ID RNPH_XANAC Reviewed; 241 AA.
AC Q8PH63;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 01-MAY-2013, entry version 58.
DE RecName: Full=Ribonuclease PH;
DE Short=RNase PH;
DE EC=2.7.7.56;
DE AltName: Full=tRNA nucleotidyltransferase;
GN Name=rph; OrderedLocusNames=XAC3397;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing
RT host specificities.";
RL Nature 417:459-463(2002).
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; AE008923; AAM38240.1; -; Genomic_DNA.
DR RefSeq; NP_643704.1; NC_003919.1.
DR ProteinModelPortal; Q8PH63; -.
DR SMR; Q8PH63; 4-240.
DR STRING; 190486.XAC3397; -.
DR EnsemblBacteria; AAM38240; AAM38240; XAC3397.
DR GeneID; 1157468; -.
DR KEGG; xac:XAC3397; -.
DR PATRIC; 24058933; VBIXanAxo33670_3518.
DR eggNOG; COG0689; -.
DR HOGENOM; HOG000229516; -.
DR KO; K00989; -.
DR OMA; MLPRATG; -.
DR ProtClustDB; PRK00173; -.
DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:HAMAP.
DR GO; GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:HAMAP.
DR HAMAP; MF_00564; RNase_PH; 1; -.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
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; SSF55666; 3_ExoRNase; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 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.
FT CHAIN 1 241 Ribonuclease PH.
FT /FTId=PRO_0000139951.
SQ SEQUENCE 241 AA; 25926 MW; AE5EE552282210EA CRC64;
MTFSRPSGRT ADQLRPVRIE RSFTRHAEGS VLVSFGDTRV LCTASVENRV PGFLRGKGEG
WVTAEYGMLP RSTHTRSDRE AARGKQGGRT LEIQRLIGRA LRACVDRNAL GERTITLDCD
VLQADGGTRT AAITGAYVAL ADAVNLLIKR GDIKKHPLIG AVAAVSVGIY RGEPVLDLDY
PEDSDCDTDM NVVMNDGGGF IELQGTAEGH AFRRDELNAL LALAEKGMGE LFALQRAALA
G
//
