RPPH_CAMJD
ID RPPH_CAMJD Reviewed; 156 AA.
AC A7H3U9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=JJD26997_1088;
OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS 269.97).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT isolated from human blood.";
RL Submitted (JUL-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; CP000768; ABS44569.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H3U9; -.
DR SMR; A7H3U9; -.
DR EnsemblBacteria; ABS44569; ABS44569; JJD26997_1088.
DR KEGG; cjd:JJD26997_1088; -.
DR HOGENOM; CLU_087195_3_0_7; -.
DR OMA; PCVGIML; -.
DR Proteomes; UP000002302; 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..156
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_1000078957"
FT DOMAIN 6..148
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT MOTIF 43..64
FT /note="Nudix box"
SQ SEQUENCE 156 AA; 18470 MW; D2C27C4D8E2680B9 CRC64;
MENEKNYRPN VAAIVLSSSY PFECKIFIAK RSDMDNIWQF PQGGIDKGES AKNALFRELK
EEIGTDEVEI IAEYPEWLSY DFPGKIVKKM YPYDGQIQKY FLVRLKHGAT ININTKHPEF
DDYQFVSVKQ IFEMINHFKK NIYVKVIKYF EEKGYI