ID   RPPH_METFK              Reviewed;         172 AA.
AC   Q1GZE7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Mfla_2123;
OS   Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=265072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT / ATCC 51484 / DSM 6875;
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   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT   "Complete sequence of Methylobacillus flagellatus KT.";
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; CP000284; ABE50390.1; -; Genomic_DNA.
DR   RefSeq; WP_011480344.1; NC_007947.1.
DR   AlphaFoldDB; Q1GZE7; -.
DR   SMR; Q1GZE7; -.
DR   STRING; 265072.Mfla_2123; -.
DR   EnsemblBacteria; ABE50390; ABE50390; Mfla_2123.
DR   KEGG; mfa:Mfla_2123; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_1_4; -.
DR   OMA; PCVGIML; -.
DR   OrthoDB; 1345242at2; -.
DR   Proteomes; UP000002440; 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..172
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_1000021961"
FT   DOMAIN          6..149
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           38..59
FT                   /note="Nudix box"
SQ   SEQUENCE   172 AA;  20877 MW;  D2AD3C2810B5EF6D CRC64;
     MIDRDGYRPN VGIILCNARN QVFWGKRIRE HSWQFPQGGI KYGESPEQAM YRELMEEVGL
     RPEHVKILGR TRDWLRYDVP TNWIKREWRG SYRGQKQIWF LLRLIGRDSD VSLRASTHPE
     FDAWRWSDYW VAMDSVIEFK RDVYRMALKE LSMHLTEHRR PRVAERVDQL VR