ID   RPPH_RHOPA              Reviewed;         168 AA.
AC   P61786;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=invA1, nudH {ECO:0000255|HAMAP-Rule:MF_00298};
GN   OrderedLocusNames=RPA0171;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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}.
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DR   EMBL; BX572593; CAE25615.1; -; Genomic_DNA.
DR   RefSeq; WP_011155739.1; NC_005296.1.
DR   AlphaFoldDB; P61786; -.
DR   SMR; P61786; -.
DR   STRING; 258594.RPA0171; -.
DR   PRIDE; P61786; -.
DR   EnsemblBacteria; CAE25615; CAE25615; RPA0171.
DR   GeneID; 66891176; -.
DR   KEGG; rpa:RPA0171; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   OMA; WAAAKRE; -.
DR   PhylomeDB; P61786; -.
DR   BioCyc; RPAL258594:TX73_RS00880-MON; -.
DR   Proteomes; UP000001426; Chromosome.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
DR   CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR   HAMAP; MF_00298; Nudix_RppH; 1.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR022927; RppH.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..168
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000057023"
FT   DOMAIN          8..159
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           47..68
FT                   /note="Nudix box"
SQ   SEQUENCE   168 AA;  19281 MW;  4C50D9753DCB6AEC CRC64;
     MARYEDLPYR TCVGVMLINR EGLVFIGRRA GGIEHVDDTH VWQMPQGGVD PGEDTWKAAK
     RELYEETSVN SVEKLAEVPD WLIYDIPRTV AGRAWKGRYR GQRQKWFAAR FTGADSEINV
     VHPGGGHKAE FTSWRWEPMH NLPELIVPFK RPVYERVVKE FSQLAAAV