ID   RPPH_HAEDU              Reviewed;         197 AA.
AC   Q7VPB7;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
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}; OrderedLocusNames=HD_0172;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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; AE017143; AAP95165.1; -; Genomic_DNA.
DR   RefSeq; WP_010944219.1; NC_002940.2.
DR   AlphaFoldDB; Q7VPB7; -.
DR   SMR; Q7VPB7; -.
DR   STRING; 233412.HD_0172; -.
DR   EnsemblBacteria; AAP95165; AAP95165; HD_0172.
DR   KEGG; hdu:HD_0172; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_2_6; -.
DR   OMA; PCVGIML; -.
DR   Proteomes; UP000001022; 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..197
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000057008"
FT   DOMAIN          6..150
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           38..59
FT                   /note="Nudix box"
SQ   SEQUENCE   197 AA;  23461 MW;  E92ED45A90ADBA82 CRC64;
     MIDFDGYRPN VGIVICNKVG QVLWARRFGQ NSWQFPQGGI NEGENIETAM YRELYEEVGL
     TKKDVRLLWA SKYWLKYKLP KRLVRNDASQ PVCIGQKQRW FLLQLVSDES AVNLKTTKSP
     EFDGWRWVSF WYPVRQVVSF KRDVYRKVMR EFAAILLNET RKGETERSVL EASDKREYQR
     RETRKSARAW NHYPKGK