/ADO
Family
6,306
false
false
This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol dioxygenases (ADOs) from animals. PCOs oxidize N-terminal cysteine residues, thus preparing the protein for N-end rule pathway-mediated proteasomal degradation [ ]. ADO is responsible for endogenous cysteamine dioxygenase activity [ ].
[ "GO:0016702" ]
[ "oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen" ]
[ "molecular_function" ]
1
[ "PFAM", "PANTHER" ]
[ "PF07847", "PTHR22966" ]
[ "PCO_ADO", "" ]
[ 6015, 6040 ]
2
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.13.11.20", "PWY-5331", "R-DDI-1614558", "R-HSA-1614558", "R-MMU-1614558" ]
[ "EC:1.13.11.20", "METACYC:PWY-5331", "REACTOME:R-DDI-1614558", "REACTOME:R-HSA-1614558", "REACTOME:R-MMU-1614558" ]
5
[ "6s0p", "6s7e", "6sbp", "7chi", "7chj", "7cxz", "7lvz", "7rei", "8u9j", "8uan", "9dma", "9dxb", "9dxu", "9dxv", "9dy4" ]
15
[ "PUB00074379", "PUB00074380" ]
[ "24599061", "17581819" ]
[ "Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway.", "Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase." ]
[ 2014, 2007 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "hydrothermal vent metagenome" ]
[ 27, 6278, 1 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 24, 1, 3, 1, 3, 2, 308, 2, 59 ]
9
true
Family
Cysteine oxygenase/2-aminoethanethiol dioxygenase
Cysteine oxygenase/2-aminoethanethiol dioxygenase
PCO/ADO
1
IPR012865
12,865
Protein of unknown function DUF1642
DUF1642
Family
1,349
false
false
This entry represents a group of phage and prophage proteins whose function is not known.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07852" ]
[ "DUF1642" ]
[ 1349 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Halobaculum halobium", "Viruses", "Zophobas morio" ]
[ 966, 1, 381, 1 ]
4
[]
[]
0
true
Family
Protein of unknown function DUF1642
Protein of unknown function DUF1642
DUF1642
3
IPR012867
12,867
Domain of unknown function DUF1648
DUF1648
Domain
7,336
false
false
This domain is found in proteins expressed by bacterial and archaeal species. One such protein is immunity protein SdpI ( ) from Bacillus subtilis, which provides protection for the cell against the toxic effects of its own SdpC killing factor, and also functions as a receptor/signal transduction protein [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF07853" ]
[ "DUF1648" ]
[ 7336 ]
1
[]
[]
[]
0
[]
0
[ "PUB00055038" ]
[ "16469701" ]
[ "A three-protein signaling pathway governing immunity to a bacterial cannibalism toxin." ]
[ 2006 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 299, 6933, 50, 54 ]
4
[]
[]
0
true
Domain
Domain of unknown function DUF1648
Domain of unknown function DUF1648
DUF1648
2
IPR012869
12,869
CopG-like ribbon-helix-helix domain
RHH_5
Domain
891
false
false
This entry represents a domain found in a group of bacterial proteins that form a ribbon-helix-helix fold. This fold occurs in many examples of bacterial antitoxins [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF07878" ]
[ "RHH_5" ]
[ 891 ]
1
[]
[]
[]
0
[]
0
[ "PUB00075548" ]
[ "15864262" ]
[ "Prokaryotic toxin-antitoxin stress response loci." ]
[ 2005 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Viruses", "metagenomes" ]
[ 11, 855, 9, 16 ]
4
[]
[]
0
true
Domain
CopG-like ribbon-helix-helix domain
CopG-like ribbon-helix-helix domain
RHH_5
6
IPR012870
12,870
Protein of unknown function DUF1666
DUF1666
Family
3,099
false
false
These sequences are derived from hypothetical plant proteins of unknown function. The region in question is approximately 250 residues long.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07891" ]
[ "DUF1666" ]
[ 3099 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Spermatophyta" ]
[ 3099 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 33, 9, 28 ]
3
true
Family
Protein of unknown function DUF1666
Protein of unknown function DUF1666
DUF1666
8
IPR012871
12,871
Protein of unknown function DUF1677, Oryza sativa
DUF1668_ORYSA
Family
4,407
false
false
The hypothetical proteins found in this family are expressed by Oryza sativa (Rice) and are of unknown function.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07893" ]
[ "DUF1668" ]
[ 4407 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Eukaryota", "Motilibacter peucedani" ]
[ 4406, 1 ]
2
[ "Oryza sativa subsp. japonica", "Zea mays" ]
[ 243, 10 ]
2
true
Family
Protein of unknown function DUF1677, Oryza sativa
Protein of unknown function DUF1677, Oryza sativa
DUF1668_ORYSA
2
IPR012873
12,873
Protein of unknown function DUF1672
DUF1672
Family
473
false
false
This family is composed of hypothetical bacterial proteins of unknown function.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07901" ]
[ "DUF1672" ]
[ 473 ]
1
[]
[]
[]
0
[ "4qpv" ]
1
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "human gut metagenome" ]
[ 471, 2 ]
2
[]
[]
0
true
Family
Protein of unknown function DUF1672
Protein of unknown function DUF1672
DUF1672
5
IPR012874
12,874
Protein of unknown function DUF1673, Methanosarcina species
DUF1673_METspp
Family
297
false
false
This family contains hypothetical proteins of unknown function found in Methanosarcina acetivorans and Methanosarcina mazei.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07895" ]
[ "DUF1673" ]
[ 297 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Methanomicrobia", "ecological metagenomes" ]
[ 294, 3 ]
2
[]
[]
0
true
Family
Protein of unknown function DUF1673, Methanosarcina species
Protein of unknown function DUF1673, Methanosarcina species
DUF1673_METspp
8
IPR012875
12,875
Succinate dehydrogenase assembly factor 4
SDHF4
Family
6,893
false
false
This entry includes SDHF4 from animals, Sdh8 from budding yeasts and some uncharacterised proteins from bacteria. Sdh8 is required for assembly of succinate dehydrogenase (SDH). It interacts with the catalytic Sdh1 subunit in the mitochondrial matrix, facilitating its association with Sdh2 and the subsequent assembly o...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07896" ]
[ "DUF1674" ]
[ 6893 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DDI-9854311", "R-HSA-9854311", "R-MMU-9854311", "R-SCE-9854311", "R-SPO-9854311" ]
[ "REACTOME:R-DDI-9854311", "REACTOME:R-HSA-9854311", "REACTOME:R-MMU-9854311", "REACTOME:R-SCE-9854311", "REACTOME:R-SPO-9854311" ]
5
[ "2k5k", "8dyd", "8dye" ]
3
[ "PUB00092519" ]
[ "24954416" ]
[ "SDHAF4 promotes mitochondrial succinate dehydrogenase activity and prevents neurodegeneration." ]
[ 2014 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences", "uncultured virus" ]
[ 3054, 3808, 30, 1 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 4, 1, 1, 3, 2, 1, 1, 2, 3, 1, 1, 2 ]
12
true
Family
Succinate dehydrogenase assembly factor 4
Succinate dehydrogenase assembly factor 4
SDHF4
3
IPR012876
12,876
Protein of unknown function DUF1677, plant
DUF1677_pln
Family
4,485
false
false
The sequences found in this family are all derived from hypothetical plant proteins of unknown function. The region features a number of highly conserved cysteine residues.
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF07911", "PTHR33108" ]
[ "DUF1677", "" ]
[ 4485, 4375 ]
2
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4485 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 29, 44, 53 ]
3
true
Family
Protein of unknown function DUF1677, plant
Protein of unknown function DUF1677, plant
DUF1677_pln
5
IPR012877
12,877
Uncharacterised oxidoreductase Dhs-27
Dhs-27
Family
2,238
false
false
This region is found in a number of Caenorhabditis elegans and Caenorhabditis briggsae proteins, in one case ( ) as a repeat. In many of the family members, this region is associated with the CHK region described by SMART as being found in zinc finger-C4 and HLH domain-containing kinases.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07914" ]
[ "DUF1679" ]
[ 2238 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 45, 2193 ]
2
[ "Caenorhabditis elegans" ]
[ 37 ]
1
true
Family
Uncharacterised oxidoreductase Dhs-27
Uncharacterised oxidoreductase Dhs-27
Dhs-27
6
IPR012878
12,878
Non-reducing end beta-L-arabinofuranosidase-like, GH127 catalytic domain
Beta-AFase-like_GH127_cat
Domain
16,879
false
false
This entry represents the catalytic domain of Non-reducing end beta-L-arabinofuranosidase from Bifidobacterium longum (Beta-AFase) and similar proteins widespread among all cellular organisms that belong to the glycoside hydrolase family 127 (GH127). This domain folds into an (α/α)6 barrel [ ]. Beta-AFase, an unusual b...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07944" ]
[ "Beta-AFase-like_GH127_cat" ]
[ 16879 ]
1
[]
[]
[]
0
[ "3wkw", "3wkx", "3wre", "3wrf", "3wrg", "4qjy", "4qk0", "5mqo", "5opj", "6ex6", "6yqh", "7bzl", "7dif", "7exu", "7exv", "7exw", "8k7x", "8k7y", "8qf2", "8qf8" ]
20
[ "PUB00075450", "PUB00151606" ]
[ "24385433", "24680821" ]
[ "Characterization of a novel β-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 protein family member.", "Crystal structure of glycoside hydrolase family 127 β-l-arabinofuranosidase from Bifidobacterium longum." ]
[ 2014, 2014 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 81, 13498, 3151, 149 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 9, 10, 24 ]
3
true
Domain
Non-reducing end beta-L-arabinofuranosidase-like, GH127 catalytic domain
Non-reducing end beta-L-arabinofuranosidase-like, GH127 catalytic domain
Beta-AFase-like_GH127_cat
7
IPR012879
12,879
PAT complex subunit CCDC47
CCDC47
Family
4,841
false
false
This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes [ ]. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by ...
