ID   RPPH_ERYLH              Reviewed;         164 AA.
AC   Q2N9Y3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, 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=ELI_07080;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594;
RX   PubMed=19168610; DOI=10.1128/jb.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(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; CP000157; ABC63508.1; -; Genomic_DNA.
DR   RefSeq; WP_011414344.1; NC_007722.1.
DR   AlphaFoldDB; Q2N9Y3; -.
DR   SMR; Q2N9Y3; -.
DR   STRING; 314225.ELI_07080; -.
DR   EnsemblBacteria; ABC63508; ABC63508; ELI_07080.
DR   KEGG; eli:ELI_07080; -.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   OMA; WAAAKRE; -.
DR   OrthoDB; 1345242at2; -.
DR   Proteomes; UP000008808; 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..164
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_1000078962"
FT   DOMAIN          12..158
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           47..68
FT                   /note="Nudix box"
SQ   SEQUENCE   164 AA;  18705 MW;  3D421099BD118FF2 CRC64;
     MASGSADHED LRYRQCAGVM LANREGLVFA AQRIDSKNLG AWQMPQGGID PGETQQEAAM
     RELEEETGVS ADLADVIARM PYPVRYDLPE ELQGKLWGGR YRGQEQHWFL ARFTGTDADI
     DIAAHNPPEF SEWKWVEPDE LPRLIVPFKR EVYRAVVKEF RSLI