ID   RF2_STRCO               Reviewed;         368 AA.
AC   Q53915; Q9L1S3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=SCO2972; ORFNames=SCE59.31c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=7545157; DOI=10.1128/jb.177.18.5342-5345.1995;
RA   Ogawara H., Urabe H., Ohtaki R., Nakamura Y.;
RT   "Properties of peptide chain release factor 2 from Streptomyces coelicolor
RT   A3(2): conserved primary structure but no frameshift regulation.";
RL   J. Bacteriol. 177:5342-5345(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; D86821; BAA13170.1; -; Genomic_DNA.
DR   EMBL; AL939114; CAB72218.1; -; Genomic_DNA.
DR   RefSeq; NP_627196.1; NC_003888.3.
DR   RefSeq; WP_003975840.1; NZ_VNID01000010.1.
DR   AlphaFoldDB; Q53915; -.
DR   SMR; Q53915; -.
DR   STRING; 100226.SCO2972; -.
DR   GeneID; 1098405; -.
DR   KEGG; sco:SCO2972; -.
DR   PATRIC; fig|100226.15.peg.3030; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_11; -.
DR   InParanoid; Q53915; -.
DR   OMA; YVFHPYQ; -.
DR   PhylomeDB; Q53915; -.
DR   Proteomes; UP000001973; 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..368
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166852"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        320..321
FT                   /note="QM -> RV (in Ref. 1; BAA13170)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  41085 MW;  278071BE1A26C493 CRC64;
     MAVVDVSEEL KSLSSTMESI EAVLDLDRLR ADIAVLEEQA AAPSLWDDPE AAQKITSKLS
     HLQAEVRKAE ALRGRIDDLG VLFEMAEEED DPDTRAEAES ELAAVRKALD EMEVRTLLSG
     EYDAREALVN IRAEAGGVDA ADFAEKLQRM YLRWAEQHGY KTEVYETSYA EEAGIKSTTF
     AVQSPYAYGT LSVEQGTHRL VRISPFDNQG RRQTSFAGVE ILPVVEQTDH IEIDESELRV
     DVYRSSGPGG QGVNTTDSAV RLTHIPTGIV VSCQNERSQI QNKATAMNVL QAKLLERRRQ
     EEQAKMDALK GDGGNSWGNQ MRSYVLHPYQ MVKDLRTEHE VGNPEAVFNG EIDGFLEAGI
     RWRKQREK