ID   RF2_MYCGI               Reviewed;         372 AA.
AC   A4TDE5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Mflv_4451;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000656; ABP46920.1; -; Genomic_DNA.
DR   RefSeq; WP_011895294.1; NC_009338.1.
DR   AlphaFoldDB; A4TDE5; -.
DR   SMR; A4TDE5; -.
DR   STRING; 350054.Mflv_4451; -.
DR   EnsemblBacteria; ABP46920; ABP46920; Mflv_4451.
DR   KEGG; mgi:Mflv_4451; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_6_0_11; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
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..372
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000075526"
FT   MOD_RES         253
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   372 AA;  41471 MW;  F8BDB82492A2DA17 CRC64;
     MDPDRQSDIA ALDTTLTTVE RVVNVDGLRG RIQQLESDAS DPKLWDDQAR AQKVTSDLSH
     AQNELRRVEE LRSRLDDLPV LYELAAEEEG AGSSEAFAEA DAELAKLRED IAGMEVRTLL
     SGEYDEREAL VNIRSGAGGV DAADWAEMLM RMYIRWAEQH DYPVEVFDTS YAEEAGIKSA
     TFAVHAPYAY GNLSVEQGTH RLVRISPFDN QSRRQTSFAD VEVLPVVETT DHIDIPEGDV
     RVDVYRSSGP GGQSVNTTDS AVRLTHIPTG IVVTCQNEKS QLQNKVSAMR VLQAKLLERK
     RLEERAEMDA LKGDGGSSWG NQMRSYVLHP YQMVKDLRTE YEVGNPAAVL DGDIDGFLEA
     GIRWRNQKVD DE