ID   RF1_METS3               Reviewed;         412 AA.
AC   A5ULL8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Msm_0891;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000678; ABQ87096.1; -; Genomic_DNA.
DR   RefSeq; WP_011954153.1; NC_009515.1.
DR   AlphaFoldDB; A5ULL8; -.
DR   SMR; A5ULL8; -.
DR   STRING; 420247.Msm_0891; -.
DR   PRIDE; A5ULL8; -.
DR   EnsemblBacteria; ABQ87096; ABQ87096; Msm_0891.
DR   GeneID; 5216024; -.
DR   KEGG; msi:Msm_0891; -.
DR   PATRIC; fig|420247.28.peg.888; -.
DR   eggNOG; arCOG01742; Archaea.
DR   HOGENOM; CLU_035759_3_0_2; -.
DR   OMA; GQEMEVV; -.
DR   Proteomes; UP000001992; 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.
FT   CHAIN           1..412
FT                   /note="Peptide chain release factor subunit 1"
FT                   /id="PRO_1000060106"
SQ   SEQUENCE   412 AA;  46509 MW;  1E881E0E3BF9DA11 CRC64;
     MAEVSSKELY KFKKTLKELS EKKGRGTELV SVYIPHDKQI SDVGKQMRDE LGQSANIKSK
     QTRKNVQSAI EVIMQRIRLF KAAPENGLVL FVGMIPRGGP GTEKMETYVF EPPEPITTYW
     YQCNNEFFLE PLEYMIEERE TYGLAVIDRK EATIATLRGK KVNILNHLTS GVPGKHKAGG
     QSQRRFDRVI DLAAHEFKKR IGEHMNEDFL ALEELEGVII GGPGFTKEEF VKGDYLNYEI
     KDKIIATVDT SYTGEFGIRE VIDKSADILN DLDVMQEKKV VQKFLHELVK DKGLASYGER
     EVRTNLIMGA VDTLLLSEDL TAMRKVFKCP SCGNEEEITV KSQSEADKLE KPCSNCGEIL
     KEESSQTLIE DFVEKAEEMN SEVELISTET EEGMQLLRAF GGVAAILRYH VG