ID   RPPH_RICCK              Reviewed;         161 AA.
AC   A8EXY5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=A1E_01365;
OS   Rickettsia canadensis (strain McKiel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=293613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=McKiel;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia canadensis.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000409; ABV73218.1; -; Genomic_DNA.
DR   RefSeq; WP_012148417.1; NC_009879.1.
DR   AlphaFoldDB; A8EXY5; -.
DR   SMR; A8EXY5; -.
DR   STRING; 293613.A1E_01365; -.
DR   EnsemblBacteria; ABV73218; ABV73218; A1E_01365.
DR   KEGG; rcm:A1E_01365; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   OMA; PCVGIML; -.
DR   OrthoDB; 1345242at2; -.
DR   Proteomes; UP000007056; 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_1000021988"
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;  18667 MW;  5392289A243A8B64 CRC64;
     MRNASKKHLD LPYRPGVGMM ILNADNHIFV GKRIDTKISA WQMPQGGIVP GETPSIAAMR
     EMLEEIGSDK GYIIAESKCW YSYDLPSFLI PKLWNGNFRG QKQRWFLIRF TGNNEDININ
     TSNPEFDQWR WASLNELLSI IIPFKRKLYQ AVVKEFDSLI Q