LiteFold/InterPro · Datasets at Hugging Face

IPR011969

11,969

Clan AA aspartic peptidase, C-terminal

Clan_AA_Asp_peptidase_C

Domain

6,235

false

Proteins containing this domain are aspartic endopeptidases belonging to MEROPS family A32 and MEROPS clan AA (from conservation of the DTG motif that include the active site aspartic acid and the fold which is similar to retropepsin) [ , ]. This entry describes the well-conserved C-terminal domain, of approximately 12...

[]

0

[ "NCBIFAM" ]

[ "TIGR02281" ]

[ "clan_AA_DTGA" ]

[ 6235 ]

1

[]

0

[ "5c9b", "5c9d", "5c9f" ]

3

[ "PUB00000093", "PUB00000349", "PUB00000522", "PUB00001330", "PUB00011023", "PUB00011707", "PUB00021296", "PUB00042504", "PUB00053567", "PUB00065205", "PUB00066803", "PUB00076754", "PUB00076755", "PUB00076784", "PUB00076785", "PUB00076786", "PUB00076911" ]

[ "2194475", "1851433", "8439290", "6795036", "10331925", "11566868", "10864493", "2682266", "19173708", "23254940", "21765428", "16395329", "25144529", "4912600", "10497172", "21751400", "26462856" ]

[ "The structure and function of the aspartic proteinases.", "Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.", "Evolutionary families of peptidases.", "Gastric proteinases--structure, function, evolution and mechanism of action.", "Crystal structure of the hy...

[ 1990, 1991, 1993, 1981, 1999, 2001, 2000, 1989, 2009, 2013, 2011, 2006, 2014, 1970, 1999, 2011, 2015 ]

17

[]

0

null

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

[ 7, 6115, 10, 103 ]

4

[]

0

true

Domain

Clan AA aspartic peptidase, C-terminal

Clan_AA_Asp_peptidase_C

4

IPR011970

11,970

Lytic murein transglycosylase

MltB_2

Domain

10,602

false

Proteins of this entries are closely related to the MltB family lytic murein transglycosylases described by and are likewise all proteobacterial, although that family and this one form clearly distinct clades. Several species have one member of each family. Many proteins of this entry(unlike the MltB family) contain an...

[]

0

[ "NCBIFAM" ]

[ "TIGR02283" ]

[ "MltB_2" ]

[ 10602 ]

1

[]

0

[ "5anz", "5ao7", "5ao8", "7qvd" ]

4

[]

0

[ "IPR031304" ]

[]

1

0

1

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

[ 10515, 25, 62 ]

3

[]

0

true

Domain

Lytic murein transglycosylase

MltB_2

9

IPR011971

11,971

Conserved hypothetical protein CHP02284

CHP02284

Family

4,821

false

This entry represents a family of uncharacterised proteins predominantly found in bacteria that includes DUF2383 domain-containing protein from Pseudomonas aeruginosa ( ). This protein shows a ferritin-like topology with a four-helix-bundle fold that lacks metal-ion-binding site typical of the ferritin family but has a...

[]

0

[ "NCBIFAM" ]

[ "TIGR02284" ]

[ "" ]

[ 4821 ]

1

[]

0

[ "4etr" ]

1

[ "PUB00065044" ]

[ "23295481" ]

[ "The AEROPATH project targeting Pseudomonas aeruginosa: crystallographic studies for assessment of potential targets in early-stage drug discovery." ]

[ 2013 ]

1

[]

[ "IPR016920" ]

0

1

0

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

[ 4768, 37, 16 ]

3

[]

0

true

Family

Conserved hypothetical protein CHP02284

CHP02284

2

IPR011972

11,972

Conserved hypothetical protein CHP02285

CHP02285

Family

854

false

Members of this family are found in several Proteobacteria, including Pseudomonas putida (strain KT2440), Bdellovibrio bacteriovorus HD100 (three members), Aeromonas hydrophila, and Chromobacterium violaceum ATCC 12472. The function is unknown.

[]

0

[ "NCBIFAM" ]

[ "TIGR02285" ]

[ "" ]

[ 854 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Diploscapter pachys", "ecological metagenomes" ]

[ 850, 1, 3 ]

3

[]

0

true

Family

Conserved hypothetical protein CHP02285

CHP02285

5

IPR011973

11,973

Phenylacetic acid degradation protein PaaD

PaaD

Family

4,304

false

This members of this family belong to the thioesterase superfamily , and are nearly always found adjacent to other genes of the phenylacetic acid degradation pathway [ ]. Their function is currently unknown, but a role as thioesterases is suggested.

[ "GO:0016790" ]

[ "thiolester hydrolase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02286" ]

[ "PaaD" ]

[ 4304 ]

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"...

[ "3.1.2.-", "PWY-3602", "PWY-5109", "PWY-6322", "PWY-6585", "PWY-6917", "PWY-6948", "PWY-6995", "PWY-6997", "PWY-7007", "PWY-7216", "PWY-7292", "PWY-7401", "PWY-7402", "PWY-7471", "PWY-7690", "PWY-7706", "PWY-7733", "PWY-7734", "PWY-7738", "PWY-7740", "PWY-7741", "PWY-7742...

[ "EC:3.1.2.-", "METACYC:PWY-3602", "METACYC:PWY-5109", "METACYC:PWY-6322", "METACYC:PWY-6585", "METACYC:PWY-6917", "METACYC:PWY-6948", "METACYC:PWY-6995", "METACYC:PWY-6997", "METACYC:PWY-7007", "METACYC:PWY-7216", "METACYC:PWY-7292", "METACYC:PWY-7401", "METACYC:PWY-7402", "METACYC:PWY-7...

34

[ "1j1y", "1psu", "1wlu", "1wlv", "1wm6", "1wn3", "2dsl", "2fs2" ]

8

[ "PUB00015494" ]

[ "11260461" ]

[ "The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications." ]

[ 2001 ]

1

[]

0

null

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

[ 74, 4195, 4, 31 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Phenylacetic acid degradation protein PaaD

PaaD

3

IPR011974

11,974

Phenylacetic acid degradation protein PaaY

PaaY

Family

802

false

Members of this family are located next to other genes organised into apparent operons for phenylacetic acid degradation [ ]. PaaY is located near the end of these gene clusters and often next to PaaX, a transcriptional regulator. PaaY has a thioesterase activity involved in the efficient growth in phenylacetic acid wh...

[]

0

[ "NCBIFAM" ]

[ "TIGR02287" ]

[ "PaaY" ]

[ 802 ]

1

[]

0

[]

0

[ "PUB00015494", "PUB00093686" ]

[ "11260461", "24983528" ]

[ "The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications.", "Insights on the regulation of the phenylacetate degradation pathway from Escherichia coli." ]

[ 2001, 2014 ]

2

[]

0

null

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

[ 1, 798, 3 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Phenylacetic acid degradation protein PaaY

PaaY

2

IPR011975

11,975

Phenylacetic acid degradation protein PaaN2

PaaN_2

Family

2,480

false

This enzyme is proposed to act in the ring-opening step of phenylacetic acid degradation [ ] which follows ligation of the acid with coenzyme A (by PaaF) and hydroxylation by a multicomponent non-heme iron hydroxylase complex (PaaGHIJK). Gene symbols have been standardized in [ ]. This enzyme is related to aldehyde deh...

[]

0

[ "NCBIFAM" ]

[ "TIGR02288" ]

[ "PaaN_2" ]

[ 2480 ]

1

[]

0

[ "5uju" ]

1

[ "PUB00015494", "PUB00015522" ]

[ "11260461", "10766858" ]

[ "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 Escherichia coli." ]

[ 2001, 2000 ]

2

[]

0

null

[ "Bacteria", "Physcomitrium patens", "unclassified sequences" ]

[ 2472, 1, 7 ]

3

[]

0

true

Family

Phenylacetic acid degradation protein PaaN2

PaaN_2

3

IPR011976

11,976

Peptidase M3B, oligoendopeptidase-related

Pept_M3B_oligopep-rel

Family

3,398

false

This family consists of probable oligoendopeptidases belonging to MEROPS peptidase family M3, subfamily M3B (clan MA(E)). The family is related to lactococcal PepF and group B streptococcal PepB ( ) but in a distinct clade with considerable sequence differences not only to but also to . Likely substrates are small pept...

[]

0

[ "NCBIFAM" ]

[ "TIGR02289" ]

[ "M3_not_pepF" ]

[ 3398 ]

1

[]

0

[ "2h1j", "2h1n", "3ahm", "3ahn", "3aho", "3sks" ]

6

[]

0

[ "IPR045090" ]

[]

1

0

1

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

[ 16, 3361, 1, 20 ]

4

[]

0

true

Family

Peptidase M3B, oligoendopeptidase-related

Pept_M3B_oligopep-rel

1

IPR011977

11,977

Peptidase M3B, oligoendopeptidase-related clade 3

Pept_M3B_clade3

Family

5,119

false

Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase...

[]

0

[ "NCBIFAM" ]

[ "TIGR02290" ]

[ "M3_fam_3" ]

[ 5119 ]

1

[]

0

[]

0

[ "PUB00003579" ]

[ "7674922" ]

[ "Evolutionary families of metallopeptidases." ]

[ 1995 ]

1

[ "IPR045090" ]

[ "IPR034006" ]

1

0

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

[ 5037, 2, 53, 27 ]

4

[]

0

true

Family

Peptidase M3B, oligoendopeptidase-related clade 3

Pept_M3B_clade3

3

IPR011978

11,978

YgfB-like

Family

10,667

false

This group of proteins includes the Escherichia coli proteins YgfB and YecA, and similar proteins mainly found in gammaproteobacteria. The function of these proteins is unknown. The crystal structure is known for the member from Haemophilus influenzae YgfB ( ), which folds into seven α-helices arranged into two domains...

[]

0

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

[ "MF_00346", "PF03695", "TIGR02292" ]

[ "UPF0149", "UPF0149", "ygfB_yecA" ]

[ 2356, 10661, 7625 ]

3

[]

0

[ "1izm", "4gyt" ]

2

[ "PUB00028713" ]

[ "15317022" ]

[ "X-ray structure of HI0817 from Haemophilus influenzae: protein of unknown function with a novel fold." ]

[ 2004 ]

1

[]

0

null

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

[ 10538, 15, 114 ]

3

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

YgfB-like

5

IPR011979

11,979

Antitoxin Xre

Antitox_Xre

Family

3,573

false

Proteins in this family are found predominantly in the Proteobacteria. Antitoxin Xre is part of a type II toxin-antitoxin (TA) system. RES toxin inhibits the cell growth in E. coli, Xre neutralises the RES toxicity [ ].

[]

0

[ "NCBIFAM" ]

[ "TIGR02293" ]

[ "TAS_TIGR02293" ]

[ 3573 ]

1

[]

0

[ "6gw6", "8gug", "9r35" ]

3

[ "PUB00093678" ]

[ "30315706" ]

[ "The RES domain toxins of RES-Xre toxin-antitoxin modules induce cell stasis by degrading NAD+" ]

[ 2019 ]

1

[]

0

null

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

[ 3544, 5, 24 ]

3

[]

0

true

Family

Antitoxin Xre

Antitox_Xre

9

IPR011980

11,980

Metal-staphylopine-binding protein CntA-like

CntA-like

Family

1,627

false

This entry represents Metal-staphylopine-binding protein CntA from Staphylococcus aureus [ , ]. CntA is involved in the import of divalent metals ions such as nickel, cobalt and zinc. It binds the metal via the metallophore StP, and transfers the StP-metal complex to the membrane-bound permease [ , ]. The ATP-binding c...

[ "GO:0016151", "GO:0020037", "GO:0015675" ]

[ "nickel cation binding", "heme binding", "nickel cation transport" ]

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

3

[ "NCBIFAM", "CDD" ]

[ "TIGR02294", "cd08489" ]

[ "nickel_nikA", "PBP2_NikA" ]

[ 1500, 1597 ]

2

[ "GP" ]

[ "GenProp0494" ]

[ "GP:GenProp0494" ]

1

[ "1uiu", "1uiv", "1zlq", "2noo", "3dp8", "3e3k", "3mvw", "3mvx", "3mvy", "3mvz", "3mw0", "3mz9", "3mzb", "3qim", "4dcx", "4dcy", "4i8c", "4i9d", "4oer", "4oes", "4wed", "5l8d", "5mwu", "5on0", "5on1", "5on4", "5on5", "5on8", "5on9", "5yh5", "5yh8", "5yhe"...

36

[ "PUB00035598", "PUB00038938", "PUB00061663", "PUB00071925", "PUB00071938", "PUB00081137", "PUB00093059", "PUB00094620", "PUB00094621" ]

[ "7934931", "16011372", "7867647", "18310026", "8003968", "27230378", "29581261", "21281641", "23279021" ]

[ "The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport system for nickel.", "Crystallographic and spectroscopic evidence for high affinity binding of FeEDTA(H2O)- to the periplasmic nickel transporter NikA.", "Purification and characterization of the periplasmic nickel-bin...

[ 1993, 2005, 1995, 2008, 1994, 2016, 2018, 2011, 2013 ]

9

[ "IPR030678" ]

[]

1

0

1

[ "Bacteria", "Methanosarcina", "Phytophthora cactorum", "unclassified sequences" ]

[ 1607, 15, 1, 4 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Metal-staphylopine-binding protein CntA-like

CntA-like

5

IPR011981

11,981

3,4-dihydroxyphenylacetate 2,3-dioxygenase, Mn/Fe-type

DHPA_dOase_Mn/Fe

Family

1,972

false

Dioxygenases catalyse the incorporation of both atoms of molecular oxygen into substrates. Cleavage of aromatic rings is one of the most important function of dioxygenases. The substrates of ring-cleavage dioxygenases can be classified into two groups according to the mode of scission of the aromatic ring. Intradiol en...

[]

0

[ "NCBIFAM" ]

[ "TIGR02295" ]

[ "HpaD" ]

[ 1972 ]

1

[ "GP" ]

[ "GenProp0231" ]

[ "GP:GenProp0231" ]

1

[ "1f1r", "1f1u", "1f1v", "1f1x", "1q0c", "1q0o", "2ig9", "2iga", "3bza", "3ecj", "3eck", "3ojj", "3ojk", "3ojn", "3ojt", "4ghc", "4ghd", "4ghe", "4ghf", "4ghg", "4ghh", "4z6l", "4z6m", "4z6n", "4z6o", "4z6p", "4z6q", "4z6r", "4z6s", "4z6t", "4z6u", "4z6v"...

37

[ "PUB00002507", "PUB00002892", "PUB00005214", "PUB00015524", "PUB00022487" ]

[ "2670937", "8126007", "7481800", "6270137", "15028678" ]

[ "Bacterial aromatic ring-cleavage enzymes are classified into two different gene families.", "Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases.", "Crystal structure of the biphenyl-cleaving extradiol dioxygenase...

[ 1989, 1994, 1995, 1981, 2004 ]

5

[]

0

null

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

[ 55, 1909, 5, 3 ]

4

[]

0

true

Family

3,4-dihydroxyphenylacetate 2,3-dioxygenase, Mn/Fe-type

DHPA_dOase_Mn/Fe

9

IPR011982

11,982

4-hydroxyphenylacetate 3-monooxygenase, reductase component

HPA_mOase_red

Family

1,291

false

This entry identifies the reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase [ ]. This enzyme catalyses the first step (hydroxylation at the 3-position) in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. 4-hydroxyphenylacetate arises from the degradation of tyrosine. These reducta...

[ "GO:0016651", "GO:0051287", "GO:0042537" ]

[ "oxidoreductase activity, acting on NAD(P)H", "NAD binding", "benzene-containing compound metabolic process" ]

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

3

[ "NCBIFAM" ]

[ "TIGR02296" ]

[ "HpaC" ]

[ 1291 ]

1

[ "EC", "GP" ]

[ "1.5.1.36", "GenProp0231" ]

[ "EC:1.5.1.36", "GP:GenProp0231" ]

2

[]

0

[ "PUB00007219" ]

[ "8077235" ]

[ "Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme." ]

[ 1994 ]

1

[]

0

null

[ "Bacteria" ]

[ 1291 ]

1

[]

0

true

Family

4-hydroxyphenylacetate 3-monooxygenase, reductase component

HPA_mOase_red

2

IPR011983

11,983

4-hydroxyphenylacetate catabolism regulatory protein HpaA

HpaA_TReg

Family

1,148

false

This putative transcriptional regulator, which contains both the substrate-binding, dimerisation domain and the helix-turn-helix DNA-binding domain of the AraC famil, is located proximal to genes of the 4-hydroxyphenylacetate catabolism pathway [ ].

[]

0

[ "NCBIFAM" ]

[ "TIGR02297" ]

[ "HpaA" ]

[ 1148 ]

1

[ "GP" ]

[ "GenProp0231" ]

[ "GP:GenProp0231" ]

1

[]

0

[ "PUB00002288" ]

[ "8550403" ]

[ "Molecular characterization of the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli W: engineering a mobile aromatic degradative cluster." ]

[ 1996 ]

1

[]

0

null

[ "Pseudomonadota" ]

[ 1148 ]

1

[]

0

true

Family

4-hydroxyphenylacetate catabolism regulatory protein HpaA

HpaA_TReg

6

IPR011984

11,984

3,4-dihydroxyphenylacetate 2,3-dioxygenase

HPCD

Family

2,043

false

3,4-dihydroxyphenylacetate (homoprotocatechuate, hpca) 2,3-dioxygenase (HPCD) catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. 4-hydroxyphenylacetate arises from the degradation of tyrosine. The enzyme incorporates both atoms of molecular oxygen into hpca, resulting in a...

