ID   RNPH_COLP3              Reviewed;         237 AA.
AC   Q48AN3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Ribonuclease PH;
DE            Short=RNase PH;
DE            EC=2.7.7.56;
DE   AltName: Full=tRNA nucleotidyltransferase;
GN   Name=rph; OrderedLocusNames=CPS_0112;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ24239.1; -; Genomic_DNA.
DR   RefSeq; YP_266880.1; -.
DR   SMR; Q48AN3; 2-237.
DR   GeneID; 3519509; -.
DR   GenomeReviews; CP000083_GR; CPS_0112.
DR   KEGG; cps:CPS_0112; -.
DR   NMPDR; fig|167879.3.peg.114; -.
DR   TIGR; CPS_0112; -.
DR   HOGENOM; Q48AN3; -.
DR   OMA; Q48AN3; YAMLPRA.
DR   BioCyc; CPSY167879:CPS_0112-MON; -.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
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; -; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR018336; Ribonuclease-PH_CS.
DR   InterPro; IPR002381; RNase_PH_bac-type.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 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    237       Ribonuclease PH.
FT                                /FTId=PRO_1000024798.
SQ   SEQUENCE   237 AA;  25588 MW;  3541AD3F3B5E510D CRC64;
     MRPSGRTLGQ IRPVTITRQF TTHAEGSVLI EFGDTKVICT ATVEVGVPRF LKGQGKGWVT
     AEYGMLPRST HTRMRREAAS GKQSGRTLEI SRLIARALRA AVDLKALGEN TISVDCDVIQ
     ADGGTRTAAI TGACVALVDA LNYMRAKDII KTNPLKHMIA AVSVGIYKGE PVADLDYPED
     SAADTDMNVV MTDTGKLIEV QGTAEEEPFS FEEMQAMLEL AKNGINELFD LQKAALS
//