ID   RF2_PARMW               Reviewed;         374 AA.
AC   Q7U3W6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=SYNW2311;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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; BX569695; CAE08826.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7U3W6; -.
DR   SMR; Q7U3W6; -.
DR   STRING; 84588.SYNW2311; -.
DR   EnsemblBacteria; CAE08826; CAE08826; SYNW2311.
DR   KEGG; syw:SYNW2311; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_220736_1_0_3; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000001422; Chromosome.
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.
FT   CHAIN           1..374
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000005017"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   374 AA;  41776 MW;  A1FFC8CE06FBB444 CRC64;
     MDLTDFKRDL SELTDRLGHA QDCLDVPALK ARQQDLEQLA AQPDFWDDQQ AAQKQMRRLD
     EVKAQLQQLA DWGGAVDDAK ATLELYELEP DEEMLTEAQE GLNQLRQGLD RWELERLLSG
     DYDKEGAVLT INAGAGGTDA QDWAQMLLRM YTRWAEDHGM KVTVDELSEG EEAGIKSCTI
     EVEGRYAYGY LRNEKGTHRL VRISPFNAND KRQTSFAGIE VMPKIDEEVD IDIPEKDLEV
     TTSRSGGAGG QNVNKVETAV RILHIPTGLA VRCTQERSQL QNKEKAMALL KAKLLVIAQE
     QRAAEIADIR GDIVEAAWGN QIRNYVFHPY QMVKDLRTSE ETNDVQAVMD GALDPFIDAS
     LRQGVDSPGA DADS