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RF2_ALIF1
ID   RF2_ALIF1               Reviewed;         365 AA.
AC   Q5E7P9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 95.
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}; OrderedLocusNames=VF_0452;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC   -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC       translation in response to the peptide chain termination codons UGA and
CC       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 factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00094}.
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DR   EMBL; CP000020; AAW84947.2; -; Genomic_DNA.
DR   RefSeq; WP_011261232.1; NC_006840.2.
DR   RefSeq; YP_203835.2; NC_006840.2.
DR   AlphaFoldDB; Q5E7P9; -.
DR   SMR; Q5E7P9; -.
DR   STRING; 312309.VF_0452; -.
DR   EnsemblBacteria; AAW84947; AAW84947; VF_0452.
DR   GeneID; 64241887; -.
DR   KEGG; vfi:VF_0452; -.
DR   PATRIC; fig|312309.11.peg.442; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_220733_1_0_6; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00094; Rel_fac_2; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004374; PrfB.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00020; prfB; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..365
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000093561"
FT   MOD_RES         252
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   365 AA;  41291 MW;  316E86B9B13BE5A2 CRC64;
     MFEINPIKNR LQDVSERTNI LRGYLDYDAK KERLEEVNAE LEQPDVWNEP ERAQALGKER
     ASLEAVVETI DLLDQGVEDV DGLLELAVEE EDQETFDEIE PELAELEAKL AKLEFRRMFS
     GDHDASDCYI DLQSGSGGTE AQDWTSMMLR MYLRWAEAKG FKVEVIEVSE GEVAGLKGAT
     VRIAGEYAYG WLRTETGVHR LVRKSPFDSS GRRHTSFASA FIYPEIDDNI QIDINPSDLR
     IDVYRASGAG GQHVNTTESA VRITHVPTNI VVQCQNDRSQ HKNKDQAMKQ LRAKLFEYEL
     QKQNAEKQAN EDAKSDIGWG SQIRSYVLDD SRIKDLRTGI ENRNTQAVLD GDLDKFIEAS
     LKSGL
 
 
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