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Database: UniProt
Entry: Q720J1
LinkDB: Q720J1
Original site: Q720J1 
ID   RNPH_LISMF              Reviewed;         248 AA.
AC   Q720J1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-APR-2018, entry version 77.
DE   RecName: Full=Ribonuclease PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            Short=RNase PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            EC=2.7.7.56 {ECO:0000255|HAMAP-Rule:MF_00564};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_00564};
GN   Name=rph {ECO:0000255|HAMAP-Rule:MF_00564};
GN   OrderedLocusNames=LMOf2365_1247;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Phosphorolytic 3'-5' exoribonuclease that plays an
CC       important role in tRNA 3'-end maturation. Removes nucleotide
CC       residues following the 3'-CCA terminus of tRNAs; can also add
CC       nucleotides to the ends of RNA molecules by using nucleoside
CC       diphosphates as substrates, but this may not be physiologically
CC       important. Probably plays a role in initiation of 16S rRNA
CC       degradation (leading to ribosome degradation) during starvation.
CC       {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside
CC       diphosphate. {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC       {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00564}.
DR   EMBL; AE017262; AAT04023.1; -; Genomic_DNA.
DR   RefSeq; WP_003726032.1; NC_002973.6.
DR   ProteinModelPortal; Q720J1; -.
DR   SMR; Q720J1; -.
DR   EnsemblBacteria; AAT04023; AAT04023; LMOf2365_1247.
DR   KEGG; lmf:LMOf2365_1247; -.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; KGKGQGW; -.
DR   GO; GO:0004540; F:ribonuclease activity; ISS:JCVI.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; ISS:JCVI.
DR   CDD; cd11362; RNase_PH_bact; 1.
DR   Gene3D; 3.30.230.70; -; 1.
DR   HAMAP; MF_00564; RNase_PH; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR002381; RNase_PH_bac-type.
DR   InterPro; IPR018336; RNase_PH_CS.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55666; SSF55666; 1.
DR   TIGRFAMs; TIGR01966; RNasePH; 1.
DR   PROSITE; PS01277; RIBONUCLEASE_PH; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase; RNA-binding; rRNA processing; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN         1    248       Ribonuclease PH.
FT                                /FTId=PRO_0000139905.
FT   REGION      124    126       Phosphate (substrate) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00564}.
FT   BINDING      86     86       Phosphate (substrate) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00564}.
SQ   SEQUENCE   248 AA;  26670 MW;  3B3F8DF5448CA80B CRC64;
     MRVDGRESNA LRNIEVTPDY LMHPEGSVLI ASGNTKVICS ASVETKVPPF MRGEGRGWIS
     AEYSMLPRAT NTRNIRESSK GKVTGRTMEI QRLIGRALRA VVDLDALGER TIWLDCDVIQ
     ADGGTRTASI TGAFIAMVMA IAKLDEAVPF AKFPVKDFLA ATSVGVLEEG GTVLDLNYVE
     DSAAQVDMNI IMTGSGAFVE LQGTGEEATF SETELAELIA LGKKGISELI EIQKETLGDK
     VTARIKGE
//
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