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RF2_CAUSK
ID   RF2_CAUSK               Reviewed;         367 AA.
AC   B0SXB7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Caul_2575;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31;
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., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) 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; CP000927; ABZ71702.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0SXB7; -.
DR   SMR; B0SXB7; -.
DR   STRING; 366602.Caul_2575; -.
DR   PRIDE; B0SXB7; -.
DR   EnsemblBacteria; ABZ71702; ABZ71702; Caul_2575.
DR   KEGG; cak:Caul_2575; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_5; -.
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..367
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000075523"
FT   MOD_RES         247
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   367 AA;  40252 MW;  D20C7ED7FE074194 CRC64;
     MSRPQRLTSS SPWDCSGGVF DWDAALRKLD ELNARVEDPT LWDRPSEAQA VSRDRASLAA
     RVGAVQELEG GLKDALEYAE LADMEGDEAL LEDARAQLKD LKDRAGRAEL EALLSGEADG
     NDCYVEINSG AGGTESCDWA GMLLRMYSRW ANAHKMSVEL VEETAGDQVG IKSATLLVKG
     ANAYGWLKTE AGVHRLVRIS PYDAAAKRHT SFASAWVYPV VDDTIEIDIN PSDVRTDTYR
     ASGAGGQHIN KTDSAVRLTH IPTGIAVACQ AGRSQHQNRE EAWKMLRARL YEAELQRREA
     AQQALEDQKT DIGWGHQIRS YVLQPYQMVK DLRTNVETSD TQGVLDGDLD AFMGASLAQR
     VGATRDA
 
 
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