ID   RPPH_DECAR              Reviewed;         182 AA.
AC   Q47IC9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Daro_0645;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(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; CP000089; AAZ45402.1; -; Genomic_DNA.
DR   RefSeq; WP_011286411.1; NC_007298.1.
DR   AlphaFoldDB; Q47IC9; -.
DR   SMR; Q47IC9; -.
DR   STRING; 159087.Daro_0645; -.
DR   EnsemblBacteria; AAZ45402; AAZ45402; Daro_0645.
DR   KEGG; dar:Daro_0645; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_1_4; -.
DR   OMA; PCVGIML; -.
DR   OrthoDB; 1345242at2; -.
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..182
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000231906"
FT   DOMAIN          6..149
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   REGION          162..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           38..59
FT                   /note="Nudix box"
SQ   SEQUENCE   182 AA;  21961 MW;  8BFC56DE3872B029 CRC64;
     MLDREGYRPN VGIILCNGRN EVFWGKRIRE HSWQFPQGGI KRGETPEEAM FRELYEEVGL
     LPEHVRILGR TKGWLRYEVP THWIKREWRG SYKGQKQIWF LLRLVGRDSD VNLRATNKPE
     FDAWRWNDYW VPLDAVIEFK RLVYEQALNE LVRFLDFDRK GPRHKKEQEP FSDVVDSVRS
     EE