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Database: UniProt
Entry: A0A318ZWR2_ASPLB
LinkDB: A0A318ZWR2_ASPLB
Original site: A0A318ZWR2_ASPLB 
ID   A0A318ZWR2_ASPLB        Unreviewed;       543 AA.
AC   A0A318ZWR2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
GN   ORFNames=BO96DRAFT_450312 {ECO:0000313|EMBL:PYH51741.1};
OS   Aspergillus lacticoffeatus (strain CBS 101883).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH51741.1, ECO:0000313|Proteomes:UP000247441};
RN   [1] {ECO:0000313|EMBL:PYH51741.1, ECO:0000313|Proteomes:UP000247441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH51741.1,
RC   ECO:0000313|Proteomes:UP000247441};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) 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}.
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DR   EMBL; KZ821376; PYH51741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318ZWR2; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000247441; Unassembled WGS sequence.
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   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd01883; EF1_alpha; 1.
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   HAMAP; MF_00118_A; EF_Tu_A; 1.
DR   InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
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   Pfam; PF02150; RNA_POL_M_15KD; 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; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:PYH51741.1};
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:PYH51741.1}.
FT   DOMAIN          89..324
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   543 AA;  59433 MW;  F6B2B057BC2C608A CRC64;
     MPLTFCPNCS NALTISRAEP TTRHPLGVNR FECRTCPYQY ALDQSWFEKT PMKQKEVEDV
     FGGKEEFANA DSMARHGLTG IFYNSKEDKT HINIVVIGHV DSGKSTTTGH LIYKCGGIDQ
     RTIEKFEKEA AELGKGSFKY AWVLDKLKSE RERGITIDIA LWKFQTGKYE VTVIDAPGHR
     DFIKNMITGT SQADCAILII ASGTGEFEAG ISKDGQTREH ALLAFTLGVR QLIVALNKMD
     TCKWSEDRYN EIVKETSNFI KKVGYNPKGV PFVPISGFNG DNMLEPSPNC PWYKGWEKET
     KAGKVTGKTL LEAIDAIEPP VRPSNKPLRL PLQDVYKISG IGTVPVGRVE TGIIAPGMVV
     TFAPANVTTE VKSVEMHHQQ LKEGVPGDNV GFNVKNVSVK EVRRGNVAGD SKNDPPLGCE
     SFTAQVIVLN HPGQVGAGYA PVLDCHTAHI ACKFAELLEK IDRRTGKSVE SSPKFIKSGD
     AAIVKMIPSK PMCVEAFTDY PPLGRFAVRD MRQTVAVGVI KAVEKKEGGS GKVTKAAQKA
     GKK
//
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