EF1A_ASHGO
ID EF1A_ASHGO Reviewed; 458 AA.
AC P41752; Q7Z8W1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=TEF; OrderedLocusNames=ADL370C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=8107673; DOI=10.1007/bf00280415;
RA Steiner S., Philippsen P.;
RT "Sequence and promoter analysis of the highly expressed TEF gene of the
RT filamentous fungus Ashbya gossypii.";
RL Mol. Gen. Genet. 242:263-271(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-397.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=12748053; DOI=10.1016/s1567-1356(03)00012-6;
RA Kurtzman C.P., Robnett C.J.;
RT "Phylogenetic relationships among yeasts of the 'Saccharomyces complex'
RT determined from multigene sequence analyses.";
RL FEMS Yeast Res. 3:417-432(2003).
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; X73978; CAA52157.1; -; Genomic_DNA.
DR EMBL; AE016817; AAS51550.1; -; Genomic_DNA.
DR EMBL; AF402087; AAP86548.1; -; Genomic_DNA.
DR PIR; S41593; S41593.
DR RefSeq; NP_983726.1; NM_209079.1.
DR AlphaFoldDB; P41752; -.
DR SMR; P41752; -.
DR STRING; 33169.AAS51550; -.
DR PRIDE; P41752; -.
DR EnsemblFungi; AAS51550; AAS51550; AGOS_ADL370C.
DR GeneID; 4619861; -.
DR KEGG; ago:AGOS_ADL370C; -.
DR eggNOG; KOG0052; Eukaryota.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P41752; -.
DR OMA; AIRDMGM; -.
DR Proteomes; UP000000591; Chromosome IV.
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"
FT /id="PRO_0000090952"
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; 49926 MW; 66C7CA74BA72D39F CRC64;
MGKEKTHVNV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETPKYHVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGV
GEFEAGISKD GQTREHALLA YTLGVKQLIV AINKMDSVKW DESRYQEIVK ETSNFIKKVG
YNPKTVPFVP ISGWNGDNMI EATTNAPWYK GWEKETKAGA VKGKTLLEAI DAIEPPVRPT
DKALRLPLQD VYKIGGIGTV PVGRVETGVI KPGMVVTFAP SGVTTEVKSV EMHHEQLEEG
VPGDNVGFNV KNVSVKEIRR GNVCGDSKND PPKAAESFNA TVIVLNHPGQ ISAGYSPVLD
CHTAHIACKF DELLEKNDRR TGKKLEDSPK FLKAGDAAMV KFVPSKPMCV EAFTDYPPLG
RFAVRDMRQT VAVGVIKSVV KSDKAGKVTK AAQKAGKK
