EF1A2_HORVU
ID EF1A2_HORVU Reviewed; 447 AA.
AC Q40034;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=BLT63;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Igri; TISSUE=Meristem;
RX PubMed=8219052; DOI=10.1007/bf00021434;
RA Dunn A.M., Morris A., Jack P.L., Hughes M.A.;
RT "A low-temperature-responsive translation elongation factor 1 alpha from
RT barley (Hordeum vulgare L.).";
RL Plant Mol. Biol. 23:221-225(1993).
RN [2]
RP PROTEIN SEQUENCE OF 155-161; 201-205 AND 335-341.
RC STRAIN=cv. Bomi; TISSUE=Starchy endosperm;
RX PubMed=11271488;
RX DOI=10.1002/1522-2683(200011)21:17<3693::aid-elps3693>3.0.co;2-i;
RA Kristoffersen H.E., Flengsrud R.;
RT "Separation and characterization of basic barley seed proteins.";
RL Electrophoresis 21:3693-3700(2000).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; Z23130; CAA80666.1; -; mRNA.
DR PIR; S39505; S39505.
DR AlphaFoldDB; Q40034; -.
DR SMR; Q40034; -.
DR PRIDE; Q40034; -.
DR ExpressionAtlas; Q40034; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
FT CHAIN 1..447
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090937"
FT DOMAIN 5..230
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 187
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 261
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 289
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250"
FT MOD_RES 306
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 362
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250"
FT MOD_RES 396
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
SQ SEQUENCE 447 AA; 49142 MW; 3046F3644F6A8483 CRC64;
MGKEKIHISI VVIGHVDSGK STTTGHLIYK LGGIDKRVIE SFEKEAAEMN KRSFKYAWVL
DKLKAERERG ITIDIALWKF ETTKYSCTVI DAPGHRDFIK NMITGTSQAD CAVLIIDSTT
GGFEAGISKD GQTREHALLA FTLGVKHMIC CCNKMDATTP KYSKSRYDEI VKEVSSYLKK
VGYNPDKVPF VPISGFEGDN MIERSSNLDW YKGPTLLEAL DQINEPKRPS EKPLRLPLQD
VYKIGGIGTV PVGRVETGVI KPGMVVTFGP TGLTTEVKSV EMHHESLLEA LPGDNVGFNV
KNVAVKDLKR GYVASNSKDD PAKEAANFTA QVIIMNHPGQ ISNGYAPVLD CHTSHIAVKF
AEIQTKIDRR SGKELEAAPK FLKNGDAGFV KMIPTKPMVV ETFAQYPPLG RFAVRDMRQT
VAVGVIKSVE KKEPTGAKVT KAAIKKK
