RF2_RHOOB
ID RF2_RHOOB Reviewed; 368 AA.
AC C1B1L3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=ROP_64610;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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; AP011115; BAH54708.1; -; Genomic_DNA.
DR RefSeq; WP_015890161.1; NC_012522.1.
DR AlphaFoldDB; C1B1L3; -.
DR SMR; C1B1L3; -.
DR STRING; 632772.ROP_64610; -.
DR EnsemblBacteria; BAH54708; BAH54708; ROP_64610.
DR KEGG; rop:ROP_64610; -.
DR PATRIC; fig|632772.20.peg.6744; -.
DR HOGENOM; CLU_036856_6_0_11; -.
DR OMA; YVFHPYQ; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000002212; 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..368
FT /note="Peptide chain release factor 2"
FT /id="PRO_1000193557"
FT MOD_RES 249
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 368 AA; 41435 MW; 374051AACE04A84C CRC64;
MHPDVSADLS ELDTTLRTVE SVLDVEELRR RIDELEHQAA DPELWNDQEH AQQVTSQLSH
SQAELRRVEE LRTRLDDMPV LYELAEDEGA EAIADADAER HSLREDIAAM EVKTMLSGEY
DERDALVNIR SGAGGVDAAD WAEMLMRMYI RWAEKHGYGV EVYDTSYAEE AGIKSATFAV
KAPYSYGTLS VEMGTHRLVR ISPFDNQGRR QTSFAEVEVL PVVETTDHID VNENDVRVDV
YRSSGPGGQS VNTTDSAVRL THIPTGIVVT CQNEKSQLQN KVSAMRVLQA KLLEVKRKEE
RAEMDALKGD GGSSWGNQMR SYVLHPYQMV KDLRTEYEVN NPSSVLDGDI DGFLESGIRW
RMRENQAS