(data stored in ACNUC7421 zone)

SWISSPROT: RNPH_EDWI9

ID   RNPH_EDWI9              Reviewed;         238 AA.
AC   C5B9C9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 43.
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=NT01EI_0049;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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. {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}.
DR   EMBL; CP001600; ACR67309.1; -; Genomic_DNA.
DR   RefSeq; WP_015869533.1; NC_012779.2.
DR   SMR; C5B9C9; -.
DR   STRING; 634503.NT01EI_0049; -.
DR   EnsemblBacteria; ACR67309; ACR67309; NT01EI_0049.
DR   GeneID; 7959768; -.
DR   KEGG; eic:NT01EI_0049; -.
DR   PATRIC; fig|634503.3.peg.42; -.
DR   eggNOG; ENOG4105ED0; Bacteria.
DR   eggNOG; COG0689; LUCA.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; KGKGQGW; -.
DR   OrthoDB; POG091H03ML; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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; 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;
DR   PRODOM; C5B9C9.
DR   SWISS-2DPAGE; C5B9C9.
KW   Complete proteome; Nucleotidyltransferase; Reference proteome;
KW   Transferase; tRNA processing.
FT   CHAIN         1    238       Ribonuclease PH.
FT                                /FTId=PRO_1000212062.
SQ   SEQUENCE   238 AA;  25237 MW;  A52720BABDF8E66F CRC64;
     MRPEGRAAGQ IRPLRLTRHY TKHAEGSVLV EFGDTKVLCT ASVDEGVPRF LKGQGQGWVT
     AEYGMLPRST HSRMAREAAK GKQGGRTMEI QRLIARSLRA AVDLKKLGEF TITLDCDVIQ
     ADGGTRTASI TGACVALADA LGALVAAGKL KESPLKGMVA AVSVGIVAGG AVCDLEYVED
     SAAETDMNVV MMEDGRMIEV QGTAEGEPFS HEELLTLLAL ARDGIGQIIQ AQKTALEQ
//

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