(data stored in ACNUC9543 zone)

SWISSPROT: RPPH_YERPA

ID   RPPH_YERPA              Reviewed;         175 AA.
AC   Q1CAS2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 68.
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=YPA_0482;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(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; CP000308; ABG12450.1; -; Genomic_DNA.
DR   RefSeq; WP_002211381.1; NZ_CP009906.1.
DR   SMR; Q1CAS2; -.
DR   EnsemblBacteria; ABG12450; ABG12450; YPA_0482.
DR   KEGG; ypa:YPA_0482; -.
DR   HOGENOM; HOG000066723; -.
DR   KO; K08311; -.
DR   OMA; RPCVGIM; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:UniProtKB-UniRule.
DR   CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR   HAMAP; MF_00298; Nudix_RppH; 1.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
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; Q1CAS2.
DR   SWISS-2DPAGE; Q1CAS2.
KW   Complete proteome; Hydrolase.
FT   CHAIN         1    175       RNA pyrophosphohydrolase.
FT                                /FTId=PRO_1000022009.
FT   DOMAIN        6    149       Nudix hydrolase. {ECO:0000255|HAMAP-
FT                                Rule:MF_00298}.
FT   MOTIF        38     59       Nudix box.
SQ   SEQUENCE   175 AA;  20893 MW;  9D6F616B4BA5DE7F CRC64;
     MIDDDGYRPN VGIVICNRQG EVLWARRYGQ HSWQFPQGGI NPGETPEQAM YRELFEEVGL
     NKKDVRILAS TRNWLRYKLP KRLVRWDTKP VCIGQKQRWF LLQLMCNEAE INMQRSSTPE
     FDGWRWVSYW YPVRQVVSFK RDVYRRVMKE FAATVMPVQE VAPPRVPPAY RRKRG
//

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