[ "GO:0005509", "GO:0032469", "GO:0005783" ]
[ "calcium ion binding", "endoplasmic reticulum calcium ion homeostasis", "endoplasmic reticulum" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER" ]
[ "PF07946", "PTHR12883" ]
[ "CCDC47", "" ]
[ 4827, 4777 ]
2
[]
[]
[]
0
[ "6w6l", "7tm3", "7tut", "9i78" ]
4
[ "PUB00097217", "PUB00097218", "PUB00097241", "PUB00097242", "PUB00097243" ]
[ "12475939", "32814900", "32820719", "30401460", "25009997" ]
[ "Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein.", "An intramembrane chaperone complex facilitates membrane protein biogenesis.", "An ER translocon for multi-pass membrane protein biogenesis.", "Bi-allelic CCDC47 Vari...
[ 2002, 2020, 2020, 2018, 2014 ]
5
[]
[]
0
0
null
[ "Candidatus Heimdallarchaeum aukensis", "Eukaryota" ]
[ 1, 4840 ]
2
[ "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...
[ 8, 1, 1, 2, 2, 4, 1, 4, 2, 1, 1, 10 ]
12
true
Family
PAT complex subunit CCDC47
PAT complex subunit CCDC47
CCDC47
9
IPR012880
12,880
Gryzun, putative trafficking through Golgi
Gryzun
Domain
1,653
false
false
The proteins featured in this family are all eukaryotic, and many of them are annotated as being Gryzun. Gryzun is distantly related to, but distinct from, the Trs130 subunit of the TRAPP complex but is absent from S. cerevisiae. RNAi of human Gryzun ( ) blocks Golgi exit. Thus the family is likely to be involved with ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07919" ]
[ "Gryzun" ]
[ 1653 ]
1
[]
[]
[]
0
[]
0
[ "PUB00075580" ]
[ "19942856" ]
[ "A genome-wide RNA interference screen identifies two novel components of the metazoan secretory pathway." ]
[ 2010 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1653 ]
1
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Domain
Gryzun, putative trafficking through Golgi
Gryzun, putative trafficking through Golgi
Gryzun
7
IPR012881
12,881
Protein of unknown function DUF1685
DUF1685
Family
4,078
false
false
The members of this family are hypothetical eukaryotic proteins of unknown function. The region in question is approximately 100 amino acid residues long.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07939" ]
[ "DUF1685" ]
[ 4078 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Embryophyta" ]
[ 4078 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 48, 20, 27 ]
3
true
Family
Protein of unknown function DUF1685
Protein of unknown function DUF1685
DUF1685
2
IPR012883
12,883
ERp29, N-terminal
ERp29_N
Domain
1,274
false
false
ERp29 ( ) is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle [ , ]. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organised into a...
[ "GO:0009306", "GO:0005788" ]
[ "protein secretion", "endoplasmic reticulum lumen" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "CDD" ]
[ "PF07912", "cd03007" ]
[ "ERp29_N", "PDI_a_ERp29_N" ]
[ 1274, 243 ]
2
[]
[]
[]
0
[ "1g7e", "1ovn", "2c0e", "2c0f", "2c0g", "2c1y", "2qc7" ]
7
[ "PUB00014099", "PUB00016490", "PUB00029610" ]
[ "11435111", "10727933", "12941941" ]
[ "Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.", "Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells evidence for a unique role in secretory-protein synthesis.", "Crystal struct...
[ 2001, 2000, 2003 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1274 ]
1
[ "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 4, 2, 3 ]
4
true
Domain
ERp29, N-terminal
ERp29, N-terminal
ERp29_N
8
IPR012885
12,885
Sdz-33, F-box domain
F-box_Sdz-33
Domain
4,855
false
false
This entry represents an F-box domain in Sdz-33, Sdz-15, Hecw-1 and uncharacterised proteins in Caenorhabditis elegans. F-box associated domain-containing protein SDZ-33 (Sdz-33) functions as the substrate recognition component of the E3 ubiquitin-protein ligase complex, mediating the ubiquitination and subsequent prot...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07735" ]
[ "FBA_2" ]
[ 4855 ]
1
[ "REACTOME", "REACTOME" ]
[ "R-CEL-4641258", "R-CEL-983168" ]
[ "REACTOME:R-CEL-4641258", "REACTOME:R-CEL-983168" ]
2
[]
0
[ "PUB00091144", "PUB00160782", "PUB00160783" ]
[ "22089131", "33514673", "2208913" ]
[ "Natural polymorphisms in C. elegans HECW-1 E3 ligase affect pathogen avoidance behaviour.", "<i>Caenorhabditis elegans</i> F-Box Protein Promotes Axon Regeneration by Inducing Degradation of the Mad Transcription Factor.", "[Long-term experience with a PACS subsystem]." ]
[ 2011, 2021, 1990 ]
3
[]
[]
0
0
null
[ "Caenorhabditis", "Thermodesulfobium acidiphilum" ]
[ 4854, 1 ]
2
[ "Caenorhabditis elegans" ]
[ 183 ]
1
true
Domain
Sdz-33, F-box domain
Sdz-33, F-box domain
F-box_Sdz-33
8
IPR012886
12,886
Formiminotransferase, N-terminal subdomain
Formiminotransferase_N
Domain
5,185
false
false
The formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD) forms a homodimer, with each protomer being comprised of two subdomains. The formiminotransferase domain has an N-terminal subdomain that is made up of a six-stranded mixed β-pleated sheet and five α-helices, which are arranged on the ex...
[ "GO:0005542", "GO:0016740" ]
[ "folic acid binding", "transferase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "SMART" ]
[ "PF07837", "SM01222" ]
[ "FTCD_N", "FTCD_N" ]
[ 5179, 5087 ]
2
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.1.2.5", "PWY-5030", "R-DDI-70921", "R-HSA-70921", "R-MMU-70921", "R-RNO-70921" ]
[ "EC:2.1.2.5", "METACYC:PWY-5030", "REACTOME:R-DDI-70921", "REACTOME:R-HSA-70921", "REACTOME:R-MMU-70921", "REACTOME:R-RNO-70921" ]
6
[ "1qd1", "1tt9", "2pfd" ]
3
[ "PUB00007432" ]
[ "10673422" ]
[ "The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 38, 1750, 3237, 160 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 8, 22, 7, 1, 10, 2, 40 ]
7
true
Domain
Formiminotransferase, N-terminal subdomain
Formiminotransferase, N-terminal subdomain
Formiminotransferase_N
7
IPR012887
12,887
GDP-fucose pyrophosphorylase domain
GDP_fucose_pyrophosphorylase
Domain
3,903
false
false
This entry represents the fucose pyrophosphorylase domain found at the N-terminal of the bifunctional L-Fucokinase/GDP-Fucose Pyrophosphorylase (FKP) enzymes such as FKGP from Arabidopsis and L-fucose kinase from animals [ , ]. In fucose-1-phosphate guanylyltransferase from human, this is the main domain of the protein...
[ "GO:0016772" ]
[ "transferase activity, transferring phosphorus-containing groups" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF07959" ]
[ "Fucose_pyrophosphorylase" ]
[ 3903 ]
1
[ "EC", "EC", "METACYC", "REACTOME", "REACTOME" ]
[ "2.7.1.52", "2.7.7.30", "PWY-6", "R-HSA-6787639", "R-MMU-6787639" ]
[ "EC:2.7.1.52", "EC:2.7.7.30", "METACYC:PWY-6", "REACTOME:R-HSA-6787639", "REACTOME:R-MMU-6787639" ]
5
[ "5yys", "9iis", "9iit" ]
3
[ "PUB00015901", "PUB00016201", "PUB00155376", "PUB00155377", "PUB00155378" ]
[ "9804772", "14686921", "15774760", "18199744", "30242642" ]
[ "GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme.", "Cloning and expression of murine enzymes involved in the salvage pathway of GDP-L-fucose.", "Human symbionts use a host-like pathway for surface fucosylation.", "A bifunctional enzyme with L-fucokinase and GDP-L-fuco...
