ID   ERF1_TETTH              Reviewed;         435 AA.
AC   Q9U8U5;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE            Short=Eukaryotic release factor 1;
DE            Short=eRF1;
GN   Name=ERF1;
OS   Tetrahymena thermophila.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10471834; DOI=10.1016/s0014-5793(99)01089-3;
RA   Karamyshev A.L., Ito K., Nakamura Y.;
RT   "Polypeptide release factor eRF1 from Tetrahymena thermophila: cDNA
RT   cloning, purification and complex formation with yeast eRF3.";
RL   FEBS Lett. 457:483-488(1999).
RN   [2]
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).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codon UGA. In
CC       T.thermophila 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; AB026195; BAA85336.1; -; mRNA.
DR   EMBL; AF298833; AAK07831.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9U8U5; -.
DR   SMR; Q9U8U5; -.
DR   PRIDE; Q9U8U5; -.
DR   OMA; GQEMEVV; -.
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..435
FT                   /note="Eukaryotic peptide chain release factor subunit 1"
FT                   /id="PRO_0000143160"
SQ   SEQUENCE   435 AA;  49559 MW;  89013ED4C8612646 CRC64;
     MEEKDQRQRN IEHFKIKKLM TRLRNTRGSG TSMVSLIIPP KKQINDSTKL ISDEFSKATN
     IKDRVNRQSV QDAMVSALQR LKLYQRTPNN GLILYCGKVL NEEGKEIKLL IDFEPYKPIN
     TSLYFCDSKF HVDELGSLLE TDPPFGFIVM DGQGALYANL QGNTKTVLNK FSVELPKKHG
     RGGQSSVRFA RLRVEKRHNY LRKVCEVATQ TFISQDKINV QGLVLAGSGD FKNELSTTQM
     FDPRLACKII KIVDVSYGGE NGLNQAIELA QESLTNVKFV QEKNVISKFF DCIAIDSGTV
     VYGVQDTMQL LLDGVIENIL CFEELTTLRV TRKNKVTEQI THIFIPPNEL NNPKHFKDGE
     HELEKIEVEN LTEWLAEHYS EFGAELYFIT DKSAEGCQFV KGFSGIGGFL RYKVDLEHIV
     NPNDEYNYEE EEGFI