[ "GO:0008687" ]

[ "3,4-dihydroxyphenylacetate 2,3-dioxygenase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM", "CDD" ]

[ "TIGR02298", "cd07370" ]

[ "HpaD_Fe", "HPCD" ]

[ 1811, 2039 ]

2

[ "GP" ]

[ "GenProp0231" ]

[ "GP:GenProp0231" ]

1

[ "8iq8" ]

1

[ "PUB00015525", "PUB00080813" ]

[ "2261999", "9179284" ]

[ "Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C.", "Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum." ]

[ 1990, 1997 ]

2

[]

0

null

[ "Bacteria", "Durusdinium trenchii", "unclassified sequences" ]

[ 2031, 1, 11 ]

3

[]

0

true

Family

3,4-dihydroxyphenylacetate 2,3-dioxygenase

HPCD

6

IPR011985

11,985

5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase

DH_HpaE

Family

3,609

false

This entry represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ...

[ "GO:0018480", "GO:1901023" ]

[ "5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity", "4-hydroxyphenylacetate catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02299" ]

[ "HpaE" ]

[ 3609 ]

1

[ "GP" ]

[ "GenProp0231" ]

[ "GP:GenProp0231" ]

1

[ "2d4e" ]

1

[ "PUB00000602" ]

[ "2194577" ]

[ "Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic semialdehyde dehydrogenase and 2-hydroxymuconic semialdehyde hydrolase from Pseudomonas CF600." ]

[ 1990 ]

1

[]

0

null

[ "Bacteria", "Candidatus Sysuiplasma superficiale", "Eukaryota", "unclassified sequences" ]

[ 3595, 2, 3, 9 ]

4

[]

0

true

Family

5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase

DH_HpaE

3

IPR011986

11,986

Extradiol ring-cleavage dioxygenase LigAB, LigA subunit

Xdiol_dOase_LigA

Domain

2,468

false

Dioxygenases catalyse the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms. Cleavage of aromatic rings is one of the most important functions of dioxygenases, which play key roles in the degradation of aromatic compounds. The substrates of ring-cleavage dioxygenases...

[]

0

[ "PFAM" ]

[ "PF07746" ]

[ "LigA" ]

[ 2468 ]

1

[]

0

[ "1b4u", "1bou", "3wku", "3wpm", "3wr3", "3wr4", "3wr8", "3wr9", "3wra", "3wrb", "3wrc", "7ltc", "7lte", "7ltf", "7lth", "7ltr", "8t1s", "8t1t", "9chi" ]

19

[ "PUB00011779", "PUB00015247", "PUB00015256" ]

[ "10467151", "15264822", "10730195" ]

[ "Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions.", "Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases.", "Catechol dioxygenases." ]

[ 1999, 2004, 1999 ]

3

[]

[ "IPR034940" ]

0

1

0

[ "Bacteria", "Brugia timori", "Thermoproteati", "ecological metagenomes" ]

[ 2428, 2, 13, 25 ]

4

[]

0

true

Domain

Extradiol ring-cleavage dioxygenase LigAB, LigA subunit

Xdiol_dOase_LigA

8

IPR011987

11,987

ATPase, V1 complex, subunit H, C-terminal

ATPase_V1-cplx_hsu_C

Domain

5,586

false

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

[ "GO:1902600", "GO:0000221" ]

[ "proton transmembrane transport", "vacuolar proton-transporting V-type ATPase, V1 domain" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF11698" ]

[ "V-ATPase_H_C" ]

[ 5586 ]

1

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

[ "R-BTA-1222556", "R-BTA-77387", "R-BTA-917977", "R-BTA-9639288", "R-BTA-983712", "R-CEL-1222556", "R-CEL-77387", "R-CEL-917977", "R-CEL-9639288", "R-CEL-983712", "R-DDI-1222556", "R-DDI-77387", "R-DDI-917977", "R-DDI-9639288", "R-DME-1222556", "R-DME-77387", "R-DME-917977", "R-DME-...

[ "REACTOME:R-BTA-1222556", "REACTOME:R-BTA-77387", "REACTOME:R-BTA-917977", "REACTOME:R-BTA-9639288", "REACTOME:R-BTA-983712", "REACTOME:R-CEL-1222556", "REACTOME:R-CEL-77387", "REACTOME:R-CEL-917977", "REACTOME:R-CEL-9639288", "REACTOME:R-CEL-983712", "REACTOME:R-DDI-1222556", "REACTOME:R-DDI-...

41

[ "1ho8", "3j9t", "3j9u", "3j9v", "5bw9", "5d80", "5vox", "5voy", "5voz", "6o7v", "6o7w", "6o7x", "6wm2", "6wm3", "6wm4", "6xbw", "6xby", "7fda", "7fdb", "7fdc", "7khr", "7tmm", "7tmo", "7tmp", "7tmq", "7tmr", "7tms", "7tmt", "7u4t", "7u8o", "7u8p", "7u8q"...

53

[ "PUB00015431", "PUB00015432", "PUB00020603", "PUB00020604", "PUB00020608", "PUB00020609", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]

[ "11416198", "14635776", "15473999", "15078220", "15907459", "15629643", "20450191", "18937357", "1385979", "9741106" ]

[ "Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae.", "Structure and assembly of the yeast V-ATPase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-...

[ 2001, 2003, 2004, 2004, 2005, 2005, 2010, 2008, 1992, 1998 ]

10

[]

0

null

[ "Eukaryota" ]

[ 5586 ]

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...

[ 9, 2, 2, 2, 5, 3, 1, 3, 5, 1, 1, 13 ]

12

true

Domain

ATPase, V1 complex, subunit H, C-terminal

ATPase_V1-cplx_hsu_C

1

IPR011989

11,989

Armadillo-like helical

ARM-like

Homologous_superfamily

900,679

false

This superfamily represents a domain consisting of a multi-helical fold comprising two curved layers of α-helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis [ ]. These superhelical structures present an extensive solvent-accessible surfa...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:1.25.10.10" ]

[ "" ]

[ 900679 ]

1

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

[ "R-BTA-1169091", "R-BTA-1222556", "R-BTA-1234176", "R-BTA-1236978", "R-BTA-140342", "R-BTA-141444", "R-BTA-174084", "R-BTA-174154", "R-BTA-174178", "R-BTA-174184", "R-BTA-177504", "R-BTA-187577", "R-BTA-195253", "R-BTA-196299", "R-BTA-201681", "R-BTA-201722", "R-BTA-202424", "R-BTA...

[ "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1222556", "REACTOME:R-BTA-1234176", "REACTOME:R-BTA-1236978", "REACTOME:R-BTA-140342", "REACTOME:R-BTA-141444", "REACTOME:R-BTA-174084", "REACTOME:R-BTA-174154", "REACTOME:R-BTA-174178", "REACTOME:R-BTA-174184", "REACTOME:R-BTA-177504", "REACTOME:R-BTA...

1,359

[ "1b3u", "1bk5", "1bk6", "1ee4", "1ee5", "1ejl", "1ejy", "1f59", "1g3j", "1gcj", "1ho8", "1i7w", "1i7x", "1ial", "1ib2", "1ibr", "1iq1", "1jdh", "1jpp", "1jpw", "1lrv", "1luj", "1m1e", "1m5n", "1m8w", "1m8x", "1m8y", "1m8z", "1o6o", "1o6p", "1oyz", "1pjm"...

1,592

[ "PUB00015442", "PUB00015443" ]

[ "10361086", "11551174" ]

[ "Topological characteristics of helical repeat proteins.", "Protein repeats: structures, functions, and evolution." ]

[ 1999, 2001 ]

2

[]

0

null

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

[ 3374, 59930, 835493, 321, 1561 ]

5

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

[ 1468, 205, 1274, 378, 1, 1332, 792, 95, 973, 1087, 78, 96, 3373 ]

13

true

Homologous_superfamily

Armadillo-like helical

ARM-like

6

IPR011990

11,990

Tetratricopeptide-like helical domain superfamily

TPR-like_helical_dom_sf

Homologous_superfamily

2,005,686

false

The domain represented in this superfamily consists of a multi-helical fold comprised of two curved layers of α-helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis [ ]. These superhelical structures present an extensive solvent-accessible...

[ "GO:0005515" ]

[ "protein binding" ]

[ "molecular_function" ]

1

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:1.25.40.10", "SSF48452" ]

[ "", "" ]

[ 1845999, 1490687 ]

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-1169091", "R-BTA-1234176", "R-BTA-1236978", "R-BTA-141430", "R-BTA-156827", "R-BTA-1650814", "R-BTA-174048", "R-BTA-174084", "R-BTA-174154", "R-BTA-174178", "R-BTA-174184", "R-BTA-176407", "R-BTA-176408", "R-BTA-176409", "R-BTA-176412", "R-BTA-177504", "R-BTA-179409", "R-BTA...

[ "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1234176", "REACTOME:R-BTA-1236978", "REACTOME:R-BTA-141430", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1650814", "REACTOME:R-BTA-174048", "REACTOME:R-BTA-174084", "REACTOME:R-BTA-174154", "REACTOME:R-BTA-174178", "REACTOME:R-BTA-174184", "REACTOME:R-BTA...

1,108

[ "1a17", "1b89", "1e96", "1elr", "1elw", "1fch", "1hh8", "1hxi", "1hz4", "1ihg", "1iip", "1iyg", "1klx", "1kt0", "1kt1", "1na0", "1na3", "1nzn", "1ouv", "1p5q", "1pc2", "1qqe", "1qz2", "1tjc", "1w3b", "1wao", "1wm5", "1xi4", "1xi5", "1xnf", "1y8m", "1ya0"...

1,801

[ "PUB00001313", "PUB00005443", "PUB00005695", "PUB00014195", "PUB00015442", "PUB00015443" ]

[ "9482716", "7667876", "1882418", "14659697", "10361086", "11551174" ]

[ "The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.", "Tetratrico peptide repeat interactions: to TPR or not to TPR?", "The TPR snap helix: a novel protein repeat motif from mitosis to transcription.", "TPR proteins: the versati...

[ 1998, 1995, 1991, 2003, 1999, 2001 ]

6

[]

0

null

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

[ 6164, 864466, 1118877, 596, 3, 15580 ]

6

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

[ 3233, 150, 784, 335, 24, 1360, 699, 88, 2289, 986, 69, 72, 3719 ]

13

true

Homologous_superfamily

Tetratricopeptide-like helical domain superfamily

TPR-like_helical_dom_sf

5

IPR011991

11,991

ArsR-like helix-turn-helix domain

ArsR-like_HTH

Domain

360,293

false

This domain is found in the arsenical resistance operon repressor (ArsR) and similar prokaryotic, metal regulated homodimeric repressors. The ArsR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology) includes several proteins that appear to dissociate from DNA in the presenc...

[]

0

[ "CDD" ]

[ "cd00090" ]

[ "HTH_ARSR" ]

[ 360293 ]

1

[ "REACTOME" ]

[ "R-HSA-9637628" ]

[ "REACTOME:R-HSA-9637628" ]

1

[ "1i1g", "1ku9", "1mkm", "1r1t", "1r1u", "1r1v", "1r22", "1r23", "1ri7", "1sfx", "1smt", "1u2w", "1ub9", "1uly", "1y0u", "2cg4", "2cwe", "2cyy", "2d1h", "2e1c", "2e7w", "2e7x", "2efn", "2efo", "2efp", "2efq", "2gqq", "2hoe", "2ia0", "2jsc", "2kjb", "2kjc"...

125

[ "PUB00003383", "PUB00004420", "PUB00086544", "PUB00086545" ]

[ "9466913", "8506147", "11683648", "10995250" ]

[ "Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins.", "A possible mechanism for metal-ion induced DNA-protein dissociation in a family of prokaryotic transcriptional regulators.", "SmtB-DNA and protein-protein interactions in the formation of the cyan...

[ 1998, 1993, 2001, 2000 ]

4

[]

[ "IPR001845", "IPR054760" ]

0

2

0

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

[ 25130, 331324, 816, 144, 3, 2876 ]

6

[ "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]

[ 7, 2 ]

2

true

Domain

ArsR-like helix-turn-helix domain

ArsR-like_HTH

2

IPR011993

11,993

PH-like domain superfamily

PH-like_dom_sf

Homologous_superfamily

918,193

false

This superfamily represents the PH domain and structurally related domains. Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of signalling proteins, where they serve as simple targeting domains that bind lipids [ , , ]. PH domains have a partly opened β-barrel topology that is ca...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:2.30.29.30" ]

[ "" ]

[ 918193 ]

1

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

[ "R-BTA-109704", "R-BTA-111933", "R-BTA-114604", "R-BTA-114608", "R-BTA-1250196", "R-BTA-1250347", "R-BTA-1257604", "R-BTA-1306955", "R-BTA-1433557", "R-BTA-1483248", "R-BTA-166016", "R-BTA-1660499", "R-BTA-1660516", "R-BTA-1660517", "R-BTA-1660661", "R-BTA-167044", "R-BTA-180292", ...

[ "REACTOME:R-BTA-109704", "REACTOME:R-BTA-111933", "REACTOME:R-BTA-114604", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-1250196", "REACTOME:R-BTA-1250347", "REACTOME:R-BTA-1257604", "REACTOME:R-BTA-1306955", "REACTOME:R-BTA-1433557", "REACTOME:R-BTA-1483248", "REACTOME:R-BTA-166016", "REACTOME:R-B...

1,770

[ "1aqc", "1awe", "1b55", "1bak", "1btk", "1btn", "1bwn", "1dbh", "1ddm", "1ddv", "1ddw", "1dro", "1dyn", "1e5w", "1eaz", "1ef1", "1egx", "1evh", "1fao", "1fb8", "1fgy", "1fgz", "1fho", "1fhw", "1fhx", "1foe", "1gc6", "1gc7", "1gg3", "1h10", "1h4r", "1i2h"...

971

[ "PUB00000936", "PUB00006171", "PUB00014130", "PUB00014131", "PUB00018031", "PUB00018222", "PUB00029080", "PUB00057291" ]

[ "8646778", "10078529", "14594214", "12694559", "15567406", "15710406", "12429733", "21119626" ]

[ "Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor.", "Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport.", "Membrane targeting by pleckstrin homology domains.", "Phosphoinositide recognition domains.", ...

[ 1996, 1999, 2004, 2003, 2005, 2005, 2003, 2010 ]

8

[]

0

null

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

[ 442, 917707, 3, 8, 33 ]

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...

[ 373, 319, 4337, 588, 2226, 1541, 51, 238, 2242, 46, 43, 714 ]

12

true

Homologous_superfamily

PH-like domain superfamily

PH-like_dom_sf

4

IPR011994

11,994

Cytidylate kinase domain

Cytidylate_kinase_dom

Domain

25,980

false

Cytidylate kinase ( ) catalyses the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.

[ "GO:0005524", "GO:0036431", "GO:0006139" ]

[ "ATP binding", "dCMP kinase activity", "nucleobase-containing compound metabolic process" ]

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

3

[ "PFAM", "CDD" ]

[ "PF02224", "cd02020" ]

[ "Cytidylate_kin", "CMPK" ]

[ 24956, 25288 ]

2

[ "EC", "METACYC" ]

[ "2.7.4.25", "PWY-7205" ]

[ "EC:2.7.4.25", "METACYC:PWY-7205" ]

2

[ "1cke", "1kdo", "1kdp", "1kdr", "1kdt", "1q3t", "2cmk", "2fem", "2feo", "2h92", "3akc", "3akd", "3r20", "3r8c", "3w8n", "3w90", "4die", "4e22", "7ckj", "7l4a" ]

20

[]

0

[]

0

null

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

[ 816, 24130, 416, 618 ]

4

[ "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]

[ 1, 1 ]

2

true

Domain

Cytidylate kinase domain

Cytidylate_kinase_dom

8

IPR011995

11,995

Orotidine 5'-phosphate decarboxylase, type 2

OMPdecase_type-2

Family

11,920

false

Orotidine 5'-phosphate decarboxylase (OMPdecase) [ , ] catalyses the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofu...