[ 1998, 2004, 2005, 2008, 2019 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 452, 3443, 8 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 9, 2, 2, 15, 4, 5, 13, 7 ]
8
true
Domain
GDP-fucose pyrophosphorylase domain
GDP-fucose pyrophosphorylase domain
GDP_fucose_pyrophosphorylase
9
IPR012889
12,889
L-fucose isomerase, N-terminal-2
Fucose_isomerase_N2
Domain
3,020
false
false
Proteins containing this domain are similar to L-fucose isomerase expressed by Escherichia coli ( , ). This enzyme corresponds to glucose-6-phosphate isomerase in glycolysis, and converts an aldo-hexose to a ketose to prepare it for aldol cleavage. The enzyme is a hexamer, with each subunit being wedge-shaped and compo...
[ "GO:0008736", "GO:0006004", "GO:0005737" ]
[ "L-fucose isomerase activity", "fucose metabolic process", "cytoplasm" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF07882" ]
[ "Fucose_iso_N2" ]
[ 3020 ]
1
[ "EC" ]
[ "5.3.1.25" ]
[ "EC:5.3.1.25" ]
1
[ "1fui", "3a9r", "3a9s", "3a9t", "4c20", "4c21", "4c22", "6k1f", "6k1g" ]
9
[ "PUB00007428" ]
[ "9367760" ]
[ "Structure and mechanism of L-fucose isomerase from Escherichia coli." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 8, 2956, 4, 52 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
L-fucose isomerase, N-terminal-2
L-fucose isomerase, N-terminal-2
Fucose_isomerase_N2
3
IPR012891
12,891
GCK domain
GCK_dom
Domain
1,421
false
false
This domain is found in proteins carrying other domains known to be involved in intracellular signalling pathways indicating that it might also be involved in these pathways. It has 4 highly conserved cysteine residues, suggesting that it can bind zinc ions. Moreover, it is found repeated in some members of this entry ...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF07802", "SM01227" ]
[ "GCK", "GCK" ]
[ 1366, 1376 ]
2
[]
[]
[]
0
[]
0
[ "PUB00099757" ]
[ "19011240" ]
[ "Structural and functional roles of the conserved cysteine residues of the redox-regulated import receptor Mia40 in the intermembrane space of mitochondria." ]
[ 2009 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1421 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 39, 5, 8 ]
3
true
Domain
GCK domain
GCK domain
GCK_dom
3
IPR012892
12,892
Gp58-like
Gp58
Domain
354
false
false
Sequences found in this entry are derived from a number of bacteriophage and prophage proteins. They are similar to gp58 ( ), a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF07902" ]
[ "Gp58" ]
[ 354 ]
1
[]
[]
[]
0
[]
0
[ "PUB00016531" ]
[ "7828907" ]
[ "Characterization of the genome region encoding structural proteins of Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H." ]
[ 1994 ]
1
[]
[]
0
0
null
[ "Bacteria", "Psylliodes chrysocephalus", "Viruses" ]
[ 314, 1, 39 ]
3
[]
[]
0
true
Domain
Gp58-like
Gp58-like
Gp58
2
IPR012893
12,893
HipA-like, C-terminal
HipA-like_C
Domain
17,708
false
false
The members of this entry are similar to a region close to the C terminus of the HipA protein expressed by various bacterial species (for example ). This protein is known to be involved in high-frequency persistence to the lethal effects of inhibition of either DNA or peptidoglycan synthesis [ ]. When expressed alone, ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07804" ]
[ "HipA_C" ]
[ 17708 ]
1
[]
[]
[]
0
[ "2wiu", "3akj", "3akk", "3akl", "3dnt", "3dnu", "3dnv", "3fbr", "3hzi", "3tpb", "3tpd", "3tpe", "3tpt", "3tpv", "4pu3", "4pu4", "4pu5", "4yg7", "5k98", "7ab3", "7ab4", "7ab5", "7vkb", "7vkc", "7wcf", "8ezr", "8ezs" ]
27
[ "PUB00016369", "PUB00016440", "PUB00055674" ]
[ "8021189", "1715862", "21098302" ]
[ "Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis.", "Structure and organization of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis.", "Helicobacter pylori proinflammatory protein up-regulates NF-kappaB as a cel...
[ 1994, 1991, 2010 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "IncJ plasmid R391", "Methanosarcinaceae", "Siphoviridae sp. ctg0K17", "unclassified sequences" ]
[ 17293, 29, 1, 5, 1, 379 ]
6
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Domain
HipA-like, C-terminal
HipA-like, C-terminal
HipA-like_C
6
IPR012896
12,896
Integrin beta subunit, tail
Integrin_bsu_tail
Domain
11,507
false
false
This entry represents the tail domain of the integrin beta subunit. It forms a four-stranded β-sheet that contains parallel and antiparallel strands and faces an α helix found at the N terminus of this domain [ ]. Interactions between the α-helix and the β-sheet are mostly hydrophobic and involve a disulphide bond. The...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF07965", "SM01242" ]
[ "Integrin_B_tail", "Integrin_B_tail" ]
[ 10080, 11497 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-1566948", "R-BTA-166016", "R-BTA-198933", "R-BTA-202733", "R-BTA-2129379", "R-BTA-216083", "R-BTA-2173789", "R-BTA-3000178", "R-BTA-6798695", "R-CEL-114608", "R-CEL-1236973", "R-CEL-2129379", "R-CEL-216083", "R-CEL-2173789", "R-CEL-3000157", "R-CEL-3000170", "R-CEL-3000178", ...
[ "REACTOME:R-BTA-1566948", "REACTOME:R-BTA-166016", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-202733", "REACTOME:R-BTA-2129379", "REACTOME:R-BTA-216083", "REACTOME:R-BTA-2173789", "REACTOME:R-BTA-3000178", "REACTOME:R-BTA-6798695", "REACTOME:R-CEL-114608", "REACTOME:R-CEL-1236973", "REACTOME:R-C...
158
[ "1jv2", "1l5g", "1m1x", "1u8c", "3fcs", "3ije", "3k6s", "3k71", "3k72", "4cak", "4g1e", "4g1m", "4mmx", "4mmy", "4mmz", "4neh", "4nen", "4o02", "4um8", "5es4", "6avq", "6avr", "6avu", "6bxj", "6mk0", "6msl", "6msu", "6naj", "7la4", "7nwl", "7nxd", "7usl"...
68
[ "PUB00006148", "PUB00009789", "PUB00015915", "PUB00015985", "PUB00026539", "PUB00035000", "PUB00035002", "PUB00057248", "PUB00160425" ]
[ "9009218", "12297042", "14689578", "2467745", "11546839", "12361595", "12234368", "12388743", "28510180" ]
[ "A structure prediction for the ligand-binding region of the integrin beta subunit: evidence for the presence of a von Willebrand factor A domain.", "Integrins: bidirectional, allosteric signaling machines.", "Integrin clipping: a novel adhesion switch?", "A novel vitronectin receptor integrin (alpha v beta x...
[ 1997, 2002, 2004, 1989, 2001, 2002, 2002, 2002, 2014 ]
9
[]
[]
0
0
null
[ "Metazoa" ]
[ 11507 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 28, 3, 32, 19, 32 ]
6
true
Domain
Integrin beta subunit, tail
Integrin beta subunit, tail
Integrin_bsu_tail
3
IPR012897
12,897
Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain
K_chnl_volt-dep_Kv1.4_TID
Domain
688
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0005249", "GO:0030955", "GO:0006813", "GO:0016020" ]
[ "voltage-gated potassium channel activity", "potassium ion binding", "potassium ion transport", "membrane" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM" ]
[ "PF07941" ]
[ "K_channel_TID" ]
[ 688 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1296072", "R-MMU-1296072", "R-RNO-1296072" ]
[ "REACTOME:R-HSA-1296072", "REACTOME:R-MMU-1296072", "REACTOME:R-RNO-1296072" ]
3
[ "1kn7", "1zto" ]
2
[ "PUB00001055", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00007312", "PUB00008322", "PUB00009378", "PUB00009391", "PUB00016528", "PUB00036044" ]
[ "1772658", "1879548", "1373731", "2448635", "2451788", "2555158", "10798390", "9305895", "11178249", "10712896", "12590144", "11343973" ]
[ "The molecular biology of K+ channels.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Droso...
[ 1991, 1991, 1992, 1988, 1988, 1989, 2000, 1997, 2000, 2000, 2003, 2000 ]
12
[]
[]
0
0
null
[ "Bacillati", "Opisthokonta" ]
[ 2, 686 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 1, 3 ]
4
true
Domain
Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain
Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain
K_chnl_volt-dep_Kv1.4_TID
5
IPR012899
12,899
LTXXQ motif family protein
LTXXQ
Family
9,433
false
false
This family summarizes bacterial proteins related to CpxP, a periplasmic protein that forms part of a two-component system which acts as a global modulator of cell-envelope stress in Gram-negative bacteria. CpxP aids in combating extracytoplasmic protein-mediated toxicity, and may also be involved in the response to al...
