ID   RPPH_POLNA              Reviewed;         235 AA.
AC   A1VK87;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Pnap_0746;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(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; CP000529; ABM36065.1; -; Genomic_DNA.
DR   RefSeq; WP_011800160.1; NC_008781.1.
DR   AlphaFoldDB; A1VK87; -.
DR   SMR; A1VK87; -.
DR   STRING; 365044.Pnap_0746; -.
DR   EnsemblBacteria; ABM36065; ABM36065; Pnap_0746.
DR   KEGG; pna:Pnap_0746; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_1_1_4; -.
DR   OMA; PLDCVIE; -.
DR   OrthoDB; 1345242at2; -.
DR   Proteomes; UP000000644; 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; 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; Reference proteome.
FT   CHAIN           1..235
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_1000021968"
FT   DOMAIN          6..149
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   REGION          184..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           38..59
FT                   /note="Nudix box"
SQ   SEQUENCE   235 AA;  27431 MW;  030E9D78F72ECCD6 CRC64;
     MLDRDGFRPN VGIILLNQRS QVFWGKRIRT HSWQFPQGGI DRGENPEQAM FRELHEEVGL
     HPQHVQVLAR TRDWLRYEVP DRFIRRDARG HYKGQKQIWF LLQLVGHDWD LNLRATNHPE
     FDAWRWNDYW VPLDVVVEFK RGVYEMALTE LSRFVPRCEF RFDARPEQRN RYLRGGLHQR
     DLLANQSGEP GSFPAAGGIP SYATRPGAPF ELPPGATFEP DPQTSFGVNA PTKKT