RF1_THEVB
ID RF1_THEVB Reviewed; 364 AA.
AC Q8DMG9;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=tlr0148;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000039; BAC07701.1; -; Genomic_DNA.
DR RefSeq; NP_680939.1; NC_004113.1.
DR RefSeq; WP_011056003.1; NC_004113.1.
DR AlphaFoldDB; Q8DMG9; -.
DR SMR; Q8DMG9; -.
DR STRING; 197221.22293869; -.
DR EnsemblBacteria; BAC07701; BAC07701; BAC07701.
DR KEGG; tel:tlr0148; -.
DR PATRIC; fig|197221.4.peg.154; -.
DR eggNOG; COG0216; Bacteria.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000000440; 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_0000177758"
FT MOD_RES 239
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 364 AA; 41197 MW; 768DE02F42CB7ECB CRC64;
MAEAYLLEKL RTVEQTFTEL TRRLADPDVA VNPTEFQKVA RSRAALEETV NAYHEWQSLN
QQLVDARQLH KEAANEPELR QMAEEEIAHL SHRIAQLEER LKILLLPRDP NDEKNIMLEI
RAGAGGDEAG IWAGDLVRMY SRYAKTQGWQ VTLVSESLAE MGGFKEAILE IKGDRVYSKL
KYESGVHRVQ RVPATEASGR IHTSTATVAV MPEVDEVEVE IDPKDIELTT ARSGGAGGQN
VNKVETAVDL YHKPTGIRIF CTEERSQLKN KERAFQILRA KLYEIKLREQ QEAITSMRRS
QVGTGDRSEK IRTYNYKDDR VTDHRLGQNF SLSSVLEGDL EPIIQACISR DQQEQLAQLA
AEQA