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Database: UniProt/TrEMBL
Entry: F2K047_MARM1
LinkDB: F2K047_MARM1
Original site: F2K047_MARM1 
ID   F2K047_MARM1            Unreviewed;       241 AA.
AC   F2K047;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   14-MAY-2014, entry version 13.
DE   RecName: Full=Ribonuclease PH;
DE            Short=RNase PH;
DE            EC=2.7.7.56;
DE   AltName: Full=tRNA nucleotidyltransferase;
GN   Name=rph; OrderedLocusNames=Marme_4053;
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028
OS   / MMB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Marinomonas.
OX   NCBI_TaxID=717774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Lucas-Elio P., Johnston A.W.B., Sanchez-Amat A., Woyke T.;
RT   "Complete sequence of Marinomonas mediterranea MMB-1.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorolytic exoribonuclease that removes nucleotide
CC       residues following the -CCA terminus of tRNA and adds nucleotides
CC       to the ends of RNA molecules by using nucleoside diphosphates as
CC       substrates (By similarity).
CC   -!- CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside
CC       diphosphate.
CC   -!- SIMILARITY: Belongs to the RNase PH family.
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DR   EMBL; CP002583; ADZ93261.1; -; Genomic_DNA.
DR   RefSeq; YP_004315097.1; NC_015276.1.
DR   EnsemblBacteria; ADZ93261; ADZ93261; Marme_4053.
DR   GeneID; 10338180; -.
DR   KEGG; mme:Marme_4053; -.
DR   PATRIC; 47233173; VBIMarMed159599_4181.
DR   KO; K00989; -.
DR   OMA; PLKQMIA; -.
DR   BioCyc; MMED717774:GCPW-4156-MONOMER; -.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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; IPR027408; PNPase/RNase_PH_dom.
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   Complete proteome; Nucleotidyltransferase; Transferase;
KW   tRNA processing.
SQ   SEQUENCE   241 AA;  26083 MW;  00F4D19DE11AC356 CRC64;
     MRPSGRAADQ LRPMKFTRNF TKHAEGSVLI ECGDTKVICT ATVVSGVPRF LKGKGQGWIT
     AEYGMLPRST HSRMDREAAR GKQGGRTVEI QRLIGRSLRA AIDLKKLGEN TITIDCDVIQ
     ADGGTRTASI SGGFVALADA VKTLVEQKKL KENPIVSQIA AISVGVYKGT PVLDLDYPED
     SNAETDMNVI MNDKGGFIEI QGTAEGAAFG DEQMMGMLSV ARKGINEIME MQRQVLFGDD
     E
//
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