(data stored in ACNUC7421 zone)

SWISSPROT: RF2_PSEHT

ID   RF2_PSEHT               Reviewed;         365 AA.
AC   Q3ILD8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 80.
DE   RecName: Full=Peptide chain release factor 2 {ECO:0000255|HAMAP-Rule:MF_00094};
DE            Short=RF-2 {ECO:0000255|HAMAP-Rule:MF_00094};
GN   Name=prfB {ECO:0000255|HAMAP-Rule:MF_00094};
GN   OrderedLocusNames=PSHAa0517;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Peptide chain release factor 2 directs the termination
CC       of translation in response to the peptide chain termination codons
CC       UGA and UAA. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release
CC       factor family. {ECO:0000255|HAMAP-Rule:MF_00094}.
DR   EMBL; CR954246; CAI85607.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3ILD8; -.
DR   SMR; Q3ILD8; -.
DR   STRING; 326442.PSHAa0517; -.
DR   EnsemblBacteria; CAI85607; CAI85607; PSHAa0517.
DR   KEGG; pha:PSHAa0517; -.
DR   eggNOG; ENOG4105CG1; Bacteria.
DR   eggNOG; COG1186; LUCA.
DR   HOGENOM; HOG000074814; -.
DR   KO; K02836; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; POG091H027X; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:InterPro.
DR   HAMAP; MF_00094; Rel_fac_2; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I_II.
DR   InterPro; IPR004374; PrfB.
DR   InterPro; IPR020853; RF2_bac.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   TIGRFAMs; TIGR00020; prfB; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILD8.
DR   SWISS-2DPAGE; Q3ILD8.
KW   Complete proteome; Cytoplasm; Methylation; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    365       Peptide chain release factor 2.
FT                                /FTId=PRO_1000005009.
FT   MOD_RES     252    252       N5-methylglutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00094}.
SQ   SEQUENCE   365 AA;  40951 MW;  67FC393507845F84 CRC64;
     MFEVNPVINQ IKEIRERTEL LRGYLDYALK QERLEEVNAE LEDSAVWNEP ERAQALGREK
     SALEAVVETI DTLVTGTDDV EGLLELAVEA EDQETFDEAQ SELADLNEQL EALEFRRMFS
     GPHDSNDAYL DLQSGSGGTE AQDWCNILLR MYLRWGEAKG FKVELVEATG GDVAGIKGAT
     VRFVGEYAYG WLRTETGVHR LVRKSPFDSS GRRHTSFASA FVYPEVDDNI EIDMNPSDLR
     IDVYRASGAG GQHVNTTESA VRITHVPTNT VVQCQNERSQ HKNKAQAMKQ LKAKLFELEL
     QQQNAEKQTQ EDSKSDIGWG SQIRSYVLDD ARIKDLRTGV ESRNTQSVLD GNLDKFIEAS
     LKSGL
//

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