ID   ERF1_OXYTR              Reviewed;         445 AA.
AC   Q9BMX3; Q9BMM2;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE            Short=Eukaryotic release factor 1;
DE            Short=eRF1;
GN   Name=ERF1;
OS   Oxytricha trifallax (Sterkiella histriomuscorum).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Sterkiella.
OX   NCBI_TaxID=94289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11160924; DOI=10.1093/nar/29.4.921;
RA   Inagaki Y., Doolittle W.F.;
RT   "Class I release factors in ciliates with variant genetic codes.";
RL   Nucleic Acids Res. 29:921-927(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11231122; DOI=10.1016/s0960-9822(01)00028-8;
RA   Lozupone C.A., Knight R.D., Landweber L.F.;
RT   "The molecular basis of nuclear genetic code change in ciliates.";
RL   Curr. Biol. 11:65-74(2001).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codon UGA. In O.trifallax
CC       UAA and UAG codes for glutamine.
CC   -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF298830; AAK07828.1; -; Genomic_DNA.
DR   EMBL; AF317832; AAK12090.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9BMX3; -.
DR   SMR; Q9BMX3; -.
DR   PRIDE; Q9BMX3; -.
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   3: Inferred from homology;
KW   Cytoplasm; Protein biosynthesis.
FT   CHAIN           1..445
FT                   /note="Eukaryotic peptide chain release factor subunit 1"
FT                   /id="PRO_0000143156"
SQ   SEQUENCE   445 AA;  49716 MW;  7D637F4C2572A09F CRC64;
     MVESIAAGQV SDNKHIEMWK VKKLISKLEH CKGNGTSMVS LIIPPKDDIN KYGKLLTGEM
     SAAQNIKSRI TKQSVVTAIT STKEKLKLYK QTPTNGLCLY CGVIYMEDGK TEKKINFDFE
     PFRPINQFLY FCGGKFQTEP LLSLLADDDK FGFIIVDGNG ALYATLQGNS REILQKITVE
     LPKKHRKGGQ SSVRFARLRE EKRHNYLRKV AELANQNFIT NDRPNVTGIV LAGNAAFKNE
     LAETDMLDKR LLPVICAVVD VSYGGENGLN EAITLAAEAL TNVKFVAEKK LVSKFFEEIA
     LDTGMIVFGV DDTMKALELG AVETVLLFEE LDINRYVLKN PVKGDTKTIY LNSTQQKDSK
     YFKDRETGMD LDVVSEDSLA EWLCHNYQNY GAQVEFITDK SQEGFQFVKG FGGIGGFLRY
     KVDIEDHHGD LGAGGDDFDP DTDFI