ID B4XVG5_9NEOP Unreviewed; 321 AA.
AC B4XVG5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=EF-1alpha {ECO:0000313|EMBL:ABX60820.1};
OS Lomographa semiclarata (bluish spring moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC Geometridae; Ennominae; Lomographa.
OX NCBI_TaxID=485638 {ECO:0000313|EMBL:ABX60820.1};
RN [1] {ECO:0000313|EMBL:ABX60820.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18672077; DOI=10.1016/j.ympev.2008.07.003;
RA Canfield M.R., Greene E., Moreau C.S., Chen N., Pierce N.E.;
RT "Exploring phenotypic plasticity and biogeography in emerald moths: A
RT phylogeny of the genus Nemoria (Lepidoptera: Geometridae).";
RL Mol. Phylogenet. Evol. 49:477-487(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; EU151696; ABX60820.1; -; Genomic_DNA.
DR AlphaFoldDB; B4XVG5; -.
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; 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:ABX60820.1};
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:ABX60820.1}.
FT DOMAIN 1..157
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 294..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABX60820.1"
FT NON_TER 321
FT /evidence="ECO:0000313|EMBL:ABX60820.1"
SQ SEQUENCE 321 AA; 34611 MW; 5E72098A3BDE0E6A CRC64;
YVTIIDAPGH RDFIKNMITG TSQADCAVLI VAAGTGEFEA GISKNGQTRE HALLAFTLGV
KQLIVGVNKM DSTEPPYSES RFEEIKKEVS SYIKKIGYNP AAVAFVPISG WHGDNMLEAS
TKMPWFKGWQ VERKEGKAEG KCLIEALDAI LPPARPTDKA LRLPLQDVYK IGGIGTVPVG
RVETGVLKPG TIVVFAPANI TTEVKSVEMH HEALQEAVPG DNVGFNVKNV SVKELRRGYV
AGDSKNNPPK GASDFTAQVI VLNHPGQISN GYTPVLDCHT AHIACKFAEI KEKVDRRTGK
STEDNPKSIK SGDAAIVNLV P
//