[ "GO:0004590", "GO:0006221" ]

[ "orotidine-5'-phosphate decarboxylase activity", "pyrimidine nucleotide biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

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

[ "MF_01215", "PTHR43375", "TIGR02127" ]

[ "OMPdecase_type2", "", "pyrF_sub2" ]

[ 8113, 11673, 11675 ]

3

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

[ "4.1.1.23", "GenProp0187", "PWY-5686", "PWY-7790", "PWY-7791" ]

[ "EC:4.1.1.23", "GP:GenProp0187", "METACYC:PWY-5686", "METACYC:PWY-7790", "METACYC:PWY-7791" ]

5

[ "2aqw", "2f84", "2fds", "2ffc", "2guu", "2q8l", "2q8z", "2qaf", "2za1", "2za2", "2za3", "2zcg", "3bar", "3bpw", "3mwa", "3n2m", "3n34", "3n3m", "3qw3", "3qw4", "3r89", "3s9y", "3v75", "3vi2", "4mjz", "6dsq", "6dsr", "6dss" ]

28

[ "PUB00002768", "PUB00003724" ]

[ "1730672", "2835631" ]

[ "The orotidine-5'-monophosphate decarboxylase gene of Myxococcus xanthus. Comparison to the OMP decarboxylase gene family.", "Sequence analysis of the DdPYR5-6 gene coding for UMP synthase in Dictyostelium discoideum and comparison with orotate phosphoribosyl transferases and OMP decarboxylases." ]

[ 1992, 1988 ]

2

[]

0

null

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

[ 426, 10805, 403, 2, 284 ]

5

[]

0

true

Family

Orotidine 5'-phosphate decarboxylase, type 2

OMPdecase_type-2

2

IPR011998

11,998

Envelope glycoprotein E, central and dimerisation domain, flavivirus

Flavi_Glycoprot_E_cen/dimer

Domain

37,280

false

Flaviviruses and alphaviruses are arthropod-borne, enveloped RNA viruses that cause infections in vertebrate hosts [ ]. These viruses have two envelope glycoproteins (also known as 'spike' glycoproteins), one that undergoes proteolytic cleavage to prime the virus (glycoproteins M and P62 in flaviviruses and alphaviruse...

[ "GO:0046983" ]

[ "protein dimerization activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF00869" ]

[ "Flavi_glycoprot" ]

[ 37280 ]

1

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

[ "2.1.1.56", "2.1.1.57", "2.7.7.48", "3.4.21.91", "3.6.1.15", "3.6.4.13", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210", "PWY-7375", "PWY-7379" ]

[ "EC:2.1.1.56", "EC:2.1.1.57", "EC:2.7.7.48", "EC:3.4.21.91", "EC:3.6.1.15", "EC:3.6.4.13", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7185", "METACYC:PWY-7198", "METACYC:PWY-7210", "METACYC:PWY-7375", "METACYC:PWY-7379" ]

13

[ "1k4r", "1n6g", "1na4", "1oan", "1ok8", "1oke", "1p58", "1svb", "1tg8", "1tge", "1thd", "1urz", "1uzg", "2b6b", "2hg0", "2i69", "2of6", "2r6p", "3c5x", "3c6d", "3c6e", "3c6r", "3g7t", "3i50", "3ixx", "3ixy", "3iya", "3iyw", "3j05", "3j0b", "3j27", "3j2p"...

202

[ "PUB00015617", "PUB00015627", "PUB00065838" ]

[ "15378043", "12759475", "23236058" ]

[ "Transmission cycles, host range, evolution and emergence of arboviral disease.", "A ligand-binding pocket in the dengue virus envelope glycoprotein.", "Structure of a dengue virus envelope protein late-stage fusion intermediate." ]

[ 2004, 2003, 2013 ]

3

[]

0

null

[ "Bacillati", "Clonorchis sinensis", "Riboviria" ]

[ 2, 1, 37277 ]

3

[]

0

true

Domain

Envelope glycoprotein E, central and dimerisation domain, flavivirus

Flavi_Glycoprot_E_cen/dimer

6

IPR012001

12,001

Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain

Thiamin_PyroP_enz_TPP-bd_dom

Domain

129,951

false

A number of enzymes require thiamine pyrophosphate (TPP) (vitamin B1) as a cofactor. It has been shown [ ] that some of these enzymes are structurally related. There are two different functional modules in the thiamin diphosphate-binding fold, the pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules. This repr...

[ "GO:0030976" ]

[ "thiamine pyrophosphate binding" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF02776" ]

[ "TPP_enzyme_N" ]

[ 129951 ]

1

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

[ "2.2.1.9", "GenProp1226", "GenProp1245", "GenProp1256", "GenProp1269", "GenProp1292", "GenProp1328", "GenProp1334", "GenProp1342", "GenProp1467", "GenProp1485", "GenProp1620", "GenProp1655", "GenProp1698", "GenProp1722", "PWY-5837", "R-DDI-389599", "R-DDI-9033241", "R-HSA-389599"...

[ "EC:2.2.1.9", "GP:GenProp1226", "GP:GenProp1245", "GP:GenProp1256", "GP:GenProp1269", "GP:GenProp1292", "GP:GenProp1328", "GP:GenProp1334", "GP:GenProp1342", "GP:GenProp1467", "GP:GenProp1485", "GP:GenProp1620", "GP:GenProp1655", "GP:GenProp1698", "GP:GenProp1722", "METACYC:PWY-5837", ...

28

[ "1bfd", "1jsc", "1mcz", "1n0h", "1ovm", "1ozf", "1ozg", "1ozh", "1pi3", "1po7", "1pow", "1pox", "1pvd", "1pyd", "1q6z", "1qpb", "1t9a", "1t9b", "1t9c", "1t9d", "1upa", "1upb", "1upc", "1v5e", "1v5f", "1v5g", "1y9d", "1ybh", "1yhy", "1yhz", "1yi0", "1yi1"...

270

[ "PUB00015103" ]

[ "8604141" ]

[ "Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution." ]

[ 1996 ]

1

[]

[ "IPR022502", "IPR047210", "IPR047213" ]

0

3

0

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

[ 2736, 105759, 19662, 8, 1786 ]

5

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

[ 30, 3, 3, 1, 8, 14, 11, 5, 34, 11, 7, 6, 43 ]

13

true

Domain

Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain

Thiamin_PyroP_enz_TPP-bd_dom

4

IPR012002

12,002

Desulforedoxin

Family

148

false

This group represents desulforedoxin, which is a stand-alone version of the desulfoferrodoxin ( ) N-terminal domain. Desulforedoxins are small (approximately 36 amino acids) homodimeric non-haem iron proteins. Each subunit contains a high-spin iron atom tetrahedrally bound to four cysteinyl sulphur atoms [ , , , ]. The...

[]

0

[ "PIRSF" ]

[ "PIRSF000075" ]

[ "Desulforedoxin" ]

[ 148 ]

1

[]

0

[ "1cfw", "1dcd", "1dhg", "1dxg", "2lk5", "2lk6" ]

6

[ "PUB00005756", "PUB00012363", "PUB00015866", "PUB00015880", "PUB00015889", "PUB00016062", "PUB00016112", "PUB00016114", "PUB00016197", "PUB00016199" ]

[ "8647238", "10422844", "11128999", "12072976", "2254288", "12588121", "7666420", "9568899", "11912914", "10215854" ]

[ "Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins.", "Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein.", "Desulfoferrodoxin: a modular protein.", "Superoxide scavenging by neelaredox...

[ 1996, 1999, 2000, 2002, 1990, 2003, 1995, 1998, 2002, 1999 ]

10

[]

0

null

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

[ 69, 68, 11 ]

3

[]

0

true

Family

Desulforedoxin

7

IPR012003

12,003

ATP-dependent 6-phosphofructokinase, prokaryotic-type

ATP_PFK_prok-type

Family

19,677

false

Phosphofructokinase (PFK) catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate, which then enters the Embden-Meyerhof pathway. PFK is a key regulatory enzyme in glycolysis [ ]. The bacterial PFKs of this group are usually allosterically activated by ADP and inhibited by phosphoenolpyruvate ...

[ "GO:0005524", "GO:0008443", "GO:0006002", "GO:0006096" ]

[ "ATP binding", "phosphofructokinase activity", "fructose 6-phosphate metabolic process", "glycolytic process" ]

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

4

[ "PIRSF" ]

[ "PIRSF000532" ]

[ "ATP_PFK_prok" ]

[ 19677 ]

1

[ "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

[ "1mto", "1pfk", "1zxx", "2pfk", "3pfk", "3u39", "4a3s", "4i36", "4i4i", "4i7e", "4pfk", "5xoe", "5xz6", "5xz7", "5xz8", "5xz9", "5xza", "6pfk" ]

18

[ "PUB00013528", "PUB00014634", "PUB00015960", "PUB00015962" ]

[ "11778837", "14585511", "156307", "4229913" ]

[ "The biochemical properties and phylogenies of phosphofructokinases from extremophiles.", "Rampant horizontal gene transfer and phospho-donor change in the evolution of the phosphofructokinase.", "Structure and control of phosphofructokinase from Bacillus stearothermophilus.", "Kinetics of the allosteric inte...

[ 2001, 2003, 1979, 1968 ]

4

[ "IPR022953" ]

[ "IPR012828", "IPR012829" ]

1

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctx254", "unclassified sequences" ]

[ 71, 19229, 95, 1, 281 ]

5

[ "Escherichia coli (strain K12)", "Mus musculus" ]

[ 1, 1 ]

2

true

Family

ATP-dependent 6-phosphofructokinase, prokaryotic-type

ATP_PFK_prok-type

1

IPR012006

12,006

tRNA nucleotidyltransferase, proteobacteria

CCA_bact

Family

7,078

false

This family predominantly consists of bacterial versions of tRNA adenylyltransferases. tRNA nuceotidyltransferases are responsible for the synthesis or repair of the 3' terminal CCA sequence of tRNA molecules. They are encoded by essential genes in almost all organisms and add the three ribonucleotides C, C, and A to t...

[ "GO:0003723", "GO:0004810", "GO:0005524", "GO:0001680" ]

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

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

4

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

[ "MF_01261", "MF_01262", "PIRSF000813" ]

[ "CCA_bact_type1", "CCA_bact_type2", "CCA_bact" ]

[ 5438, 5408, 7058 ]

3

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

[ "2.7.7.72", "3.1.3.-", "3.1.4.-", "PWY-4702", "PWY-5491", "PWY-5978", "PWY-6129", "PWY-6148", "PWY-6352", "PWY-6365", "PWY-6366", "PWY-6368", "PWY-6456", "PWY-6575", "PWY-6627", "PWY-6664", "PWY-6686", "PWY-6689", "PWY-6720", "PWY-6724", "PWY-6955", "PWY-6990", "PWY-6991"...

[ "EC:2.7.7.72", "EC:3.1.3.-", "EC:3.1.4.-", "METACYC:PWY-4702", "METACYC:PWY-5491", "METACYC:PWY-5978", "METACYC:PWY-6129", "METACYC:PWY-6148", "METACYC:PWY-6352", "METACYC:PWY-6365", "METACYC:PWY-6366", "METACYC:PWY-6368", "METACYC:PWY-6456", "METACYC:PWY-6575", "METACYC:PWY-6627", "ME...

42

[]

0

[ "PUB00005837", "PUB00007363", "PUB00011196", "PUB00013566", "PUB00015829", "PUB00015862" ]

[ "9868367", "10447505", "10943560", "10075991", "12526808", "15210699" ]

[ "The HD domain defines a new superfamily of metal-dependent phosphohydrolases.", "Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events.", "A specialized version of the HD hydrolase domain implicated i...

[ 1998, 1999, 1999, 1999, 2002, 2004 ]

6

[]

0

null

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

[ 6956, 34, 6, 2, 80 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

tRNA nucleotidyltransferase, proteobacteria

CCA_bact

6

IPR012010

12,010

Urease, gamma subunit

Urease_gamma

Family

8,840

false

Urease (urea amidohydrolase, ) is a nickel-dependent metalloenzyme that catalyses the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. T...

[ "GO:0009039", "GO:0019627" ]

[ "urease activity", "urea metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "PIRSF" ]

[ "MF_00739", "PIRSF001223" ]

[ "Urease_gamma", "Urease_gamma" ]

[ 8572, 8266 ]

2

[ "EC", "METACYC" ]

[ "3.5.1.5", "PWY-5704" ]

[ "EC:3.5.1.5", "METACYC:PWY-5704" ]

2

[ "1a5k", "1a5l", "1a5m", "1a5n", "1a5o", "1ef2", "1ejr", "1ejs", "1ejt", "1eju", "1ejv", "1ejw", "1ejx", "1fwa", "1fwb", "1fwc", "1fwd", "1fwe", "1fwf", "1fwg", "1fwh", "1fwi", "1fwj", "1ie7", "1kra", "1krb", "1krc", "1s3t", "1ubp", "2fvh", "2kau", "2ubp"...

73

[ "PUB00004994", "PUB00005206", "PUB00010725" ]

[ "9144792", "7754395", "7565414" ]

[ "An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.", "The crystal structure of urease from Klebsiella aerogenes.", "Molecular biology of microbial ureases." ]

[ 1997, 1995, 1995 ]

3

[ "IPR002026" ]

[]

1

0

1

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

[ 138, 8627, 4, 71 ]

4

[]

0

true

Family

Urease, gamma subunit

Urease_gamma

6

IPR012013

12,013

Integrin beta-4 subunit

Integrin_bsu-4

Family

401

false

The beta 4 subunit differs from other beta subunits in three ways: 1) the cytoplasmic domain is larger; 2) it lacks some of the conserved cysteines in the extracellular domain; and 3) it has a unique domain organisation. Integrin alpha-6/beta-4 is a receptor for laminin. It plays a critical structural role in the hemid...

[ "GO:0007160", "GO:0007229", "GO:0031581", "GO:0048870", "GO:0008305" ]

[ "cell-matrix adhesion", "integrin-mediated signaling pathway", "hemidesmosome assembly", "cell motility", "integrin complex" ]

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

5

[ "PIRSF" ]

[ "PIRSF002513" ]

[ "Integrin_B4" ]

[ 401 ]

1

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

[ "R-HSA-2022090", "R-HSA-3000157", "R-HSA-3000170", "R-HSA-446107", "R-HSA-9725554", "R-MMU-3000157", "R-MMU-3000170", "R-MMU-446107", "R-RNO-3000157", "R-RNO-3000170", "R-RNO-446107" ]

[ "REACTOME:R-HSA-2022090", "REACTOME:R-HSA-3000157", "REACTOME:R-HSA-3000170", "REACTOME:R-HSA-446107", "REACTOME:R-HSA-9725554", "REACTOME:R-MMU-3000157", "REACTOME:R-MMU-3000170", "REACTOME:R-MMU-446107", "REACTOME:R-RNO-3000157", "REACTOME:R-RNO-3000170", "REACTOME:R-RNO-446107" ]

11

[]

0

[ "PUB00009789", "PUB00015870", "PUB00015894", "PUB00015903", "PUB00015904", "PUB00015915", "PUB00015923", "PUB00015967", "PUB00015985", "PUB00016048", "PUB00016135", "PUB00035000", "PUB00035002", "PUB00062810", "PUB00062811" ]

[ "12297042", "9166594", "9402004", "2311578", "2311577", "14689578", "2542022", "15157503", "2467745", "1976638", "7982032", "12361595", "12234368", "12482924", "19403692" ]

[ "Integrins: bidirectional, allosteric signaling machines.", "Genomic organization of the human integrin beta4 gene.", "Integrin cytoplasmic domains as connectors to the cell's signal transduction apparatus.", "Cloning and sequence analysis of beta-4 cDNA: an integrin subunit that contains a unique 118 kd cyto...

[ 2002, 1997, 1997, 1990, 1990, 2004, 1989, 1996, 1989, 1990, 1994, 2002, 2002, 2003, 2009 ]

15

[ "IPR015812" ]

[]

1

0

1

[ "Theria" ]

[ 401 ]

1

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

[ 3, 2, 5 ]

3

true

Family

Integrin beta-4 subunit

Integrin_bsu-4

4

IPR012014

12,014

Retroelement-encoded protein, env-related

Retroelement_env

Family

4

false

Members of this group are encoded by LTR-retrotransposons and have sequence similarity to env genes of retroviruses [ ]. ZAM and Idefix are two LTR-retrotransposons from Drosophila melanogaster and are similar in structure to vertebrate retroviruses. In most strains where the distribution has been studied, ZAM appears ...

[]

0

[ "PIRSF" ]

[ "PIRSF004631" ]

[ "Retroelement_env" ]

[ 4 ]

1

[]

0

[]

0

[ "PUB00014660", "PUB00014661", "PUB00014662", "PUB00014663" ]

[ "11865056", "10331252", "14585982", "11293795" ]

[ "Coupling of enhancer and insulator properties identified in two retrotransposons modulates their mutagenic impact on nearby genes.", "Mobilization of two retroelements, ZAM and Idefix, in a novel unstable line of Drosophila melanogaster.", "The 5' untranslated region and Gag product of Idefix, a long terminal ...

[ 2002, 1999, 2003, 2000 ]

4

[]

0

null

[ "Drosophila melanogaster" ]

[ 4 ]

1

[ "Drosophila melanogaster" ]

[ 4 ]

1

true

Family

Retroelement-encoded protein, env-related

Retroelement_env

3

IPR012015

12,015

Uncharacterised conserved protein HTH transcriptional regulator, archaea

UCP_HTH_arc

Family

618

false

This family consists of functionally uncharacterised proteins, which contain an N-terminal HTH (Winged helix-turn-helix) DNA-binding domain.

[]

0

[ "PIRSF" ]

[ "PIRSF004955" ]

[ "HTH_arch" ]

[ 618 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Dehalococcoidaceae", "Methanobacteriati", "unclassified sequences" ]

[ 12, 597, 9 ]

3

[]

0

true

Family

Uncharacterised conserved protein HTH transcriptional regulator, archaea

UCP_HTH_arc

2

IPR012017

12,017

Origin-associated protein OapB-like

OapB-like

Family

518

false

This entry includes archaeal proteins whose function is unclear. Some members of this entry have been described as OapB/Arvb, encoded by oapB gene which is part of the three-gene cluster oapABC (origin-associated proteins), involved in generation of extracellular vesicles (arv, archaeal vesiculating GTAse) [ , ]. It ha...

