ID   RF1_PYRAE               Reviewed;         388 AA.
AC   Q8ZU81;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Peptide chain release factor subunit 1;
DE   AltName: Full=Translation termination factor aRF1;
GN   Name=prf1; OrderedLocusNames=PAE2906;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64527.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZU81; -.
DR   SMR; Q8ZU81; -.
DR   STRING; 178306.PAE2906; -.
DR   EnsemblBacteria; AAL64527; AAL64527; PAE2906.
DR   KEGG; pai:PAE2906; -.
DR   PATRIC; fig|178306.9.peg.2173; -.
DR   eggNOG; arCOG01742; Archaea.
DR   HOGENOM; CLU_035759_3_0_2; -.
DR   InParanoid; Q8ZU81; -.
DR   OMA; GQEMEVV; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0018444; C:translation release factor complex; IBA:GO_Central.
DR   GO; GO:1990825; F:sequence-specific mRNA binding; IBA:GO_Central.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IBA:GO_Central.
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; 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..388
FT                   /note="Peptide chain release factor subunit 1"
FT                   /id="PRO_0000143181"
SQ   SEQUENCE   388 AA;  43509 MW;  8584F3CE64AD7066 CRC64;
     MSFNRPPNGV YYIRSAVELR AFVNLLKKFK GYATTLITLY INAERPIPDV VNLLRSEWST
     AANIKDKTTR THVQDTLERI INNLKGEAKA PENGMAVFAG FHMINQGNYE WVYYVVIPPQ
     PINTFKYICD TAFHTELLED QLHAGVVYGI VVIERGEAVI ALLKGGQWEV VKSVEFFVPG
     KHHAGGQSAN RFKRQTEHLA EAFYKMVAEE ANKIFLQIPT LKGIIVAGPG PTKEDFLEEG
     GLDYRLKDKI LAIVPACCAN EYGVMEAIRN AQEQLKESEY VKAKEVMDKV MYYAVKKSEY
     LVYGRERALK ALEMGIADII VIAEELGEDA VLEVIMKAEE KGIKVEVVPR GVEESKTLMQ
     AFGGYVALLS TPVWVLEQQL SIAEAAQR