EF1A_YARLI
ID EF1A_YARLI Reviewed; 460 AA.
AC O59949; Q6CCI4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=TEF; OrderedLocusNames=YALI0C09141g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9802206;
RX DOI=10.1002/(sici)1097-0061(1998100)14:14<1267::aid-yea327>3.0.co;2-2;
RA Mueller S., Sandal T., Kamp-Hansen P., Dalboege H.;
RT "Comparison of expression systems in the yeasts Saccharomyces cerevisiae,
RT Hansenula polymorpha, Klyveromyces lactis, Schizosaccharomyces pombe and
RT Yarrowia lipolytica. Cloning of two novel promoters from Yarrowia
RT lipolytica.";
RL Yeast 14:1267-1283(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; AF054510; AAC08585.1; -; mRNA.
DR EMBL; CR382129; CAG81931.1; -; Genomic_DNA.
DR RefSeq; XP_501628.1; XM_501628.1.
DR AlphaFoldDB; O59949; -.
DR SMR; O59949; -.
DR STRING; 4952.CAG81931; -.
DR PRIDE; O59949; -.
DR EnsemblFungi; CAG81931; CAG81931; YALI0_C09141g.
DR GeneID; 2909710; -.
DR KEGG; yli:YALI0C09141g; -.
DR VEuPathDB; FungiDB:YALI0_C09141g; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; O59949; -.
DR OMA; AIRDMGM; -.
DR Proteomes; UP000001300; Chromosome C.
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 2: Evidence at transcript level;
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..460
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090972"
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 317
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 317
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 391
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT CONFLICT 334
FT /note="K -> N (in Ref. 1; AAC08585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 50084 MW; B7847B058CC9F91B CRC64;
MGKEKTHVNL VVIGHVDAGK STTTGHLIYK CGGIDKRTIE KFEKEADELG KGSFKYAWVL
DKLKAERERG ITIDIALWKF QTPKYYVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGV
GEFEAGISKD GQTREHALLA FTLGVKQLIV AINKMDSVKW SQDRYNEICK ETANFVKKVG
YNPKSVPFVP ISGWNGDNMI EASTNCDWYK GWTKETKAGE VKGKTLLEAI DAIEPPVRPS
DKPLRLPLQD VYKIGGIGTV PVGRVETGVI KAGMVVTFAP ANVTTEVKSV EMHHEILPDG
GFPGDNVGFN VKNVSVKDIR RGNVAGDSKN DPPKGCDSFN AQVIVLNHPG QIGAGYAPVL
DCHTAHIACK FDTLIEKIDR RTGKKMEDSP KFIKSGDAAI VKMVPSKPMC VEAFTEYPPL
GRFAVRDMRQ TVAVGVIKSV EKSDKAGGKV TKAAQKAAKK
