EF1A_PSEMZ
ID EF1A_PSEMZ Reviewed; 19 AA.
AC P85915;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000250|UniProtKB:P25698};
DE Short=EF-1-alpha {ECO:0000250|UniProtKB:P25698};
DE Flags: Fragments;
OS Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC Pseudotsuga.
OX NCBI_TaxID=3357;
RN [1] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT "A proteomics approach to identify proteins differentially expressed in
RT Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL J. Proteomics 71:425-438(2008).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC Tu/EF-1A subfamily. {ECO:0000255}.
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DR PRIDE; P85915; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN <1..>19
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000397943"
FT NON_CONS 9..10
FT /evidence="ECO:0000303|PubMed:18602030"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:18602030"
FT NON_TER 19
FT /evidence="ECO:0000303|PubMed:18602030"
SQ SEQUENCE 19 AA; 1990 MW; 1667EBE056E8E083 CRC64;
RXSDKPLRIG GIGTVPVGR