RF1_METST
ID RF1_METST Reviewed; 411 AA.
AC Q2NEL3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Msp_1363;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57740.1; -; Genomic_DNA.
DR RefSeq; WP_011406939.1; NC_007681.1.
DR AlphaFoldDB; Q2NEL3; -.
DR SMR; Q2NEL3; -.
DR STRING; 339860.Msp_1363; -.
DR PRIDE; Q2NEL3; -.
DR EnsemblBacteria; ABC57740; ABC57740; Msp_1363.
DR GeneID; 41325933; -.
DR KEGG; mst:Msp_1363; -.
DR eggNOG; arCOG01742; Archaea.
DR HOGENOM; CLU_035759_3_0_2; -.
DR OMA; GQEMEVV; -.
DR OrthoDB; 32191at2157; -.
DR Proteomes; UP000001931; 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..411
FT /note="Peptide chain release factor subunit 1"
FT /id="PRO_1000060107"
SQ SEQUENCE 411 AA; 46549 MW; 837D8AC8F0478AAD CRC64;
MSDVSSKEIY EVKKTLKELE DKKGRGTELV SVYIPPEKQI SDVAKQMRDE LGQSANIKSK
QTRKNVQSAI EVIIQRLKLF PKPPEKGLVM FVGMIPKGGP GTEKMETYVF QPPEAVQTYT
YHCDSQFFVE PLKQIIEYKE VYGVVVLDRK ESTIATLRGK RIDIIKHLTS GVPGKHKAGG
QSQRRFDRVI ELAAHEFLKR IGRHVDEAFL PLKDELKGVL IGGPGHTKND FVDGEYIHYE
IHDKIINIVD TSYTGDFGIR EVIDESADTL DEMDIMQEKK FMRKFLTGLI SESGLSTYGE
KEVRQNLQMG AVETLLISEN LKSKRQTYTC PACNTVDVIT TRQHQEPPEK RCPKCNEVMK
ITKTQETAEE LIELAEEVKT HVEVISIETE EGTQLDKAFG GIAGILRYKV K