ID Q2LB04_9NEOP Unreviewed; 413 AA.
AC Q2LB04;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF1-alpha {ECO:0000313|EMBL:ABC68697.1};
OS Atlanteuptychia ernestina.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Satyrini; Euptychiina; Atlanteuptychia.
OX NCBI_TaxID=1648414 {ECO:0000313|EMBL:ABC68697.1};
RN [1] {ECO:0000313|EMBL:ABC68697.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16563805; DOI=10.1016/j.ympev.2006.02.007;
RA Pena C., Wahlberg N., Weingartner E., Kodandaramaiah U., Nylin S.,
RA Freitas A.V., Brower A.V.;
RT "Higher level phylogeny of Satyrinae butterflies (Lepidoptera: Nymphalidae)
RT based on DNA sequence data.";
RL Mol. Phylogenet. Evol. 40:29-49(2006).
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; DQ338936; ABC68697.1; -; Genomic_DNA.
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 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; 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; IPR009001; Transl_elong_EF1A/Init_IF2_C.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
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:ABC68697.1};
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:ABC68697.1}.
FT DOMAIN 1..271
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABC68697.1"
FT NON_TER 413
FT /evidence="ECO:0000313|EMBL:ABC68697.1"
SQ SEQUENCE 413 AA; 45178 MW; 41F0EA43D757304F CRC64;
HVDSGKSTTT GHLIYKCGGI DNGTIEKFEK EAQEMGKGSF KYAWVLDKLK AERERGITID
IALWKFETAK YYVTIIDAPG HRDFIKNMIT GTSQADCAVL IVAAGTGEFE AGISKNGQTR
EHALLAFTLG VKQLIVGVNK MDSTEPPYSE SRFEEIKKEV SSYIKKIGYN PAAVAFVPIS
GWHGDNMLEP SXKMPWFXGW XVERXDGKAD GKCLIXALDA XXXXXXXXXX XXXXXXXXXX
XXXXXGXVTV XXVETGILKT GTIVVFAPAN ITTEVKSVEM HHEALXEAVP GDNVRFNVKN
VSVKELRRGY VAGDSKNNPP KGAADFNAQV IVLNHPXQIS NGYTPVLDCH TAHIACKFAE
IKEKVDRRTG KSTEDNPKSI KSGDAAIVNL VPSKPLCVEA FQEFPPLGRF AVR
//
