(data stored in ACNUC7421 zone)

SWISSPROT: RPPH_PSEAB

ID   RPPH_PSEAB              Reviewed;         159 AA.
AC   Q02U79;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   30-AUG-2017, entry version 62.
DE   RecName: Full=RNA pyrophosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00298};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00298};
DE   AltName: Full=(Di)nucleoside polyphosphate hydrolase {ECO:0000255|HAMAP-Rule:MF_00298};
GN   Name=rppH {ECO:0000255|HAMAP-Rule:MF_00298};
GN   Synonyms=nudH {ECO:0000255|HAMAP-Rule:MF_00298};
GN   OrderedLocusNames=PA14_04390;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Accelerates the degradation of transcripts by removing
CC       pyrophosphate from the 5'-end of triphosphorylated RNA, leading to
CC       a more labile monophosphorylated state that can stimulate
CC       subsequent ribonuclease cleavage. {ECO:0000255|HAMAP-
CC       Rule:MF_00298}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00298};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00298}.
DR   EMBL; CP000438; ABJ15300.1; -; Genomic_DNA.
DR   RefSeq; WP_003084400.1; NC_008463.1.
DR   ProteinModelPortal; Q02U79; -.
DR   SMR; Q02U79; -.
DR   EnsemblBacteria; ABJ15300; ABJ15300; PA14_04390.
DR   KEGG; pau:PA14_04390; -.
DR   HOGENOM; HOG000066723; -.
DR   KO; K08311; -.
DR   OMA; RPCVGIM; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR   HAMAP; MF_00298; Nudix_RppH; 1.
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   InterPro; IPR022927; RppH.
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;
DR   PRODOM; Q02U79.
DR   SWISS-2DPAGE; Q02U79.
KW   Complete proteome; Hydrolase.
FT   CHAIN         1    159       RNA pyrophosphohydrolase.
FT                                /FTId=PRO_1000021971.
FT   DOMAIN        6    149       Nudix hydrolase. {ECO:0000255|HAMAP-
FT                                Rule:MF_00298}.
FT   MOTIF        38     59       Nudix box.
SQ   SEQUENCE   159 AA;  18759 MW;  05E119F7B82FCBE8 CRC64;
     MIDSDGFRPN VGIILANEAG QVLWARRINQ EAWQFPQGGI NDRETPEEAL YRELNEEVGL
     EAGDVRILAC TRGWLRYRLP QRLVRTHSQP LCIGQKQKWF LLRLMSDEAR VRMDITSKPE
     FDGWRWVSYW YPLGQVVTFK REVYRRALKE LAPRLLARD
//

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