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