ID   D8A5K8_ECOMS            Unreviewed;       120 AA.
AC   D8A5K8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   29-APR-2015, entry version 28.
DE   RecName: Full=Nucleoside triphosphatase NudI {ECO:0000256|HAMAP-Rule:MF_01846};
DE            EC=3.6.1.19 {ECO:0000256|HAMAP-Rule:MF_01846};
DE   AltName: Full=Pyrimidine deoxynucleoside triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01846};
DE   AltName: Full=dCTP diphosphatase {ECO:0000256|HAMAP-Rule:MF_01846};
DE   AltName: Full=dTTP diphosphatase {ECO:0000256|HAMAP-Rule:MF_01846};
DE   AltName: Full=dUTP diphosphatase {ECO:0000256|HAMAP-Rule:MF_01846};
GN   Name=nudI {ECO:0000256|HAMAP-Rule:MF_01846,
GN   ECO:0000313|EMBL:EFK21550.1};
GN   ORFNames=HMPREF9530_01802 {ECO:0000313|EMBL:EFK21550.1};
OS   Escherichia coli (strain MS 21-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK21550.1};
RN   [1] {ECO:0000313|EMBL:EFK21550.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK21550.1};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates,
CC       with a preference for pyrimidine deoxynucleoside triphosphates
CC       (dUTP, dTTP and dCTP). {ECO:0000256|HAMAP-Rule:MF_01846}.
CC   -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC       nucleotide + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01846}.
CC   -!- CATALYTIC ACTIVITY: dCTP + H(2)O = dCMP + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01846}.
CC   -!- CATALYTIC ACTIVITY: dTTP + H(2)O = dTMP + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01846}.
CC   -!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01846}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01846};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01846}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudI subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01846}.
CC   -!- SIMILARITY: Contains 1 nudix hydrolase domain. {ECO:0000256|HAMAP-
CC       Rule:MF_01846}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFK21550.1}.
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DR   EMBL; ADTR01000165; EFK21550.1; -; Genomic_DNA.
DR   ProteinModelPortal; D8A5K8; -.
DR   EnsemblBacteria; EFK21550; EFK21550; HMPREF9530_01802.
DR   PATRIC; 41828291; VBIEscCol155740_1777.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.79.10; -; 1.
DR   HAMAP; MF_01846; Nudix_NudI; 1.
DR   InterPro; IPR023781; Nucleoside_triphosphatase_NudI.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01846,
KW   ECO:0000256|SAAS:SAAS00167526};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01846};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01846}.
FT   MOTIF        17     38       Nudix box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01846}.
SQ   SEQUENCE   120 AA;  13925 MW;  0239D7C72F84AB84 CRC64;
     MADDRGVFPG QWALSGGGVE PGERIEEALR REIREELGEQ LLLTEITPWT FSDDIRTKTY
     ADGRKEEIYM IYLIFDCVSA NREVKINEEF QDYAWVKPED LAHYDLNVAT RKTLRLKGLL
//