EF1A_MAIZE
ID EF1A_MAIZE Reviewed; 447 AA.
AC Q41803;
DT 15-JUL-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=EF1A;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Honey Vantum;
RX PubMed=8534856; DOI=10.1007/bf00020988;
RA Berberich T., Sugawara K., Harada M., Kusano T.;
RT "Molecular cloning, characterization and expression of an elongation factor
RT 1 alpha gene in maize.";
RL Plant Mol. Biol. 29:611-615(1995).
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; D45408; BAA08249.1; -; Genomic_DNA.
DR PIR; S66339; S66339.
DR AlphaFoldDB; Q41803; -.
DR SMR; Q41803; -.
DR STRING; 4577.GRMZM2G153541_P06; -.
DR PaxDb; Q41803; -.
DR PRIDE; Q41803; -.
DR MaizeGDB; 25449; -.
DR eggNOG; KOG0052; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q41803; 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; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..447
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090939"
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; 49233 MW; 1CBC5B54883A179C CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK LGGIDKRVIE RFEKEAAEMN KRSFKYAWVL
DKLKAERERG ITIDIALWKF ETTKYYCTVI DAPGHRDFIK NMITGTSQAD CAVLIIDSTT
GGFEAGISKD GQTREHALLA FTLGVKQMIC CCNKMDATTP KYSKARYDEI VKEVSSYLKK
VGYNPDKIHF VPISGFEGDN MIERSTNLDW YKGPTLLEAL DLINEPKRPS DKPLRLPLQD
VYKIGGIGTV PVGRVETGVI KPGMVVTFGP TGLTTEVKSV EMHHEALQEA LPGDNVGFNV
KNVAVKDLKR GYVASGSKDD PAKEAASFTS QVIIMNHPGQ IGNGYAPVLD CHTSHIAVKF
AELVTKIDRR SGKELEKEPK FLKNGDAGMV KMVPTKPMVV ETFSQYPPLG RFAVRDMRQT
VAVGVIKSVE KKDPTGAKVT KAAAKKK
