ID Q8MWJ0_PANCO Unreviewed; 363 AA.
AC Q8MWJ0;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Elongation factor 1-alpha {ECO:0000313|EMBL:AAM53494.1};
DE Flags: Fragment;
GN Name=Ef-1a {ECO:0000313|EMBL:AAM53494.1};
OS Panorpa communis (Common scorpionfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Mecoptera; Panorpidae; Panorpa.
OX NCBI_TaxID=52816 {ECO:0000313|EMBL:AAM53494.1};
RN [1] {ECO:0000313|EMBL:AAM53494.1}
RP NUCLEOTIDE SEQUENCE.
RA Whiting M.F.;
RT "Mecoptera is paraphyletic: Multiple genes and phylogeny of Mecoptera and
RT Siphonaptera.";
RL Zool. Scr. 31:93-104(2002).
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}.
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; AF423857; AAM53494.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8MWJ0; -.
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; 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; 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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:AAM53494.1};
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:AAM53494.1}.
FT DOMAIN 1..177
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAM53494.1"
FT NON_TER 363
FT /evidence="ECO:0000313|EMBL:AAM53494.1"
SQ SEQUENCE 363 AA; 39380 MW; 84990816A4EF0789 CRC64;
ERERGITIDI ALWKFETAKY YVTIIDAPGH RDFIKNMITG TSQADCAVLI VAAGTGEFEA
GISKNGQTRE HALLAFTLGV KQLIVGVNKM DSTEPPYSES RFEEIKKEVS SYIKKIGYNP
AAVAFVPISG WHGDNMLEVS SKMGWFKGWA VERKEGKADG KCLIEALDAI LPPARPTDKP
LRLPLQDVYK IGGIGTVPVG RVETGVLKPG TVVVFAPANL TTEVKSVEMH HEALQEAVPG
DNVGFNVKNV SVKELRRGYV AGDSKANPPK GAADFTAQVI VLNHPGQISN GYTPVLDCHT
AHIACKFAEI KEKVDRRTGK STEDNPKAIK SGDAAIVVLV PSKPMCVESF QEFPPLGRFA
VRD
//
