(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMN8_DEBHA

ID   Q6BMN8_DEBHA            Unreviewed;       458 AA.
AC   Q6BMN8;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 110.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN   OrderedLocusNames=DEHA2D02376g {ECO:0000313|EMBL:CAG86703.1},
GN   DEHA2F03828g {ECO:0000313|EMBL:CAG88847.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88847.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88847.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599}, and CBS767
RC   {ECO:0000313|EMBL:CAG88847.1};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2] {ECO:0000313|EMBL:CAG88847.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS767 {ECO:0000313|EMBL:CAG88847.1};
RA   Genoscope - CEA;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000256|RuleBase:RU000325}.
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|RuleBase:RU000325}.
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DR   EMBL; CR382136; CAG86703.1; -; Genomic_DNA.
DR   EMBL; CR382138; CAG88847.1; -; Genomic_DNA.
DR   RefSeq; XP_458571.1; XM_458571.1.
DR   RefSeq; XP_460533.1; XM_460533.1.
DR   STRING; 4959.XP_460533.1; -.
DR   EnsemblFungi; CAG86703; CAG86703; DEHA2D02376g.
DR   EnsemblFungi; CAG88847; CAG88847; DEHA2F03828g.
DR   GeneID; 2901793; -.
DR   GeneID; 2903438; -.
DR   KEGG; dha:DEHA2D02376g; -.
DR   KEGG; dha:DEHA2F03828g; -.
DR   HOGENOM; HOG000229291; -.
DR   KO; K03231; -.
DR   OMA; YKGWTKE; -.
DR   OrthoDB; 1150082at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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   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; TF_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;
DR   PRODOM; Q6BMN8.
DR   SWISS-2DPAGE; Q6BMN8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Elongation factor {ECO:0000256|RuleBase:RU000325};
KW   GTP-binding {ECO:0000256|RuleBase:RU000325};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000325};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU000325};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN        5    240       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
SQ   SEQUENCE   458 AA;  49931 MW;  83C20F16E695742D CRC64;
     MGKEKTHVNL VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL
     DKLKAERERG ITIDIALWKF ETPKFHVTII DAPGHRDFIK NMITGTSQAD CAILIIAGGI
     GEFEAGISKD GQTREHALLA YTLGVKQLIV AINKMDSVKW DKNRYDEIVK ECSNFVKKVG
     FNPKSVPFVP ISGWNGDNMI EASPNCPWYK GWEKETKAGK SSGKTLLEAI DAIEPPSRPT
     DKPLRLPLQD VYKIGGIGTV PVGRVETGII KAGMVVTFAP AGVTTEVKSV EMHHEQLTEG
     VPGDNVGFNV KNVSVKEIRR GNVCGDSKND TPKGCDSFAA QVIVLNHPGQ ISSGYSPVLD
     CHTAHIACKF DTLIEKIDRR TGKKLEDNPK FIKSGDAAIV KMVPSKPMCV EAFTDYPPLG
     RFAVRDMRQT VAVGVIKSVE KSDKAGKVTK AAQKAAKK
//

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