ID   RPPH_BRUC2              Reviewed;         178 AA.
AC   A9M874;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
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=BCAN_A1874;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-2007) 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; CP000872; ABX62872.1; -; Genomic_DNA.
DR   RefSeq; WP_004688740.1; NC_010103.1.
DR   AlphaFoldDB; A9M874; -.
DR   SMR; A9M874; -.
DR   GeneID; 58775178; -.
DR   KEGG; bcs:BCAN_A1874; -.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   PhylomeDB; A9M874; -.
DR   Proteomes; UP000001385; Chromosome I.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
DR   CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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   PANTHER; PTHR11839; UDP/ADP-SUGAR PYROPHOSPHATASE; 1.
DR   PANTHER; PTHR11839:SF15; URIDINE DIPHOSPHATE GLUCOSE PYROPHOSPHATASE NUDT14; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 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_1000078953"
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
//