RF1_ACIC1
ID RF1_ACIC1 Reviewed; 364 AA.
AC A0LSK4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=Acel_0641;
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 1 directs the termination of
CC translation in response to the peptide chain termination codons UAG and
CC UAA. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR EMBL; CP000481; ABK52414.1; -; Genomic_DNA.
DR RefSeq; WP_011719477.1; NC_008578.1.
DR AlphaFoldDB; A0LSK4; -.
DR SMR; A0LSK4; -.
DR STRING; 351607.Acel_0641; -.
DR EnsemblBacteria; ABK52414; ABK52414; Acel_0641.
DR KEGG; ace:Acel_0641; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_11; -.
DR OMA; ISDHRVG; -.
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_00093; Rel_fac_1; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004373; RF-1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR TIGRFAMs; TIGR00019; prfA; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT CHAIN 1..364
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000004852"
FT MOD_RES 230
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 364 AA; 40237 MW; CE637944BB35966B CRC64;
MFEAVEEVLR EYADLERRLA DPAVHADPRT ARTLGRRYAQ LGPIVEAYRR WKALDADVAA
AHELAAADPA FRAEIPALEA EREAVAERLR SLLAPADPND GKDVIMQIKA GEGGEESALF
AGDLLRMYLR YAERRGWKTE ILDATESDLG GYKDVTVAIR ADGSEGAWSR LKFEGGVHRV
QRVPVTESQG RIHTSAVGVL VMPEAEEVDV QIDPNDLRID VFRSSGPGGQ SVNTTDSAVR
ITHLPTGIVV SCQNEKSQLQ NKETALRILR SRLLALAQEE AEAQAAAQRR SQVRTVDRSE
RIRTYNFPEN RISDHRVNYK AYNLDQVLDG DLDGVIQALV DADAAARLAA AEQDPTRPVL
SRQR