ID C1IZV5_9PEZI Unreviewed; 313 AA.
AC C1IZV5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=TEF1 {ECO:0000313|EMBL:ACJ60576.1};
OS Ericboehmia curtisii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Hysteriales; Hysteriaceae; Ericboehmia.
OX NCBI_TaxID=574794 {ECO:0000313|EMBL:ACJ60576.1};
RN [1] {ECO:0000313|EMBL:ACJ60576.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 198.34 {ECO:0000313|EMBL:ACJ60576.1};
RX PubMed=19422072; DOI=10.1016/j.mycres.2008.12.001;
RA Boehm E.W., Schoch C.L., Spatafora J.W.;
RT "On the evolution of the Hysteriaceae and Mytilinidiaceae
RT (Pleosporomycetidae, Dothideomycetes, Ascomycota) using four nuclear
RT genes.";
RL Mycol. Res. 113:461-479(2009).
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; FJ161093; ACJ60576.1; -; Genomic_DNA.
DR AlphaFoldDB; C1IZV5; -.
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 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:ACJ60576.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:ACJ60576.1}.
FT DOMAIN 1..125
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACJ60576.1"
FT NON_TER 313
FT /evidence="ECO:0000313|EMBL:ACJ60576.1"
SQ SEQUENCE 313 AA; 34001 MW; 8751E101DAECE04F CRC64;
IIAAGTGEFE AGISKDGQTR EHALLAYTLG VKQLIVAINK MDTTKWSEER YNEIIKETSN
FIKKVGYNPK TVPFVPISGF NGDNMIEPSP NCPWYKGWEK ETKTKASGKT LLEAIDNIDP
PARPSDKPLR LPLQDVYKIG GIGTVPVGRV ETGTIKAGMV VTFAPAGVTT EVKSVEMHHE
QLTEGLPGDN VGFNVKNVSV KEIRRGNVAG DSKNDPPKGC DSFNAQVIVL NHPGQVGAGY
APVLDCHTAH IACKFSELLE KIDRRTGKSI ENNPKTIKSG DAAIVKMIPS KPMCVEAFTE
YPPLGRFAVR DMV
//