ID   RPPH_BRUA2              Reviewed;         178 AA.
AC   Q2YLJ4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 76.
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=BAB1_1844;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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=CAJ11800.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM040264; CAJ11800.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002964914.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YLJ4; -.
DR   SMR; Q2YLJ4; -.
DR   STRING; 359391.BAB1_1844; -.
DR   EnsemblBacteria; CAJ11800; CAJ11800; BAB1_1844.
DR   GeneID; 3788760; -.
DR   KEGG; bmf:BAB1_1844; -.
DR   PATRIC; fig|359391.11.peg.357; -.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   PhylomeDB; Q2YLJ4; -.
DR   Proteomes; UP000002719; 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; Reference proteome.
FT   CHAIN           1..178
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000231900"
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;  19887 MW;  E748DE6D42CB8E91 CRC64;
     MSEHKGPTGA MVDPESLPYR PCVGLMVLNK AGLVWAGRRI VIPGDEMDGA TQLWQMPQGG
     IDKGEDPAQA ALRELYEETG MTSVSLLEEA SDWINYDLPP HLMGLALKGK YRGQTQKWFA
     YRFEGDESEI AINPPPGGHT AEFDCWEWKP MADLPNLIVP FKRKVYEQVV ATFRHLAA