ID D8WM56_9AGAR Unreviewed; 344 AA.
AC D8WM56;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Translation elongation factor 1-alpha {ECO:0000313|EMBL:ADK11810.1};
DE Flags: Fragment;
GN Name=tef1 {ECO:0000313|EMBL:ADK11810.1};
OS Hygrocybe coccinea.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Hygrophoraceae; Hygrocybe.
OX NCBI_TaxID=378274 {ECO:0000313|EMBL:ADK11810.1};
RN [1] {ECO:0000313|EMBL:ADK11810.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AFTOL-ID 1715 {ECO:0000313|EMBL:ADK11810.1};
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; GU187705; ADK11810.1; -; Genomic_DNA.
DR AlphaFoldDB; D8WM56; -.
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 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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:ADK11810.1};
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:ADK11810.1}.
FT DOMAIN 1..149
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADK11810.1"
FT NON_TER 344
FT /evidence="ECO:0000313|EMBL:ADK11810.1"
SQ SEQUENCE 344 AA; 37529 MW; E4DE484372648368 CRC64;
APGHRDFIKN MITGTSQADC AILIIAVGTG EFEAGICKDG QTREHALLAF TLGVRQLIVA
INKMDTTKWS EDRFNEIVKE TSTFIKKVGY NPKAVAFVPI SGWHGDNMLE ESPNMTWYKG
WTRETKGGVV KGKTLLDAID PIEPPVRPHD KPLRLPLQDV YKIGGIGTVP VGRVETGIIK
AGMVVTFAPS NVTTEVKSVE MHHEQLEQGN PGDNVGFNVK NVSVKDIRRG NVASDSKNDP
AKEAASFNAQ VIVLNHPGQI SAGYAPVLDC HTAHIACKFA ELLEKIDRRT GKTMEQSPKS
VKSGDACIVK LIPSKPMCVE TYNEYPPLGR FAVRDMRQTV AVGV
//
