ID   EF1A2_XENLA             Reviewed;         461 AA.
AC   P17507; Q68FJ2;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Elongation factor 1-alpha, oocyte form;
DE            Short=EF-1-alpha-O;
DE            Short=EF-1AO;
DE   AltName: Full=42S p48;
GN   Name=eef1ao;
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].
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Oocyte;
RX   PubMed=1765266; DOI=10.1016/0378-1119(91)90608-e;
RA   Frydenberg J., Poulsen K., Petersen A.K.B., Lund A., Olesen O.F.;
RT   "Isolation and characterization of the gene encoding EF-1 alpha O, an
RT   elongation factor 1-alpha expressed during early development of Xenopus
RT   laevis.";
RL   Gene 109:185-192(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 139-461.
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   [5]
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; X52976; CAA37168.1; -; mRNA.
DR   EMBL; M67485; AAA49702.1; -; Genomic_DNA.
DR   EMBL; M67481; AAA49702.1; JOINED; Genomic_DNA.
DR   EMBL; M67483; AAA49702.1; JOINED; Genomic_DNA.
DR   EMBL; M67484; AAA49702.1; JOINED; Genomic_DNA.
DR   EMBL; M75873; AAA49701.1; -; Genomic_DNA.
DR   EMBL; BC079786; AAH79786.1; -; mRNA.
DR   EMBL; X56698; CAA40028.1; -; mRNA.
DR   PIR; JH0530; JH0530.
DR   RefSeq; NP_001081521.1; NM_001088052.1.
DR   AlphaFoldDB; P17507; -.
DR   SMR; P17507; -.
DR   BioGRID; 99228; 3.
DR   IntAct; P17507; 2.
DR   DNASU; 397890; -.
DR   GeneID; 397890; -.
DR   KEGG; xla:397890; -.
DR   CTD; 397890; -.
DR   Xenbase; XB-GENE-1218993; eef1a1o.L.
DR   OMA; DPPMQAG; -.
DR   OrthoDB; 1150082at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 397890; Expressed in ovary and 16 other tissues.
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_0000090900"
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"
SQ   SEQUENCE   461 AA;  50123 MW;  2CCDC71C6EA245A2 CRC64;
     MGKEKIHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
     DKLKAERERG ITIDISLWKF ETGKFYITII DAPGHRDFIK NMITGTSQAD CAVLIVAGGV
     GEFEAGISKN GQTREHALLA FTLGVKQLII GVNKMDSTEP PFSQKRFEEI TKEVSAYIKK
     IGYNPATVPF VPISGWHGDN MLEASTNMPW FKGWKIERKE GNASGVTLLE ALDCIIPPQR
     PTAKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMIVTF APSNVTTEVK SVEMHHEALQ
     EALPGDNVGF NVKNISVKDI RRGNVAGDSK NDPPMQAGSF TAQVIILNHP GQISAGYAPV
     LDCHTAHIAC KFAELKQKID RRSGKKLEDD PKFLKSGDAA IVEMIPGKPM CVESFSDYPP
     LGRFAVRDMR QTVAVGVIKG VDKKAASSGK VTKSAVKAGK K