[]

0

[ "PFAM", "PIRSF" ]

[ "PF09846", "PIRSF004977" ]

[ "OapB", "UCP004977" ]

[ 518, 491 ]

2

[]

0

[]

0

[ "PUB00154442", "PUB00154443" ]

[ "31769790", "38408251" ]

[ "Bioinformatic and genetic characterization of three genes localized adjacent to the major replication origin of Haloferax volcanii.", "Extracellular vesicle formation in Euryarchaeota is driven by a small GTPase." ]

[ 2019, 2024 ]

2

[]

0

null

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

[ 507, 2, 9 ]

3

[]

0

true

Family

Origin-associated protein OapB-like

OapB-like

3

IPR012019

12,019

FeGP cofactor biosynthesis protein HcgB, guanylyltransferase

HcgB

Family

78

false

This entry represents the guanylyltransferase component of the Iron-guanylylpyridinol (FeGP) cofactor biosynthesis protein HcgB [ , ]. HcgB transfers the guanosine monophosphate (GMP) moiety from guanosine triphosphate (GTP) to a pyridinol precursor [ ].

[]

0

[ "PFAM", "PIRSF" ]

[ "PF11576", "PIRSF005018" ]

[ "HcgB", "UCP005018" ]

[ 78, 52 ]

2

[]

0

[ "3brc", "3wb0", "3wb1", "3wb2", "5d5p", "5d5q" ]

6

[ "PUB00098596", "PUB00152291" ]

[ "25882909", "28294213" ]

[ "Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor.", "Towards artificial methanogenesis: biosynthesis of the [Fe]-hydrogenase cofactor and characterization of the semi-synthetic hydrogenase." ]

[ 2015, 2017 ]

2

[]

0

null

[ "Desulfurobacterium", "Methanobacteriota", "bioreactor metagenome" ]

[ 4, 73, 1 ]

3

[]

0

true

Family

FeGP cofactor biosynthesis protein HcgB, guanylyltransferase

HcgB

6

IPR012020

12,020

AB hydrolase 4 family

ABHD4

Family

15,633

false

This entry represents a group of abhydrolase domain-containing proteins, including mammalian ABHD1/2/3/15 and budding yeast Eht1, Eeb1 and YMR210W. Human ABHD3 is a phospholipase that may play a role in phospholipids remodeling. It may selectively cleave myristate (C14)-containing phosphatidylcholines through its predo...

[]

0

[ "PIRSF" ]

[ "PIRSF005211" ]

[ "Ab_hydro_YheT" ]

[ 15633 ]

1

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

[ "3.1.1", "R-BTA-1483191", "R-CEL-1483191", "R-DDI-1483191", "R-HSA-1483191", "R-MMU-1483191", "R-SCE-1483191" ]

[ "EC:3.1.1", "REACTOME:R-BTA-1483191", "REACTOME:R-CEL-1483191", "REACTOME:R-DDI-1483191", "REACTOME:R-HSA-1483191", "REACTOME:R-MMU-1483191", "REACTOME:R-SCE-1483191" ]

7

[]

0

[ "PUB00074273", "PUB00074274", "PUB00074275" ]

[ "21926997", "16361250", "15721306" ]

[ "Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids.", "The Saccharomyces cerevisiae EHT1 and EEB1 genes encode novel enzymes with medium-chain fatty acid ethyl ester synthesis and hydrolysis capacity.", "Increase of smooth muscle cell migration and of intimal hyperplasia in m...

[ 2011, 2006, 2005 ]

3

[]

0

null

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

[ 8176, 7380, 3, 74 ]

4

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

[ 7, 3, 7, 4, 1, 9, 6, 1, 2, 10, 3, 3 ]

12

true

Family

AB hydrolase 4 family

ABHD4

1

IPR012022

12,022

Protein of unknown function UCP005295

UCP005295

Family

2,950

false

Members of this group are predicted to be metal-dependent hydrolases based on sequence analysis. They are related to Mg-dependent DNases and contain a TadD DNase domain. However, the similarity is not strong enough to confidently predict that these proteins are necessarily DNases and not some other type of metal-depend...

[]

0

[ "PIRSF", "PANTHER" ]

[ "PIRSF005295", "PTHR42658" ]

[ "UCP005295_TatD", "" ]

[ 2499, 2950 ]

2

[]

0

[ "3guw" ]

1

[ "PUB00004994" ]

[ "9144792" ]

[ "An evolutionary treasure: unification of a broad set of amidohydrolases related to urease." ]

[ 1997 ]

1

[ "IPR001130" ]

[]

1

0

1

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

[ 302, 2612, 4, 32 ]

4

[]

0

true

Family

Protein of unknown function UCP005295

UCP005295

4

IPR012025

12,025

Methanogenesis marker 6 protein

Methan_mark_6

Family

251

false

The exact function of this protein unknown, but likely is linked to methanogenesis or a process closely connected to it.

[]

0

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

[ "PF09875", "PIRSF005642", "TIGR03272" ]

[ "DUF2102", "UCP005642", "methan_mark_6" ]

[ 251, 199, 233 ]

3

[ "GP" ]

[ "GenProp0722" ]

[ "GP:GenProp0722" ]

1

[]

0

[]

0

[]

0

null

[ "Archaea", "ecological metagenomes" ]

[ 245, 6 ]

2

[]

0

true

Family

Methanogenesis marker 6 protein

Methan_mark_6

1

IPR012027

12,027

Formylmethanofuran dehydrogenase, subunit A

Formylmethanofuran_DH_asu

Family

1,189

false

Formylmethanofuran dehydrogenase ( ) is found in methanogenic and sulphate-reducing archaea. The enzyme contains molybdenum or tungsten, a molybdopterin guanine dinuceotide cofactor (MGD) and iron-sulphur clusters [ ]. It catalyses the reversible reduction of CO 2 and methanofuran via N-carboxymethanofuran (carbamate) ...

[]

0

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

[ "PIRSF006453", "TIGR03121", "cd01304" ]

[ "FwdA", "one_C_dehyd_A", "FMDH_A" ]

[ 1036, 1189, 421 ]

3

[ "GP" ]

[ "GenProp0671" ]

[ "GP:GenProp0671" ]

1

[ "5t5i", "5t5m", "5t61", "6s6y", "7bkb", "7bkc", "8rja" ]

7

[ "PUB00000170", "PUB00001777", "PUB00007126", "PUB00008259", "PUB00015859", "PUB00016174", "PUB00016198", "PUB00042893", "PUB00042895", "PUB00081793" ]

[ "9818358", "2570735", "8672295", "8125106", "8575452", "8954165", "11532013", "9342247", "12492476", "2128800" ]

[ "The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme.", "Organization of the yeast URA2 gene: identification of a defective dihydroorotase-like d...

[ 1998, 1989, 1996, 1994, 1995, 1996, 2001, 1997, 2003, 1990 ]

10

[]

0

null

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

[ 420, 741, 1, 27 ]

4

[]

0

true

Family

Formylmethanofuran dehydrogenase, subunit A

Formylmethanofuran_DH_asu

4

IPR012028

12,028

Guanylylpyridinol adenylase HcgE

HcgE

Family

58

false

This entry represents Guanylylpyridinol adenylase HcgE, Uncharacterized protein MJ0693 and similar proteins that contain a divergent form of a domain based on the common NAD/FAD-binding fold. Members are distantly related to the HesA/MoeB/ThiF group of NAD/FAD-binding fold enzymes. HcgE is an adenylyltransferase from M...

[]

0

[ "PIRSF" ]

[ "PIRSF006529" ]

[ "UCP006529_dinclt" ]

[ 58 ]

1

[]

0

[ "3wv7", "3wv8", "3wv9" ]

3

[ "PUB00098596" ]

[ "25882909" ]

[ "Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor." ]

[ 2015 ]

1

[]

0

null

[ "Methanobacteriota" ]

[ 58 ]

1

[]

0

true

Family

Guanylylpyridinol adenylase HcgE

HcgE

8

IPR012029

12,029

MJ0405

Family

220

false

This family of hypothetical archaeal proteins has no known function including Uncharacterized protein MJ0405.

[]

0

[ "PFAM", "PIRSF" ]

[ "PF09884", "PIRSF006557" ]

[ "DUF2111", "UCP006557_sign" ]

[ 220, 142 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Archaea", "ecological metagenomes" ]

[ 215, 5 ]

2

[]

0

true

Family

MJ0405

6

IPR012031

12,031

MTH0776-like

Family

290

false

This entry represents a family of archaeal proteins with an important role in methanogenesis, including MTH0776 from Methanobacterium thermoautotrophicum. This protein assume an α-β globular structure consisting of six β-strands and three α-helices forming the secondary structural topological arrangement of α1-β1-α2-β2...

[]

0

[ "PFAM", "PIRSF" ]

[ "PF08979", "PIRSF006577" ]

[ "DUF1894", "UCP006577" ]

[ 290, 202 ]

2

[]

0

[ "1z9v" ]

1

[ "PUB00035386" ]

[ "16222557" ]

[ "Solution Structure of MTH0776 from Methanobacterium thermoautotrophicum." ]

[ 2005 ]

1

[]

0

null

[ "Methanobacteriota", "ecological metagenomes" ]

[ 281, 9 ]

2

[]

0

true

Family

MTH0776-like

5

IPR012032

12,032

MJ0065

Family

264

false

This entry includes Uncharacterized protein MJ0065 from archaea.

[]

0

[ "PFAM", "PIRSF" ]

[ "PF09890", "PIRSF006598" ]

[ "DUF2117", "UCP006598" ]

[ 264, 139 ]

2

[]

0

[]

0

[ "PUB00160784" ]

[ "38748582" ]

[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of Escherichia coli." ]

[ 2024 ]

1

[]

0

null

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

[ 253, 4, 7 ]

3

[]

0

true

Family

MJ0065

3

IPR012033

12,033

MJ0452

Family

188

false

This entry includes Uncharacterized protein MJ0452. The structure of the Methanothermobacter thermautotrophicus (Methanobacterium thermoformicicum) protein has been determined but no evidence of the function is available yet.

[]

0

[ "PFAM", "PIRSF" ]

[ "PF09001", "PIRSF006600" ]

[ "DUF1890", "UCP006600" ]

[ 188, 164 ]

2

[]

0

[ "1kjn" ]

1

[]

0

[]

0

null

[ "Methanobacteriota", "ecological metagenomes" ]

[ 182, 6 ]

2

[]

0

true

Family

MJ0452

4

IPR012036

12,036

Bacteriophage Mu, Probable terminase, large subunit gp28

Phage_Mu_Gp28

Family

1,082

false

This entry represents Probable terminase, large subunit gp28 from the Bacteriophage Mu and similar proteins from tailed bacteriophages and prophages from Proteobacteria. Gp28 may be related to viral DNA translocation into empty capsids and act as an endonuclease that cuts the viral genome to initiate and to end a packa...

[]

0

[ "PIRSF" ]

[ "PIRSF007056" ]

[ "UCP007056" ]

[ 1082 ]

1

[]

0

[]

0

[]

0

[]

0

null

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

[ 1038, 35, 9 ]

3

[]

0

true

Family

Bacteriophage Mu, Probable terminase, large subunit gp28

Phage_Mu_Gp28

2

IPR012037

12,037

Alpha/beta-hydrolase family

Alpha/beta-hydrolase_fam

Family

1,731

false

This is a family of α/β hydrolases which may function as lipases. This domain is the catalytic domain and includes the catalytic triad and the GXSXG sequence motif which is a characteristic of these enzymes [ ].

[]

0

[ "PIRSF" ]

[ "PIRSF007542" ]

[ "UCP007542" ]

[ 1731 ]

1

[]

0

[]

0

[ "PUB00066711" ]

[ "21333648" ]

[ "Novel transmembrane lipases of alpha/beta hydrolase fold." ]

[ 2011 ]

1

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 1726, 5 ]

2

[]

0

true

Family

Alpha/beta-hydrolase family

Alpha/beta-hydrolase_fam

2

IPR012038

12,038

Uncharacterised conserved protein UCP009471

UCP009471

Family

1,150

false

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

[]

0

[ "PIRSF" ]

[ "PIRSF009471" ]

[ "UCP009471" ]

[ 1150 ]

1

[]

0

[]

0

[ "PUB00160784" ]

[ "38748582" ]

[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of Escherichia coli." ]

[ 2024 ]

1

[]

0

null

[ "Bacteria", "Methanobacteriota", "ecological metagenomes" ]

[ 1136, 8, 6 ]

3

[]

0

true

Family

Uncharacterised conserved protein UCP009471

UCP009471

6

IPR012039

12,039

Uncharacterised conserved protein UCP012281

UCP012281

Family

951

false

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

[]

0

[ "PIRSF" ]

[ "PIRSF012281" ]

[ "UCP012281" ]

[ 951 ]

1

[]

0

[]

0

[ "PUB00160784" ]

[ "38748582" ]

[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of Escherichia coli." ]

[ 2024 ]

1

[]

0

null

[ "Pseudomonadota" ]

[ 951 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Uncharacterised conserved protein UCP012281

UCP012281

4

IPR012040

12,040

Formylmethanofuran dehydrogenase, subunit D

Formylmethanofuran_DH_dsu

Family

342

false

This entry represents subunit D (FmdD and FwdD) of formylmethanofuran dehydrogenase. The other subunits are subunit A ( ), subunit B ( ), subunit C ( ), subunit E ( ), subunit F. Some organisms also encode a fusion of the C and D subunits ( ). Members of this entry contain a molybdopterin dinucleotide binding domain. T...

[]

0

[ "PIRSF" ]

[ "PIRSF015873" ]

[ "FwdD" ]

[ 342 ]

1

[]

0

[ "2ki8", "5t5i", "5t5m", "5t61", "8rja" ]

5

[ "PUB00000170", "PUB00008259", "PUB00015859", "PUB00016174", "PUB00042893", "PUB00042895" ]

[ "9818358", "8125106", "8575452", "8954165", "9342247", "12492476" ]

[ "The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme.", "Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR ...

[ 1998, 1994, 1995, 1996, 1997, 2003 ]

6

[]

0

null

[ "Archaea", "ecological metagenomes" ]

[ 330, 12 ]

2

[]

0

true

Family

Formylmethanofuran dehydrogenase, subunit D

Formylmethanofuran_DH_dsu

9

IPR012041

12,041

CPxCG-like zinc finger protein

Znf_CPxCG-like

Family

657

false

This family includes small CPxCG-related zinc finger archaeal proteins, which are thought to bind DNA and to be potential transcriptional regulators. These zinc fingers are characterised by the specific CPxCG pattern (variants CPxCx and CxxCG) and a second Cys/His pattern potentially more general, being 7-40 residues a...

[]

0

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

[ "PF19769", "PIRSF015877", "PTHR42195" ]

[ "CPxCG_zf", "UCP015877", "" ]

[ 657, 589, 654 ]

3

[]

0

[]

0

[ "PUB00095525" ]

[ "24930989" ]

[ "The transcriptional activator NrpA is crucial for inducing nitrogen fixation in Methanosarcina mazei Go1 under nitrogen-limited conditions." ]

[ 2014 ]

1

[]

0

null

[ "Archaea", "ecological metagenomes" ]

[ 646, 11 ]

2

[]

0

true

Family

CPxCG-like zinc finger protein

Znf_CPxCG-like

7

IPR012042

12,042

Inorganic triphosphatase NeuTTM/CthTTM-like

NeuTTM/CthTTM-like

Family

5,729

false

This entry includes bacterial CYTH-domain containing proteins such as NeuTTM ( ) from Nitrosomonas europaea [ ] and CthTTM ( ) from Clostridium thermocellum [ ] They both have a high PPPase activity (though CthTM was less specific) but neither had any significant adenylyl cyclase activity [ ]. CYTH domain proteins act ...

[]

0

[ "PIRSF", "PANTHER" ]

[ "PIRSF016487", "PTHR40114" ]

[ "CYTH_UCP016487", "" ]

[ 5384, 5615 ]

2

[]

0

[ "2fbl", "3typ" ]

2

[ "PUB00076458", "PUB00076460", "PUB00076462", "PUB00076464" ]

[ "22984449", "21840996", "17303560", "24021036" ]

[ "High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved.", "A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism.", "Novel triphosphate phosphohydrolase activity of Clostridium thermocellum TTM, a member of th...

[ 2012, 2011, 2007, 2013 ]

4

[]

0

null

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

[ 9, 5548, 22, 31, 119 ]

5

[]

0

true

Family

Inorganic triphosphatase NeuTTM/CthTTM-like

NeuTTM/CthTTM-like

8

IPR012043

12,043

Pantoate kinase

PoK

Family

967

false

Pantoate kinase (PoK) is an enzyme that belongs to the GHMP kinase family, specifically the PoK subfamily. It is responsible for phosphorylating (R)-pantoate to form (R)-4-phosphopantoate, a crucial step in the coenzyme A (CoA) biosynthesis pathway. ATP is the preferred phosphate donor for this reaction, although UTP c...