[ "GO:0042597" ]
[ "periplasmic space" ]
[ "cellular_component" ]
1
[ "PFAM", "PIRSF", "CDD" ]
[ "PF07813", "PIRSF034445", "cd09916" ]
[ "LTXXQ", "CpxP_Spy", "CpxP_like" ]
[ 8874, 2799, 4696 ]
3
[]
[]
[]
0
[ "3itf", "3o39", "3oeo", "3qzc", "5ihf", "5io8", "5wnw", "5wo1", "5wo2", "5wo3", "6bie", "6owx", "6owy", "6owz" ]
14
[ "PUB00016508", "PUB00016553", "PUB00055384", "PUB00061476" ]
[ "9068658", "9473036", "20799348", "21239493" ]
[ "A new periplasmic protein of Escherichia coli which is synthesized in spheroplasts but not in intact cells.", "CpxP, a stress-combative member of the Cpx regulon.", "The crystal structure Escherichia coli Spy.", "Structural basis for two-component system inhibition and pilus sensing by the auxiliary CpxP pro...
[ 1997, 1998, 2010, 2011 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Thermococcus litoralis", "unclassified sequences" ]
[ 9324, 19, 1, 89 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
LTXXQ motif family protein
LTXXQ motif family protein
LTXXQ
8
IPR012900
12,900
G-box binding protein, multifunctional mosaic region
MFMR
Domain
3,421
false
false
This region is often found to the N terminus of the basic-leucine zipper domain ( ). It is between 150 and 200 amino acids in length. The N-terminal half of this domain is rich in proline residues and has been termed the PRD (proline rich domain) [ ], whereas the C-terminal half is more polar and has been called the MF...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07777" ]
[ "MFMR" ]
[ 3421 ]
1
[]
[]
[]
0
[]
0
[ "PUB00016443", "PUB00016500" ]
[ "11722549", "8127687" ]
[ "Plant bZIP G-box binding factors. Modular structure and activation mechanisms.", "Novel conserved sequence motifs in plant G-box binding proteins and implications for interactive domains." ]
[ 2001, 1994 ]
2
[]
[]
0
0
null
[ "Streptophytina" ]
[ 3421 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 23, 14, 54 ]
3
true
Domain
G-box binding protein, multifunctional mosaic region
G-box binding protein, multifunctional mosaic region
MFMR
2
IPR012901
12,901
Carnosine N-methyltransferase
CARME
Family
6,098
false
false
This family includes Carnosine N-methyltransferase ( ), conserved from yeast to human, that catalyses the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. It a...
[ "GO:0008757" ]
[ "S-adenosylmethionine-dependent methyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PANTHER", "SMART" ]
[ "PF07942", "PTHR12303", "SM01296" ]
[ "CARME", "", "N2227" ]
[ 6031, 6014, 5888 ]
3
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.1.1.22", "R-DDI-70921", "R-DME-70921", "R-GGA-70921", "R-HSA-70921", "R-MMU-70921", "R-RNO-70921", "R-SCE-70921", "R-SPO-70921" ]
[ "EC:2.1.1.22", "REACTOME:R-DDI-70921", "REACTOME:R-DME-70921", "REACTOME:R-GGA-70921", "REACTOME:R-HSA-70921", "REACTOME:R-MMU-70921", "REACTOME:R-RNO-70921", "REACTOME:R-SCE-70921", "REACTOME:R-SPO-70921" ]
9
[ "5x62", "5yf0", "5yf1", "5yf2" ]
4
[ "PUB00098813", "PUB00098814", "PUB00098815", "PUB00158949" ]
[ "26001783", "29463897", "28654751", "38514639" ]
[ "UPF0586 Protein C9orf41 Homolog Is Anserine-producing Methyltransferase.", "Molecular basis for histidine N1 position-specific methylation by CARNMT1.", "Substrate Recognition Mechanism of the Putative Yeast Carnosine N-methyltransferase.", "An evolutionary mechanism to assimilate new nutrient sensors into t...
[ 2015, 2018, 2017, 2024 ]
4
[]
[ "IPR016853" ]
0
1
0
[ "Bacteria", "Eukaryota" ]
[ 29, 6069 ]
2
[ "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...
[ 16, 2, 3, 1, 4, 1, 1, 3, 3, 2, 1, 10 ]
12
true
Family
Carnosine N-methyltransferase
Carnosine N-methyltransferase
CARME
1
IPR012902
12,902
Prokaryotic N-terminal methylation site
N_methyl_site
PTM
126,085
false
false
This short motif directs methylation of the conserved phenylalanine residue. It is most often found at the N terminus of pilins and other proteins involved in secretion (see , , and ).
[]
[]
[]
0
[ "PFAM", "PROSITE", "NCBIFAM" ]
[ "PF07963", "PS00409", "TIGR02532" ]
[ "N_methyl", "PROKAR_NTER_METHYL", "IV_pilin_GFxxxE" ]
[ 116930, 83217, 116067 ]
3
[ "GP" ]
[ "GenProp0295" ]
[ "GP:GenProp0295" ]
1
[ "1ay2", "1oqw", "2hi2", "2hil", "2m7g", "2pil", "3jc8", "3jc9", "3sok", "5g23", "5g24", "5kua", "5vxx", "5vxy", "5wda", "6gv9", "6vk9", "6xxd", "6xxe", "7tgg", "8p2v", "8p36", "8p3b", "8pfb", "8pij", "8piz", "8pjp", "8qqd", "8qqj", "8tj2", "8tob", "8tum"...
36
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 16, 123338, 51, 144, 2536 ]
5
[ "Escherichia coli (strain K12)" ]
[ 8 ]
1
true
PTM
Prokaryotic N-terminal methylation site
Prokaryotic N-terminal methylation site
N_methyl_site
6
IPR012903
12,903
Nif11 domain
Nif11
Domain
1,625
false
false
This domain is found mainly in the Cyanobacteria and in Proteobacteria such as the nitrogen-fixing bacterium Azotobacter vinelandii. It is found in Nif11, a protein described in Azotobacter as linked to nitrogen fixation [ ]. It also constitutes a leader peptide in Nif11-derived peptides (N11P), which are thought to be...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07862" ]
[ "Nif11" ]
[ 1625 ]
1
[]
[]
[]
0
[]
0
[ "PUB00016451", "PUB00055015", "PUB00068006" ]
[ "2644218", "20500830", "20479271" ]
[ "Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii.", "Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family.", "Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobact...
[ 1989, 2010, 2010 ]
3
[]
[ "IPR022516" ]
0
1
0
[ "Bacteria", "Methanoplanus endosymbiosus", "Mycobacterium phage Mendokysei", "ecological metagenomes" ]
[ 1589, 5, 1, 30 ]
4
[]
[]
0
true
Domain
Nif11 domain
Nif11 domain
Nif11
6
IPR012904
12,904
8-oxoguanine DNA glycosylase, N-terminal
OGG_N
Domain
7,197
false
false
The presence of 8-oxoguanine residues in DNA can give rise to G-C to T-A transversion mutations. This enzyme is found in archaeal, bacterial and eukaryotic species, and is specifically responsible for the process which leads to the removal of 8-oxoguanine residues. It has DNA glycosylase activity ( ) and DNA lyase acti...
[ "GO:0003684", "GO:0008534", "GO:0006289" ]
[ "damaged DNA binding", "oxidized purine nucleobase lesion DNA N-glycosylase activity", "nucleotide-excision repair" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF07934" ]
[ "OGG_N" ]
[ 7197 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.2.2.-", "4.2.99.18", "PWY-2681", "PWY-5316", "PWY-5381", "PWY-7342", "PWY-7564", "PWY-8106", "R-DME-110329", "R-DME-110330", "R-DME-110331", "R-DME-110357", "R-HSA-110328", "R-HSA-110329", "R-HSA-110330", "R-HSA-110331", "R-HSA-110357", "R-HSA-5649702", "R-HSA-9656255", "R-H...
[ "EC:3.2.2.-", "EC:4.2.99.18", "METACYC:PWY-2681", "METACYC:PWY-5316", "METACYC:PWY-5381", "METACYC:PWY-7342", "METACYC:PWY-7564", "METACYC:PWY-8106", "REACTOME:R-DME-110329", "REACTOME:R-DME-110330", "REACTOME:R-DME-110331", "REACTOME:R-DME-110357", "REACTOME:R-HSA-110328", "REACTOME:R-HSA...
34
[ "1ebm", "1fn7", "1hu0", "1ko9", "1lwv", "1lww", "1lwy", "1m3h", "1m3q", "1n39", "1n3a", "1n3c", "1yqk", "1yql", "1yqm", "1yqr", "2i5w", "2nob", "2noe", "2nof", "2noh", "2noi", "2nol", "2noz", "2xhi", "3f0z", "3f10", "3i0w", "3i0x", "3ih7", "3ktu", "4ejy"...
73
[ "PUB00013719", "PUB00016467" ]
[ "10706276", "11902834" ]
[ "Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA.", "Reciprocal \"flipping\" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase." ]
[ 2000, 2002 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 549, 2186, 4409, 53 ]
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)", "...
[ 3, 3, 3, 14, 4, 1, 3, 4, 1, 4 ]
10
true
Domain
8-oxoguanine DNA glycosylase, N-terminal
8-oxoguanine DNA glycosylase, N-terminal
OGG_N
6
IPR012905
12,905
PA-IL-like
PA-IL
Family
145
false
false
The members of this family are similar to the galactophilic lectin-1 expressed by Pseudomonas aeruginosa (PA-IL, ). Lectins recognising specific carbohydrates found on the surface of host cells are known to be involved in the initiation of infections by this organism. The protein is thought to be organised into an exte...
