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EF1A3_XENLA
ID   EF1A3_XENLA             Reviewed;         461 AA.
AC   P17508;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Elongation factor 1-alpha, oocyte form;
DE   AltName: Full=EF-1-alpha-O1;
DE            Short=EF-1AO1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1988459; DOI=10.1083/jcb.112.2.237;
RA   Coppard N.J., Poulsen K., Madsen H.O., Frydenberg J., Clark B.F.C.;
RT   "42Sp48 in previtellogenic Xenopus oocytes is structurally homologous to
RT   EF-1 alpha and may be a stage-specific elongation factor.";
RL   J. Cell Biol. 112:237-243(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-461.
RC   TISSUE=Oocyte;
RX   PubMed=2362804; DOI=10.1093/nar/18.12.3489;
RA   Dje M.K., Mazabraud A., Viel A., le Maire M., Denis H., Crawford E.T.,
RA   Brown D.D.;
RT   "Three genes under different developmental control encode elongation factor
RT   1-alpha in Xenopus laevis.";
RL   Nucleic Acids Res. 18:3489-3493(1990).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1894690; DOI=10.1083/jcb.114.6.1109;
RA   Deschamps S., Morales J., Mazabraud A., le Maire M., Denis H., Brown D.D.;
RT   "Two forms of elongation factor 1 alpha (EF-1 alpha O and 42Sp50), present
RT   in oocytes, but absent in somatic cells of Xenopus laevis.";
RL   J. Cell Biol. 114:1109-1111(1991).
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   -!- TISSUE SPECIFICITY: Oocyte.
CC   -!- DEVELOPMENTAL STAGE: 3 EF-1-alpha are expressed under different
CC       developmental control in Xenopus laevis.
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; X56699; CAA40029.1; -; mRNA.
DR   EMBL; X52977; CAA37169.1; -; mRNA.
DR   PIR; S13806; S13806.
DR   AlphaFoldDB; P17508; -.
DR   SMR; P17508; -.
DR   IntAct; P17508; 2.
DR   PRIDE; P17508; -.
DR   Proteomes; UP000186698; Genome assembly.
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;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P68104"
FT   CHAIN           2..461
FT                   /note="Elongation factor 1-alpha, oocyte form"
FT                   /id="PRO_0000090901"
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="N,N,N-trimethylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P68104"
FT   MOD_RES         301
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         374
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        139
FT                   /note="L -> F (in Ref. 2; CAA37169)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   461 AA;  50195 MW;  F55AE74BCD8C5BEC CRC64;
     MGKEKIHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
     DKLKAERERG ITIDISLWKF ETGKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAGGV
     GEFEAGISKN GQTREHALLA FTLGVKQLII GVNKMDSTEP PFSQKRFEEI TKEVSAYIKK
     IGYNPATVPF VPISGWHGDN MLEASTNMPW FKGWKIERKE GNASGITLLE ALDCIIPPQR
     PTNKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMIVTF APSNVTTEVK SVEMHHEALV
     EALPGDNVGF NVKNISVKDI RRGNVAGDSK NDPPMQAGSF TAQVIILNHP GQISAGYAPV
     LDCHTAHIAC KFAELKQKID RRSGKKLEDD PKFLKSGDAA IVEMIPGKPM CVETFSDYPP
     LGRFAVRDMR QTVAVGVIKG VDKKLASSGK VTKSAAKAGK K
 
 
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