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Database: UniProt
Entry: Q479A2
LinkDB: Q479A2
Original site: Q479A2 
ID   RNPH_DECAR              Reviewed;         238 AA.
AC   Q479A2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   01-OCT-2014, entry version 53.
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=Daro_3851;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str.
RT   RCB: indications of a surprisingly complex life-style and cryptic
RT   anaerobic pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
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. {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   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00564}.
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DR   EMBL; CP000089; AAZ48579.1; -; Genomic_DNA.
DR   RefSeq; YP_287049.1; NC_007298.1.
DR   ProteinModelPortal; Q479A2; -.
DR   SMR; Q479A2; 2-237.
DR   STRING; 159087.Daro_3851; -.
DR   EnsemblBacteria; AAZ48579; AAZ48579; Daro_3851.
DR   GeneID; 3568022; -.
DR   KEGG; dar:Daro_3851; -.
DR   PATRIC; 21606396; VBIDecAro89105_3838.
DR   eggNOG; COG0689; -.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; PLKQMIA; -.
DR   OrthoDB; EOG6CZQQP; -.
DR   BioCyc; DARO159087:GI5B-3929-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; Reference proteome;
KW   Transferase; tRNA processing.
FT   CHAIN         1    238       Ribonuclease PH.
FT                                /FTId=PRO_1000024800.
SQ   SEQUENCE   238 AA;  25696 MW;  7B447A21130B4C1E CRC64;
     MRPSQRQPDQ LRTVRITRNF TRHAEGSVLI EMGDTRVLCT ASVEENVPPF LRGKGQGWVT
     AEYGMLPRAT HTRSSREAAK GKQTGRTQEI QRLIGRALRS VIDLKALGER QITLDCDVLQ
     ADGGTRCASI TGAWVALYEA CDKLVQAGKL PANPVRDHVA AISVGIYKGA PVLDLDYPED
     SDCDTDMNVV MTGAGGIVEI QGTAEGEPFT REQMSVLVDL ATLGVRHLVA AQQSALAA
//
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