ID   RF2_THEM4               Reviewed;         369 AA.
AC   A6LN93;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=Tmel_1549;
OS   Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=391009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermosipho melanesiensis BI429.";
RL   Submitted (MAY-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; CP000716; ABR31394.1; -; Genomic_DNA.
DR   RefSeq; WP_012057753.1; NC_009616.1.
DR   AlphaFoldDB; A6LN93; -.
DR   SMR; A6LN93; -.
DR   STRING; 391009.Tmel_1549; -.
DR   PRIDE; A6LN93; -.
DR   EnsemblBacteria; ABR31394; ABR31394; Tmel_1549.
DR   KEGG; tme:Tmel_1549; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_0; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000001110; 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..369
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000005018"
FT   MOD_RES         249
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   369 AA;  43069 MW;  F6D133ECA603EDD0 CRC64;
     MIDYELKQRI DEVKKRYEDI VKVFHPEDKK KELEELEKLM GESDFWNDQK RAKEISQNAQ
     RIRKIIDDMV DIENKLEDLE AGLELLEEDA TFLDTIKQLI DDIERKVKTF ELELILNEKF
     DSSNAYLSIH PGAGGTESQD WASMLLRMYM RWAERRGFDV QIVDYQPGEE AGIKSAMLYI
     KGEYVYGYLK YERGVHRLVR ISPFDANKRR HTSFASVNVM PEIEDDIDVE INPEDLRIDT
     YRASGAGGQY VNKTESAVRI THIPTGIVVT CQTERSQLQN KETAMKVLKA RLYQLELEKR
     QKQLEEIQGE LKDISWGNQI RSYVFQPYTM VKDHRTNVET GNIDAVMDGD IDIFIESELI
     FFAKSKNKK