ID   RPPH_BARCL              Reviewed;         173 AA.
AC   Q9KK72;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=ialA, invA, nudH {ECO:0000255|HAMAP-Rule:MF_00298};
OS   Bartonella clarridgeiae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=56426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Marston E.L.;
RT   "Cloning of invasion-associated protein A (invA) gene from Bartonella
RT   clarridgeiae.";
RL   Submitted (APR-1999) 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; AF140364; AAF79926.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KK72; -.
DR   SMR; Q9KK72; -.
DR   OMA; PCVGIML; -.
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; IPR020476; Nudix_hydrolase.
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   PRINTS; PR00502; NUDIXFAMILY.
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..173
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000056993"
FT   DOMAIN          11..164
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           52..73
FT                   /note="Nudix box"
SQ   SEQUENCE   173 AA;  20329 MW;  4A68431D2B857886 CRC64;
     MDTIVDFKAL PYRKCVGILV FNYEGKVWVG RRLMTVSHAN VDMSKLWQLP QGGINQGEKP
     IDAARRELYE ETGIQSVKLI KEAQDWFEYD FPQELMGHVL NNKYRGQTQK WFSFQFTGEI
     SEITINPPPD GNKAEFDQWK WVDLEELPSI VVSFKKHVYT QVVKEFRNSF KYL