ID   EF1A2_OSCTI             Reviewed;         459 AA.
AC   Q2HJN8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Elongation factor 1-alpha 2;
DE            Short=EF-1-alpha-2;
GN   Name=eft-2;
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; AY928338; AAY17222.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2HJN8; -.
DR   SMR; Q2HJN8; -.
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..459
FT                   /note="Elongation factor 1-alpha 2"
FT                   /id="PRO_0000303015"
FT   DOMAIN          5..242
FT                   /note="tr-type G"
FT   REGION          14..21
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          70..74
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          91..94
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          153..156
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          194..196
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         301
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         374
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  50079 MW;  4371BD93B049B0C9 CRC64;
     MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL
     DKLKAERERG ITIDIALWKF ETAKFYVTII DAPGHRDFIK NMITGTSQAD CAVLVVACGT
     GEFEAGISKN GQTREHALLA QTLGVKQMIV ACNKMDSTEP PFSEKRFEEI ITEVKSFIKK
     IGYNPATIPF VPISGFNGDN MLEPSANMSW YKGWSVERKE GNASGKTLLE ALDCIIPPQR
     PTDRPLRLPL QDVYKIGGIG TVPVGRVETG VIKPGMVVTF APQNVTTEVK SVEMHHESLP
     EAQPGDNVGF NVKNVSVKDI RRGSVCSDSK NDPAKESKSF TAQVIVMNHP GQIGAGYTPV
     LDCHTAHIAC KFAELKEKVD RRTGKKVEDP PKFLKSGDAG IVELIPTKPL CVEAFTDYAP
     LGRFAVRDMR QTVAVGVIKG VTKDDGSGGK VTKSAAKKK