ID   ERF1_BLEMU              Reviewed;         436 AA.
AC   Q5CD95;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE            Short=Eukaryotic release factor 1;
DE            Short=eRF1;
GN   Name=eRF1;
OS   Blepharisma musculus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Blepharismidae; Blepharisma.
OX   NCBI_TaxID=197864;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Stock Lenin;
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 UAG. In
CC       B.musculus UGA codes for tryptophan.
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; AB086370; BAD90945.1; -; mRNA.
DR   AlphaFoldDB; Q5CD95; -.
DR   SMR; Q5CD95; -.
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_0000143147"
SQ   SEQUENCE   436 AA;  49639 MW;  5B9400B9A742D4C2 CRC64;
     MEGDELTQNI EQWKIKRLID NLDKARGNGT SLISLIIPPR EQLPIINKMI TEEYGKSSNI
     KSRIVRQAVQ SALTSTKERL KLYNNRLPAN GLILYCGEVI NEEGVCEKKY TIDFQPYRAI
     NTTLYICDNK FHTQPLKDLL VMDDKFGFII IDGNGALFGT LQGNTREVLH KFSVDLPKKH
     RRGGQSALRF SRLRMESRNN YLRKVAEQSV VQFISNDKVN VAGLIIAGSA EFKNVLVQSD
     LFDQRLAAKV LKIVDVAYGG ENGFTQAIEL SADTLSNIKF IREKKVMSKF FEEVAQDTKK
     YCYGVEDTMR SLIMGAIEVI LLFENLNFTR YVLKNPTTGA EKTLYLTPEQ EENHDNFMEN
     GEELEALEKG PLPEWIVDNY MKFGAGLEFI TDRSQEGAQF VRGFGGLGAF LRYQVDMAHL
     NAGEEELDEE WDDDFM