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF07828", "PIRSF020485" ]
[ "PA-IL", "PA-IL" ]
[ 145, 11 ]
2
[]
[]
[]
0
[ "1l7l", "1oko", "1uoj", "2vxj", "2wyf", "3zyb", "3zyf", "3zyh", "4a6s", "4al9", "4cp9", "4cpb", "4ljh", "4lk6", "4lk7", "4lkd", "4lke", "4lkf", "4yw6", "4yw7", "4ywa", "5d21", "5mih", "5odu", "5ofi", "5ofx", "5ofz", "6ygq", "6yo3", "6yoh", "7fio", "7fjh"...
38
[ "PUB00016484" ]
[ "1429650" ]
[ "Analysis of the amino acid sequence of the Pseudomonas aeruginosa galactophilic PA-I lectin." ]
[ 1992 ]
1
[]
[]
0
0
null
[ "Acyrthosiphon pisum", "Bacteria" ]
[ 1, 144 ]
2
[]
[]
0
true
Family
PA-IL-like
PA-IL-like
PA-IL
1
IPR012906
12,906
Transcriptional repressor PaaX-like, N-terminal
PaaX-like_N
Domain
8,167
false
false
This entry describes the N-terminal region of Transcriptional repressor PaaX from Escherichia coli and similar bacterial proteins. PaaX is involved in metabolism of phenylacetic acid [ , , ]. The gene product has been shown to bind to the promoter sites and repress their transcription [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF07848" ]
[ "PaaX" ]
[ 8167 ]
1
[]
[]
[]
0
[ "3kfw", "3l09", "8a39" ]
3
[ "PUB00010200", "PUB00015494", "PUB00015522" ]
[ "9748275", "11260461", "10766858" ]
[ "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.", "The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications.", "Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in ...
[ 1998, 2001, 2000 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Opisthokonta", "Siphoviridae sp. ctiMP24", "unclassified sequences" ]
[ 33, 8075, 2, 1, 56 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Transcriptional repressor PaaX-like, N-terminal
Transcriptional repressor PaaX-like, N-terminal
PaaX-like_N
1
IPR012907
12,907
Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal
Peptidase_S11_C
Domain
22,267
false
false
Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...
[ "GO:0009002", "GO:0006508" ]
[ "serine-type D-Ala-D-Ala carboxypeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "SMART" ]
[ "PF07943", "SM00936" ]
[ "PBP5_C", "PBP5_C" ]
[ 22091, 20322 ]
2
[ "EC", "METACYC", "METACYC" ]
[ "3.4.16.4", "PWY-5265", "PWY-6471" ]
[ "EC:3.4.16.4", "METACYC:PWY-5265", "METACYC:PWY-6471" ]
3
[ "1hd8", "1nj4", "1nzo", "1nzu", "1sdn", "1xp4", "1z6f", "3a3j", "3beb", "3bec", "3it9", "3ita", "3itb", "3mfd", "3mzd", "3mze", "3mzf", "4drt", "4k91", "5fsr", "5j8x", "5tr7", "6ntz", "6osu" ]
24
[ "PUB00000522", "PUB00003576", "PUB00016400" ]
[ "8439290", "7845208", "10967102" ]
[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution." ]
[ 1993, 1994, 2001 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Stx2-converting phage 1717", "unclassified sequences" ]
[ 22026, 41, 1, 199 ]
4
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Domain
Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal
Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal
Peptidase_S11_C
4
IPR012908
12,908
GPI inositol-deacylase PGAP1-like alpha/beta domain
PGAP1-ab_dom-like
Domain
10,150
false
false
This domain is found in GPI inositol-deacylase PGAP1 and related proteins. It is found toward the N terminus and it is a lipase domain with a typical α/β/α hydrolase architecture [ ]. PGAP1 is an endoplasmic reticulum membrane protein with a catalytic serine-containing motif that is conserved in a number of lipases. PG...
[ "GO:0016788" ]
[ "hydrolase activity, acting on ester bonds" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF07819" ]
[ "PGAP1" ]
[ 10150 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-162791", "R-MMU-162791", "R-RNO-162791" ]
[ "REACTOME:R-HSA-162791", "REACTOME:R-MMU-162791", "REACTOME:R-RNO-162791" ]
3
[ "6wpx", "6wpy", "8k9q", "8k9r", "8k9t" ]
5
[ "PUB00055596", "PUB00094351", "PUB00155994" ]
[ "14734546", "6319176", "38167496" ]
[ "Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p.", "Hepatic adenylate cyclase and phosphodiesterase activity during acute ethionine intoxication.", "Molecular basis of the inositol deacylase PGAP1 involved in quality control of GPI-AP biogen...
[ 2004, 1984, 2024 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "Viruses", "metagenomes" ]
[ 3564, 6550, 2, 5, 29 ]
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...
[ 13, 1, 2, 1, 3, 1, 2, 6, 3, 1, 1, 26 ]
12
true
Domain
GPI inositol-deacylase PGAP1-like alpha/beta domain
GPI inositol-deacylase PGAP1-like alpha/beta domain
PGAP1-ab_dom-like
6
IPR012909
12,909
PHA accumulation regulator DNA-binding, N-terminal
PHA_DNA-bd_N
Domain
5,168
false
false
This domain is found at the N terminus of the polyhydroxyalkanoate (PHA) synthesis regulators. These regulators have been shown to directly bind DNA and PHA [ ]. The invariant nature of this domain compared to the C-terminal domain(s) suggests that it contains the DNA-binding function.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07879" ]
[ "PHB_acc_N" ]
[ 5168 ]
1
[]
[]
[]
0
[]
0
[ "PUB00013500" ]
[ "12081972" ]
[ "A repressor protein, PhaR, regulates polyhydroxyalkanoate (PHA) synthesis via its direct interaction with PHA." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 5097, 9, 62 ]
3
[]
[]
0
true
Domain
PHA accumulation regulator DNA-binding, N-terminal
PHA accumulation regulator DNA-binding, N-terminal
PHA_DNA-bd_N
4
IPR012910
12,910
TonB-dependent receptor, plug domain
Plug_dom
Domain
352,625
false
false
This entry represents the plug domain, which has been shown to be an independently folding subunit of the TonB-dependent receptors [ ]. It acts as the channel gate, blocking the pore until the channel is bound by a ligand. At this point it undergoes conformational changes and opens the channel. In Escherichia coli the ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07715" ]
[ "Plug" ]
[ 352625 ]
1
[ "GP", "REACTOME", "REACTOME" ]
[ "GenProp0543", "R-HSA-9638334", "R-HSA-9638482" ]
[ "GP:GenProp0543", "REACTOME:R-HSA-9638334", "REACTOME:R-HSA-9638482" ]
3
[ "1by3", "1by5", "1fcp", "1fep", "1fi1", "1kmo", "1kmp", "1nqe", "1nqf", "1nqg", "1nqh", "1pnz", "1po0", "1po3", "1qff", "1qfg", "1qjq", "1qkc", "1ujw", "1xkh", "1xkw", "2fcp", "2grx", "2gsk", "2guf", "2hdf", "2hdi", "2iah", "2o5p", "2w16", "2w6t", "2w6u"...
152
[ "PUB00006673", "PUB00014980", "PUB00014981", "PUB00014984", "PUB00014986", "PUB00015225", "PUB00035726", "PUB00035727" ]
[ "9886293", "14499604", "9865695", "12652322", "11872840", "15111112", "15993072", "12957833" ]
[ "Crystal structure of the outer membrane active transporter FepA from Escherichia coli.", "The Escherichia coli outer membrane cobalamin transporter BtuB: structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation.", "Transmembrane sig...
[ 1999, 2003, 1998, 2003, 2002, 2004, 2005, 2003 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 5, 348587, 502, 18, 3513 ]
5
[ "Escherichia coli (strain K12)" ]
[ 10 ]
1
true
Domain
TonB-dependent receptor, plug domain
TonB-dependent receptor, plug domain
Plug_dom
4
IPR012911
12,911
Protein serine/threonine phosphatase 2C, C-terminal
PP2C_C
Domain
4,539
false
false
Protein phosphatase 2C (PP2C, also known as Protein phosphatase 1) is involved in regulating cellular responses to stress in various eukaryotes. It consists of two domains: an N-terminal catalytic domain and a C-terminal domain characteristic of mammalian PP2Cs. This domain consists of three antiparallel α helices, one...
