ID   ERF1_DILMA              Reviewed;         436 AA.
AC   Q5CD96;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE            Short=Eukaryotic release factor 1;
DE            Short=eRF1;
GN   Name=eRF1;
OS   Dileptus margaritifer (Ciliate) (Amphileptus margaritifer).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Litostomatea;
OC   Haptoria; Haptorida; Dileptidae; Dileptus.
OX   NCBI_TaxID=197863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Stock L / Golinska;
RX   PubMed=15716103; DOI=10.1016/j.gene.2004.11.046;
RA   Kim O.T.P., Yura K., Go N., Harumoto T.;
RT   "Newly sequenced eRF1s from ciliates: the diversity of stop codon usage and
RT   the molecular surfaces that are important for stop codon interactions.";
RL   Gene 346:277-286(2005).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codons UAA and possibly
CC       also UAG and UGA. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AB086369; BAD90944.1; -; mRNA.
DR   AlphaFoldDB; Q5CD96; -.
DR   SMR; Q5CD96; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.30.420.60; -; 1.
DR   Gene3D; 3.30.960.10; -; 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; 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   2: Evidence at transcript level;
KW   Cytoplasm; Protein biosynthesis.
FT   CHAIN           1..436
FT                   /note="Eukaryotic peptide chain release factor subunit 1"
FT                   /id="PRO_0000143152"
SQ   SEQUENCE   436 AA;  49571 MW;  90373CE8BB973E3C CRC64;
     MLDKDEDAEY ERSVEMFRLK KLIHKLDNLK GSGTSMISLI INYKDQINPF MKMLVDEVGK
     ASNIKSRVTR QNVTDALTST MEKLKLYNKT PNNGLIIYCG LASEGDSGEK MFKIDMEPFK
     PINTSLYRCD SVFHTEEVKK LLEDNDRFGF LIMDGNGSLF GSVQGATRTV IQKFLVDLPK
     KHGRGGQSSN RFARIRTERR HNYLRKVAET MTAVFITNDR PNVKGLILAG SADFKTDLNK
     SDLFDPRLSP LVIKIVDIAY GGENGFNQAI ELSSDALRNV KFVHEKKIVG RFFDEISKDT
     GRFVFGLKDT MEGLEYGAVE VLMIFENLEH NRLSLKDNNN TVTFKIFPKK ETPSGNKFRD
     ENGVEYEIID NTPLSEWFLD NYKKFGTHLE IITDKSSEGN QFVKGFGGIG GILRYKMEQT
     HGDVETEDAF NEDDFI