RF1_METSB
ID RF1_METSB Reviewed; 360 AA.
AC B8EI32;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=Msil_1564;
OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS 13906 / BL2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=395965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2;
RX PubMed=20472789; DOI=10.1128/jb.00506-10;
RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT "Complete genome sequence of the aerobic facultative methanotroph
RT Methylocella silvestris BL2.";
RL J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK50514.1; -; Genomic_DNA.
DR RefSeq; WP_012590584.1; NC_011666.1.
DR AlphaFoldDB; B8EI32; -.
DR SMR; B8EI32; -.
DR STRING; 395965.Msil_1564; -.
DR EnsemblBacteria; ACK50514; ACK50514; Msil_1564.
DR KEGG; msl:Msil_1564; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_5; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000002257; 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..360
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000193497"
FT REGION 283..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 39869 MW; 6F4E35C96125C87F CRC64;
MLPQEKLDLI LRRYDEVSAR LNEAVEPALY VQLSREFAGL EQVAAAIRDY RSQMQEVEGL
AAMLADPTTD SEMRGLAEEE LRDAKERLEA LEHQLKIALL PKDAADERSA ILEVRAGTGG
DEAALFAGDL FRMYQRYAES KGWSVEIISA NEGAAGGFKE IIAEIAGRGV FAKLKFESGA
HRVQRVPDTE TQGRIHTSAA TVAVLPEAQE VDVEINEADL KIDTMRAQGA GGQHVNKTES
AIRITHIPTG TIVFVQDERS QHKNRARAMA LLRSRIYDEQ RQKLDAERAA DRRSQVGSGD
RSERIRTYNF PQGRVTDHRI NLTLYKLDKV ITGEALDEVI DALTTHHQAA LLADSESGGL