[ "GO:0000287", "GO:0004721", "GO:0030145" ]
[ "magnesium ion binding", "phosphoprotein phosphatase activity", "manganese ion binding" ]
[ "molecular_function", "molecular_function", "molecular_function" ]
3
[ "PFAM" ]
[ "PF07830" ]
[ "PP2C_C" ]
[ 4539 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.3.16", "R-BTA-1169408", "R-BTA-2173795", "R-BTA-380972", "R-HSA-1169408", "R-HSA-2173795", "R-HSA-380972", "R-HSA-9700645", "R-HSA-9725370", "R-MMU-1169408", "R-MMU-2173795", "R-MMU-380972", "R-RNO-1169408", "R-RNO-2173795", "R-RNO-380972" ]
[ "EC:3.1.3.16", "REACTOME:R-BTA-1169408", "REACTOME:R-BTA-2173795", "REACTOME:R-BTA-380972", "REACTOME:R-HSA-1169408", "REACTOME:R-HSA-2173795", "REACTOME:R-HSA-380972", "REACTOME:R-HSA-9700645", "REACTOME:R-HSA-9725370", "REACTOME:R-MMU-1169408", "REACTOME:R-MMU-2173795", "REACTOME:R-MMU-38097...
15
[ "1a6q", "3fxj", "3fxk", "3fxl", "3fxm", "3fxo", "4ra2", "4raf", "4rag" ]
9
[ "PUB00001297" ]
[ "9003755" ]
[ "Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Metazoa" ]
[ 4539 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 16, 16, 13, 10, 19 ]
5
true
Domain
Protein serine/threonine phosphatase 2C, C-terminal
Protein serine/threonine phosphatase 2C, C-terminal
PP2C_C
3
IPR012912
12,912
Plasmid pRiA4b, Orf3-like domain
Plasmid_pRiA4b_Orf3-like
Domain
8,494
false
false
Members of this entry are similar to the protein product of ORF-3 ( ) found on plasmid pRiA4 in the bacterium Agrobacterium rhizogenes. This plasmid is responsible for tumorigenesis at wound sites of plants infected by this bacterium, but the ORF-3 product does not seem to be involved in the pathogenetic process [ ]. O...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF07929", "PTHR41878" ]
[ "PRiA4_ORF3", "" ]
[ 8493, 5307 ]
2
[]
[]
[]
0
[ "2i1s" ]
1
[ "PUB00016577" ]
[ "2226811" ]
[ "Characterization of the virA gene of the agropine-type plasmid pRiA4 of Agrobacterium rhizogenes." ]
[ 1990 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 182, 7422, 766, 124 ]
4
[]
[]
0
true
Domain
Plasmid pRiA4b, Orf3-like domain
Plasmid pRiA4b, Orf3-like domain
Plasmid_pRiA4b_Orf3-like
3
IPR012913
12,913
Protein OS9-like domain
OS9-like_dom
Domain
7,513
false
false
This entry represents a domain found in the OS9 protein, which is a lectin that functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD) [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF07915" ]
[ "PRKCSH" ]
[ 7513 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-382556", "R-HSA-5358346", "R-HSA-5362768", "R-HSA-5678895", "R-HSA-901032", "R-MMU-382556", "R-MMU-5358346", "R-RNO-382556", "R-RNO-5358346", "R-SPO-5358346" ]
[ "REACTOME:R-HSA-382556", "REACTOME:R-HSA-5358346", "REACTOME:R-HSA-5362768", "REACTOME:R-HSA-5678895", "REACTOME:R-HSA-901032", "REACTOME:R-MMU-382556", "REACTOME:R-MMU-5358346", "REACTOME:R-RNO-382556", "REACTOME:R-RNO-5358346", "REACTOME:R-SPO-5358346" ]
10
[ "3aih", "6f99", "6f9a", "6vk3", "8kes", "8ket", "8kev", "9lwu", "9og0", "9uav" ]
10
[ "PUB00086554" ]
[ "17932042" ]
[ "OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum." ]
[ 2007 ]
1
[ "IPR044865" ]
[]
1
0
1
[ "Eukaryota", "bird metagenome" ]
[ 7511, 2 ]
2
[ "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...
[ 4, 2, 3, 2, 44, 10, 1, 2, 11, 1, 2, 8 ]
12
true
Domain
Protein OS9-like domain
Protein OS9-like domain
OS9-like_dom
5
IPR012914
12,914
Purine catabolism PurC-like domain
PucR_dom
Domain
16,084
false
false
This domain is found in the purine catabolism regulatory protein expressed by Bacillus subtilis (PucR, ). PucR is thought to be a transcriptional regulator of genes involved in the purine degradation pathway, and may contain a LysR-like DNA-binding domain [ ]. It is similar to LysR-type regulators in that it represses ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07905" ]
[ "PucR" ]
[ 16084 ]
1
[]
[]
[]
0
[]
0
[ "PUB00016396", "PUB00057827" ]
[ "11344136", "12029039" ]
[ "Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator.", "Transcription analysis of the Bacillus subtilis PucR regulon and identification of a cis-acting sequence required for PucR-regulate...
[ 2001, 2002 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 16033, 4, 47 ]
3
[]
[]
0
true
Domain
Purine catabolism PurC-like domain
Purine catabolism PurC-like domain
PucR_dom
3
IPR012916
12,916
RED-like, N-terminal
RED_N
Domain
4,263
false
false
This domain contains sequences that are similar to the N-terminal region of Red protein ( ). This and related proteins contain a RED repeat which consists of a number of RE and RD sequence elements [ ]. The region in question has several conserved NLS sequences and a putative trimeric coiled-coil region [ ], suggesting...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07808" ]
[ "RED_N" ]
[ 4263 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-72163", "R-MMU-72163", "R-RNO-72163" ]
[ "REACTOME:R-HSA-72163", "REACTOME:R-MMU-72163", "REACTOME:R-RNO-72163" ]
3
[ "5o9z", "6q8i", "8qo9", "8qzs" ]
4
[ "PUB00016574", "PUB00090272", "PUB00090273" ]
[ "10216252", "28781166", "22351768" ]
[ "Isolation, sequencing and expression of RED, a novel human gene encoding an acidic-basic dipeptide repeat.", "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation.", "RED, a spindle pole-associated protein, is required for kinetochore localization of MAD1, mitotic progression, and activ...
[ 1999, 2017, 2012 ]
3
[]
[]
0
0
null
[ "Acetivibrio clariflavus (strain DSM 19732 / NBRC 101661 / EBR45)", "Eukaryota" ]
[ 1, 4262 ]
2
[ "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", "Schizosaccharomyces pombe (stra...
[ 4, 1, 1, 1, 11, 6, 1, 5, 6, 1, 9 ]
11
true
Domain
RED-like, N-terminal
RED-like, N-terminal
RED_N
5
IPR012917
12,917
Protein of unknown function DUF3294
DUF3294
Family
331
false
false
This family was annotated as mitochondrial ribosomal protein Mrp8, based on the presumed similarity of the S.cerevisiae protein to an E.coli mitochondrial ribosomal protein. However, this similarity is spurious, and the function is not known.
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF07957", "PIRSF022944" ]
[ "DUF3294", "Ribosomal_MRP8_mit" ]
[ 331, 59 ]
2
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Candidatus Iainarchaeum sp.", "Eukaryota", "Pseudomonadota" ]
[ 1, 326, 4 ]
3
[ "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 1 ]
1
true
Family
Protein of unknown function DUF3294
Protein of unknown function DUF3294
DUF3294
2
IPR012918
12,918
RTP801-like
RTP801-like
Family
2,244
false
false
RTP801, also known as REDD1, is the protein product of a hypoxia-inducible factor 1 (HIF-1)- responsive gene and is thought to be involved in various cellular processes [ ]. Both RTP801 and RTP801-like (REDD2) work downstream of AKT and upstream of TSC2 to inhibit mTOR, a serine/threonine kinase that plays an essential...
[ "GO:0009968", "GO:0005737" ]
[ "negative regulation of signal transduction", "cytoplasm" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PANTHER" ]
[ "PF07809", "PTHR12478" ]
[ "RTP801_C", "" ]
[ 2243, 2218 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-5628897", "R-DME-5628897", "R-DRE-5628897", "R-HSA-5628897", "R-MMU-5628897", "R-RNO-5628897", "R-XTR-5628897" ]
[ "REACTOME:R-BTA-5628897", "REACTOME:R-DME-5628897", "REACTOME:R-DRE-5628897", "REACTOME:R-HSA-5628897", "REACTOME:R-MMU-5628897", "REACTOME:R-RNO-5628897", "REACTOME:R-XTR-5628897" ]
7
[ "3lq9", "7mop" ]
2
[ "PUB00016594", "PUB00057842", "PUB00057843" ]
[ "11884613", "15632201", "16423342" ]
[ "Identification of a novel hypoxia-inducible factor 1-responsive gene, RTP801, involved in apoptosis.", "The stress-inducted proteins RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway.", "scylla and charybde, homologues of the human apoptotic gene RTP801, are required for h...
