RF1_THET8
ID RF1_THET8 Reviewed; 354 AA.
AC P96077; Q5SGZ0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Peptide chain release factor 1;
DE Short=RF-1;
GN Name=prfA {ECO:0000303|PubMed:9258437}; OrderedLocusNames=TTHA1940;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=9258437; DOI=10.1016/s0300-9084(97)83516-x;
RA Ito K., Nakamura Y.;
RT "Cloning and overexpression of polypeptide release factor 1 of Thermus
RT thermophilus.";
RL Biochimie 79:287-292(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:4V4R}
RP X-RAY CRYSTALLOGRAPHY (5.90 ANGSTROMS) OF 28-378 IN COMPLEX WITH 70S
RP RIBOSOME, FUNCTION, AND SUBUNIT.
RX PubMed=16377566; DOI=10.1016/j.cell.2005.09.039;
RA Petry S., Brodersen D.E., Murphy F.V., Dunham C.M., Selmer M., Tarry M.J.,
RA Kelley A.C., Ramakrishnan V.;
RT "Crystal structures of the ribosome in complex with release factors RF1 and
RT RF2 bound to a cognate stop codon.";
RL Cell 123:1255-1266(2005).
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 (Probable). {ECO:0000305|PubMed:16377566,
CC ECO:0000305|PubMed:9258437}.
CC -!- SUBUNIT: Interacts with the ribosome (PubMed:16377566).
CC {ECO:0000269|PubMed:16377566}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
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DR EMBL; D87366; BAA13349.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71763.1; -; Genomic_DNA.
DR RefSeq; WP_011173949.1; NC_006461.1.
DR RefSeq; YP_145206.1; NC_006461.1.
DR PDB; 4V4R; X-ray; 5.90 A; AY=1-354.
DR PDBsum; 4V4R; -.
DR AlphaFoldDB; P96077; -.
DR SMR; P96077; -.
DR STRING; 300852.55773322; -.
DR EnsemblBacteria; BAD71763; BAD71763; BAD71763.
DR GeneID; 3169506; -.
DR KEGG; ttj:TTHA1940; -.
DR PATRIC; fig|300852.9.peg.1911; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_0; -.
DR OMA; ISDHRVG; -.
DR PhylomeDB; P96077; -.
DR EvolutionaryTrace; P96077; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methylation; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..354
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177762"
FT MOD_RES 230
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 40093 MW; 49868D246BB3339E CRC64;
MLDKLDRLEE EYRELEALLS DPEVLKDKGR YQSLSRRYAE MGEVIGLIRE YRKVLEDLEQ
AESLLDDPEL KEMAKAEREA LLARKEALEK ELERHLLPKD PMDERDAIVE IRAGTGGEEA
ALFARDLFNM YLRFAEEMGF ETEVLDSHPT DLGGFSKVVF EVRGPGAYGT FKYESGVHRV
QRVPVTETQG RIHTSTATVA VLPKAEEEDF ALNMDEIRID VMRASGPGGQ GVNTTDSAVR
VVHLPTGIMV TCQDSRSQIK NREKALMILR SRLLEMKRAE EAERLRKTRL AQIGTGERSE
KIRTYNFPQS RVTDHRIGFT THDLEGVLSG HLTPILEALK RADQERQLAA LAEG