RF2_ACIC1
ID RF2_ACIC1 Reviewed; 369 AA.
AC A0LVP4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Acel_1732;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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; CP000481; ABK53504.1; -; Genomic_DNA.
DR RefSeq; WP_011720567.1; NC_008578.1.
DR AlphaFoldDB; A0LVP4; -.
DR SMR; A0LVP4; -.
DR STRING; 351607.Acel_1732; -.
DR EnsemblBacteria; ABK53504; ABK53504; Acel_1732.
DR KEGG; ace:Acel_1732; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_036856_6_0_11; -.
DR OMA; YVFHPYQ; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000008221; 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_1000004969"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 369 AA; 41612 MW; 4DDDF39AE947D02E CRC64;
MQPQDPHEHL KDLDTRLAGI EQVLDLPAMR REAADLERQA ADPGLWNDPE NAQRVTSRLS
FLQAEIRRVE GLRKRLDDVM VLFELAEAEN DEPTRTEALA EMAALQKAID DLEVRTLLSG
EYDAREALVT INSQAGGVDA ADWAQMLLRM YLRWAERHGY PTEILDTSYA EEAGIKSATF
IVHAPFTYGL LAAEHGTHRL VRISPFDNQA RRQTSFAGVD VVPVVEKTDH IDIPEDEIRV
DVFRSSGPGG QGVNTTDSAV RITHLPTGIV VTCQNERSQL QNRATAMMVL QARLLERRRQ
EEAAKLAALR GETTTSWGTQ IRNYVLHPYQ LVKDLRTEVE TSNTAGVLDG EIDEFIDAGV
RWRRQRERR