ID   RPPH_PSEAE              Reviewed;         159 AA.
AC   Q9X4P2;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 112.
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}; OrderedLocusNames=PA0336;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PA14;
RX   PubMed=10051655; DOI=10.1073/pnas.96.5.2408;
RA   Tan M.-W., Rahme L.G., Sternberg J.A., Tompkins R.G., Ausubel F.M.;
RT   "Pseudomonas aeruginosa killing of Caenorhabditis elegans used to identify
RT   P. aeruginosa virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:2408-2413(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Accelerates the degradation of transcripts by removing
CC       pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a
CC       more labile monophosphorylated state that can stimulate subsequent
CC       ribonuclease cleavage. {ECO:0000255|HAMAP-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}.
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; AF116285; AAD22458.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG03725.1; -; Genomic_DNA.
DR   PIR; C83604; C83604.
DR   RefSeq; NP_249027.1; NC_002516.2.
DR   RefSeq; WP_003084400.1; NZ_QZGE01000016.1.
DR   AlphaFoldDB; Q9X4P2; -.
DR   SMR; Q9X4P2; -.
DR   STRING; 287.DR97_3302; -.
DR   PaxDb; Q9X4P2; -.
DR   EnsemblBacteria; AAG03725; AAG03725; PA0336.
DR   GeneID; 882290; -.
DR   KEGG; pae:PA0336; -.
DR   PATRIC; fig|208964.12.peg.354; -.
DR   PseudoCAP; PA0336; -.
DR   HOGENOM; CLU_087195_3_1_6; -.
DR   InParanoid; Q9X4P2; -.
DR   OMA; PCVGIML; -.
DR   PhylomeDB; Q9X4P2; -.
DR   BioCyc; PAER208964:G1FZ6-339-MON; -.
DR   PHI-base; PHI:7474; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0034353; F:RNA pyrophosphohydrolase activity; IMP:PseudoCAP.
DR   GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
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;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..159
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000057017"
FT   DOMAIN          6..149
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           38..59
FT                   /note="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