ID A0A1X9FXZ4_9HYPO Unreviewed; 302 AA. AC A0A1X9FXZ4; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 27-MAR-2024, entry version 13. DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870}; DE Flags: Fragment; GN Name=EF-1a {ECO:0000313|EMBL:AHY24892.1}; OS Aschersonia sp. JZQ-2014a. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Aschersonia. OX NCBI_TaxID=1481783 {ECO:0000313|EMBL:AHY24892.1}; RN [1] {ECO:0000313|EMBL:AHY24892.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GXNG2012-05 {ECO:0000313|EMBL:AHY24890.1}, GXSW2012-02 RC {ECO:0000313|EMBL:AHY24891.1}, GXSW2012-04 RC {ECO:0000313|EMBL:AHY24892.1}, GXSW2012-08 RC {ECO:0000313|EMBL:AHY24893.1}, HNQX2012-06 RC {ECO:0000313|EMBL:AHY24894.1}, HNQX2012-11 RC {ECO:0000313|EMBL:AHY24895.1}, and HNXL2012-05 RC {ECO:0000313|EMBL:AHY24897.1}; RA Qiu J.Z., Qiu Y.F., Su Y.B., He X.Y., Su S.B., Wang P.K., Qiu Y.B.; RT "Molecular systematic of Aschersonia."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- 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; KF137691; AHY24890.1; -; Genomic_DNA. DR EMBL; KF137692; AHY24891.1; -; Genomic_DNA. DR EMBL; KF137693; AHY24892.1; -; Genomic_DNA. DR EMBL; KF137694; AHY24893.1; -; Genomic_DNA. DR EMBL; KF137695; AHY24894.1; -; Genomic_DNA. DR EMBL; KF137696; AHY24895.1; -; Genomic_DNA. DR EMBL; KF137698; AHY24897.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1X9FXZ4; -. 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; 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 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:AHY24892.1}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein biosynthesis {ECO:0000313|EMBL:AHY24892.1}. FT DOMAIN 1..130 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AHY24892.1" FT NON_TER 302 FT /evidence="ECO:0000313|EMBL:AHY24892.1" SQ SEQUENCE 302 AA; 32506 MW; 0332AC5DB176E32A CRC64; CAILIIAAGT GEFEAGISKD GQTREHALLA YTLGVKQLIV AINKMDTAKW AEARYQEIIK ETSNFIKKVG YNPKTVAFVP ISGFNGDNML QASTNCPWYK GWEKETKAGK STGKTLLEAI DSIEPPKRPT DKPLRLPLQD VYKIGGIGTV PVGRIETGVL KPGMVVTFAP SNVTTEVKSV EMHHEQLAEG VPGDNVGFNV KNVSVKDIRR GNVAGDTKND PPQGAASFDA QVIVLNHPGQ VGAGYAPVLD CHTAHIACKF AEIREKIDRR TGKAVEEAPK FIKSGDSAIV KMVPSKPMCV EA //