ID   RPPH_PASMU              Reviewed;         198 AA.
AC   P57809;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
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}, pnhA;
GN   OrderedLocusNames=PM0082;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serogroup A:1 / X73;
RA   Tworek T.N., Chang C.I., Ruffolo C.G.;
RT   "The nudix hydrolase, PnhA is associated with the ability of Pasteurella
RT   multocida to infect host cells.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AY442169; AAR14276.1; -; Genomic_DNA.
DR   EMBL; AE004439; AAK02166.1; -; Genomic_DNA.
DR   RefSeq; WP_005722417.1; NC_002663.1.
DR   AlphaFoldDB; P57809; -.
DR   SMR; P57809; -.
DR   STRING; 747.DR93_1991; -.
DR   EnsemblBacteria; AAK02166; AAK02166; PM0082.
DR   KEGG; pmu:PM0082; -.
DR   HOGENOM; CLU_087195_3_2_6; -.
DR   OMA; PCVGIML; -.
DR   Proteomes; UP000000809; 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..198
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000057015"
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   198 AA;  23344 MW;  1A58860440BEAA8B CRC64;
     MIDFDGYRPN VGIVICNSKG QVLWAKRYGQ NSWQFPQGGI NDNESAEQAM YRELFEEVGL
     SPKDVKILYI SKHWLRYKLP KRLLRYDSKP VCIGQKQRWF LLQLVSDEKN INMQSSKSPE
     FDGWRWVSFW YPVRQVVSFK KEVYRKAMKE FASVLFDGAK ENLLSSKSNE SDLKTHHTTK
     KSTFLTKHSK KHFHKSRG