ID Q7Z8X5_9ASCO Unreviewed; 376 AA.
AC Q7Z8X5;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Hanseniaspora vineae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=56409 {ECO:0000313|EMBL:AAP86532.1};
RN [1] {ECO:0000313|EMBL:AAP86532.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL Y-17529 {ECO:0000313|EMBL:AAP86532.1};
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 {ECO:0000256|RuleBase:RU000325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249,
CC ECO:0000256|RuleBase:RU000325}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF402071; AAP86532.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7Z8X5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:AAP86532.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:AAP86532.1}.
FT DOMAIN 1..219
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP86532.1"
FT NON_TER 376
FT /evidence="ECO:0000313|EMBL:AAP86532.1"
SQ SEQUENCE 376 AA; 41273 MW; 105A2E09810C298A CRC64;
TTTGHLIYKC GGIDKRTIEK FEKEAAELGK GSFKYAWVLD KLKAERERGI TIDIALWKFE
TPKYQVTVID APGHRDFIKN MITGTSQADC AILIIAGGVG EFEAGISKDG QTREHALLAY
TLGVKQLIVA INKMDSVKWD ESRYQEIVKE TSNFIKKVGY NPKTVAFVPI SGWNGDNMIE
ATTNAPWYKG WEKEVKGNVV KGKTLLEAID SIDPPSRPTD KPLRLPLQDV YKIGGIGTVP
VGRVETGVIK PGMVVTFAPA GVTTEVKSVE MHHEQLTEGL PGDNVGFNVK NVSVKEIRRG
NVCGDSKNDP PQNSISFNAQ VIILNHPGQI SAGYSPVLDC HTAHIACRFD ELIQKNDRRS
GKKLEDAPKF LKAGDA
//
