ID   RF1_METVS               Reviewed;         419 AA.
AC   A6UPD8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Mevan_0453;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000742; ABR54360.1; -; Genomic_DNA.
DR   RefSeq; WP_011972263.1; NC_009634.1.
DR   AlphaFoldDB; A6UPD8; -.
DR   SMR; A6UPD8; -.
DR   STRING; 406327.Mevan_0453; -.
DR   EnsemblBacteria; ABR54360; ABR54360; Mevan_0453.
DR   GeneID; 5325327; -.
DR   KEGG; mvn:Mevan_0453; -.
DR   eggNOG; arCOG01742; Archaea.
DR   HOGENOM; CLU_035759_3_0_2; -.
DR   OMA; GQEMEVV; -.
DR   OrthoDB; 32191at2157; -.
DR   Proteomes; UP000001107; 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..419
FT                   /note="Peptide chain release factor subunit 1"
FT                   /id="PRO_1000060108"
SQ   SEQUENCE   419 AA;  47635 MW;  82F11E67DB3EA8EF CRC64;
     MSENSSTDMY LFKKSLKELK GKRGKGTELI SVYVPAGRRL SDISQHLRQE LSQSSNIKSK
     TTMKNVQSAI EVILQRLKLL KEPLEKGVII FAGMIPRGGP GTEKMEVYVL EPPEPVKTFI
     YRCDSEFYTE SLEDFIQDTE VYGVILVDRN EATIGTVKGK TITVLKKLTS GVPGKFKAGG
     QSARRLERLI DDAAHQFMVR IGEYSTESFM PILEEKKLRG LLIGGPGNTK NEFAEKDFLH
     HELKKKIIDT FDLCYTEEFG IRELLEKASD LLRDLDLMKE KNLIQKFFKE LIKDDGGLSA
     YGESQVMRYL EMGAIDTLIV TEDIELTRVT IKCNNCNFKQ EINVKTRDLY KFEDEVKTKI
     CKQCSGSMYI EEEKDIIEYL SELCNIHNSD IVVVSTDTEE GSQISKAFKG MAAILRYKI