[]

0

[ "HAMAP", "PIRSF", "PANTHER" ]

[ "MF_02223", "PIRSF016896", "PTHR42282" ]

[ "Pantoate_kinase", "GHMP_arc_MJ0969", "" ]

[ 890, 830, 967 ]

3

[ "EC", "METACYC" ]

[ "2.7.1.169", "PWY-6654" ]

[ "EC:2.7.1.169", "METACYC:PWY-6654" ]

2

[ "6jbc", "6jbd" ]

2

[ "PUB00015644", "PUB00015669", "PUB00015675", "PUB00015730", "PUB00015835", "PUB00060435" ]

[ "11188689", "12771135", "8382990", "12001237", "12796487", "19666462" ]

[ "Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily.", "Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis.", "Convergent evolution of similar enzymatic function on different protein ...

[ 2000, 2003, 1993, 2002, 2003, 2009 ]

6

[]

[ "IPR054946" ]

0

1

0

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

[ 901, 33, 33 ]

3

[]

0

true

Family

Pantoate kinase

PoK

8

IPR012047

12,047

Aconitase X

AcnX

Family

1,092

false

Distant sequence similarity and comparative genomic analysis shows aconitase X (AcnX) is a subfamily of aconitase enzymes [ ]. However, Aconitase X (corresponding gene known as LhpI) is a cis-3-hydroxy-L-proline dehydratase containing mononuclear Fe(III), but not the [4Fe-4S] cluster. Bacteria with the LhpI gene could ...

[]

0

[ "NCBIFAM", "PIRSF" ]

[ "NF051439", "PIRSF036630" ]

[ "C3LHypDHLhpIPSEAE", "UCP036630" ]

[ 1031, 1057 ]

2

[ "EC" ]

[ "4.2.1.171" ]

[ "EC:4.2.1.171" ]

1

[ "7cnp", "7cnq", "7d2r" ]

3

[ "PUB00080857", "PUB00088769" ]

[ "14568143", "27929065" ]

[ "Filling a gap in the central metabolism of archaea: prediction of a novel aconitase by comparative-genomic analysis.", "Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase." ]

[ 2003, 2016 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)", "unclassified sequences" ]

[ 601, 487, 1, 3 ]

4

[]

0

true

Family

Aconitase X

AcnX

5

IPR012048

12,048

Formylmethanofuran dehydrogenase, fused subunit C/D

Formylmethanofuran_DH_csu/dsu

Family

14

false

Formylmethanofuran dehydrogenase ( ) is found in methanogenic and sulphate-reducing archaea. The enzyme contains molybdenum or tungsten, a molybdopterin guanine dinuceotide cofactor (MGD) and iron-sulphur clusters [ ]. It catalyses the reversible reduction of CO 2 and methanofuran via N-carboxymethanofuran (carbamate) ...

[ "GO:0018493", "GO:0030151", "GO:0015948" ]

[ "formylmethanofuran dehydrogenase activity", "molybdenum ion binding", "methanogenesis" ]

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

3

[ "PIRSF" ]

[ "PIRSF036633" ]

[ "FmdC_D" ]

[ 14 ]

1

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

[ "1.2.7.12", "PWY-5209", "PWY-7784", "PWY-8305" ]

[ "EC:1.2.7.12", "METACYC:PWY-5209", "METACYC:PWY-7784", "METACYC:PWY-8305" ]

4

[]

0

[ "PUB00000170", "PUB00008259", "PUB00015859", "PUB00016174", "PUB00042893", "PUB00042895" ]

[ "9818358", "8125106", "8575452", "8954165", "9342247", "12492476" ]

[ "The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme.", "Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR ...

[ 1998, 1994, 1995, 1996, 1997, 2003 ]

6

[]

0

null

[ "Methanomada group" ]

[ 14 ]

1

[]

0

true

Family

Formylmethanofuran dehydrogenase, fused subunit C/D

Formylmethanofuran_DH_csu/dsu

4

IPR012049

12,049

Menaquinone:cytochrome c reductase, cytochrome b/c subunit

MenaQ_cyt_c_Rdtase_cyt_b/c-su

Family

590

false

The qcr operon in Bacillus subtilis encodes the menaquinone:cytochrome c reductase complex, which is closely related to but distinct from mitochondrial cytochrome bc1 and chloroplast b6f complexes. QcrA is similar to Rieske-type iron-sulphur proteins; QcrB is similar in size and sequence to b-type cytochromes from b6f ...

[ "GO:0005506", "GO:0009055", "GO:0020037", "GO:0016020" ]

[ "iron ion binding", "electron transfer activity", "heme binding", "membrane" ]

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

4

[ "PIRSF" ]

[ "PIRSF036636" ]

[ "QcrC" ]

[ 590 ]

1

[]

0

[]

0

[ "PUB00015936" ]

[ "7592464" ]

[ "The cytochrome bc complex (menaquinone:cytochrome c reductase) in Bacillus subtilis has a nontraditional subunit organization." ]

[ 1995 ]

1

[ "IPR051811" ]

[]

1

0

1

[ "Bacilli" ]

[ 590 ]

1

[]

0

true

Family

Menaquinone:cytochrome c reductase, cytochrome b/c subunit

MenaQ_cyt_c_Rdtase_cyt_b/c-su

2

IPR012052

12,052

Sporulation transcription factor Spo0A

Spore_0_A

Family

2,926

false

Members of this group are response regulators/transcription factors that contain CheY-like receiver (phosphoacceptor) domain and a unique DNA-binding domain. Spo0A controls the entry of Bacillus subtilis into the developmental process of sporulation [ ]. Activation of the Spo0A transcription factor by phosphorylation s...

[ "GO:0003677", "GO:0005509", "GO:0006355", "GO:0043937", "GO:0051606" ]

[ "DNA binding", "calcium ion binding", "regulation of DNA-templated transcription", "regulation of sporulation", "detection of stimulus" ]

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

5

[ "PIRSF", "NCBIFAM" ]

[ "PIRSF002937", "TIGR02875" ]

[ "Res_reg_Spo0A", "spore_0_A" ]

[ 2820, 2923 ]

2

[ "GP" ]

[ "GenProp0610" ]

[ "GP:GenProp0610" ]

1

[ "1fc3", "1lq1" ]

2

[ "PUB00014649", "PUB00014652" ]

[ "11286862", "8464402" ]

[ "Lessons and questions from the structure of the Spo0A activation domain.", "Bacillus subtilis sporulation: regulation of gene expression and control of morphogenesis." ]

[ 2001, 1993 ]

2

[]

0

null

[ "Bacteria", "Phytophthora kernoviae 00238/432", "metagenomes" ]

[ 2897, 1, 28 ]

3

[]

0

true

Family

Sporulation transcription factor Spo0A

Spore_0_A

9

IPR012061

12,061

Glutamate synthase, large subunit domain 3 stand-alone protein

Glu_synth_lsu_3

Family

2,380

false

The large (alpha, GltB) subunit of bacterial glutamate synthase (GOGAT) consists of three domains: N-terminal domain (amidotransferase domain) or related (in archaeal GOGAT), central domain and the FMN-binding domain, and C-terminal domain. This family represents a stand-alone form of the C-terminal domain. The stand-a...

[]

0

[ "PIRSF" ]

[ "PIRSF006519" ]

[ "GOGAT_dom3" ]

[ 2380 ]

1

[]

0

[]

0

[ "PUB00008698", "PUB00009386", "PUB00013982", "PUB00015710" ]

[ "11967268", "10357231", "11188694", "11230537" ]

[ "Structural studies on the synchronization of catalytic centers in glutamate synthase.", "Glutamate synthase: a complex iron-sulfur flavoprotein.", "Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase.", "Phylogenetic analyses of two \"archaeal\"...

[ 2002, 1999, 2000, 2001 ]

4

[]

[ "IPR035710" ]

0

1

0

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

[ 238, 2113, 29 ]

3

[]

0

true

Family

Glutamate synthase, large subunit domain 3 stand-alone protein

Glu_synth_lsu_3

4

IPR012066

12,066

Uroporphyrin-III C-methyltransferase, fungi

Met1_fungi

Family

1,158

false

This entry represents Met1, an uroporphyrinogen-III C-methyltransferase that is involved in the biosynthesis of siroheme and is required for sulfate assimilation and methionine biosynthesis [ , , ].

[ "GO:0004851", "GO:0000103", "GO:0019354" ]

[ "uroporphyrin-III C-methyltransferase activity", "sulfate assimilation", "siroheme biosynthetic process" ]

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

3

[ "PIRSF" ]

[ "PIRSF036555" ]

[ "SUMT_yeast" ]

[ 1158 ]

1

[]

0

[]

0

[ "PUB00014702", "PUB00016134", "PUB00078117" ]

[ "10051442", "9003798", "1479340" ]

[ "The role of Saccharomyces cerevisiae Met1p and Met8p in sirohaem and cobalamin biosynthesis.", "Siroheme biosynthesis in Saccharomyces cerevisiae requires the products of both the MET1 and MET8 genes.", "Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilation." ]

[ 1999, 1997, 1992 ]

3

[]

0

null

[ "Eukaryota" ]

[ 1158 ]

1

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

[ 1, 1, 1 ]

3

true

Family

Uroporphyrin-III C-methyltransferase, fungi

Met1_fungi

5

IPR012069

12,069

Uncharacterised protein family, CYTH/CHAD/HD-like domain-containing

UPF_CYTH/CHAD/HD-like

Family

30

false

This group includes uncharacterised proteins from Methanosarcina spp. with CYTH and CHAD domains, and a central HD-like domain. CYTH domain proteins may play a central role in the interface between nucleotide and polyphosphate metabolism [ ]. Based on the conservation of catalytic residues, CYTH domains are likely to c...

[]

0

[ "PIRSF" ]

[ "PIRSF036568" ]

[ "CYTH_CHAD_HD" ]

[ 30 ]

1

[]

0

[]

0

[ "PUB00010433" ]

[ "12456267" ]

[ "The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates." ]

[ 2002 ]

1

[]

0

null

[ "Methanosarcina" ]

[ 30 ]

1

[]

0

true

Family

Uncharacterised protein family, CYTH/CHAD/HD-like domain-containing

UPF_CYTH/CHAD/HD-like

9

IPR012070

12,070

Arogenate dehydrogenase 2

Arogenate_DH_2

Family

295

false

Proteins in this entry belong to the prephenate dehydrogenase (PDH) domain superfamily ( ). Members of this group catalyse a step in tyrosine biosynthesis in the shikimate pathway, which is present only in bacteria, archaea, fungi, and plants [ ]. Many of the PDH enzymes are able to use the alternative intermediates of...

[ "GO:0033730", "GO:0006571" ]

[ "arogenate dehydrogenase (NADP+) activity", "L-tyrosine biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF" ]

[ "PIRSF036577" ]

[ "PDH_ADH_plant" ]

[ 295 ]

1

[]

0

[]

0

[ "PUB00011044", "PUB00011046", "PUB00015637", "PUB00016002" ]

[ "12354106", "2123197", "11476485", "3556217" ]

[ "Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana.", "A single cyclohexadienyl dehydrogenase specifies the prephenate dehydrogenase and arogenate dehydrogenase components of the dual pathways to L-tyrosine in Pseudomonas aeruginosa.", "The biosynt...

[ 2002, 1990, 2001, 1987 ]

4

[ "IPR045011" ]

[]

1

0

1

[ "Coxiella burnetii", "Viridiplantae" ]

[ 2, 293 ]

2

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

[ 2, 2, 3 ]

3

true

Family

Arogenate dehydrogenase 2

Arogenate_DH_2

4

IPR012071

12,071

Chemotaxis glutamate methyltransferase

Chemotax_glutamate_MeTrfase

Family

85

false

Members of this group contain a divergent form of CheB-like protein-glutamate methylesterase domain in the C-terminal region. This domain is usually found fused with CheY-like receiver (response regulator) domain, forming CheB response regulator methylesterase ( ). The stand-alone form is presumed to be involved in the...

[]

0

[ "PIRSF" ]

[ "PIRSF036592" ]

[ "Methlestr_CheB" ]

[ 85 ]

1

[]

0

[]

0

[ "PUB00011107", "PUB00015775" ]

[ "10049806", "11912013" ]

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

[ 1998, 2002 ]

2

[]

0

null

[ "Lysobacteraceae" ]

[ 85 ]

1

[]

0

true

Family

Chemotaxis glutamate methyltransferase

Chemotax_glutamate_MeTrfase

9

IPR012072

12,072

LytTR signal transduction protein, putative

Sigtransdc_LytTR

Family

133

false

Members of this group contain a C-terminal LytTR DNA-binding transcriptional regulator domain [ ] and an N-terminal domain that is also present in a distinct group of methyl-accepting chemotaxis proteins typified by Bacillus subtilis YfmS). Therefore, these proteins are predicted to be involved in transcriptional regul...

[]

0

[ "PIRSF" ]

[ "PIRSF036613" ]

[ "LytTR" ]

[ 133 ]

1

[]

0

[]

0

[ "PUB00009981" ]

[ "12034833" ]

[ "A novel type of conserved DNA-binding domain in the transcriptional regulators of the AlgR/AgrA/LytR family." ]

[ 2002 ]

1

[ "IPR046947" ]

[]

1

0

1

[ "Bacillaceae" ]

[ 133 ]

1

[]

0

true

Family

LytTR signal transduction protein, putative

Sigtransdc_LytTR

6

IPR012073

12,073

LytTR MHYT transcriptional regulator

LytTR_MHYT

Family

264

false

This entry includes the CoxC protein from the CO-metabolizing bacterium Oligotropha carboxidovorans [ ]. In the CoxC and CoxH proteins, the LytTR DNA-binding transcriptional regulator domain [ ] is found in association with MHYT, a recently described sensor domain, which contains six transmembrane segments carrying con...

[]

0

[ "PIRSF" ]

[ "PIRSF036615" ]

[ "MHYT_LytTR" ]

[ 264 ]

1

[]

0

[]

0

[ "PUB00009981", "PUB00011525", "PUB00016193" ]

[ "12034833", "10433972", "11728710" ]

[ "A novel type of conserved DNA-binding domain in the transcriptional regulators of the AlgR/AgrA/LytR family.", "Sequence analysis, characterization and CO-specific transcription of the cox gene cluster on the megaplasmid pHCG3 of Oligotropha carboxidovorans.", "MHYT, a new integral membrane sensor domain." ]

[ 2002, 1999, 2001 ]

3

[]

0

null

[ "Alphaproteobacteria", "marine sediment metagenome" ]

[ 263, 1 ]

2

[]

0

true

Family

LytTR MHYT transcriptional regulator

LytTR_MHYT

5

IPR012074

12,074

GAF-ANTAR transcription anti-termination regulator, putative

GAF_ANTAR

Family

9,205

false

Members of this group are predicted signal transduction proteins containing cytoplasmic sensor domain GAF and an RNA-binding anti-terminator ANTAR domain. In members of this group, regulation/signal receiving is predicted to be performed by the GAF domain. GAF is a ubiquitous signalling/sensory domain. It has been orig...

[]

0

[ "PIRSF" ]

[ "PIRSF036625" ]

[ "GAF_ANTAR" ]

[ 9205 ]

1

[]

0

[]

0

[ "PUB00005474", "PUB00011096", "PUB00011191", "PUB00011193", "PUB00011194", "PUB00016007" ]

[ "9433123", "10966457", "10508151", "11796212", "8918468", "2153290" ]

[ "The GAF domain: an evolutionary link between diverse phototransducing proteins.", "Two-component signal transduction.", "Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex.", "ANTAR: an RNA-binding domain in transcription antitermination regulator...

[ 1997, 2000, 1999, 2002, 1996, 1990 ]

6

[]

0

null

[ "Bacteria", "Pleodorina starrii", "metagenomes" ]

[ 9179, 1, 25 ]

3

[]

0

true

Family

GAF-ANTAR transcription anti-termination regulator, putative

GAF_ANTAR

5

IPR012075

12,075

Glutamate synthase, large subunit domains 1/3 fusion

Glu_synth_lsu_1/3

Family

81

false

The large (alpha, GltB) subunit of bacterial glutamate synthase (GOGAT) consists of three domains: N-terminal domain (amidotransferase domain ), central (consisting of and the FMN-binding domain ), and C-terminal domain. This family of sequences represent a fusion of the N-terminal (amidotransferase) domain and the C-t...

[]

0

[ "PIRSF" ]

[ "PIRSF036632" ]

[ "GOGAT_lg_1_3" ]

[ 81 ]

1

[]

0

[]

0

[ "PUB00008698", "PUB00009386", "PUB00013982", "PUB00015710" ]

[ "11967268", "10357231", "11188694", "11230537" ]

[ "Structural studies on the synchronization of catalytic centers in glutamate synthase.", "Glutamate synthase: a complex iron-sulfur flavoprotein.", "Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase.", "Phylogenetic analyses of two \"archaeal\"...

