ID   RF1_HALWD               Reviewed;         416 AA.
AC   Q18FC0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=HQ_3241A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ53338.1; -; Genomic_DNA.
DR   RefSeq; WP_011572443.1; NC_008212.1.
DR   AlphaFoldDB; Q18FC0; -.
DR   SMR; Q18FC0; -.
DR   STRING; 362976.HQ_3241A; -.
DR   EnsemblBacteria; CAJ53338; CAJ53338; HQ_3241A.
DR   GeneID; 4193965; -.
DR   KEGG; hwa:HQ_3241A; -.
DR   eggNOG; arCOG01742; Archaea.
DR   HOGENOM; CLU_035759_3_0_2; -.
DR   OMA; GQEMEVV; -.
DR   Proteomes; UP000001975; 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..416
FT                   /note="Peptide chain release factor subunit 1"
FT                   /id="PRO_1000060102"
SQ   SEQUENCE   416 AA;  46638 MW;  7AE4D98B2F698A5C CRC64;
     MSTDAEDVSN DRRKYEFRKV IEELREYEGS GTQLVTIYIP PDRQVSDVVA HITQEHSEAS
     NIKSKQTRTN VQDALTSIKD RLRYYDTYPP DNGIVLFSGA VSTGGGQTTM VTRSLESPPE
     PVQSFRYHCD SDFLTDPLED MLADKGLFGL IVLDRREANV GWLKGKRVEP VKSASSLVPG
     KQRKGGQSAQ RFARLRLEAI DNFYQEVAGM ANDLFVPKRH EIDGVLVGGP SPTKDEFLDG
     DYLHHELGDV VVGKFDVSYT DESGLHDLVD SAQDVLADQE VMKDKAEMEE FFEKLHGGEE
     ATYGFEPTRK NLMMGAVDRL LLSEDLRSDV VVYECPDGHE EYEVIDRRHD DPEHTCSDCG
     SASEKTERED VIEYLMSIAE QRGTETKFIS TDFEKGEQLH NAFGGIAGIL RYATGI