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ERF1_LOXST
ID   ERF1_LOXST              Reviewed;         436 AA.
AC   Q5CD84;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE            Short=Eukaryotic release factor 1;
DE            Short=eRF1;
GN   Name=eRF1;
OS   Loxodes striatus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Karyorelictea; Loxodida; Loxodidae; Loxodes.
OX   NCBI_TaxID=6009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 codon UGA. In L.striatus
CC       UAA and UAG codes for glutamine.
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; AB105075; BAD90946.1; -; mRNA.
DR   AlphaFoldDB; Q5CD84; -.
DR   SMR; Q5CD84; -.
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; 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_0000143155"
SQ   SEQUENCE   436 AA;  49811 MW;  CED116F5EF298786 CRC64;
     MDVEQEDAIK GWKIRRLIEY LEKAKGNGTS LISLIIPPKE QISLINQKLT DAHGRAQNIK
     SKAVQKAVQD AIISTKQKLS VIKQIPPNGL ILYCGKFIGE DEKTEKQILE VLEPLRAINT
     TFFLCENTFY TQPLRDMLQE QDKFGFIIMD GNGSLFGTLQ GNAREILHKF DVDLPKKHGR
     GGQSALRFAR LRLEKRHNYM KKVAEVAINC FIQNDRVNVL GIVLAGAAEF KNELAANEYL
     DQRIRAKVVT IIDVNYGGEN GFNQAIELSQ VQLQNVKFIK EKNLITKLFE EVAQNSITVC
     YGLTDTMKAL EMGAVETLVI WENLEFIWFK LKNPVTKEES TVVLSPQQAT EKNHFQDEAN
     QCELNIVERF ALTEWLIDNY KNYGARLEFV TDRSQEGSQF VKGFGGICGF LRYEVNFEKM
     EFQEEEGYLD PDEDFL
 
 
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