ID   RPPH_RHOPB              Reviewed;         175 AA.
AC   Q21CZ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=RPC_0168;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) 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; CP000301; ABD85743.1; -; Genomic_DNA.
DR   RefSeq; WP_011470651.1; NC_007925.1.
DR   AlphaFoldDB; Q21CZ3; -.
DR   SMR; Q21CZ3; -.
DR   STRING; 316056.RPC_0168; -.
DR   EnsemblBacteria; ABD85743; ABD85743; RPC_0168.
DR   KEGG; rpc:RPC_0168; -.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   OMA; WAAAKRE; -.
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; IPR015797; NUDIX_hydrolase-like_dom_sf.
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.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..175
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_1000021982"
FT   DOMAIN          8..159
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           47..68
FT                   /note="Nudix box"
SQ   SEQUENCE   175 AA;  19886 MW;  2336FB3E7D86E273 CRC64;
     MTRYDDLPYR TCVGMMLLNA EGLVFIGRRL GGIEHVDETH VWQMPQGGVD PGEDPWTAAK
     RELYEETSVR SVEKLGEIAD WLIYDIPRTV AGRSWKGRYR GQRQKWYAVR FTGDDSEIDV
     VSPGGGHKAE FISWRWEPMQ NLPDLIVPFK RPVYERVVKE FAALAKDAAK VSGGG