ID   A9XIY1_9HYPO            Unreviewed;       326 AA.
AC   A9XIY1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE   Flags: Fragment;
GN   Name=tef {ECO:0000313|EMBL:ABU98730.1};
OS   Cordyceps bifusispora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=48690 {ECO:0000313|EMBL:ABU98730.1};
RN   [1] {ECO:0000313|EMBL:ABU98730.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EFCC 8260 {ECO:0000313|EMBL:ABU98730.1};
RX   PubMed=18490993; DOI=10.3114/sim.2007.57.01;
RA   Sung G.-H., Hywel-Jones N.L., Sung J.-M., Luangsa-ard J.J., Shrestha B.,
RA   Spatafora J.W.;
RT   "Phylogenetic classification of Cordyceps and the clavicipitaceous fungi.";
RL   Stud. Mycol. 57:5-59(2007).
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; EF468747; ABU98730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9XIY1; -.
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; IPR004160; Transl_elong_EFTu/EF1A_C.
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:ABU98730.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:ABU98730.1}.
FT   DOMAIN          1..141
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABU98730.1"
FT   NON_TER         326
FT                   /evidence="ECO:0000313|EMBL:ABU98730.1"
SQ   SEQUENCE   326 AA;  35322 MW;  9B02C74DB15568AC CRC64;
     KNMITGTSQA DCAILIIAAG TGEFEAGISK DGQTREHALL AFTLGVKQLI VAINKMDTTQ
     WSEARFQEII KETSNFIKKV GYNPKTVAFV PISGFHGDNM LAASTNCPWY KGWEKETKSG
     KYTGKTLLEA IDSIEPPTRP TDKPLRLPLQ DVYKIGGIGT VPVGRVETGI IKPGMVVTFA
     PSNVTTEVKS VEMHHEQLPE GVPGDNVGFN VKNVSVKEIR RGNVAGDSKN DPPMGAASFN
     AQVIVINHPG QIGNGYAPVL DCHTAHIACK FSELLEKIDR RTGKSVENNP KFIKSGDSAI
     VKMVPSKPMC VEAFTDYPPL GRFAVR
//