RPPH_RHOP2
ID RPPH_RHOP2 Reviewed; 167 AA.
AC Q2J3I9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, 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};
GN OrderedLocusNames=RPB_0260;
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) 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; CP000250; ABD04971.1; -; Genomic_DNA.
DR RefSeq; WP_011439161.1; NC_007778.1.
DR AlphaFoldDB; Q2J3I9; -.
DR SMR; Q2J3I9; -.
DR STRING; 316058.RPB_0260; -.
DR EnsemblBacteria; ABD04971; ABD04971; RPB_0260.
DR KEGG; rpb:RPB_0260; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_087195_3_0_5; -.
DR OMA; WAAAKRE; -.
DR OrthoDB; 1345242at2; -.
DR Proteomes; UP000008809; 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; 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 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..167
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_1000021980"
FT DOMAIN 8..158
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT MOTIF 47..68
FT /note="Nudix box"
SQ SEQUENCE 167 AA; 19390 MW; 28CDDD25F81D4A8B CRC64;
MARYEDLPYR TCVGMMLINR AGLVFIGRRA GGIEHVDDTH VWQMPQGGVD PGEDTWEAAK
RELYEETNVR SVEKIAEVPD WLIYDIPRTV AGRAWKGRYR GQRQKWFAIR FTGQDSEIDI
IAPPGHKSEF TSWRWEPMLN LPDLIVPFKR PVYERVVKEF SQLAIAV