ID B2BQT9_LIMLR Unreviewed; 298 AA.
AC B2BQT9;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=EF-1a {ECO:0000313|EMBL:ABV09005.1};
OS Limenitis lorquini (Lorquin's admiral) (Basilarchia lorquini).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Limenitidinae; Limenitidini; Limenitis.
OX NCBI_TaxID=342678 {ECO:0000313|EMBL:ABV09005.1};
RN [1] {ECO:0000313|EMBL:ABV09005.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18285285; DOI=10.1098/rspb.2007.1766;
RA Prudic K.L., Oliver J.C.;
RT "Once a Batesian mimic, not always a Batesian mimic: mimic reverts back to
RT ancestral phenotype when the model is absent.";
RL Proc. R. Soc. B 275:1125-1132(2008).
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; EF643329; ABV09005.1; -; Genomic_DNA.
DR AlphaFoldDB; B2BQT9; -.
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 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; IPR004160; Transl_elong_EFTu/EF1A_C.
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:ABV09005.1};
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:ABV09005.1}.
FT DOMAIN 1..151
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABV09005.1"
FT NON_TER 298
FT /evidence="ECO:0000313|EMBL:ABV09005.1"
SQ SEQUENCE 298 AA; 32100 MW; B9D130282395890D CRC64;
APGHRDFIKN MITGTSQADC AVLIVAAGTG EFEAGISKNG QTREHALLAF TLGVKQLIVG
VNKMDSTEPP YSESRFEEIK KEVSSYIKKI GYNPAAVAFV PISGWHGDNM LEASTKMPWF
KGWAVERKEG KADGKCLIEA LDAILPPARP TDKALRLPLQ DVYKIGGIGT VPVGRVETGV
LKPGTVVVFA PANITTEVKS VEMHHEALQE AVPGDNVGFN VKNVSVKELR RGYVAGDSKN
NPPKGAADFT AQVIVLNHPG QISNGYTPVL DCHTAHIACK FAEIKEKVDR RSGKSTEE
//