[ 2002, 1999, 2000, 2001 ]

4

[]

0

null

[ "Archaea" ]

[ 81 ]

1

[]

0

true

Family

Glutamate synthase, large subunit domains 1/3 fusion

Glu_synth_lsu_1/3

8

IPR012078

12,078

Methane/phenol monooxygenase, hydroxylase component

MP_mOase_hydro

Family

1,494

false

This group represents the hydroxylase component of aromatic and alkene monooxygenases such as methane monooxygenase ( ) phenol 2-monooxygenase ( ), toluene-4-monooxygenase ( ) from Pseudomonas mendocina, and alkene monooxygenase ( ) from Xanthobacter autotrophicus. Aromatic and alkene monooxygenase hydroxylases (AAMH) ...

[ "GO:0016709" ]

[ "oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen" ]

[ "molecular_function" ]

1

[ "PIRSF", "CDD" ]

[ "PIRSF000040", "cd01058" ]

[ "MMOH_comp", "AAMH_B" ]

[ 1470, 1176 ]

2

[]

0

[ "1fyz", "1fz0", "1fz1", "1fz2", "1fz3", "1fz4", "1fz5", "1fz6", "1fz7", "1fz8", "1fz9", "1fzh", "1fzi", "1mhy", "1mhz", "1mmo", "1mty", "1t0q", "1t0r", "1t0s", "1xmf", "1xmg", "1xmh", "1xu3", "1xu5", "1xvb", "1xvc", "1xvd", "1xve", "1xvf", "1xvg", "2inc"...

90

[ "PUB00012263", "PUB00016235", "PUB00016237", "PUB00016243", "PUB00021642", "PUB00025088", "PUB00036067", "PUB00088050" ]

[ "7753034", "15544", "15379538", "810352", "11456616", "11297417", "9329079", "9312093" ]

[ "Localization and organization of phenol degradation genes of Pseudomonas putida strain H.", "Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b.", "NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsul...

[ 1995, 1977, 2004, 1975, 2001, 2001, 1997, 1997 ]

8

[ "IPR003430" ]

[]

1

0

1

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

[ 1466, 2, 14, 12 ]

4

[]

0

true

Family

Methane/phenol monooxygenase, hydroxylase component

MP_mOase_hydro

8

IPR012079

12,079

Bifunctional aldehyde-alcohol dehydrogenase

Bifunc_Ald-ADH

Family

6,943

false

This enzyme has two NAD+-dependent activities: alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ACDH) [ , , ]. It controls ethanol and acetate production under aerobic conditions [ ]. The N-terminal region of the protein is highly homologous to aldehyde:NAD(+) oxidoreductases, whereas the C-terminal region i...

[ "GO:0004022", "GO:0008774", "GO:0006066", "GO:0015976" ]

[ "alcohol dehydrogenase (NAD+) activity", "acetaldehyde dehydrogenase (acetylating) activity", "alcohol metabolic process", "carbon utilization" ]

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

4

[ "NCBIFAM", "PIRSF" ]

[ "NF010378", "PIRSF000111" ]

[ "PRK13805.1", "ALDH_ADH" ]

[ 6937, 6510 ]

2

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

[ "1.1.1.1", "1.2.1", "PWY-3162", "PWY-5057", "PWY-5076", "PWY-5078", "PWY-5079", "PWY-5082", "PWY-5480", "PWY-5486", "PWY-5751", "PWY-6313", "PWY-6333", "PWY-6342", "PWY-6587", "PWY-6802", "PWY-6871", "PWY-7013", "PWY-7111", "PWY-7396" ]

[ "EC:1.1.1.1", "EC:1.2.1", "METACYC:PWY-3162", "METACYC:PWY-5057", "METACYC:PWY-5076", "METACYC:PWY-5078", "METACYC:PWY-5079", "METACYC:PWY-5082", "METACYC:PWY-5480", "METACYC:PWY-5486", "METACYC:PWY-5751", "METACYC:PWY-6313", "METACYC:PWY-6333", "METACYC:PWY-6342", "METACYC:PWY-6587", ...

20

[ "6ahc", "6tqh", "6tqm", "7bvp", "7dag", "8uhw", "9ldk" ]

7

[ "PUB00015881", "PUB00070748", "PUB00070749", "PUB00070750", "PUB00070751", "PUB00160956" ]

[ "7980441", "23201265", "18726959", "6998946", "10922373", "36928033" ]

[ "Purification and molecular characterization of the NAD(+)-dependent acetaldehyde/alcohol dehydrogenase from Entamoeba histolytica.", "The bifunctional aldehyde-alcohol dehydrogenase controls ethanol and acetate production in Entamoeba histolytica under aerobic conditions.", "Aldehyde-alcohol dehydrogenase and/...

[ 1994, 2013, 2009, 1980, 2000, 2023 ]

6

[]

0

null

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

[ 6822, 110, 1, 10 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Bifunctional aldehyde-alcohol dehydrogenase

Bifunc_Ald-ADH

6

IPR012081

12,081

Alkyl hydroperoxide reductase subunit F

Alkyl_hydroperoxide_Rdtase_suF

Family

7,852

false

Alkyl hydroperoxide reductase subunit F (AhpF) is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein d...

[ "GO:0050660", "GO:0051287", "GO:0102039", "GO:0000302" ]

[ "flavin adenine dinucleotide binding", "NAD binding", "NADH-dependent peroxiredoxin activity", "response to reactive oxygen species" ]

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

4

[ "PIRSF", "NCBIFAM" ]

[ "PIRSF000238", "TIGR03140" ]

[ "AhpF", "AhpF" ]

[ 7737, 7823 ]

2

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

[ "1.8.1.-", "GenProp0676", "PWY-5336", "PWY-6050", "PWY-6932", "PWY-7462", "PWY-7534" ]

[ "EC:1.8.1.-", "GP:GenProp0676", "METACYC:PWY-5336", "METACYC:PWY-6050", "METACYC:PWY-6932", "METACYC:PWY-7462", "METACYC:PWY-7534" ]

7

[ "1fl2", "1hyu", "4o5q", "4o5u", "4xvg", "4ykf", "4ykg" ]

7

[ "PUB00015995", "PUB00042839" ]

[ "12483614", "10482511" ]

[ "Molecular cloning and transcriptional analysis of the alkyl hydroperoxide reductase genes from Pseudomonas putida KT2442.", "Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate Anaerobe bacteroides fragilis." ]

[ 2001, 1999 ]

2

[]

0

null

[ "Bacteria", "Candidatus Methanomethylicus mesodigestus", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]

[ 7813, 1, 4, 33, 1 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Alkyl hydroperoxide reductase subunit F

Alkyl_hydroperoxide_Rdtase_suF

1

IPR012083

12,083

Arylsulfatase

Family

1,667

false

Arylsulphatase from the multicellular green flagellate Volvox carteri is a 649 amino acid polypeptide [ ]. Like arylsulphatases in other organisms, it occurs in the periplasm. In Pseudomonas aeruginosa PAO1, however, this enzyme does not appear to be periplasmic or membrane-associated [ ]. The synthesis of arylsufatase...

[ "GO:0004065", "GO:0018958" ]

[ "arylsulfatase activity", "phenol-containing compound metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF" ]

[ "PIRSF000972" ]

[ "Arylsulf_plant" ]

[ 1667 ]

1

[]

0

[]

0

[ "PUB00001466", "PUB00016065", "PUB00043515" ]

[ "8681943", "8168504", "7744061" ]

[ "The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri.", "An inducible arylsulfatase of Volvox carteri with properties suitable for a reporter-gene system. Purification, characterization and molecular cloning.", "Pur...

[ 1996, 1994, 1995 ]

3

[]

0

null

[ "Eukaryota" ]

[ 1667 ]

1

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]

[ 1 ]

1

true

Family

Arylsulfatase

2

IPR012085

12,085

Globin, nematode

Globin_nematode

Family

244

false

Globins are haem-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family that is widely distributed in many organisms [ ]. Globins have evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric gl...

[ "GO:0005506", "GO:0019825", "GO:0020037", "GO:0015671" ]

[ "iron ion binding", "oxygen binding", "heme binding", "oxygen transport" ]

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

4

[ "PIRSF" ]

[ "PIRSF002026" ]

[ "Nematode_globin" ]

[ 244 ]

1

[]

0

[ "1ash", "2wtg", "2wth" ]

3

[ "PUB00015878", "PUB00015883", "PUB00016016", "PUB00016057", "PUB00016129", "PUB00029465", "PUB00035865", "PUB00035866", "PUB00035867", "PUB00035868", "PUB00035869", "PUB00035870", "PUB00035871", "PUB00035872", "PUB00035873", "PUB00035877", "PUB00055425", "PUB00055462", "PUB000554...

[ "10671515", "7891734", "15096613", "8325507", "1465385", "12962627", "16600051", "17540514", "11092893", "11481493", "15598488", "16888280", "15598493", "15339940", "15804833", "17084861", "15804834", "17540516", "17701548", "21495624" ]

[ "A hemoglobin with an optical function.", "Sequence, expression and evolution of the globins of the parasitic nematode Nippostrongylus brasiliensis.", "Ancestral hemoglobins in Archaea.", "Novel gene structure and evolutionary context of Caenorhabditis elegans globin.", "Ascaris hemoglobin gene: plant-like ...

[ 2000, 1994, 2004, 1993, 1992, 2003, 2006, 2007, 2001, 2001, 2005, 2006, 2005, 2004, 2004, 2007, 2004, 2007, 2007, 2011 ]

20

[]

0

null

[ "Nematoda" ]

[ 244 ]

1

[ "Caenorhabditis elegans" ]

[ 1 ]

1

true

Family

Globin, nematode

Globin_nematode

8

IPR012089

12,089

tRNA-cytidine(32) 2-sulfurtransferase

tRNA_Cyd_32_2_STrfase

Family

8,101

false

This entry represents tRNA-cytidine(32) 2-sulfurtransferase (also known as 2-thiocytidine tRNA biosynthesis protein, TtcA) and its homologues. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-st...

[ "GO:0008033" ]

[ "tRNA processing" ]

[ "biological_process" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01850", "NF007972" ]

[ "TtcA", "PRK10696.1" ]

[ 7978, 8100 ]

2

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

[ "2.8.1.-", "PWY-5303", "PWY-6675", "PWY-6892", "PWY-7250", "PWY-7887", "PWY-7888", "PWY-7889", "PWY-7891", "PWY-7892", "PWY-7904", "PWY-8164", "PWY-8179" ]

[ "EC:2.8.1.-", "METACYC:PWY-5303", "METACYC:PWY-6675", "METACYC:PWY-6892", "METACYC:PWY-7250", "METACYC:PWY-7887", "METACYC:PWY-7888", "METACYC:PWY-7889", "METACYC:PWY-7891", "METACYC:PWY-7892", "METACYC:PWY-7904", "METACYC:PWY-8164", "METACYC:PWY-8179" ]

13

[]

0

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00014303", "PUB00044701", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "7731953", "14729701", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 1994, 2004, 2000, 2002 ]

11

[ "IPR035107" ]

[]

1

0

1

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

[ 8004, 38, 59 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

tRNA-cytidine(32) 2-sulfurtransferase

tRNA_Cyd_32_2_STrfase

2

IPR012090

12,090

Chromosome partition protein MukB

MukB

Family

2,647

false

MukB is a 170kDa protein that is involved in ATP-dependent chromosome partitioning during cell division in Escherichia coli [ , ]. Its domain structure is reminiscent of the eukaryotic motor proteins kinesin and myosin [ ]. MukB, like SMC (structural maintenance of chromosomes) proteins with which it shares function, h...

[ "GO:0003677", "GO:0005524", "GO:0007059", "GO:0030261", "GO:0009295" ]

[ "DNA binding", "ATP binding", "chromosome segregation", "chromosome condensation", "nucleoid" ]

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

5

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

[ "MF_01800", "NF003422", "PIRSF005246" ]

[ "MukB", "PRK04863.1", "MukB" ]

[ 1931, 2647, 2211 ]

3

[ "GP" ]

[ "GenProp1180" ]

[ "GP:GenProp1180" ]

1

[ "7nyw", "7nyx", "7nyy", "7nyz", "7nz0", "7nz2", "7nz3", "7nz4", "9gm6", "9gm7", "9gm8", "9gm9", "9gma" ]

13

[ "PUB00009946", "PUB00015945", "PUB00016034" ]

[ "10545328", "1464330", "9688555" ]

[ "Crystal structure of the N-terminal domain of MukB: a protein involved in chromosome partitioning.", "E.coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities.", "Interaction of the N-terminal domain of MukB with the...

[ 1999, 1992, 1998 ]

3

[]

0

null

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

[ 2642, 4, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Chromosome partition protein MukB

MukB

4

IPR012091

12,091

Peptidase M54, archaemetzincin, archaeal/bacterial

Pept_M54_archaemetzncn_arc/bac

Family

859

false

This entry represents the archaeal zinc-dependent peptidases and homologous bacterial sequences that belong to the MEROPS peptidase family M54, more commonly known as the archaemetzincins. Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may b...

[ "GO:0008237", "GO:0008270", "GO:0006508" ]

[ "metallopeptidase activity", "zinc ion binding", "proteolysis" ]

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

3

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

[ "MF_01842", "NF033823", "PIRSF005785" ]

[ "Archaemetzincin", "archmetzin", "Zn-prot_arch" ]

[ 491, 717, 795 ]

3

[]

0

[ "2x7m", "3lmc", "3zvs", "4a3w", "4axq" ]

5

[ "PUB00003579" ]

[ "7674922" ]

[ "Evolutionary families of metallopeptidases." ]

[ 1995 ]

1

[ "IPR012962" ]

[]

1

0

1

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

[ 589, 239, 6, 25 ]

4

[]

0

true

Family

Peptidase M54, archaemetzincin, archaeal/bacterial

Pept_M54_archaemetzncn_arc/bac

6

IPR012092

12,092

8-oxoguanine DNA glycosylase/AP lyase Ogg

DNA_glyclase/AP_lyase_Ogg

Family

650

false

This entry represents bifunctional, thermostable 8-oxoguanine DNA glycosylase/DNA lyase enzymes (OGG or OG glycosylases), which are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents [ ]. Most damage to bases in DNA is repaired by the base excision repair pathway [ ]. These enzymes have...

[ "GO:0003906", "GO:0016799", "GO:0006281" ]

[ "DNA-(apurinic or apyrimidinic site) endonuclease activity", "hydrolase activity, hydrolyzing N-glycosyl compounds", "DNA repair" ]

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

3

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

[ "MF_00241", "NF002305", "PF22175", "PIRSF005954" ]

[ "Ogg", "PRK01229.1", "Ogg-HhH", "Thrmst_ogg" ]

[ 356, 334, 650, 321 ]

4

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

[ "3.2.2.-", "4.2.99.18", "PWY-2681", "PWY-5316", "PWY-5381", "PWY-7342", "PWY-7564", "PWY-8106" ]

[ "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" ]

8

[ "3fhf", "3fhg", "3knt", "3n0u" ]

4

[ "PUB00016141", "PUB00018046", "PUB00029978", "PUB00042929", "PUB00058533", "PUB00058617" ]

[ "10521423", "15588838", "14517230", "14503888", "19446526", "20083120" ]

[ "Characterization of an 8-oxoguanine DNA glycosylase from Methanococcus jannaschii.", "Base excision repair.", "Crystal structures of 3-methyladenine DNA glycosylase MagIII and the recognition of alkylated bases.", "Recognition and removal of oxidized guanines in duplex DNA by the base excision repair enzymes...

[ 1999, 2004, 2003, 2003, 2009, 2010 ]

6

[]

0

null

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

[ 142, 468, 40 ]

3

[]

0

true

Family

8-oxoguanine DNA glycosylase/AP lyase Ogg

DNA_glyclase/AP_lyase_Ogg

4

IPR012096

12,096

ATPase, PP-loop, MJ1638-related

ATPase_PP-loop_MJ1638

Family

82

false

The PP-loop motif appears to be a modified version of the P-loop of nucleotide binding domain that is involved in phosphate binding [ ]. Named PP-motif, since it appears to be a part of a previously uncharacterised ATP pyrophophatase domain. ATP sulfurylases, Escherichia coli NtrL, and Bacillus subtilis OutB consist of...

[]

0

[ "PIRSF" ]

[ "PIRSF006601" ]

[ "ATPase_UCP006601" ]

[ 82 ]

1

[]

0

[]

0

[ "PUB00014303", "PUB00016132" ]

[ "7731953", "12012333" ]

[ "A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.", "Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA." ]

[ 1994, 2002 ]

2

[]

0

null

[ "Methanobacteriota" ]

[ 82 ]

1

[]

0

true

Family

ATPase, PP-loop, MJ1638-related

ATPase_PP-loop_MJ1638

9

IPR012097

12,097

Opacity-associated protein B

OapB

Family

122

false

This group represents an opacity-associated protein B [ ].

[]

0

[ "PIRSF" ]

[ "PIRSF007352" ]

[ "OapB" ]

[ 122 ]

1

[]

0

[]

0

[ "PUB00020973" ]

[ "8559074" ]

[ "Identification and characterization of a cell envelope protein of Haemophilus influenzae contributing to phase variation in colony opacity and nasopharyngeal colonization." ]

[ 1995 ]

1

[]

0

null

[ "Pasteurellaceae" ]

[ 122 ]

1

[]

0

true

Family

Opacity-associated protein B

OapB

9

IPR012098

12,098

SRP-independent targeting protein 3

SND3_fun

Family

2,283

false

SRP-independent targeting protein 3 (SND3, previously known as PHO88) is localized to the endoplasmic reticulum (ER). SND3 works together with SND1 and SND2; these proteins function in parallel with the SRP and GET pathways to target a broad range of substrates to the ER. The SND proteins constitute an alternative targ...

