ID   EF1A3_OSCTI             Reviewed;         460 AA.
AC   Q2HJN6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Elongation factor 1-alpha 3;
DE            Short=EF-1-alpha-3;
GN   Name=eft-3;
OS   Oscheius tipulae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Rhabditinae;
OC   Oscheius.
OX   NCBI_TaxID=141969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CEW1;
RA   Akamine R.N., Winter C.E.;
RT   "Four eEF1A genes from a Rhabditid nematode.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY928340; AAY17224.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2HJN6; -.
DR   SMR; Q2HJN6; -.
DR   PRIDE; Q2HJN6; -.
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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_A; EF_Tu_A; 1.
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   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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis.
FT   CHAIN           1..460
FT                   /note="Elongation factor 1-alpha 3"
FT                   /id="PRO_0000303016"
FT   DOMAIN          6..243
FT                   /note="tr-type G"
FT   REGION          15..22
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          71..75
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          92..95
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          154..157
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          195..197
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         302
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         375
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   460 AA;  50048 MW;  8FED68E2F2A5FD39 CRC64;
     MGKGDKTHIN IVVIGHVDSG KSTTTGHLIY KCGGIDKRTI EKFEKEAQEM GKGSFKYAWV
     LDKLKAERER GITIDIALWK FETAKFYVTI IDAPGHRDFI KNMITGTSQA DCAVLVVACG
     TGEFEAGISK NGQTREHALL AQTLGVKQMI VACNKMDSTE PPFSEKRFDE IVTEVKSFLK
     KVGYNPATIP FVPISGFNGD NMLEPSSNMS WYKGWSVERK EGNASGKTLI EALDCIIPPQ
     RPTDRPLRLP LQDVYKIGGI GTVPVGRVET GVIKPGMVVT FAPQNVTTEV KSVEMHHESL
     PEASPGDNVG FNVKNVSVKD IRRGSVCSDS KNDPAKESKN FTAQVIVMNH PGQISAGYTP
     VLDCHTAHIA CKFAELKEKV DRRTGKSTEA SPKFLKSGDA GIVELIPTKP PCVESFTDYA
     PLGRFAVRDM RQTVAVGVIK SVTKDDGSGG KVTKSAAKKK