(data stored in ACNUC8465 zone)

SWISSPROT: B6HG06_PENRW

ID   B6HG06_PENRW            Unreviewed;       186 AA.
AC   B6HG06;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE            Short=ITPase {ECO:0000256|HAMAP-Rule:MF_03148};
DE            Short=Inosine triphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE            EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_03148};
DE   AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE   AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE   AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE   AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE            Short=NTPase {ECO:0000256|HAMAP-Rule:MF_03148};
GN   ORFNames=Pc20g00590 {ECO:0000313|EMBL:CAP85388.1}, PCH_Pc20g00590
GN   {ECO:0000313|EMBL:CAP85388.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85388.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85388.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
CC       nucleotides such as inosine triphosphate (ITP), deoxyinosine
CC       triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their
CC       respective monophosphate derivatives. The enzyme does not
CC       distinguish between the deoxy- and ribose forms. Probably excludes
CC       non-canonical purines from RNA and DNA precursor pools, thus
CC       preventing their incorporation into RNA and DNA and avoiding
CC       chromosomal lesions. {ECO:0000256|HAMAP-Rule:MF_03148}.
CC   -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC       nucleotide + diphosphate. {ECO:0000256|HAMAP-Rule:MF_03148,
CC       ECO:0000256|SAAS:SAAS00721545}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03148,
CC       ECO:0000256|SAAS:SAAS00721538}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_03148, ECO:0000256|RuleBase:RU003781,
CC       ECO:0000256|SAAS:SAAS00721539}.
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DR   EMBL; AM920435; CAP85388.1; -; Genomic_DNA.
DR   RefSeq; XP_002562621.1; XM_002562575.1.
DR   STRING; 500485.XP_002562621.1; -.
DR   EnsemblFungi; CAP85388; CAP85388; PCH_Pc20g00590.
DR   GeneID; 8307716; -.
DR   KEGG; pcs:Pc20g00590; -.
DR   eggNOG; KOG3222; Eukaryota.
DR   eggNOG; COG0127; LUCA.
DR   HOGENOM; HOG000293320; -.
DR   KO; K01519; -.
DR   OMA; YDPIFQP; -.
DR   OrthoDB; EOG092C523G; -.
DR   BioCyc; PCHR:PC20G00590-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00515; HAM1; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_03148; HAM1_NTPase; 1.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR027502; ITPase.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   PANTHER; PTHR11067; PTHR11067; 1.
DR   Pfam; PF01725; Ham1p_like; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00042; TIGR00042; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HG06.
DR   SWISS-2DPAGE; B6HG06.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|SAAS:SAAS00721512};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00721541};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|SAAS:SAAS00721547};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_03148};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|SAAS:SAAS00721543};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|SAAS:SAAS00721522};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|SAAS:SAAS00721527};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03148};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT   REGION       10     15       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03148}.
FT   REGION       66     67       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03148}.
FT   REGION      142    145       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03148}.
FT   REGION      169    170       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03148}.
FT   METAL        38     38       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_03148}.
FT   METAL        66     66       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_03148}.
FT   BINDING      50     50       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03148}.
FT   BINDING     164    164       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03148}.
SQ   SEQUENCE   186 AA;  20801 MW;  F29EC6E80C7CB0FE CRC64;
     MTLTKLNFIT GNKNKLLEVR AILGKVIEVD NQEVDVPEIQ GTIEEIAKEK ARRAAEAING
     PALTEDTALE FHALKGLPGP YIKSFMEKLG HEGLNKMLDG FEDRTAEAVC TFAFCRGPGE
     EPIVFQGRTE GAIVRPRGSG NFGWDAIFEY DGKQTYAEMD KEEKNKISHR YKALVKLQQW
     LAEGQQ
//

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