ID   EF1A2_CANAL             Reviewed;         458 AA.
AC   Q59QD6; A0A1D8PED0; P16017; Q5A743;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Elongation factor 1-alpha 2;
DE            Short=EF-1-alpha 2;
GN   Name=TEF2; OrderedLocusNames=CAALFM_C108380WA;
GN   ORFNames=CaO19.382, CaO19.8012;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=2180914; DOI=10.1128/jb.172.4.2036-2045.1990;
RA   Sundstrom P., Smith D., Sypherd P.S.;
RT   "Sequence analysis and expression of the two genes for elongation factor 1
RT   alpha from the dimorphic yeast Candida albicans.";
RL   J. Bacteriol. 172:2036-2045(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; M29935; AAA34340.1; -; Genomic_DNA.
DR   EMBL; CP017623; AOW26476.1; -; Genomic_DNA.
DR   RefSeq; XP_710148.2; XM_705056.2.
DR   RefSeq; XP_717655.2; XM_712562.2.
DR   AlphaFoldDB; Q59QD6; -.
DR   SMR; Q59QD6; -.
DR   STRING; 237561.Q59QD6; -.
DR   PRIDE; Q59QD6; -.
DR   GeneID; 3646502; -.
DR   GeneID; 3648254; -.
DR   KEGG; cal:CAALFM_C108380WA; -.
DR   KEGG; cal:CAALFM_C208370CA; -.
DR   CGD; CAL0000196876; TEF2.
DR   VEuPathDB; FungiDB:C2_08370C_A; -.
DR   HOGENOM; CLU_007265_3_5_1; -.
DR   InParanoid; Q59QD6; -.
DR   OMA; AIRDMGM; -.
DR   OrthoDB; 1150082at2759; -.
DR   PRO; PR:Q59QD6; -.
DR   Proteomes; UP000000559; Chromosome 1.
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; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   CHAIN           2..458
FT                   /note="Elongation factor 1-alpha 2"
FT                   /id="PRO_0000413176"
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;  50012 MW;  C737C498FE923B09 CRC64;
     MGKEKTHVNV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL
     DKLKAERERG ITIDIALWKF ETPKYHVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGT
     GEFEAGISKD GQTREHALLA YTLGVKQLIV AVNKMDSVKW DKNRFEEIIK ETSNFVKKVG
     YNPKTVPFVP ISGWNGDNMI EPSTNCPWYK GWEKETKSGK VTGKTLLEAI DAIEPPTRPT
     DKPLRLPLQD VYKIGGIGTV PVGRVETGII KAGMVVTFAP AGVTTEVKSV EMHHEQLAEG
     VPGDNVGFNV KNVSVKEIRR GNVCGDSKND PPKGCDSFNA QVIVLNHPGQ ISAGYSPVLD
     CHTAHIACKF DTLVEKIDRR TGKKLEENPK FVKSGDAAIV KMVPTKPMCV EAFTDYPPLG
     RFAVRDMRQT VAVGVIKSVE KSDKAGKVTK AAQKAAKK