RPPH_BURMA
ID RPPH_BURMA Reviewed; 216 AA.
AC Q62GV7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=BMA2518;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000010; AAU50102.1; -; Genomic_DNA.
DR RefSeq; WP_004194263.1; NC_006348.1.
DR RefSeq; YP_104064.1; NC_006348.1.
DR AlphaFoldDB; Q62GV7; -.
DR SMR; Q62GV7; -.
DR STRING; 243160.BMA2518; -.
DR EnsemblBacteria; AAU50102; AAU50102; BMA2518.
DR GeneID; 56594253; -.
DR KEGG; bma:BMA2518; -.
DR PATRIC; fig|243160.12.peg.2597; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_087195_0_1_4; -.
DR OMA; PCVGIML; -.
DR Proteomes; UP000006693; Chromosome 1.
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..216
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_0000231901"
FT DOMAIN 6..149
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT REGION 159..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..59
FT /note="Nudix box"
SQ SEQUENCE 216 AA; 25263 MW; BB9E37FD1C8BA662 CRC64;
MLDREGFRPN VGIILLNAHN EVFWGKRLRE HSWQFPQGGI KYGETPMQAM YRELHEETGL
LPEHVKIIGR TRDWLRYEVP DKFIKREVRG HYRGQKQIWF LLRMVGRDCD ICLRATDHPE
FDAWRWNEYW VPLDAVIEFK RDVYQLALTE LSRFLRRPAQ RTDKSRGPRA PRYPRVANGH
AASEAPAAID TSAVCSEVEP GANALDETPP RVSLRD