ID D8A5K8_ECOMS Unreviewed; 120 AA. AC D8A5K8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 26-NOV-2014, entry version 24. DE RecName: Full=Nucleoside triphosphatase NudI {ECO:0000256|HAMAP-Rule:MF_01846}; DE EC=3.6.1.- {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: Nucleoside triphosphate + H(2)O = nucleoside CC monophosphate + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01846}. CC -!- COFACTOR: CC Note=Magnesium. {ECO:0000256|HAMAP-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 -!- SIMILARITY: Contains nudix hydrolase domain. CC {ECO:0000256|SAAS:SAAS00025283}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:0050355; F:triphosphatase 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:SAAS00029529}; 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 //