ID   RPPH_BRUSU              Reviewed;         178 AA.
AC   Q8FYM9; G0K7Q2;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 85.
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=ialA, nudH {ECO:0000255|HAMAP-Rule:MF_00298};
GN   OrderedLocusNames=BR1836, BS1330_I1830;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN30731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AEM19148.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014291; AAN30731.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002997; AEM19148.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004688740.1; NZ_KN046804.1.
DR   AlphaFoldDB; Q8FYM9; -.
DR   SMR; Q8FYM9; -.
DR   EnsemblBacteria; AEM19148; AEM19148; BS1330_I1830.
DR   GeneID; 45125116; -.
DR   GeneID; 55591431; -.
DR   KEGG; bms:BR1836; -.
DR   KEGG; bsi:BS1330_I1830; -.
DR   PATRIC; fig|204722.21.peg.3461; -.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   PhylomeDB; Q8FYM9; -.
DR   Proteomes; UP000007104; Chromosome I.
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.
FT   CHAIN           1..178
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000056999"
FT   DOMAIN          18..171
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           59..80
FT                   /note="Nudix box"
SQ   SEQUENCE   178 AA;  19854 MW;  A65C7ADEE2D6333C CRC64;
     MSKHKGPTGA MVDPESLPYR PCVGLMVLNK AGLVWAGRRI VIPGDEMDGA TQLWQMPQGG
     IDKGEDPAQA ALRELYEETG MTSVSLLEEA SDWINYDLPP HLVGLALKGK YRGQTQKWFA
     YRFEGDESEI AINPPPGGHT AEFDCWEWKP MADLPNLIVP FKRKVYEQVV ATFRHLAA