RPPH_SHESH
ID RPPH_SHESH Reviewed; 172 AA.
AC A8FSC0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Ssed_1132;
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000821; ABV35743.1; -; Genomic_DNA.
DR RefSeq; WP_012141479.1; NC_009831.1.
DR AlphaFoldDB; A8FSC0; -.
DR SMR; A8FSC0; -.
DR STRING; 425104.Ssed_1132; -.
DR EnsemblBacteria; ABV35743; ABV35743; Ssed_1132.
DR KEGG; sse:Ssed_1132; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_087195_3_1_6; -.
DR OMA; PCVGIML; -.
DR OrthoDB; 1345242at2; -.
DR Proteomes; UP000002015; 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..172
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_1000078979"
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 172 AA; 20623 MW; 08FF386694A6BA2B CRC64;
MIDSDGFRAN VGIIICNRFG QVMWARRFGQ HSWQFPQGGV DEGETPEEAM FRELYEEVGL
RPEHVQILTS TRSWLRYRLP KRLIRQDSKP VCIGQKQKWF LLQLKSNESA IDLNACGHPE
FDDWRWVSYW YPVRQVVSFK RDVYRKVMKE FAPTALPFQT REHHHSRRGR RR