ID   ERF1_DIDNA              Reviewed;         437 AA.
AC   Q5CD97;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE            Short=Eukaryotic release factor 1;
DE            Short=eRF1;
GN   Name=eRF1;
OS   Didinium nasutum.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Litostomatea;
OC   Haptoria; Haptorida; Didiniidae; Didinium.
OX   NCBI_TaxID=5997;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Stock 777 / ATCC 30399;
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; AB086368; BAD90943.1; -; mRNA.
DR   AlphaFoldDB; Q5CD97; -.
DR   SMR; Q5CD97; -.
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..437
FT                   /note="Eukaryotic peptide chain release factor subunit 1"
FT                   /id="PRO_0000143151"
SQ   SEQUENCE   437 AA;  49712 MW;  7E193D761D04DBF5 CRC64;
     MIQSEEDLEY ERNVEMFRLK RLIAKLESMK GSGTSMITLI INFKDQINIH ARMLAEEVGK
     ASNIKSRVTR QNVTDALTST LEKLKLYNKT PPNGLVIFCG LVQQEDGGEK MIKIDLEPFK
     PINTTLYKCD SVFHTEEVRK LLEDNDKFGF IIMDGNGSLF GTLQGSTRTV LLKFNVDLPK
     KHGRGGQSAN RFARIRIEKR RNYLRKVAES TTACFITNDM PNVKGLILAG SAEFKNDLQK
     SDLFDLRLQP IVIKLVDISY GGENGFNQAI ELSSDALKSV KFIHEKKVIG KFFDEIAKDT
     GKYVFGIKDT LEAMDMGSVD ILIIYENLEY NRLILRDAND NIVNETLHKN KCPSGSKYKN
     ETTGVEYEVL DNIPLTEWFM DNYKKYVSHL EIVTDKSSEG SQFLKGFGGI GGILRYKMDT
     DFDDTENNNE WNDDDFI