RPPH_RALSO
ID RPPH_RALSO Reviewed; 238 AA.
AC Q8XVL3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
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}; OrderedLocusNames=RSc2817;
GN ORFNames=RS00288;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD16524.1; -; Genomic_DNA.
DR RefSeq; WP_011002724.1; NC_003295.1.
DR AlphaFoldDB; Q8XVL3; -.
DR SMR; Q8XVL3; -.
DR STRING; 267608.RSc2817; -.
DR EnsemblBacteria; CAD16524; CAD16524; RSc2817.
DR GeneID; 60502317; -.
DR KEGG; rso:RSc2817; -.
DR PATRIC; fig|267608.8.peg.2868; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_087195_1_0_4; -.
DR OMA; PLDCVIE; -.
DR Proteomes; UP000001436; Chromosome.
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..238
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_0000057020"
FT DOMAIN 6..149
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT REGION 161..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..59
FT /note="Nudix box"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 27745 MW; EA48DEB48DA0674A CRC64;
MLDREGFRPN VGIILINARN EVFWGKRIGE HSWQFPQGGI KYGETPEQAM YRELHEEVGL
LPEHVRIVGR TRDWLRYEVP DKFIRREIRG HYRGQKQIWF LLRMVGRDCD IQLRATEHPE
FDAWRWSQYW VPLDAVIEFK REVYQMALSE LSRFVQRSHR APLSPYGRGG PHRERDGRDN
RAGGQAGRND QNTRGQRQPP TLMVTTSTVI VETVITSRPA AQPIDSSNPD DTPSKDSL
