ID   RF1_THEAC               Reviewed;         417 AA.
AC   Q9HKR2;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Peptide chain release factor subunit 1;
DE   AltName: Full=Translation termination factor aRF1;
GN   Name=prf1; OrderedLocusNames=Ta0534;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codons UAA, UAG and UGA.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AL445064; CAC11674.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HKR2; -.
DR   SMR; Q9HKR2; -.
DR   STRING; 273075.Ta0534; -.
DR   EnsemblBacteria; CAC11674; CAC11674; CAC11674.
DR   KEGG; tac:Ta0534; -.
DR   eggNOG; arCOG01742; Archaea.
DR   HOGENOM; CLU_035759_3_0_2; -.
DR   OMA; GQEMEVV; -.
DR   Proteomes; UP000001024; 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..417
FT                   /note="Peptide chain release factor subunit 1"
FT                   /id="PRO_0000143186"
SQ   SEQUENCE   417 AA;  48035 MW;  73B0DA353CBE8EEC CRC64;
     MLFMEDDEQI RRYEFKRALE ELSKLHGRGT ELISLYIPPD KQISDVVAYL RDEYSTSSNI
     KSKSTRKNVL AAIESIMARL KYYKTPPPNG FVFFEGHIAT RGDQTEMYTK IIEPPEPITT
     FMYKCDSEFH LEMLKTMLEE KEIYGLIVID RKEATVGFLN GTRIEVVDNV QSQVPSKHHQ
     GGQSSRRFER LIEIAANEFF KKVGEIANNA FMPKIKDIRA IFLGGPGATK EYFFEKDYLR
     NEVKEKIKDL FDVGYTDESG LRELVEKASE SIKDMKISKE KDLMNRFLRE VRKPDGGLAI
     YGEQAIRDAL EQKMVDLLLI SEGLRKVRYT YRCPTCQAEL TLNQEPNEWP VCEKDGTPME
     LVAEDDFIED LYRLAKESGA QVEIISDQSE EGKLLKQAFG GMAAVLRFIR KDNVQMM