ID A7TKD1_VANPO Unreviewed; 457 AA.
AC A7TKD1;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN ORFNames=Kpol_538p18 {ECO:0000313|EMBL:EDO17258.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO17258.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480407; EDO17258.1; -; Genomic_DNA.
DR RefSeq; XP_001645116.1; XM_001645066.1.
DR AlphaFoldDB; A7TKD1; -.
DR STRING; 436907.A7TKD1; -.
DR GeneID; 5545464; -.
DR KEGG; vpo:Kpol_538p18; -.
DR eggNOG; KOG0052; Eukaryota.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; A7TKD1; -.
DR OMA; RDMGQTV; -.
DR OrthoDB; 5477300at2759; -.
DR PhylomeDB; A7TKD1; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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 CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000000267}.
FT DOMAIN 5..240
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 457 AA; 49791 MW; 9E8F1F55EB2B1D48 CRC64;
MGKEKSHVNV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETPKYQVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGV
GEFEAGISKD GQTREHALLA YTLGVKQLIV AVNKMDSVNW DESRFQEICK ETSNFIKKVG
YNPKTVPFVP ISGWNGDNMI EATTNAPWYK GWEKETKAGV VKGKTLLEAI DAIVQPTRPT
DKALRLPLQD VYKIGGIGTV PVGRVETGVI KPGMVVTFAP AGVTTEVKSV EMHHEQLTEG
LPGDNVGFNV KNVSVKEIRR GNVCGDSKND PPKASESFNA TVIVLNHPGQ ISAGYSPVLD
CHTAHIACRF DELLEKNDRR SGKKLEDSPK FLKSGDAALV KFVPSKPMCV EAFTDYPPLG
RFAVRDMRQT VAVGVIKSVV KTDKAGKVTK AAQKAAK
//
