ID   RF1_PYRFU               Reviewed;         420 AA.
AC   Q8U0J4;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=PF1593;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81717.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8U0J4; -.
DR   SMR; Q8U0J4; -.
DR   STRING; 186497.PF1593; -.
DR   EnsemblBacteria; AAL81717; AAL81717; PF1593.
DR   KEGG; pfu:PF1593; -.
DR   PATRIC; fig|186497.12.peg.1659; -.
DR   eggNOG; arCOG01742; Archaea.
DR   HOGENOM; CLU_035759_3_0_2; -.
DR   OMA; GQEMEVV; -.
DR   PhylomeDB; Q8U0J4; -.
DR   Proteomes; UP000001013; 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..420
FT                   /note="Peptide chain release factor subunit 1"
FT                   /id="PRO_0000143182"
SQ   SEQUENCE   420 AA;  47954 MW;  77167B25A8B883C4 CRC64;
     MRVMTSRDAQ LYELKKKIDE LKKIRGRGTE LISLYIPAGY DLSKVMQQLR EEYSTAQNIK
     SKTTRKNVLG ALERAMQHLK LYKQTPENGL ALFVGNVSEM EGVTDIRLWA IIPPEPLNVR
     LYRCDQTFVT EPLEEMLRVK EAYGLITVEK NEATIGILRG KRIEVLDELT SNVPGKTRAG
     GQSARRYERI REQETHEFMK RIGEHANRIF LPLLESGELK GIIVGGPGPT KEEFVEGDYL
     HHELKKKIIG IVDISYHGEY GLRELVAKAA DILRDHEVIR ERNLVNEFLK HIVKDTGLAT
     YGEREVRKAL ELGAVDTLLI SEGYDKVRVH VKCNNCGWEE LKTMSEEEYE AYKKRIQTCP
     KCGSQNLTFE KWEVAEELIK IAEEAGSNVE IISLDTEEGQ QFYRAFGGLG AILRFRIQGV