[ 2002, 2005, 2006 ]
3
[]
[]
0
0
null
[ "Eumetazoa" ]
[ 2244 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 5, 5, 5 ]
5
true
Family
RTP801-like
RTP801-like
RTP801-like
5
IPR012919
12,919
SUN domain
SUN_dom
Domain
19,313
false
false
Sad1/UNC-84 (SUN)-domain proteins are inner nuclear membrane (INM) proteins that are part of bridging complexes linking cytoskeletal elements with the nucleoskeleton. Originally identified based on an ~150-amino acid region of homology between the C terminus of the Schizosaccharomyces pombe Sad1 protein and the Caenorh...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF07738", "PS51469" ]
[ "Sad1_UNC", "SUN" ]
[ 18899, 16623 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-983168", "R-DME-983168", "R-HSA-1221632", "R-HSA-983168", "R-MMU-983168" ]
[ "REACTOME:R-CEL-983168", "REACTOME:R-DME-983168", "REACTOME:R-HSA-1221632", "REACTOME:R-HSA-983168", "REACTOME:R-MMU-983168" ]
5
[ "3unp", "4dxr", "4dxs", "4dxt", "4fi9", "5ed8", "5ywz", "6r15", "6r16", "6r2i", "6wmd", "6wme", "6wmf", "6wmg", "7z8y", "8b46", "8b5x" ]
17
[ "PUB00057231", "PUB00072664", "PUB00072665", "PUB00100392" ]
[ "15611647", "16923827", "19807882", "18820457" ]
[ "Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex.", "The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the spindle pole body with the nuclear envelope.", "Characterization of SUN-domain proteins at the higher plant nuclear envelope.", "Drosophi...
[ 2004, 2006, 2010, 2007 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "marine sediment metagenome" ]
[ 12, 19300, 1 ]
3
[ "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...
[ 23, 11, 57, 9, 38, 14, 2, 15, 32, 2, 2, 21 ]
12
true
Domain
SUN domain
SUN domain
SUN_dom
4
IPR012920
12,920
Ribosomal RNA methyltransferase, SPB1-like, C-terminal
rRNA_MeTfrase_SPB1-like_C
Domain
4,547
false
false
This domain is found at the C terminus SPB1-like proteins. This domain interacts with the meandering tail of Erb1 and its removal is required to form the pre-mature inter-subunit surface of the Arx1/Nog2 particle [ , ]. SPB1 is an adoMet-dependent rRNA methyltransferase required for proper assembly of pre-ribosomal par...
[ "GO:0008168", "GO:0006364", "GO:0005634" ]
[ "methyltransferase activity", "rRNA processing", "nucleus" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF07780" ]
[ "Spb1_C" ]
[ 4547 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...
[ "2.1.1.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-5987", "PWY-601", "PWY-6045"...
[ "EC:2.1.1.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", "METACYC:PWY-5729", "METACYC:PWY-5...
149
[ "6elz", "6em5", "6ylx", "7nac", "7nad", "7ohr", "7ohv", "7r6k", "7r6q", "7r72", "7r7a", "7u0h", "8esq", "8esr", "8etc", "8etj", "8fkp", "8fkq", "8fkr", "8fks", "8fkt", "8fku", "8fkv", "8fkw", "8fkx", "8fky", "8i9t", "8i9v", "8i9w", "8i9x", "8i9y", "8i9z"...
35
[ "PUB00016377", "PUB00056208", "PUB00068804", "PUB00068805", "PUB00100534", "PUB00100535" ]
[ "10556316", "15546625", "10648622", "22195017", "32668200", "29245012" ]
[ "Spb1p is a putative methyltransferase required for 60S ribosomal subunit biogenesis in Saccharomyces cerevisiae.", "Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage.", "Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind ...
[ 1999, 2004, 2000, 2011, 2020, 2017 ]
6
[]
[]
0
0
null
[ "Eukaryota", "bird metagenome" ]
[ 4545, 2 ]
2
[ "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...
[ 7, 3, 2, 1, 2, 1, 1, 4, 2, 1, 1, 12 ]
12
true
Domain
Ribosomal RNA methyltransferase, SPB1-like, C-terminal
Ribosomal RNA methyltransferase, SPB1-like, C-terminal
rRNA_MeTfrase_SPB1-like_C
8
IPR012921
12,921
Spen paralogue and orthologue SPOC, C-terminal
SPOC_C
Domain
14,460
false
false
Spen (split end) proteins regulate the expression of key transcriptional effectors in diverse signalling pathways. They are large proteins characterised by N-terminal RNA-binding motifs and a highly conserved C-terminal SPOC (Spen paralog and ortholog C-terminal) domain. The function of the SPOC domain is unknown, but ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07744" ]
[ "SPOC" ]
[ 14460 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1221632", "R-HSA-9013422", "R-HSA-9845323", "R-MMU-9013422" ]
[ "REACTOME:R-HSA-1221632", "REACTOME:R-HSA-9013422", "REACTOME:R-HSA-9845323", "REACTOME:R-MMU-9013422" ]
4
[ "1ow1", "2rt5", "4bxz", "5kxf", "6ic8", "6ic9", "6q2v", "6q5y", "7z1k", "7z27", "8ou1" ]
11
[ "PUB00013949" ]
[ "12897056" ]
[ "A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling." ]
[ 2003 ]
1
[]
[ "IPR010912" ]
0
1
0
[ "Eukaryota" ]
[ 14460 ]
1
[ "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...
[ 53, 2, 22, 6, 19, 13, 1, 17, 18, 1, 1, 33 ]
12
true
Domain
Spen paralogue and orthologue SPOC, C-terminal
Spen paralogue and orthologue SPOC, C-terminal
SPOC_C
5
IPR012922
12,922
ORF D-335-like
ORF_D-335
Domain
123
false
false
The sequences featured in this family are similar to a probable integrase ( ) expressed by the SSV1 virus of the archaeon Sulfolobus shibatae. This protein may be necessary for the integration of the virus into the host genome by a process of site-specific recombination [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF07935" ]
[ "SSV1_ORF_D-335" ]
[ 123 ]
1
[]
[]
[]
0
[]
0
[ "PUB00014897" ]
[ "1926776" ]
[ "Complete nucleotide sequence of the virus SSV1 of the archaebacterium Sulfolobus shibatae." ]
[ 1991 ]
1
[]
[]
0
0
null
[ "Aporhodopirellula aestuarii", "Fuselloviridae", "Sulfolobaceae" ]
[ 1, 9, 113 ]
3
[]
[]
0
true
Domain
ORF D-335-like
ORF D-335-like
ORF_D-335
7
IPR012923
12,923
Chromosome segregation in meiosis protein 3
Csm3
Domain
3,984
false
false
This entry represents a domain found in a group of proteins, including Csm3 from budding yeasts, Swi3 from fission yeasts and TIPIN from animals. They are involved in DNA replication and the maintenance of replication fork stability [ , , ].
[ "GO:0006974", "GO:0031297", "GO:0005634" ]
[ "DNA damage response", "replication fork processing", "nucleus" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF07962" ]
[ "Swi3" ]
[ 3984 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-5693607", "R-HSA-5693607", "R-MMU-5693607", "R-RNO-5693607" ]
[ "REACTOME:R-DME-5693607", "REACTOME:R-HSA-5693607", "REACTOME:R-MMU-5693607", "REACTOME:R-RNO-5693607" ]
4
[ "6skl", "6xwx", "7pfo", "7plo", "7pmk", "7pmn", "8b9a", "8b9b", "8b9c", "8b9d", "8kg6", "8ouw", "8xgc", "9e2w", "9e2x" ]
15
[ "PUB00016387", "PUB00066967", "PUB00077532" ]
[ "15367656", "22842922", "17116885" ]
[ "Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.", "Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress.", "Tipin and Timeless form a mutually protective complex required for genotoxic stress resist...
[ 2004, 2012, 2006 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3984 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 5, 1, 3, 2, 5, 4, 1, 3, 7, 1, 1, 4 ]
12
true
Domain
Chromosome segregation in meiosis protein 3
Chromosome segregation in meiosis protein 3
Csm3
8
IPR012924
12,924
TfuA-like, core
TfuA_core
Domain
1,686
false
false
This domain consists of a group of sequences that are similar to the core of TfuA protein ( ). TfuA plays a crucial dual role in peptide backbone thioamidation, functioning as both a hydrolase and a protein interaction mediator. It catalyses the hydrolysis of ThiS-COSH using a Ser/Lys catalytic pair to generate sulfide...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07812" ]
[ "TfuA" ]
[ 1686 ]
1
[]
[]
[]
0
[ "6xp8" ]
1
[ "PUB00016421", "PUB00093716", "PUB00158997" ]
[ "8763943", "28880150", "33707784" ]
[ "A newly discovered gene, tfuA, involved in the production of the ribosomally synthesized peptide antibiotic trifolitoxin.", "Post-translational thioamidation of methyl-coenzyme M reductase, a key enzyme in methanogenic and methanotrophic Archaea.", "Functional elucidation of TfuA in peptide backbone thioamidat...
