RPPH_SHEPW
ID RPPH_SHEPW Reviewed; 173 AA.
AC B8CQL0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=swp_3796;
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877;
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ30476.1; -; Genomic_DNA.
DR RefSeq; WP_020913819.1; NC_011566.1.
DR AlphaFoldDB; B8CQL0; -.
DR SMR; B8CQL0; -.
DR STRING; 225849.swp_3796; -.
DR EnsemblBacteria; ACJ30476; ACJ30476; swp_3796.
DR KEGG; swp:swp_3796; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_087195_3_1_6; -.
DR OMA; PCVGIML; -.
DR OrthoDB; 1345242at2; -.
DR Proteomes; UP000000753; 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..173
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_1000119477"
FT DOMAIN 6..149
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT MOTIF 38..59
FT /note="Nudix box"
SQ SEQUENCE 173 AA; 20532 MW; 9018ED7BDD712D5E CRC64;
MIDSDGFRAN VGIIICNRSG QVMWARRFGQ HSWQFPQGGV DEGESAEEAM YRELYEEVGL
RPEHVQILAS TRSWLRYRLP KRLIRQDSKP VCIGQKQKWF LLQLKSSENA IDLNACGHPE
FDDWRWVSYW YPVRQVVSFK RDVYRKVMKE FAPTTLPLQV KESNHKRRGM RRN