RF1_METM7
ID RF1_METM7 Reviewed; 419 AA.
AC A6VG76;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=MmarC7_0383;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
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; CP000745; ABR65452.1; -; Genomic_DNA.
DR RefSeq; WP_011976787.1; NC_009637.1.
DR AlphaFoldDB; A6VG76; -.
DR SMR; A6VG76; -.
DR STRING; 426368.MmarC7_0383; -.
DR EnsemblBacteria; ABR65452; ABR65452; MmarC7_0383.
DR GeneID; 5327983; -.
DR KEGG; mmz:MmarC7_0383; -.
DR eggNOG; arCOG01742; Archaea.
DR HOGENOM; CLU_035759_3_0_2; -.
DR OMA; GQEMEVV; -.
DR OrthoDB; 32191at2157; -.
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_1000060105"
SQ SEQUENCE 419 AA; 47201 MW; 71F4887FB7E8E22A CRC64;
MSGNSSTDMY LFKKSLRELK GKKGKGTELI SVYVPAGRRL SDISQYLRQE LSQSSNIKSK
TTMKNVQSAI EVILQRLKLL KEPLEMGVII FAGMIPRGGP GTEKMEVYVL EPPEPVKTFV
YRCDSLFYTD PLEDFIQDTE VYGVILVDRN EATIGTVKGK TITVLKKLTS GVPGKFKAGG
QSARRLERLI DDAAHQFMVR IGEYATESFM PILEEKKLKG LLLGGPGNTK NEFAEKDYLH
HELKKKIIDT FDLCYTEEFG IRELLEKASD LLRDLDLMKE KNLIQRFFKE LIKDDGGLSA
YGEAQVMKYL GMGAIDTLIV TEDIGITRVT VKCNNCDYTQ EVNVKTNEMF KFEDQLKTKA
CPTCGGAMYI DEEKDIIEYL SELCNVHNTD IIVVSTDTEE GSQISRAFKG MAAILRYKL