ID   RPPH_COXBU              Reviewed;         228 AA.
AC   Q83BF8;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-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};
GN   OrderedLocusNames=CBU_1551;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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: In the C-terminal section; belongs to the Nudix hydrolase
CC       family. RppH subfamily. {ECO:0000305}.
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DR   EMBL; AE016828; AAO91048.1; -; Genomic_DNA.
DR   RefSeq; NP_820534.1; NC_002971.3.
DR   RefSeq; WP_010958294.1; NC_002971.4.
DR   AlphaFoldDB; Q83BF8; -.
DR   SMR; Q83BF8; -.
DR   STRING; 227377.CBU_1551; -.
DR   EnsemblBacteria; AAO91048; AAO91048; CBU_1551.
DR   GeneID; 1209461; -.
DR   KEGG; cbu:CBU_1551; -.
DR   PATRIC; fig|227377.7.peg.1552; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_0_6; -.
DR   OMA; PCVGIML; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0034353; F:RNA pyrophosphohydrolase activity; IBA:GO_Central.
DR   GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
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; IPR020084; NUDIX_hydrolase_CS.
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.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..228
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000057004"
FT   DOMAIN          76..221
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   REGION          1..70
FT                   /note="Unknown"
FT   REGION          71..228
FT                   /note="RppH domain"
FT   MOTIF           109..130
FT                   /note="Nudix box"
SQ   SEQUENCE   228 AA;  26730 MW;  EAC865EB786DAB77 CRC64;
     MEKRSGIGRL YQGSFFNRYS RAGGNPGAPS VRCARVRGDD GVLVFTPFGN DRRGTSSTTM
     KQWVKMMNDI VIDKRGFRLG VGMVIMNRQG ELLWGRRVGN PDAWQFPQGG LLPNETLREA
     LNRELDEEVG LSPHDVIYLR ETRQWISYRL PKKFRRPEHR GPVCIGQRQK WFLLQFTGKD
     DAISLDHCSQ PEFDQWRWVD YWYPVDHVVE FKRDVYQKVL TEFAEFIR