ERF1_STYMT
ID ERF1_STYMT Reviewed; 445 AA.
AC Q9BMM1;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 29-SEP-2021, entry version 65.
DE RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE Short=Eukaryotic release factor 1;
DE Short=eRF1;
GN Name=ERF1;
OS Stylonychia mytilus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5950;
RN [1]
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 Stylonchia
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF317833; AAK12091.1; -; Genomic_DNA.
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_0000143159"
SQ SEQUENCE 445 AA; 49671 MW; 0F3622FEA1BD50B8 CRC64;
MVESIAAGQV GDNKHIEMWK IKRLINKLEN CKGNGTSMVS LIIPPKEDIN KSGKLLVGEL
SAAQNIKSRI TRQSVITAIT STKEKLKLYR QTPTNGLCIY CGVILMEDGK TEKKINFDFE
PFRPINQFMY FCGGKFQTEP LTTLLADDDK FGFIIVDGNG ALYATLQGNS REILQKITVE
LPKKHRKGGQ SSVRFARLRE EKRHNYLRKV AELAGSNFIT NDKPNVTGLV LAGNAGFKNE
LSETDMLDKR LLPIIVSIVD VSYGGENGLN EAITLSADAL TNVKFVAEKK LVSKFFEEIS
LDTGMIVFGV QDTMKALELG AVETILLFEE LEITRYVIKN PVKGDTRTLF LNPTQQKDSK
YFKDQASGLD MDVISEDQLA EWLCHNYQNY XAQVEFITDK SQEGYQFVKG FGGIGGFLRY
KVDMEEALGD VGDGGDDFDP DTDFI