ID O02477_9HEXA Unreviewed; 364 AA.
AC O02477;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Tomocerus sp. jcrjws2.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Tomoceroidea; Tomoceridae; Tomocerus.
OX NCBI_TaxID=58789 {ECO:0000313|EMBL:AAC03158.1};
RN [1] {ECO:0000313|EMBL:AAC03158.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9287423;
RA Regier J.C., Shultz J.W.;
RT "Molecular phylogeny of the major arthropod groups indicates polyphyly of
RT crustaceans and a new hypothesis for the origin of hexapods.";
RL Mol. Biol. Evol. 14:902-913(1997).
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; U90059; AAC03158.1; -; mRNA.
DR AlphaFoldDB; O02477; -.
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:SF170; ELONGATION FACTOR 1-ALPHA 2; 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 2: Evidence at transcript level;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:AAC03158.1};
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:AAC03158.1}.
FT DOMAIN 1..183
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC03158.1"
FT NON_TER 364
FT /evidence="ECO:0000313|EMBL:AAC03158.1"
SQ SEQUENCE 364 AA; 39629 MW; 10DB88FF4EE54F46 CRC64;
LDKLKAERER GITIDIALWK FETAKYYVTI IDAPGHRDFI KNMITGTSQA DCAVLIVAAG
TGEFEAGISK NGQTREHALL AYTLGVKQLI VGVNKMDSTE PPYSETRFEE IKKEVSNYIK
KIGYNPAAVA FVPISGWNGD NMLEVSDKMS WFKGWKVERK DGNADGKCLI EALDAILPPS
RPTDKALRLP LQDVYKIGGI GTVPVGRVET GILKPGMVVT FAPTALTTEV KSVEMHHEAL
TEAVPGDNVG FNVKNVSVKE LRRGYVAGDT KVSPPKGAAD FSAQVIVLNH PGQISNGYCP
VLDCHTAHIA CKFQEIKEKC DRRTGKTTEE NPKAIKSGDA AIVTLVPTKP MCVEAFTDFP
PLGR
//
