ID   RF2_SALAI               Reviewed;         373 AA.
AC   A8M3R1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Sare_0917;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
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., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-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; CP000850; ABV96834.1; -; Genomic_DNA.
DR   RefSeq; WP_012181144.1; NC_009953.1.
DR   AlphaFoldDB; A8M3R1; -.
DR   SMR; A8M3R1; -.
DR   STRING; 391037.Sare_0917; -.
DR   EnsemblBacteria; ABV96834; ABV96834; Sare_0917.
DR   GeneID; 5703810; -.
DR   KEGG; saq:Sare_0917; -.
DR   PATRIC; fig|391037.6.peg.936; -.
DR   eggNOG; COG1186; 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..373
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000075528"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   373 AA;  41417 MW;  8EA4097C2AA56AB1 CRC64;
     MTDADFAEQL KDLDTTLRNI ESVLDIDRLR ADKARLEEAA SAPDLWDDQA RAQQVTSQLS
     YVNGEITKLT DLRSRLDDTQ VLLELAEAES DPGVLTEVAA EITGLAKSID EMEVRTLLSG
     EYDSREALVA IRAGAGGVDA ADFAEMLLRM YLRWAERHGY PTEVYETSYA EEAGLKSATF
     TVKVPYAYGT LSVESGTHRL VRISPFDNQG RRQTSFAGVE VLPVVEQTDH IDIPENEMRT
     DVYRSSGPGG QSVNTTDSAV RITHIPTGIV VTCQNEKSQL QNKASALRVL QARLLERKRQ
     EEQAKLQGLK TDAAGSWGDQ MRSYVLHPYQ MVKDLRTEQE TGSPSSVFDG ELDAFIEAGI
     RWRKQQQLSG DNV