ID   RF2_ROSDO               Reviewed;         374 AA.
AC   Q165J6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=RD1_2819;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG32347.1; -; Genomic_DNA.
DR   RefSeq; WP_011568963.1; NZ_FOOO01000002.1.
DR   AlphaFoldDB; Q165J6; -.
DR   SMR; Q165J6; -.
DR   STRING; 375451.RD1_2819; -.
DR   EnsemblBacteria; ABG32347; ABG32347; RD1_2819.
DR   KEGG; rde:RD1_2819; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_5; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000007029; 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; Reference proteome.
FT   CHAIN           1..374
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000057625"
FT   MOD_RES         250
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   374 AA;  41476 MW;  F4C04F22072769D4 CRC64;
     MRADVQNTIE KIQKSLDLLA QRLDVETAPY RLEEFNARVE DPTLWDDPDA AQKLMRERQM
     LVDAMATHDS IKQEMADNIE LIELGEMEDD ADVVSDAENA LRALEETAAK KELEALLDGE
     ADSNDTFLEV NAGAGGTESC DWASMLARMY VRWAEKKGYK VELQSMSDGD EAGIKSATYK
     ITGLNAYGWL KSESGVHRLV RISPFDSAAK RHTSFSSVWV YPVVDDNIDI EVNPADIRID
     TYRSSGAGGQ HVNTTDSAVR ITHHPTGIVV TSSEKSQHQN RDIAMKALKS RLYQLELDRR
     NAAINEAHEN KGDAGWGNQI RSYVLQPYQM VKDLRTNFET SDTKGVLDGD LDGFMAATLA
     LDASGKTRAE AQNG