ID E5BB53_LUCCA Unreviewed; 380 AA.
AC E5BB53;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF-1a {ECO:0000313|EMBL:CBX87329.1};
OS Lucilia caesar (Green bottle fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=65466 {ECO:0000313|EMBL:CBX87329.1};
RN [1] {ECO:0000313|EMBL:CBX87329.1}
RP NUCLEOTIDE SEQUENCE.
RA McDonagh L.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBX87329.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21867590; DOI=10.1017/S0031182011001089;
RA McDonagh L.M., Stevens J.R.;
RT "The molecular systematics of blowflies and screwworm flies (Diptera:
RT Calliphoridae) using 28S rRNA, COX1 and EF-1a: insights into the evolution
RT of dipteran parasitism.";
RL Parasitology 138:1760-1777(2011).
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; FR719239; CBX87329.1; -; Genomic_DNA.
DR AlphaFoldDB; E5BB53; -.
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:CBX87329.1};
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:CBX87329.1}.
FT DOMAIN 1..194
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CBX87329.1"
SQ SEQUENCE 380 AA; 41310 MW; 6968E9A5626A04FF CRC64;
MGKGSFKYAW VLDKLKAERE RGITIDIALW KFETSKYYVT IIDAPGHRDF IKNMITGTSQ
ADCAVLIVAA GTGEFEAGIS KNGQTREHAL LAFTLGVKQL IVGVNKMDSS EPPYSEARYE
EIKKEVSSYI KKIGYNPASV AFVPISGWHG DNMLEASTNM PWFKGWKIER KDGNAEGKTL
IDALDAILPP TRPTEKPLRL PLQDVYKIGG IGTVPVGRVE TGVLKPGTVV VFAPANITTE
VKSVEMHHEA LVEAVPGDNV GFNVKNVSVK ELRRGYVAGD SKANPPKGAA DFTAQVIVLN
HPGQISNGYT PVLDCHTAHI ACKFAEIKEK VDRRSGKTTE DQPNSSSLVM PPSSTWSPPS
LCALKPSKNS PHWVVSLSVT
//