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 27-MAR-2024, entry version 81.
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; Pseudomonadota; 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 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 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; 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
//