[ 1996, 2017, 2021 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Sordariales", "ecological metagenomes", "uncultured Caudovirales phage" ]
[ 212, 1463, 2, 8, 1 ]
5
[]
[]
0
true
Domain
TfuA-like, core
TfuA-like, core
TfuA_core
3
IPR012925
12,925
TipAS antibiotic-recognition domain
TipAS_dom
Domain
10,416
false
false
TipAL is a bacterial transcriptional regulator of the MerR family. The tipA gene can be expressed as a long form, TipAL, and a short form, TipAS, which constitutes the C-terminal part of TipAL. TipAS forms the antibiotic-recognition domain [ ]. This domain, which has an α-helical globin-like fold, is also found at the ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07739" ]
[ "TipAS" ]
[ 10416 ]
1
[]
[]
[]
0
[ "1ny9", "2mbz", "2mc0", "3qao", "6et8", "6h95", "6h96", "6h97", "6hai", "7cla", "8rky" ]
11
[ "PUB00015229", "PUB00055552", "PUB00055553" ]
[ "12682015", "10200972", "10498730" ]
[ "Structural basis for antibiotic recognition by the TipA class of multidrug-resistance transcriptional regulators.", "Mta, a global MerR-type regulator of the Bacillus subtilis multidrug-efflux transporters.", "Identification of a regulator that controls stationary-phase expression of catalase-peroxidase in Cau...
[ 2003, 1999, 1999 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "metagenomes", "unclassified Caudoviricetes" ]
[ 10283, 8, 7, 116, 2 ]
5
[]
[]
0
true
Domain
TipAS antibiotic-recognition domain
TipAS antibiotic-recognition domain
TipAS_dom
4
IPR012926
12,926
TMEM120A/B
TMEM120A/B
Family
5,183
false
false
This entry represents a group of transmembrane proteins including TACAN (also known as TMEM120A) and TMEM120B. TMEM120A is involved in mechanosensation and plays an essential role in lipid metabolism and adipocyte differentiation [ , ]. It was first described as an ion channel that contributes to sensing mechanical pai...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM", "PANTHER" ]
[ "PF07851", "PTHR21433" ]
[ "TMEM120A-B", "" ]
[ 5183, 5082 ]
2
[]
[]
[]
0
[ "7cxr", "7f3t", "7f3u", "7f6v", "7f73", "7n0k", "7n0l", "7n7p" ]
8
[ "PUB00094219", "PUB00094220", "PUB00158954", "PUB00158955", "PUB00158956", "PUB00158957" ]
[ "32084332", "26024229", "36420836", "34374645", "34409941", "34465718" ]
[ "TACAN Is an Ion Channel Involved in Sensing Mechanical Pain.", "TMEM120A and B: Nuclear Envelope Transmembrane Proteins Important for Adipocyte Differentiation.", "Regulation of PKD2 channel function by TACAN.", "TMEM120A is a coenzyme A-binding membrane protein with structural similarities to ELOVL fatty ac...
[ 2020, 2015, 2023, 2021, 2021, 2021 ]
6
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5183 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 21, 1, 8, 3, 8, 5, 6, 8, 15 ]
9
true
Family
TMEM120A/B
TMEM120A/B
TMEM120A/B
6
IPR012927
12,927
Effector protease OspD3-like, N-terminal
Toxin_15_N
Domain
528
false
false
This domain is present in the N-terminal region of the ShET2 enterotoxin and the Effector protease OspD3 from Shigella flexneri, Ankyrin repeat protein A (ARPA) from Escherichia coli and related sequences from bacteria. OspD3 is an effector protease that disrupts necroptosis in host cells by mediating proteolytic cleav...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07906" ]
[ "Toxin_15" ]
[ 528 ]
1
[]
[]
[]
0
[]
0
[ "PUB00084320", "PUB00162553" ]
[ "28085133", "32657447" ]
[ "EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation.", "A unique bacterial tactic to circumvent the cell death crosstalk induced by blockade of caspase-8." ]
[ 2017, 2020 ]
2
[]
[]
0
0
null
[ "Bacteria", "human gut metagenome" ]
[ 521, 7 ]
2
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Effector protease OspD3-like, N-terminal
Effector protease OspD3-like, N-terminal
Toxin_15_N
4
IPR012928
12,928
Clostridium neurotoxin, receptor binding N-terminal
Toxin_rcpt-bd_N
Domain
372
false
false
The Clostridium neurotoxin family is composed of tetanus neurotoxin and seven serotypes of botulinum neurotoxin. These toxins act as inhibitors of neurotransmitter release [ , ]. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain ( ), the central translocation domai...
[ "GO:0005576" ]
[ "extracellular region" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF07953" ]
[ "Toxin_R_bind_N" ]
[ 372 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.24.69", "R-HSA-5250955", "R-HSA-5250958", "R-HSA-5250968", "R-HSA-5250971", "R-HSA-5250981", "R-HSA-5250982", "R-HSA-5250989", "R-HSA-5250992" ]
[ "EC:3.4.24.69", "REACTOME:R-HSA-5250955", "REACTOME:R-HSA-5250958", "REACTOME:R-HSA-5250968", "REACTOME:R-HSA-5250971", "REACTOME:R-HSA-5250981", "REACTOME:R-HSA-5250982", "REACTOME:R-HSA-5250989", "REACTOME:R-HSA-5250992" ]
9
[ "1a8d", "1af9", "1d0h", "1dfq", "1diw", "1dll", "1epw", "1f31", "1fv2", "1fv3", "1g9a", "1g9b", "1g9c", "1g9d", "1i1e", "1s0b", "1s0c", "1s0d", "1s0e", "1s0f", "1s0g", "1yxw", "1yyn", "1z0h", "2nm1", "2np0", "2nyy", "2nz9", "2vu9", "2vua", "2vxr", "3azv"...
150
[ "PUB00016466", "PUB00088575", "PUB00088576" ]
[ "9783750", "1328520", "23435179" ]
[ "Crystal structure of botulinum neurotoxin type A and implications for toxicity.", "Tetanus toxin inhibits depolarization-stimulated protein phosphorylation in rat cortical synaptosomes: effect on synapsin I phosphorylation and translocation.", "Botulinum toxins: mechanisms of action, antinociception and clinic...
[ 1998, 1992, 2013 ]
3
[]
[]
0
0
null
[ "Bacteria", "Caudoviricetes", "Eukaryota", "metagenomes" ]
[ 332, 8, 27, 5 ]
4
[]
[]
0
true
Domain
Clostridium neurotoxin, receptor binding N-terminal
Clostridium neurotoxin, receptor binding N-terminal
Toxin_rcpt-bd_N
7
IPR012929
12,929
Nucleoprotein, TPR/MLP1-2 domain
Nucleoprot-TPR/MLP1-2_dom
Domain
4,575
false
false
This domain is found in several proteins, including TPR protein and yeast myosin-like protein 1 (MLP1) and MPL2. TPR and MLP1/2 share several features; for example, they have coiled-coil regions and are associated with nuclear pores [ , , ]. TPR is thought to be a component of nuclear pore complex-attached intranuclear...
[ "GO:0006606" ]
[ "protein import into nucleus" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF07926" ]
[ "TPR_MLP1_2" ]
[ 4575 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "GenProp2036", "R-DME-159227", "R-DME-159230", "R-DME-159231", "R-DME-159236", "R-DME-170822", "R-DME-3108214", "R-DME-3301854", "R-DME-4085377", "R-DME-4551638", "R-DME-4615885", "R-DME-5578749", "R-HSA-1169408", "R-HSA-159227", "R-HSA-159230", "R-HSA-159231", "R-HSA-159236", "R-H...
[ "GP:GenProp2036", "REACTOME:R-DME-159227", "REACTOME:R-DME-159230", "REACTOME:R-DME-159231", "REACTOME:R-DME-159236", "REACTOME:R-DME-170822", "REACTOME:R-DME-3108214", "REACTOME:R-DME-3301854", "REACTOME:R-DME-4085377", "REACTOME:R-DME-4551638", "REACTOME:R-DME-4615885", "REACTOME:R-DME-55787...
86
[]
0
[ "PUB00016402", "PUB00016576", "PUB00075590", "PUB00075591" ]
[ "9024684", "7798308", "10085285", "12531921" ]
[ "Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments.", "Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex.", "Proteins c...
[ 1997, 1994, 1999, 2003 ]
4
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4575 ]
1
[ "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)", "...
[ 4, 9, 2, 1, 3, 1, 1, 4, 1, 1, 38 ]
11
true
Domain
Nucleoprotein, TPR/MLP1-2 domain
Nucleoprotein, TPR/MLP1-2 domain
Nucleoprot-TPR/MLP1-2_dom
1
IPR012930
12,930
TraC-like
TraC
Family
740
false
false
The members of this family are sequences that are similar to TraC ( ) from Rhizobium etli. The gene encoding this protein is one of a group of genes found on plasmid p42a of Rhizobium etli (strain CFN 42/ATCC 51251) that are thought to be involved in the process of plasmid self-transmission. Mobilisation of plasmid p42...
[]
[]
[]
0
[ "PFAM" ]
[ "PF07820" ]
[ "TraC" ]
[ 740 ]
1
[ "GP" ]
[ "GenProp0490" ]
[ "GP:GenProp0490" ]
1
[]
0
[ "PUB00016590" ]
[ "12591886" ]
[ "Conjugative transfer of p42a from rhizobium etli CFN42, which is required for mobilization of the symbiotic plasmid, is regulated by quorum sensing." ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Pseudomonadati", "marine sediment metagenome" ]
[ 739, 1 ]
2
[]
[]
0
true
Family
TraC-like
TraC-like
TraC
2