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Inosine triphosphate pyrophosphatase (ITPase) (Inosine triphosphatase) (EC 3.6.1.9) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase)

 A0A0L0P597_CANAR        Unreviewed;       211 AA.
A0A0L0P597;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
05-DEC-2018, entry version 22.
RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
Short=ITPase {ECO:0000256|HAMAP-Rule:MF_03148};
Short=Inosine triphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_03148};
AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
Short=NTPase {ECO:0000256|HAMAP-Rule:MF_03148};
Name=HAM1 {ECO:0000256|HAMAP-Rule:MF_03148};
ORFNames=QG37_01492 {ECO:0000313|EMBL:KNE01420.1};
Candida auris (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Metschnikowiaceae; Clavispora;
Clavispora/Candida clade.
NCBI_TaxID=498019 {ECO:0000313|EMBL:KNE01420.1, ECO:0000313|Proteomes:UP000037122};
[1] {ECO:0000313|Proteomes:UP000037122}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=6684 {ECO:0000313|Proteomes:UP000037122};
PubMed=26346253; DOI=10.1186/s12864-015-1863-z;
Chatterjee S., Alampalli S.V., Nageshan R.K., Chettiar S.T., Joshi S.,
Tatu U.S.;
"Draft genome of a commonly misdiagnosed multidrug resistant pathogen
Candida auris.";
BMC Genomics 16:686-686(2015).
-!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
nucleotides such as inosine triphosphate (ITP), deoxyinosine
triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their
respective monophosphate derivatives. The enzyme does not
distinguish between the deoxy- and ribose forms. Probably excludes
non-canonical purines from RNA and DNA precursor pools, thus
preventing their incorporation into RNA and DNA and avoiding
chromosomal lesions. {ECO:0000256|HAMAP-Rule:MF_03148}.
-!- CATALYTIC ACTIVITY:
Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317;
EC=3.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721545};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
Note=Binds 1 divalent metal cation per subunit; can use either
Mg(2+) or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_03148};
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721538}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148}.
Nucleus {ECO:0000256|HAMAP-Rule:MF_03148}.
-!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
Rule:MF_03148, ECO:0000256|RuleBase:RU003781,
ECO:0000256|SAAS:SAAS00721539}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KNE01420.1}.
-----------------------------------------------------------------------
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EMBL; LGST01000011; KNE01420.1; -; Genomic_DNA.
RefSeq; XP_018171143.1; XM_018311011.1.
EnsemblFungi; KNE01420; KNE01420; QG37_01492.
GeneID; 28875290; -.
KEGG; caur:QG37_01492; -.
KO; K01519; -.
Proteomes; UP000037122; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-UniRule.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
CDD; cd00515; HAM1; 1.
Gene3D; 3.90.950.10; -; 1.
HAMAP; MF_03148; HAM1_NTPase; 1.
InterPro; IPR002637; Ham1p-like.
InterPro; IPR027502; ITPase.
InterPro; IPR029001; ITPase-like_fam.
PANTHER; PTHR11067; PTHR11067; 1.
Pfam; PF01725; Ham1p_like; 1.
SUPFAM; SSF52972; SSF52972; 1.
TIGRFAMs; TIGR00042; TIGR00042; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000037122};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721512};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00721541};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721547};
Manganese {ECO:0000256|HAMAP-Rule:MF_03148};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721543};
Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721522};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721527};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03148}.
REGION 25 30 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03148}.
REGION 91 92 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03148}.
REGION 167 170 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03148}.
REGION 195 196 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03148}.
METAL 63 63 Magnesium or manganese.
{ECO:0000256|HAMAP-Rule:MF_03148}.
METAL 91 91 Magnesium or manganese.
{ECO:0000256|HAMAP-Rule:MF_03148}.
BINDING 75 75 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03148}.
BINDING 190 190 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03148}.
SEQUENCE 211 AA; 23281 MW; CA5F4ACBD54F44B5 CRC64;
MSIGCEFLLL PEDIITMSKT ITFVTGNSNK LKEVIAILGG QPGPEGSKVG NFTVVNKSLD
LDEVQGTIET VTIHKAKEAA RQVNGAVLVE DTCLAFNAMN DLPGPYIKWF LKAIGLQGLV
DMLYKFEDKG AKAVCTFGYC EGPESEVKLF QGITKGKIVD SRGPTDFGWD SVFEPEGFNE
TYAEMDKSVK NTISHRFRAL DKLREFLKIQ E


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