ID   EF1A2_MUCCL             Reviewed;         458 AA.
AC   P14864;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
GN   Name=TEF-2;
OS   Mucor circinelloides f. lusitanicus (Mucor racemosus var. lusitanicus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=29924;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 1216b / BCRC 32522 / CBS 277.49 / NRRL 3631;
RX   PubMed=3697088; DOI=10.1093/nar/15.23.9997;
RA   Sundstrom P., Lira L.M., Choi D., Linz J.E., Sypherd P.S.;
RT   "Sequence analysis of the EF-1 alpha gene family of Mucor racemosus.";
RL   Nucleic Acids Res. 15:9997-10005(1987).
RN   [2]
RP   SEQUENCE REVISION.
RA   Sundstrom P.;
RL   Submitted (JAN-1990) to the EMBL/GenBank/DDBJ databases.
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; X17476; CAA35507.1; -; Genomic_DNA.
DR   AlphaFoldDB; P14864; -.
DR   SMR; P14864; -.
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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW   Protein biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   CHAIN           2..458
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090965"
FT   DOMAIN          5..240
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          192..194
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:P02994"
FT   MOD_RES         3
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         3
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         30
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         79
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         316
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         316
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         390
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
SQ   SEQUENCE   458 AA;  49941 MW;  7FEB444FD4FC7957 CRC64;
     MGKEKTHVNV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL
     DKLKAERERG ITIDIALWKF ETPKYNVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGT
     GEFEAGISKD GQTREHALLA FTLGFRQLIV AINKMDTTKW SQDRYNEIVK EVSGFIKKIG
     FNPKSVPFVP ISGWHGDNML DESTNMPWFK GWNKETKAGS KTGKTLLEAI DAIEPPVRPS
     DKPLRLPLQD VYKIGGIGTV PVGRVETGTI KAGMVVNFAP AAVTTEVKSV EMHHETLTEG
     LPGDNVGFNV KNVSVKDIRR GNVCSDSKND PAKESASFTA QVIILNHPGQ ISAGYAPVLD
     CHTAHIACKF SELIEKIDRR SGKKMEDSPK FVKSGDSAIV KMVPSKPMCV EAYTDYPPLG
     RFAVRDMRQT VAVGVIKAVE KVDKAGKVTK AAAKASKK