ID   EF1A_EIMBO              Reviewed;         346 AA.
AC   Q07051;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
DE   Flags: Fragment;
OS   Eimeria bovis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyst;
RX   PubMed=8426605; DOI=10.1016/0166-6851(93)90239-t;
RA   Abrahamsen M.S., Clark T.G., Mascolo P., Speer C.A., White M.W.;
RT   "Developmental gene expression in Eimeria bovis.";
RL   Mol. Biochem. Parasitol. 57:1-14(1993).
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   -!- DEVELOPMENTAL STAGE: Expressed at high levels in fully sporulated
CC       oocysts and merozoites. Low levels found in unsporulated oocysts.
CC       Absent in partially sporulated oocysts.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; M98839; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A48470; A48470.
DR   AlphaFoldDB; Q07051; -.
DR   SMR; Q07051; -.
DR   PRIDE; Q07051; -.
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   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; 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   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           <1..346
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090921"
FT   DOMAIN          <1..127
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         49..52
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   346 AA;  37504 MW;  5C6A65531886BBE0 CRC64;
     GTSQADVALL VVPADQGGFE GAFSKEGQTR EHALLAFTLG VKQMIVGINK MDATTPDKYS
     ETRFNEIQAE VSRYLKTVGY NPEKVPFVPI SGFMGDNMVE RSSNMPWYKG KILVEALDNV
     EPPKRPSDKP LRLPLQDVYK IGGIGTVPVG RVETGILKPG MVVCFAPTGL QTEVKSVEMH
     HTQLEQAVPG DNVGFNVKNV SVKDVKRGHV ASDSKNDPAK AAASFQAQVI VLHHPGQINP
     GYSPVVDCHT AHIACKFAVL EKRLDRRSGK ALEDDPKFIK TGDAAIIKME PSKPMCVESF
     IEYPPLGRFA VRDMKQTVAV GVIKGVEKKE AGGKVTKSAQ KATGKK