ID C0IZS1_9MUSC Unreviewed; 342 AA.
AC C0IZS1;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF1a {ECO:0000313|EMBL:ACN88522.1};
OS Blepharoneura sp. 27 MC-2007.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Blepharoneura.
OX NCBI_TaxID=535242 {ECO:0000313|EMBL:ACN88522.1};
RN [1] {ECO:0000313|EMBL:ACN88522.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ble-109 {ECO:0000313|EMBL:ACN88522.1};
RX PubMed=18487192; DOI=10.1126/science.1155832;
RA Condon M.A., Scheffer S.J., Lewis M.L., Swensen S.M.;
RT "Hidden neotropical diversity: greater than the sum of its parts.";
RL Science 320:928-931(2008).
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, ECO:0000256|RuleBase:RU000325}.
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 ECO:0000256|RuleBase:RU000325}.
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DR EMBL; EU602296; ACN88522.1; -; Genomic_DNA.
DR AlphaFoldDB; C0IZS1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 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; 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; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ACN88522.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ACN88522.1}.
FT DOMAIN 1..216
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACN88522.1"
FT NON_TER 342
FT /evidence="ECO:0000313|EMBL:ACN88522.1"
SQ SEQUENCE 342 AA; 37293 MW; 3BCF66D2EC44CD84 CRC64;
LIYKCGGIDK RTIEKFEKEA QEMGKGSFKY AWVLDKLKAE RERGITIDIA LWKFETAKYY
VTIIDAPGHR DFIKNMITGT SQADCAVLIV AAGTGEFEAG ISKNGQTREH ALLAFTLGVK
QLIVGVNKMD SSEPPYSEAR YEEIKKEVSS YIKKIGYNPA AVAFVPISGW HGDNMLEASS
NMPWFKGWKV ERKEGNAEGK TLIDALDAIL PPSRPTDKAL RLPLQDVYKI GGIGTVPVGR
VETGVLKPGM VVVFAPANIT TEVKSVEMHH EALPEAVPGD NVGFNVKNVS VKELRRGYVA
GDSKANPPKG AADFTAQVIV LNHPGQIANG YTPVLDCHTA HI
//
