ID   RPPH_RICAE              Reviewed;         161 AA.
AC   C3PMT3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=RAF_ORF0297;
OS   Rickettsia africae (strain ESF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=347255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ESF-5;
RX   PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA   Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA   Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT   "Analysis of the Rickettsia africae genome reveals that virulence
RT   acquisition in Rickettsia species may be explained by genome reduction.";
RL   BMC Genomics 10:166-166(2009).
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; CP001612; ACP53243.1; -; Genomic_DNA.
DR   RefSeq; WP_012719499.1; NC_012633.1.
DR   AlphaFoldDB; C3PMT3; -.
DR   SMR; C3PMT3; -.
DR   EnsemblBacteria; ACP53243; ACP53243; RAF_ORF0297.
DR   KEGG; raf:RAF_ORF0297; -.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   OMA; PCVGIML; -.
DR   Proteomes; UP000002305; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Metal-binding.
FT   CHAIN           1..161
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_1000204938"
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;  18692 MW;  AAA66AD37247D461 CRC64;
     MSNSSKKHFD LPYRPGVGMM ILNADNHIFV GKRIDTKISA WQMPQGGIVP GETPSIAAMR
     EMLEEIGSDK GYIIAESKFW YSYDVPSFLI PKLWNGNFRG QQQRWFLIRF TGNNEDININ
     TSNPEFDQWR WASLDELLSI IIPFKRKLYQ AVVKEFESLI Q