ID E5E7V8_9PEZI Unreviewed; 327 AA.
AC E5E7V8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
OS Colletotrichum sp. GJS08_147.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=926764 {ECO:0000313|EMBL:ADQ55435.1};
RN [1] {ECO:0000313|EMBL:ADQ55435.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GJS08_147 {ECO:0000313|EMBL:ADQ55435.1};
RX PubMed=20943565; DOI=10.3852/09-244;
RA Rojas E.I., Rehner S.A., Samuels G.J., Van Bael S.A., Herre E.A.,
RA Cannon P., Chen R., Pang J., Wang R., Zhang Y., Peng Y.Q., Sha T.;
RT "Colletotrichum gloeosporioides s.l. associated with Theobroma cacao and
RT other plants in Panama: multilocus phylogenies distinguish host-associated
RT pathogens from asymptomatic endophytes.";
RL Mycologia 102:1318-1338(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}.
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; GU994495; ADQ55435.1; -; Genomic_DNA.
DR AlphaFoldDB; E5E7V8; -.
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:ADQ55435.1};
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:ADQ55435.1}.
FT DOMAIN 1..140
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADQ55435.1"
FT NON_TER 327
FT /evidence="ECO:0000313|EMBL:ADQ55435.1"
SQ SEQUENCE 327 AA; 35269 MW; 005DBA08234C8471 CRC64;
NMITGTSQAD CAILIIAAGT GEFEAGISKD GQTREHALLA YTLGVKQLIV AINKMDTTKW
SEDRYQEIIK ETSNFIKKVG YNPKTVAFVP ISGFHGDNML APTTNASWYK GWEKEGKGGK
VTGKTLLEAI DSIEPPKRPT DKPLRLPLQD VYKIGGIGTV PVGRIETGVL KPGMVVTFAP
ANVTTEVKSV EMHHEQLTEG VPGDNVGFNV KNVSVKDIRR GNVAGDSKND PPAGAASFNA
QVIVLNHPGQ VGAGYAPVLD CHTAHIACKF SEILEKIDRR TGKSVENNPK FIKSGDAAIV
KMVPSKPMCV EPFTDYPPLG RFAVRDM
//