RF2_CORDI
ID RF2_CORDI Reviewed; 369 AA.
AC Q6NIM2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=DIP0746;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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; BX248356; CAE49268.1; -; Genomic_DNA.
DR RefSeq; WP_010934526.1; NC_002935.2.
DR AlphaFoldDB; Q6NIM2; -.
DR SMR; Q6NIM2; -.
DR STRING; 257309.DIP0746; -.
DR EnsemblBacteria; CAE49268; CAE49268; DIP0746.
DR GeneID; 29422103; -.
DR KEGG; cdi:DIP0746; -.
DR HOGENOM; CLU_036856_6_0_11; -.
DR OMA; YVFHPYQ; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000002198; 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..369
FT /note="Peptide chain release factor 2"
FT /id="PRO_0000166814"
FT MOD_RES 249
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 369 AA; 41329 MW; 94C4E84991EE4F55 CRC64;
MRPETQSAVT QLDSTLTTIE KVMNPEDLES RVRELEQQAS DPTLWDDPDT AQKVTTELSS
VQAKLKKLST LRQRIDDLPV MYELADEEGE DALALADEEL AELTADVEAL EVKTMLSGEY
DSREAVINIR SGAGGVDAAD WAEMLMRMYI RWAEKNDHKV DIYDISYAEE AGIKSATFVV
HGEYMYGQLS VEQGAHRLVR ISPFDNQGRR QTSFAEIEVL PVVEQTDHID IPDSEVRVDV
YRSSGPGGQS VNTTDSAVRL THIPTGIVVT CQNEKSQIQN KASAMRVLQA KLLERKRQEE
RAELDALGAG GNASWGNQMR SYVLHPYQMV KDLRTNYEVN DPQKVLDGDI DGLLEAGIRW
RMAEQQGQN