RPPH_HELPG
ID RPPH_HELPG Reviewed; 155 AA.
AC B5Z8M3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=HPG27_1172;
OS Helicobacter pylori (strain G27).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27;
RX PubMed=18952803; DOI=10.1128/jb.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI27922.1; -; Genomic_DNA.
DR RefSeq; WP_000902584.1; NC_011333.1.
DR AlphaFoldDB; B5Z8M3; -.
DR SMR; B5Z8M3; -.
DR EnsemblBacteria; ACI27922; ACI27922; HPG27_1172.
DR KEGG; hpg:HPG27_1172; -.
DR HOGENOM; CLU_087195_3_0_7; -.
DR OMA; PCVGIML; -.
DR OrthoDB; 1345242at2; -.
DR Proteomes; UP000001735; 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.
FT CHAIN 1..155
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_1000115281"
FT DOMAIN 5..147
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT MOTIF 42..63
FT /note="Nudix box"
SQ SEQUENCE 155 AA; 18492 MW; 6B0C88076801ECA5 CRC64;
MLHKKYRPNV AAIIMSPDYP NTCEVFIAER IDIEGAWQFP QGGIDEGETP LEALHRELLE
EIGTNEIEIL AQYPRWIAYD FPSNMEHKFY AFDGQKQRYF LVRLKHANNI DLNKHTPEFR
AYQFIHLKDL LKKIVPFKRQ VYRQVIAYFK RDGYL