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Database: UniProt
Entry: D8WM58_9AGAR
LinkDB: D8WM58_9AGAR
Original site: D8WM58_9AGAR 
ID   D8WM58_9AGAR            Unreviewed;       344 AA.
AC   D8WM58;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Translation elongation factor 1-alpha {ECO:0000313|EMBL:ADK11812.1};
DE   Flags: Fragment;
GN   Name=tef1 {ECO:0000313|EMBL:ADK11812.1};
OS   Hebeloma velutipes.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX   NCBI_TaxID=91683 {ECO:0000313|EMBL:ADK11812.1};
RN   [1] {ECO:0000313|EMBL:ADK11812.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AFTOL-ID 980 {ECO:0000313|EMBL:ADK11812.1};
RX   PubMed=20648753; DOI=10.3852/09-288;
RA   Binder M., Larsson K.H., Matheny P.B., Hibbett D.S.;
RT   "Amylocorticiales ord. nov. and Jaapiales ord. nov.: early diverging clades
RT   of agaricomycetidae dominated by corticioid forms.";
RL   Mycologia 102:865-880(2010).
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}.
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DR   EMBL; GU187707; ADK11812.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8WM58; -.
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; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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   InterPro; IPR004161; EFTu-like_2.
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   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; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:ADK11812.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:ADK11812.1}.
FT   DOMAIN          1..148
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADK11812.1"
FT   NON_TER         344
FT                   /evidence="ECO:0000313|EMBL:ADK11812.1"
SQ   SEQUENCE   344 AA;  37209 MW;  BF52CD3CEEDD38E8 CRC64;
     PGHRDFIKNM ITGTSQADCA IVIIAGGSGE FEAGISKDGQ TLEHALLAFT LGVRQLMVAV
     NKMDTTKWSE DRFTEIVKET STFIKKVGFN PKAVAFVSIS GWHGDNMLEE SPNMTWFKGW
     TKETKGGVVK GKTLLDAIDA IEPPVRPSDK PLRLPLQDVY KIGGIGTVPV GRVETGIIKA
     GMVVTFAPSN VTTEVKSVEM HHEQLEQGNP GDNVGFNVKN VSVKDIRRGN VASDSKNDPA
     KEAASFNAQV IVLNHPGQIG AGYAPVLDCH TAHIACKFAE LIEKIDRRTG KSIENAPKFV
     KSGDAAIVKL IPSKPMCVES YNEYPPLGRF AVRDMRQTVA VGVI
//
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