RF1_THESM
ID RF1_THESM Reviewed; 415 AA.
AC C5ZZZ5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Peptide chain release factor subunit 1 {ECO:0000255|HAMAP-Rule:MF_00424};
DE AltName: Full=Translation termination factor aRF1 {ECO:0000255|HAMAP-Rule:MF_00424};
GN Name=prf1 {ECO:0000255|HAMAP-Rule:MF_00424}; OrderedLocusNames=TSIB_1927;
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12597 / MM 739;
RX PubMed=19447963; DOI=10.1128/aem.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(2009).
CC -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC (translation) in response to the termination codons UAA, UAG and UGA.
CC {ECO:0000255|HAMAP-Rule:MF_00424}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC {ECO:0000255|HAMAP-Rule:MF_00424}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00424}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_00424}.
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DR EMBL; CP001463; ACS90976.1; -; Genomic_DNA.
DR RefSeq; WP_015850192.1; NC_012883.1.
DR AlphaFoldDB; C5ZZZ5; -.
DR SMR; C5ZZZ5; -.
DR STRING; 604354.TSIB_1927; -.
DR PRIDE; C5ZZZ5; -.
DR EnsemblBacteria; ACS90976; ACS90976; TSIB_1927.
DR GeneID; 8096939; -.
DR KEGG; tsi:TSIB_1927; -.
DR eggNOG; arCOG01742; Archaea.
DR HOGENOM; CLU_035759_3_0_2; -.
DR OMA; GQEMEVV; -.
DR OrthoDB; 32191at2157; -.
DR Proteomes; UP000009079; 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 Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.420.60; -; 1.
DR Gene3D; 3.30.960.10; -; 1.
DR HAMAP; MF_00424; Rel_fact_arch_1; 1.
DR InterPro; IPR042226; eFR1_2_sf.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR024049; eRF1_1_sf.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR020918; Peptide_chain-rel_aRF1.
DR InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR PANTHER; PTHR10113; PTHR10113; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR SMART; SM01194; eRF1_1; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF55481; SSF55481; 1.
DR TIGRFAMs; TIGR03676; aRF1/eRF1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Protein biosynthesis; Reference proteome.
FT CHAIN 1..415
FT /note="Peptide chain release factor subunit 1"
FT /id="PRO_1000206060"
SQ SEQUENCE 415 AA; 47314 MW; 2FF6694C867CB69F CRC64;
MSHKSAEMYE LKKKVEELKK IRGRATELVS LYIPADYDLN KVMQQLREEY GTAQNIKSKT
TRKNVLGALE RAMQHLKLYR QTPETGLALF VGNVSEQEGV SDIRVFAIVP PEPLNVRLYR
CDQTFVTEPL EEMLRVKDAY GLITVEKNEA TIGILRGKKI EVIEDLTSNV PGKTRAGGQS
ARRYERIREQ EAHEFMKRIG EHASSVFLPL LEKDELKGII IGGPGPTKEE FVEGEYLHHE
LRKRILGVVD ISYHGEYGLR ELVEKASDIL REHEAVKERK LVQQFFKHLV KDTGLITYGE
KEVRKALELG AVDILLLSEG YDRVRVKALC NNCGWEELKT MTEAEFELYK KNLKACPKCN
SQNISVEKWD VAEELIKIAE EGGAEVEIIS LDTEEGQQFY KAFGGIAAIL RYKLQ