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Database: UniProt
Entry: Q9GSK7_9DIOP
LinkDB: Q9GSK7_9DIOP
Original site: Q9GSK7_9DIOP 
ID   Q9GSK7_9DIOP            Unreviewed;       344 AA.
AC   Q9GSK7;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Elongation factor-1 alpha {ECO:0000313|EMBL:AAG30439.1};
DE   Flags: Fragment;
GN   Name=EF-1a {ECO:0000313|EMBL:AAG30439.1};
OS   Diasemopsis meigenii.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Diopsoidea;
OC   Diopsidae; Diasemopsis.
OX   NCBI_TaxID=139646 {ECO:0000313|EMBL:AAG30439.1};
RN   [1] {ECO:0000313|EMBL:AAG30439.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12116597; DOI=10.1080/106351501750107512;
RA   Baker R.H., Wilkinson G.S., DeSalle R.;
RT   "Phylogenetic utility of different types of molecular data used to infer
RT   evolutionary relationships among stalk-eyed flies (Diopsidae).";
RL   Syst. Biol. 50:87-105(2001).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003982}.
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; AF303182; AAG30439.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9GSK7; -.
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; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00483; EF-1_alpha; 1.
DR   PANTHER; PTHR23115:SF236; ELONGATION FACTOR 1-ALPHA 1; 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; 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:AAG30439.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein biosynthesis {ECO:0000313|EMBL:AAG30439.1}.
FT   DOMAIN          1..164
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAG30439.1"
FT   NON_TER         344
FT                   /evidence="ECO:0000313|EMBL:AAG30439.1"
SQ   SEQUENCE   344 AA;  37255 MW;  EF1DCABDA88B5452 CRC64;
     KFETSKYYVT IIDAPGHRDF IKNMITGTSQ ADCAVLIVAA GTGEFEAGIS KNGQTREHAL
     LAFTLGVKQL IVGVNKMDSS EPPYSEARYE EIKKEVSSYI KKIGYNPAAV AFVPISGWHG
     DNMLEPSTNM PWFKGWKIER KEGNAEGKTL IDALDAILPP SRPTEKPLRL PLQDVYKIGG
     IGTVPVGRVE TGVLKPGCVV VFAPANITTE VKSVEMHHEA LTEAVPGDNV GFNVKNVSVK
     ELRRGYVAGD SKNSPPKGAA DFTAQVIVLN HPGQIGNGYT PVLDCHTAHI ACKFAEIKEK
     VDRRSGKTTE ENPKFIKSGD AAIVNLVPSK PLCVESFQEF PPLG
//
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