ID   RPPH_RICBR              Reviewed;         161 AA.
AC   Q1RHV9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, 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=nudH {ECO:0000255|HAMAP-Rule:MF_00298};
GN   OrderedLocusNames=RBE_0974;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05055.1; -; Genomic_DNA.
DR   RefSeq; WP_011477635.1; NC_007940.1.
DR   AlphaFoldDB; Q1RHV9; -.
DR   SMR; Q1RHV9; -.
DR   STRING; 336407.RBE_0974; -.
DR   EnsemblBacteria; ABE05055; ABE05055; RBE_0974.
DR   KEGG; rbe:RBE_0974; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   OMA; PCVGIML; -.
DR   OrthoDB; 1345242at2; -.
DR   Proteomes; UP000001951; 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; IPR020084; NUDIX_hydrolase_CS.
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.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..161
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000277998"
FT   DOMAIN          12..154
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           46..67
FT                   /note="Nudix box"
SQ   SEQUENCE   161 AA;  18604 MW;  59246E5537037006 CRC64;
     MNKTSKKHLA LPYRPGVGMM ILNADNKIFV GKRIDTKISA WQMPQGGIVP GETPSIAAMR
     EMLEEIGSSK GYIIAESKCW YSYDVPSFLI PKLWDGNFRG QKQRWFLIRF TGTNEDININ
     TLNPEFDEWR WASLDELLSI IIPFKRKLYQ AVVKEFESLI Q