ID   RPPH_RICCN              Reviewed;         161 AA.
AC   Q92IV0;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=invA, nudH {ECO:0000255|HAMAP-Rule:MF_00298};
GN   OrderedLocusNames=RC0320;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02858.1; -; Genomic_DNA.
DR   PIR; H97739; H97739.
DR   RefSeq; WP_010976978.1; NC_003103.1.
DR   AlphaFoldDB; Q92IV0; -.
DR   SMR; Q92IV0; -.
DR   GeneID; 927499; -.
DR   KEGG; rco:RC0320; -.
DR   PATRIC; fig|272944.4.peg.367; -.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:UniProt.
DR   CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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   PANTHER; PTHR23114; M7GPPPN-MRNA HYDROLASE; 1.
DR   PANTHER; PTHR23114:SF17; M7GPPPN-MRNA HYDROLASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; Nudix; 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_0000057024"
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;  18657 MW;  4B27422BC247CC79 CRC64;
     MSNSSKKHLD LPYRPGVGMM ILNANNHIFV GKRIDTKISA WQMPQGGIVP GETPSIAAMR
     EMLEEIGSDK GYIIAESKFW YSYDVPSFLI PKLWNGNFRG QKQRWFLIRF TGNNEDININ
     TSNPEFDQWR WASLDELLSI IIPFKRKLYQ AVVKEFESLI Q
//