ID   EF1A_TETPY              Reviewed;         435 AA.
AC   Q04634;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
DE   AltName: Full=14 nm filament-associated protein;
OS   Tetrahymena pyriformis.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1385189; DOI=10.1016/0014-4827(92)90062-d;
RA   Kurasawa Y., Numata O., Katoh M., Hirano H., Chiba J., Watanabe Y.;
RT   "Identification of Tetrahymena 14-nm filament-associated protein as
RT   elongation factor 1 alpha.";
RL   Exp. Cell Res. 203:251-258(1992).
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; D11083; BAA01856.1; -; mRNA.
DR   PIR; A49171; A49171.
DR   AlphaFoldDB; Q04634; -.
DR   SMR; Q04634; -.
DR   PRIDE; Q04634; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..435
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090930"
FT   DOMAIN          6..231
FT                   /note="tr-type G"
FT   REGION          15..22
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          71..75
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          92..95
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          154..157
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          195..197
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         92..96
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   435 AA;  48298 MW;  57FEF054BCF908CA CRC64;
     MARGDKVHIN LVVIGHVDSG KSTTTGHLIY KCGGIDKRVI EKFEKESAEQ GKGSFKYAWV
     LDKLKAERER GITIDISLWK FETAKYHFTI IDAPGHRDFI KNMITGTSQA DVAILMIASP
     QGEFEAGISK DGQTREHALL AFTLGVKQMI VCLNKMDEKT VNFSEERYQE IKKELSDYLK
     KVGYKPDTIP FIPISGFNGD NMLERSTNAP WYKGPILVEA LDALEPPKRP VDKPLRLPLQ
     DVYKIGGIGT VPVGRVETGV IKPGMSIQFA PNKVIAECKS VEMHHEQLPE AVPGDNVGFN
     IKGVSVKDIR RGNVASDAKN DPAKEAATFY SQVIIMNHPG QIQAGYTPVL DCHTAHIACK
     FETIHDKIDR RTGKSQEENP KFIKNGDAAL VTLIPTKALC VEVFQEYPPL GRYAVRDMKQ
     TVAVGVIKKV EKKDK