[ "GO:0045047", "GO:0005783" ]

[ "protein targeting to ER", "endoplasmic reticulum" ]

[ "biological_process", "cellular_component" ]

2

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

[ "PF10032", "PIRSF008756", "PTHR28112" ]

[ "Pho88", "P_tr_PHO88", "" ]

[ 2283, 1395, 2199 ]

3

[]

0

[ "9i78" ]

1

[ "PUB00016170", "PUB00083911" ]

[ "8709965", "27905431" ]

[ "A putative membrane protein, Pho88p, involved in inorganic phosphate transport in Saccharomyces cerevisiae.", "The SND proteins constitute an alternative targeting route to the endoplasmic reticulum." ]

[ 1996, 2016 ]

2

[]

0

null

[ "Eukaryota", "Herbiconiux daphne" ]

[ 2282, 1 ]

2

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

[ 1, 1, 2 ]

3

true

Family

SRP-independent targeting protein 3

SND3_fun

8

IPR012099

12,099

Midasin

Family

3,605

false

Midasin (MDN1, REA1) is a is a member of the AAA(+) family of ATPases. It is a nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits [ , , , ].

[ "GO:0016887", "GO:0000027", "GO:0005634" ]

[ "ATP hydrolysis activity", "ribosomal large subunit assembly", "nucleus" ]

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

3

[ "PIRSF" ]

[ "PIRSF010340" ]

[ "Midasin" ]

[ 3605 ]

1

[]

0

[ "5jcs", "6hyp", "6i26", "6i27", "6or5", "6or6", "6orb", "6ylf", "6ylh" ]

9

[ "PUB00053246", "PUB00056113", "PUB00056196", "PUB00073617" ]

[ "19737519", "15528184", "15260980", "20542003" ]

[ "Mechanochemical removal of ribosome biogenesis factors from nascent 60S ribosomal subunits.", "Rea1, a dynein-related nuclear AAA-ATPase, is involved in late rRNA processing and nuclear export of 60 S subunits.", "A pre-ribosome with a tadpole-like structure functions in ATP-dependent maturation of 60S subunit...

[ 2009, 2004, 2004, 2010 ]

4

[]

0

null

[ "Eukaryota" ]

[ 3605 ]

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...

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

12

true

Family

Midasin

3

IPR012100

12,100

DNA-damage-repair/toleration protein, DRT102

DRT102

Family

380

false

Plants employ DNA-damage-repair/toleration (DRT) activities to resist UV radiation. This family represents DNA-damage-repair/toleration protein DRT102 [ ].

[]

0

[ "PIRSF" ]

[ "PIRSF011609" ]

[ "DRT102" ]

[ 380 ]

1

[]

0

[]

0

[ "PUB00015896" ]

[ "8329681" ]

[ "Selection of Arabidopsis cDNAs that partially correct phenotypes of Escherichia coli DNA-damage-sensitive mutants and analysis of two plant cDNAs that appear to express UV-specific dark repair activities." ]

[ 1993 ]

1

[ "IPR003500" ]

[]

1

0

1

[ "Tracheophyta" ]

[ 380 ]

1

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

[ 5, 3, 3 ]

3

true

Family

DNA-damage-repair/toleration protein, DRT102

DRT102

2

IPR012101

12,101

Biotinidase-like, eukaryotic

Biotinidase-like_euk

Family

2,829

false

These secondary amidases participate in vitamin recycling. Biotinidase ( ) has both a hydrolase and a transferase activity. It hydrolyses free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin ...

[ "GO:0016811" ]

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

[ "molecular_function" ]

1

[ "PIRSF", "CDD" ]

[ "PIRSF011861", "cd07567" ]

[ "Biotinidase", "biotinidase_like" ]

[ 2054, 2825 ]

2

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

[ "3.5.1", "R-CFA-163125", "R-CFA-199220", "R-CFA-6798695", "R-DME-196780", "R-HSA-163125", "R-HSA-196780", "R-HSA-199220", "R-HSA-3371598", "R-HSA-6798695", "R-MMU-163125", "R-MMU-196780", "R-MMU-199220", "R-MMU-6798695", "R-RNO-196780" ]

[ "EC:3.5.1", "REACTOME:R-CFA-163125", "REACTOME:R-CFA-199220", "REACTOME:R-CFA-6798695", "REACTOME:R-DME-196780", "REACTOME:R-HSA-163125", "REACTOME:R-HSA-196780", "REACTOME:R-HSA-199220", "REACTOME:R-HSA-3371598", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-163125", "REACTOME:R-MMU-196780", "R...

15

[ "4cyf", "4cyg", "4cyy", "7slv", "7slx", "7sly", "9izl" ]

7

[ "PUB00016852", "PUB00016878", "PUB00085989", "PUB00085990", "PUB00085996", "PUB00086000" ]

[ "11380987", "12504683", "19322213", "14966568", "11042271", "18845537" ]

[ "The nitrilase superfamily: classification, structure and function.", "Catalysis in the nitrilase superfamily.", "Expression of the vanin gene family in normal and inflamed human skin: induction by proinflammatory cytokines.", "Vanin-1(-/-) mice show decreased NSAID- and Schistosoma-induced intestinal inflamm...

[ 2001, 2002, 2009, 2004, 2000, 2008 ]

6

[ "IPR040154" ]

[]

1

0

1

[ "Eukaryota" ]

[ 2829 ]

1

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

[ 1, 6, 8, 5, 12 ]

5

true

Family

Biotinidase-like, eukaryotic

Biotinidase-like_euk

8

IPR012103

12,103

Peptidase S8A, bacillopeptidase F

Pept_S8A_Bpr

Family

263

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...

[]

0

[ "PIRSF" ]

[ "PIRSF015477" ]

[ "Bpr" ]

[ 263 ]

1

[]

0

[]

0

[ "PUB00000522", "PUB00003576", "PUB00015944", "PUB00016217", "PUB00035098", "PUB00035099" ]

[ "8439290", "7845208", "2108961", "15375126", "10656993", "9572109" ]

[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "Cloning, genetic organization, and characterization of a structural gene encoding bacillopeptidase F from Bacillus subtilis.", "Hetero- and autoprocessing of the extracellular metalloprotease (Mpr) in Bacillus subtilis.", "Subtilase-...

[ 1993, 1994, 1990, 2004, 2000, 1998 ]

6

[ "IPR015500" ]

[]

1

0

1

[ "Bacilli" ]

[ 263 ]

1

[]

0

true

Family

Peptidase S8A, bacillopeptidase F

Pept_S8A_Bpr

1

IPR012104

12,104

PHO85 cyclin 1/2/9

PHO85_cyclin_1/2/9

Family

423

false

Pho85 is a non-essential cyclin-dependent kinase (CDK) involved in the cell cycle [ ]. Pho85 is controlled by 10 cyclins that may be grouped into 2 families according to cyclin box sequence similarity [ ]: the Pho80 family (Pho80, Pcl6, Pcl7, Pcl8, and Pcl10) and the Pcl1,2 family (Pcl1, Pcl2, Pcl5, Pcl9 and ClG1). Exc...

[ "GO:0019901", "GO:0000079", "GO:0051726" ]

[ "protein kinase binding", "regulation of cyclin-dependent protein serine/threonine kinase activity", "regulation of cell cycle" ]

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

3

[ "PIRSF" ]

[ "PIRSF016511" ]

[ "Cyclin_Pcl" ]

[ 423 ]

1

[]

0

[]

0

[ "PUB00073602", "PUB00073603" ]

[ "9032248", "24049669" ]

[ "A family of cyclin-like proteins that interact with the Pho85 cyclin-dependent kinase.", "Redundancy or specificity? The role of the CDK Pho85 in cell cycle control." ]

[ 1997, 2013 ]

2

[ "IPR013922" ]

[]

1

0

1

[ "Eukaryota" ]

[ 423 ]

1

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

[ 1, 3 ]

2

true

Family

PHO85 cyclin 1/2/9

PHO85_cyclin_1/2/9

5

IPR012105

12,105

Sperm surface protein Sp17

Sp17

Family

301

false

Sp17 was originally proposed to be a sperm-specific protein that plays a role in sperm-egg interactions by binding to the zona pellucida via two conserved heparin-binding motifs [ ]. Later, it was found expressed in other tissues and may have a regulatory role in an A-kinase anchoring protein complex [ , ].

[ "GO:0007339", "GO:0016020" ]

[ "binding of sperm to zona pellucida", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PIRSF" ]

[ "PIRSF016533" ]

[ "Sp17" ]

[ 301 ]

1

[]

0

[ "8j07", "9fqr" ]

2

[ "PUB00015885", "PUB00084986", "PUB00084987" ]

[ "7525387", "12530914", "19604394" ]

[ "Sequence of a rabbit sperm zona pellucida binding protein and localization during the acrosome reaction.", "A re-evaluation of sperm protein 17 (Sp17) indicates a regulatory role in an A-kinase anchoring protein complex, rather than a unique role in sperm-zona pellucida binding.", "Sperm protein 17 is expresse...

[ 1994, 2002, 2009 ]

3

[]

0

null

[ "Eukaryota" ]

[ 301 ]

1

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

[ 3, 3, 2 ]

3

true

Family

Sperm surface protein Sp17

Sp17

1

IPR012106

12,106

Protease, Mu phage/prophage I type

Phage_Mu_Gp1

Family

2,160

false

This entry includes protease I (Gp1) from Bacteriophage Mu. It is involved in virion assembly/maturation and may cleave the portal protein to yield mature procapsids competent for DNA packaging [ , , ].

[]

0

[ "PFAM", "PIRSF" ]

[ "PF10123", "PIRSF016624" ]

[ "Mu-like_Pro", "Mu_prophg_I" ]

[ 2160, 1274 ]

2

[]

0

[]

0

[ "PUB00015900", "PUB00077061", "PUB00077062" ]

[ "11922669", "8599204", "9495752" ]

[ "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like prophages in Haemophilus, Neisseria and Deinococcus.", "Bacteriophage Mu head assembly.", "Assembly of both the head and tail of bacteriophage Mu is blocked in Escherichia coli groEL and groES mutants." ]

[ 2002, 1996, 1998 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobrevibacter arboriphilus JCM 13429 = DSM 1125", "Viruses", "unclassified sequences" ]

[ 1901, 3, 1, 211, 44 ]

5

[]

0

true

Family

Protease, Mu phage/prophage I type

Phage_Mu_Gp1

4

IPR012108

12,108

ADP-ribosylarginine hydrolase

ADP-ribosylarg_hydro

Family

1,328

false

This enzyme catalyzes the reverse reaction of mono-ADP-ribosylation by removing ADP-ribose from arginine residues in ADP-ribosylated proteins. NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyse opposing arms of the putative ADP-ribosylation cycle.

[ "GO:0000287", "GO:0003875", "GO:0051725" ]

[ "magnesium ion binding", "ADP-ribosylarginine hydrolase activity", "protein de-ADP-ribosylation" ]

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

3

[ "PIRSF" ]

[ "PIRSF016939" ]

[ "ADP_ribslarg_hdr" ]

[ 1328 ]

1

[]

0

[ "3hfw", "6g28", "6g2a", "6iux" ]

4

[ "PUB00008412", "PUB00015992" ]

[ "8349667", "10358013" ]

[ "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase.", "Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases." ]

[ 1993, 1999 ]

2

[ "IPR005502" ]

[]

1

0

1

[ "Eumetazoa" ]

[ 1328 ]

1

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

[ 3, 3, 3, 4 ]

4

true

Family

ADP-ribosylarginine hydrolase

ADP-ribosylarg_hydro

9

IPR012110

12,110

Pyruvate decarboxylase/indolepyruvate decarboxylase-like

PDC/IPDC-like

Family

12,053

false

This entry represents part of a family of closely related, thiamine pyrophosphate-dependent enzymes includes indolepyruvate decarboxylase (IPDC, )[ , ], pyruvate decarboxylase (PDC, ) [ ], branched-chain alpha-ketoacid decarboxylase, etc [ ]. PDC catalyses the conversion of pyruvate to acetaldehyde and CO2 in alcoholic...

[ "GO:0016831" ]

[ "carboxy-lyase activity" ]

[ "molecular_function" ]

1

[ "PIRSF", "PANTHER" ]

[ "PIRSF036565", "PTHR43452" ]

[ "Pyruvt_ip_decrb", "" ]

[ 9639, 12053 ]

2

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

[ "4.1.1", "4.1.1.1", "PWY-5082", "PWY-5486", "PWY-5768", "PWY-6330", "PWY-6873", "PWY-7396" ]

[ "EC:4.1.1", "EC:4.1.1.1", "METACYC:PWY-5082", "METACYC:PWY-5486", "METACYC:PWY-5768", "METACYC:PWY-6330", "METACYC:PWY-6873", "METACYC:PWY-7396" ]

8

[ "1ovm", "1pvd", "1pyd", "1qpb", "1zpd", "2nxw", "2q5j", "2q5l", "2q5o", "2q5q", "2vbf", "2vbg", "2vbi", "2vjy", "2vk1", "2vk4", "2vk8", "2w93", "2wva", "2wvg", "2wvh", "3oe1", "4cok", "4zp1", "5euj", "5npu", "5tma", "6efg", "6efh", "6vgs", "8hp2", "8hp4"...

38

[ "PUB00015910", "PUB00042068", "PUB00049666", "PUB00102228", "PUB00102231", "PUB00102234" ]

[ "12752451", "17403037", "18084069", "8202090", "18086676", "16274227" ]

[ "Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid.", "The crystal structure of phenylpyruvate decarboxylase from Azospirillum brasilense at 1.5 A resolution. Implications for i...

[ 2003, 2007, 2007, 1994, 2008, 2005 ]

6

[]

[ "IPR017764", "IPR017765" ]

0

2

0

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

[ 22, 4531, 7478, 22 ]

4

[ "Arabidopsis thaliana", "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" ]

[ 19, 3, 27, 5, 4, 30 ]

6

true

Family

Pyruvate decarboxylase/indolepyruvate decarboxylase-like

PDC/IPDC-like

5

IPR012112

12,112

DNA repair protein Rev1

REV1

Family

3,241

false

Rev1 is a deoxycytidyl transferase involved in translesion DNA synthesis (TLS) pathway to bypass DNA lesions during replication [ ]. During TLS, Y-family DNA polymerase (Poleta, Polkappa, Poliota and Rev1) incorporates a nucleotide opposite the DNA lesion, and then Polzeta (consitst of Rev3 and Rev7) carries out primer...

[ "GO:0003684", "GO:0016779", "GO:0006281", "GO:0042276" ]

[ "damaged DNA binding", "nucleotidyltransferase activity", "DNA repair", "error-prone translesion synthesis" ]

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

4

[ "PIRSF" ]

[ "PIRSF036573" ]

[ "REV1" ]

[ 3241 ]

1

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

[ "2.7.7.-", "PWY-6322", "PWY-6626", "PWY-6749", "PWY-6955", "PWY-6998", "PWY-7127", "PWY-7419", "PWY-7529", "PWY-7706", "PWY-7719", "PWY-7735", "PWY-7737", "PWY-7769", "PWY-7888", "PWY-7904", "PWY-8117", "PWY-8179", "R-DME-110312", "R-DME-5655862", "R-DME-5656121", "R-GGA-35...

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

38

[ "8tlq", "8tlt" ]

2

[ "PUB00016110", "PUB00065262", "PUB00073483", "PUB00073484" ]

[ "11278384", "23143872", "8751446", "11711549" ]

[ "Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain.", "Structural insights into the assembly of human translesion polymerase complexes.", "Deoxycytidyl transferase activity of yeast REV1 protein.", "Mechanisms of dCMP transferase reactions c...

[ 2001, 2012, 1996, 2002 ]

4

[]

0

null

[ "Eukaryota" ]

[ 3241 ]

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...

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

12

true

Family

DNA repair protein Rev1

REV1

9

IPR012115

12,115

Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase

CDP-ribitol_syn

Family

945

false

This group represents a bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase. It catalyzes the NADPH-dependent reduction of D-ribulose 5-phosphate to D-ribitol 5-phosphate and the further reaction of D-ribitol 5-phosphate with CTP to form CDP-ribitol [ , ].

[]

0

[ "PIRSF" ]

[ "PIRSF036586" ]

[ "CDP-ribitol_syn" ]

[ 945 ]

1

[]

0

[]

0

[ "PUB00015956", "PUB00016014" ]

[ "10094675", "7752885" ]

[ "acs1 of Haemophilus influenzae type a capsulation locus region II encodes a bifunctional ribulose 5-phosphate reductase- CDP-ribitol pyrophosphorylase.", "Region II of the Haemophilus influenzae type be capsulation locus is involved in serotype-specific polysaccharide synthesis." ]

[ 1999, 1995 ]

2

[ "IPR034683" ]

[]

1

0

1

[ "Bacteria", "Methanobacteriati", "metagenomes" ]

[ 936, 5, 4 ]

3

[]

0

true

Family

Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase

CDP-ribitol_syn

3

IPR012116

12,116

Glycine/sarcosine/betaine reductase complex, protein C, alpha subunit

Gly_reductase_pC_asu

Family

608

false

This group represents a glycine/sarcosine/betaine reductase complex, component C, alpha subunit. Please see the following relevant references: [ , , ].

