EF1A_ARTSA
ID EF1A_ARTSA Reviewed; 462 AA.
AC P02993;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
OS Artemia salina (Brine shrimp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Anostraca; Artemiidae; Artemia.
OX NCBI_TaxID=85549;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-462, METHYLATION AT
RP LYS-36; LYS-55; LYS-79; LYS-219 AND LYS-318, AND BLOCKAGE OF N-TERMINUS.
RX PubMed=6203745;
RA van Hemert F.J., Amons R., Pluijms W.J.M., van Ormondt H., Moeller W.;
RT "The primary structure of elongation factor EF-1 alpha from the brine
RT shrimp Artemia.";
RL EMBO J. 3:1109-1113(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3514211; DOI=10.1111/j.1432-1033.1986.tb09514.x;
RA Lenstra J.A., van Vliet A., Arnberg A.C., van Hemert F.J., Moeller W.;
RT "Genes coding for the elongation factor EF-1 alpha in Artemia.";
RL Eur. J. Biochem. 155:475-483(1986).
RN [3]
RP PROTEIN SEQUENCE OF 70-114; 135-154; 219-266 AND 277-398, METHYLATION AT
RP LYS-79; LYS-219 AND LYS-318, AND ETHANOLAMINYLATION AT GLU-374.
RX PubMed=6337879; DOI=10.1016/0014-5793(83)80115-x;
RA Amons R., Pluijms W., Roobol K., Moller W.;
RT "Sequence homology between EF-1 alpha, the alpha-chain of elongation factor
RT 1 from Artemia salina and elongation factor EF-Tu from Escherichia coli.";
RL FEBS Lett. 153:37-42(1983).
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 -!- PTM: The N-terminus is blocked.
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; X03349; CAA27055.1; -; mRNA.
DR EMBL; X03704; CAA27334.1; -; Genomic_DNA.
DR EMBL; X03705; CAA27334.1; JOINED; Genomic_DNA.
DR EMBL; X03706; CAA27334.1; JOINED; Genomic_DNA.
DR EMBL; X03707; CAA27334.1; JOINED; Genomic_DNA.
DR EMBL; X03708; CAA27334.1; JOINED; Genomic_DNA.
DR PIR; A25056; EFSS1A.
DR AlphaFoldDB; P02993; -.
DR SMR; P02993; -.
DR iPTMnet; P02993; -.
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 INIT_MET 1
FT /note="Removed"
FT CHAIN 2..462
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090917"
FT DOMAIN 5..242
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 2
FT /note="Blocked amino end (Gly)"
FT MOD_RES 36
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:6203745"
FT MOD_RES 55
FT /note="N6-methyllysine"
FT /evidence="ECO:0000305|PubMed:6203745"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:6203745,
FT ECO:0000269|PubMed:6337879"
FT MOD_RES 219
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:6203745,
FT ECO:0000269|PubMed:6337879"
FT MOD_RES 318
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:6203745,
FT ECO:0000269|PubMed:6337879"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000305|PubMed:6337879"
FT CONFLICT 33
FT /note="G -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="G -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50567 MW; 2C83303EC2CD079A CRC64;
MGKEKIHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETAKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PFSEARFEEI KKEVSAYIKK
IGYNPAAVAF VPISGWHGDN MLEASDRLPW YKGWNIERKE GKADGKTLLD ALDAILPPSR
PTEKPLRLPL QDVYKIGGIG TVPVGRVETG IIKPGMIVTF APANITTEVK SVEMHHESLE
QASPGDNVGF NVKNVSVKEL RRGYVASDSK NNPARGSQDF FAQVIVLNHP GQISNGYTPV
LDCHTAHIAC KFAEIKEKCD RRTGKTTEAE PKFIKSGDAA MITLVPSKPL CVEAFSDFPP
LGRFAVRDMR QTVAVGVIKS VNFKDPTAGK VTKAAEKAGK KK
