ID   EF1A_ONCVO              Reviewed;         464 AA.
AC   P27592;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
OS   Onchocerca volvulus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=6282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1779985; DOI=10.1016/0166-6851(91)90169-7;
RA   Alarcon C.M., Donelson J.E.;
RT   "Translational elongation factor 1 alpha (EF-1 alpha) of Onchocerca
RT   volvulus.";
RL   Mol. Biochem. Parasitol. 48:105-108(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   -!- 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; M64333; AAA29416.1; -; mRNA.
DR   PIR; A45618; A45618.
DR   AlphaFoldDB; P27592; -.
DR   SMR; P27592; -.
DR   STRING; 6282.P27592; -.
DR   PRIDE; P27592; -.
DR   HOGENOM; CLU_007265_3_5_1; -.
DR   Proteomes; UP000024404; Unassembled WGS sequence.
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; 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; PS51722; G_TR_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..464
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090927"
FT   DOMAIN          5..242
FT                   /note="tr-type G"
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         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   464 AA;  50724 MW;  CE8F8CF43EE1D991 CRC64;
     MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL
     DKLKAERERG IQIDIALWKF ETPKYYITII DAPGHRDFIK NMITGTSQAD CAVLVVACGT
     GEFEAGISKN GQTREHALLA QTLGVKQMIV ACNKMDSTDP PFSEARFGEV TTEVSNYIKK
     IGYNPKSIPF VPISGFNGDN MLEPSANMPW FKGWSVERKE GTMTGKTLLE ALDSVVPPQR
     PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILKPGMIVTF APQNLTTEVK SVEMHHEALQ
     EALPGDNVGF NVKNISIKDI RRGSVASDSK NDPAKETKMF TAQVIIMNHP GQISAGYTPV
     LDCHTAHIAC KFAELKEKVD RRSGKKVEDN PKSLKSGDAG IIDLIPTKPL CVETFTEYPP
     LGRFAVRDMR QTVAVGVIKN VDKSEGVGKV QKAAQKAGVG GKKK