[]

0

[ "NCBIFAM", "PIRSF" ]

[ "NF040747", "PIRSF036593" ]

[ "reduct_C_alpha", "GrdD" ]

[ 608, 521 ]

2

[]

0

[]

0

[ "PUB00015969", "PUB00015983", "PUB00016079", "PUB00105939" ]

[ "11737196", "1587286", "8223622", "9799288" ]

[ "Cys359 of GrdD is the active-site thiol that catalyses the final step of acetyl phosphate formation by glycine reductase from Eubacterium acidaminophilum.", "Purification and characterization of protein PC, a component of glycine reductase from Eubacterium acidaminophilum.", "Components of glycine reductase fr...

[ 2001, 1992, 1993, 1998 ]

4

[ "IPR003664" ]

[]

1

0

1

[ "Bacteria", "metagenomes" ]

[ 601, 7 ]

2

[]

0

true

Family

Glycine/sarcosine/betaine reductase complex, protein C, alpha subunit

Gly_reductase_pC_asu

5

IPR012121

12,121

ATPase, PP-loop, MJ1599-related

ATPase_PP-loop_MJ1599

Family

76

false

The PP-loop motif appears to be a modified version of the P-loop of nucleotide binding domain that is involved in phosphate binding [ ]. Named PP-motif, since it appears to be a part of a previously uncharacterised ATP pyrophophatase domain. ATP sulfurylases, Escherichia coli NtrL, and Bacillus subtilis OutB consist of...

[]

0

[ "PIRSF" ]

[ "PIRSF036668" ]

[ "ATPase_UCP036668" ]

[ 76 ]

1

[]

0

[]

0

[ "PUB00014303", "PUB00016132" ]

[ "7731953", "12012333" ]

[ "A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.", "Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA." ]

[ 1994, 2002 ]

2

[]

0

null

[ "Methanobacteriota" ]

[ 76 ]

1

[]

0

true

Family

ATPase, PP-loop, MJ1599-related

ATPase_PP-loop_MJ1599

2

IPR012122

12,122

ATPase, PP-loop, MJ1016-related

ATPase_PP-loop_MJ1016

Family

64

false

The PP-loop motif appears to be a modified version of the P-loop of nucleotide binding domain that is involved in phosphate binding [ ]. Named PP-motif, since it appears to be a part of a previously uncharacterised ATP pyrophophatase domain. ATP sulfurylases, Escherichia coli NtrL, and Bacillus subtilis OutB consist of...

[]

0

[ "PIRSF" ]

[ "PIRSF036670" ]

[ "ATPase_UCP036670" ]

[ 64 ]

1

[]

0

[]

0

[ "PUB00014303", "PUB00016132" ]

[ "7731953", "12012333" ]

[ "A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.", "Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA." ]

[ 1994, 2002 ]

2

[]

0

null

[ "Methanobacteriota" ]

[ 64 ]

1

[]

0

true

Family

ATPase, PP-loop, MJ1016-related

ATPase_PP-loop_MJ1016

8

IPR012127

12,127

Cytochrome c prime

Cyt_c_prime

Family

4,423

false

Cytochromes c (cytC) can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide range of ...

[ "GO:0005506", "GO:0009055", "GO:0020037", "GO:0042597" ]

[ "iron ion binding", "electron transfer activity", "heme binding", "periplasmic space" ]

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

4

[ "PIRSF" ]

[ "PIRSF000027" ]

[ "Cytc_c_prime" ]

[ 4423 ]

1

[]

0

[ "1a7v", "1bbh", "1cgn", "1cgo", "1cpq", "1cpr", "1e83", "1e84", "1e85", "1e86", "1eky", "1gqa", "1jaf", "1mqv", "1nbb", "1rcp", "1s05", "2ccy", "2j8w", "2j9b", "2xl6", "2xl8", "2xld", "2xle", "2xlh", "2xlm", "2xlo", "2xlv", "2xlw", "2xm0", "2xm4", "2ykz"...

75

[ "PUB00000609", "PUB00000610", "PUB00000611", "PUB00003313" ]

[ "1646016", "1646017", "1646027", "8230224" ]

[ "Bacterial 4-alpha-helical bundle cytochromes.", "Sequence variability in bacterial cytochromes c.", "Ligand binding properties of cytochromes c'.", "Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 A resolution." ]

[ 1991, 1991, 1991, 1993 ]

4

[ "IPR002321" ]

[ "IPR015984" ]

1

0

[ "Bacteria", "Cyprideis torosa", "metagenomes" ]

[ 4382, 1, 40 ]

3

[]

0

true

Family

Cytochrome c prime

Cyt_c_prime

1

IPR012128

12,128

Phycobilisome, alpha/beta subunit

Phycobilisome_asu/bsu

Family

11,616

false

Cyanobacteria and red algae harvest light through water-soluble complexes, called phycobilisomes, which are attached to the outer face of the thylakoid membrane [ ]. These complexes are capable of transferring the absorbed energy to the photosynthetic reaction centre with greater than 95% efficiency. Phycobilisomes con...

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

[ "photosynthesis", "phycobilisome" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "PIRSF" ]

[ "PF00502", "PIRSF000081" ]

[ "Phycobilisome", "Phycocyanin" ]

[ 11616, 5274 ]

2

[]

0

[ "1all", "1b33", "1b8d", "1cpc", "1eyx", "1f99", "1gh0", "1ha7", "1i7y", "1jbo", "1kn1", "1ktp", "1lia", "1on7", "1phn", "1qgw", "1xf6", "1xg0", "2bv8", "2c7j", "2c7k", "2c7l", "2j96", "2uul", "2uum", "2uun", "2v8a", "2vjh", "2vjr", "2vjt", "2vml", "3brp"...

169

[ "PUB00023549", "PUB00024707", "PUB00024819", "PUB00033344", "PUB00033345" ]

[ "10388620", "11134927", "11463658", "15238265", "7783202" ]

[ "Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A resolution.", "Crystallization and 2.2 A resolution structure of R-phycoerythrin from Gracilaria chilensis: a case of perfect hemihedral twinning.", "Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobili...

[ 1999, 2001, 2001, 2004, 1995 ]

5

[]

[ "IPR006245", "IPR006246", "IPR006247" ]

0

3

0

[ "Bacteria", "Eukaryota", "Methanothermobacter tenebrarum" ]

[ 9376, 2239, 1 ]

3

[]

0

true

Family

Phycobilisome, alpha/beta subunit

Phycobilisome_asu/bsu

3

IPR012129

12,129

Phytochrome A/B/C/D/E

Phytochrome_A-E

Family

2,465

false

This group represent phytochrome A to E.

[ "GO:0009881", "GO:0042803", "GO:0006355", "GO:0009585", "GO:0017006" ]

[ "photoreceptor activity", "protein homodimerization activity", "regulation of DNA-templated transcription", "red, far-red light phototransduction", "protein-tetrapyrrole linkage" ]

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

5

[ "PIRSF" ]

[ "PIRSF000084" ]

[ "Phytochrome" ]

[ 2465 ]

1

[]

0

[ "7rzw", "8f5z", "8iff", "8isi", "8isj", "8isk", "8yb4" ]

7

[]

0

[ "IPR001294" ]

[]

1

0

1

[ "Streptophyta" ]

[ 2465 ]

1

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

[ 59, 36, 18 ]

3

true

Family

Phytochrome A/B/C/D/E

Phytochrome_A-E

3

IPR012130

12,130

Photoactive yellow-protein

PYP

Family

256

false

Members of this family are photoactive yellow protein, a cytosolic, 14kDa light-sensing protein which has a 4-hydroxycinnamyl (p-coumaric acid) chromophore covalently linked to a Cys residue. The enzyme 4-coumarate--CoA ligase as described by is required for its biosynthesis. The modified Cys is in a PAS domain, freque...

[ "GO:0009881", "GO:0007602" ]

[ "photoreceptor activity", "phototransduction" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF", "NCBIFAM" ]

[ "PIRSF000087", "TIGR02373" ]

[ "PYP", "photo_yellow" ]

[ 244, 131 ]

2

[]

0

[ "1d7e", "1f98", "1f9i", "1gsv", "1gsw", "1gsx", "1kou", "1mzu", "1nwz", "1odv", "1ot6", "1ot9", "1ota", "1otb", "1otd", "1ote", "1oti", "1s1y", "1s1z", "1s4r", "1s4s", "1t18", "1t19", "1t1a", "1t1b", "1t1c", "1ts0", "1ts6", "1ts7", "1ts8", "1ugu", "1uwn"...

106

[]

0

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 253, 3 ]

2

[]

0

true

Family

Photoactive yellow-protein

PYP

9

IPR012131

12,131

Histidinol dehydrogenase

Hstdl_DH

Family

31,423

false

Histidinol dehydrogenase (HDH) catalyses the terminal step in the biosynthesis of histidine in bacteria, fungi, and plants, the four-electron oxidation of L-histidinol to histidine. In 4-electron dehydrogenases, a single active site catalyses 2 separate oxidation steps: oxidation of the substrate alcohol to an intermed...

[ "GO:0016616", "GO:0046872", "GO:0051287" ]

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

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

3

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

[ "MF_01024", "PF00815", "PR00083", "PTHR21256", "TIGR00069", "cd06572" ]

[ "HisD", "Histidinol_dh", "HOLDHDRGNASE", "", "hisD", "Histidinol_dh" ]

[ 24882, 31388, 30853, 31279, 30296, 30168 ]

6

[ "EC", "GP" ]

[ "1.1.1.23", "GenProp0109" ]

[ "EC:1.1.1.23", "GP:GenProp0109" ]

2

[ "1k75", "1kae", "1kah", "1kar", "4g07", "4g09", "4gic", "5vlb", "5vlc", "5vld", "6an0", "8v35", "8v36", "8v37", "8wwe", "8xsq", "9cp7", "9cp8", "9cp9", "9ivy", "9lbv" ]

21

[ "PUB00000285", "PUB00004740" ]

[ "3533140", "2034659" ]

[ "A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase.", "Structural and functional conservation of histidinol dehydrogenase between plants and microbes." ]

[ 1986, 1991 ]

2

[]

[ "IPR016298", "IPR022695", "IPR043678" ]

0

3

0

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

[ 867, 26181, 3662, 713 ]

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" ]

[ 3, 1, 1, 2, 1, 1, 9 ]

7

true

Family

Histidinol dehydrogenase

Hstdl_DH

5

IPR012132

12,132

Glucose-methanol-choline oxidoreductase

GMC_OxRdtase

Family

81,352

false

Proteins in this entry are members of the glucose-methanol-choline oxidoreductase family of flavoenzymes [ ]. These enzymes catalyse diverse reaction and include glucose dehydrogenase ( ), alcohol oxidase ( ), glucose oxidase ( ), choline dehydrogenase ( ), and cyclase atC from Aspergillus terreus which oxidizes terrem...

[ "GO:0050660" ]

[ "flavin adenine dinucleotide binding" ]

[ "molecular_function" ]

1

[ "PIRSF", "PANTHER" ]

[ "PIRSF000137", "PTHR11552" ]

[ "Alcohol_oxidase", "" ]

[ 69323, 76335 ]

2

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

[ "1.1.99", "1.1.99.1", "R-HSA-6798163", "R-MMU-6798163", "R-RNO-6798163" ]

[ "EC:1.1.99", "EC:1.1.99.1", "REACTOME:R-HSA-6798163", "REACTOME:R-MMU-6798163", "REACTOME:R-RNO-6798163" ]

5

[ "1cf3", "1gal", "1gpe", "1ju2", "1kdg", "1naa", "2jbv", "3fim", "3gdn", "3gdp", "3ljp", "3nne", "3q9t", "3qvp", "3qvr", "3red", "3t37", "4h7u", "4ha6", "4mjw", "4qi4", "4qi5", "4udp", "4udq", "4udr", "4ynt", "4ynu", "4z24", "4z25", "4z26", "5eb4", "5eb5"...

102

[ "PUB00003282", "PUB00021936", "PUB00023505", "PUB00023935", "PUB00033347", "PUB00082617" ]

[ "1542121", "11566130", "10194345", "10216293", "9523716", "25265334" ]

[ "GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities.", "The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase.", "Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active sit...

[ 1992, 2001, 1999, 1999, 1998, 2014 ]

6

[]

[ "IPR011533", "IPR023978" ]

0

2

0

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

[ 109, 29348, 51225, 1, 108, 561 ]

6

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

[ 47, 1, 1, 44, 1, 4, 3, 5, 14, 3, 29 ]

11

true

Family

Glucose-methanol-choline oxidoreductase

GMC_OxRdtase

8

IPR012133

12,133

Alpha-hydroxy acid dehydrogenase, FMN-dependent

Alpha-hydoxy_acid_DH_FMN

Family

34,924

false

This group represents alpha-hydroxy acid FMN-dependent dehydrogenases, including human glycolate oxidase (GO), L-lactate oxidase (LOX) [ ] and bacterial L-lactate dehydrogenase. GO catalyses the FMN-dependent oxidation of glycolate to glyoxylate and glyoxylate to oxalate. The latter is a key metabolite in kidney stone ...

[ "GO:0010181", "GO:0016491" ]

[ "FMN binding", "oxidoreductase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PIRSF", "CDD" ]

[ "PIRSF000138", "cd02809" ]

[ "Al-hdrx_acd_dh", "alpha_hydroxyacid_oxid_FMN" ]

[ 32966, 26308 ]

2

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

[ "R-BTA-390918", "R-BTA-9033241", "R-DDI-389661", "R-DDI-390918", "R-DDI-9033241", "R-HSA-389661", "R-HSA-390918", "R-HSA-9033241", "R-MMU-389661", "R-MMU-390918", "R-MMU-9033241", "R-RNO-389661", "R-RNO-390918", "R-RNO-9033241" ]

[ "REACTOME:R-BTA-390918", "REACTOME:R-BTA-9033241", "REACTOME:R-DDI-389661", "REACTOME:R-DDI-390918", "REACTOME:R-DDI-9033241", "REACTOME:R-HSA-389661", "REACTOME:R-HSA-390918", "REACTOME:R-HSA-9033241", "REACTOME:R-MMU-389661", "REACTOME:R-MMU-390918", "REACTOME:R-MMU-9033241", "REACTOME:R-RNO...

14

[ "1al7", "1al8", "1gox", "1gyl", "1huv", "1kbj", "1p4c", "1p5b", "1qcw", "1tb3", "2a7n", "2a7p", "2a85", "2cdh", "2du2", "2e77", "2j6x", "2nli", "2nzl", "2rdt", "2rdu", "2rdw", "2w0u", "2zfa", "3giy", "3sgz", "4rje", "4yl2", "5ebu", "5qib", "5qic", "5qid"...

98

[ "PUB00043803", "PUB00043804", "PUB00082314" ]

[ "18215067", "18367206", "25372119" ]

[ "Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.", "X-ray structures of Aerococcus viridans lactate oxidase and its complex with D-lactate at pH 4.5 show an alpha-hydroxyacid oxidation mechanism.", "Identification of a 12-gene Fusaric Acid...

[ 2008, 2008, 2015 ]

3

[]

[ "IPR014080", "IPR020920", "IPR023989" ]

0

3

0

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

[ 117, 22105, 12330, 372 ]

4

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

[ 33, 2, 6, 4, 1, 3, 6, 2, 5, 4, 1, 31 ]

12

true

Family

Alpha-hydroxy acid dehydrogenase, FMN-dependent

Alpha-hydoxy_acid_DH_FMN

4

IPR012134

12,134

Glutamate-5-semialdehyde dehydrogenase

Glu-5-SA_DH

Family

24,856

false

Gamma-glutamyl phosphate reductase (GPR), also known as glutamate-5-semialdehyde dehydrogenase, catalyses the second step of proline biosynthesis, the NADPH-dependent reversible reduction of gamma-glutamyl phosphate to glutamate-5-semialdehyde as shown below. L-glutamyl 5-phosphate + NADPH + H(+) = L-glutamate 5-semial...

[ "GO:0004350", "GO:0050661", "GO:0055129" ]

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

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

3

[ "PIRSF" ]

[ "PIRSF000151" ]

[ "GPR" ]

[ 24856 ]

1

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

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

[ "EC:1.2.1.41", "METACYC:PWY-6922", "REACTOME:R-SCE-8964539", "REACTOME:R-SCE-9837999", "REACTOME:R-SPO-8964539", "REACTOME:R-SPO-9837999" ]

6

[ "1o20", "1vlu", "2h5g", "4ghk", "4jbe", "8zok", "8zon", "8zoo" ]

8

[ "PUB00004804", "PUB00005656", "PUB00029304", "PUB00033269" ]

[ "1384052", "8896266", "14705032", "11375165" ]

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

[ 1992, 1996, 2004, 2001 ]

4

[]

0

null

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

[ 260, 22661, 1594, 1, 340 ]

5

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

[ 1, 1, 1, 1, 4 ]

5

true

Family

Glutamate-5-semialdehyde dehydrogenase

Glu-5-SA_DH

2