(data stored in SCRATCH zone)

SWISSPROT: Q3KJ17_PSEPF

ID   Q3KJ17_PSEPF            Unreviewed;       205 AA.
AC   Q3KJ17;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABA72239.1};
GN   OrderedLocusNames=Pfl01_0495 {ECO:0000313|EMBL:ABA72239.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72239.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72239.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72239.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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DR   EMBL; CP000094; ABA72239.1; -; Genomic_DNA.
DR   RefSeq; WP_011332160.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0495; -.
DR   EnsemblBacteria; ABA72239; ABA72239; Pfl01_0495.
DR   KEGG; pfo:Pfl01_0495; -.
DR   eggNOG; ENOG41087AY; Bacteria.
DR   eggNOG; ENOG410ZYVG; LUCA.
DR   HOGENOM; HOG000045857; -.
DR   KO; K01515; -.
DR   OMA; EQAYQWM; -.
DR   BioCyc; PFLU205922:G1G4S-500-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   InterPro; IPR004385; NDP_pyrophosphatase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   TIGRFAMs; TIGR00052; TIGR00052; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   4: Predicted;
DR   PRODOM; Q3KJ17.
DR   SWISS-2DPAGE; Q3KJ17.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704}.
FT   DOMAIN       51    189       Nudix hydrolase. {ECO:0000259|PROSITE:
FT                                PS51462}.
SQ   SEQUENCE   205 AA;  23147 MW;  0CD1263CD7FE5612 CRC64;
     MTDFAKAIPT AVDIVRREQC YKGFYKLDRL HLRHELFAGG MSREINREVF VRHDAVCMLP
     YDPQRDEVVL IEQFRVGALG KTDNPWLVEL VAGLIDKDEQ PEEVAHREAQ EEAGLDIKAL
     WPMTKYFPSP GGSNEFVHLY LGRCSTEGAG GLHGLEEEAE DIRVTVWAFE DALQAVRDGR
     IANAASIIAL QWLALNRAEV RGLWS
//

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