EF1A4_OSCTI
ID EF1A4_OSCTI Reviewed; 459 AA.
AC Q2HJN9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Elongation factor 1-alpha 4;
DE Short=EF-1-alpha-4;
GN Name=eft-4;
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:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AY928337; AAY17221.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2HJN9; -.
DR SMR; Q2HJN9; -.
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 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 4"
FT /id="PRO_0000303017"
FT DOMAIN 5..242
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
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; 50212 MW; 5814E0B71FF53A19 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 NEKNVSVKDI RRGSVCSDSK NDPAKESKSF TAQVIVMNHP GQIGAGYTPV
LDCHTAHIAC KFAELKEKVD RRTGKKVEDL PKFLKSGDAG IVELIPTKPL CVEAFTDYAP
LGRFAVRDMR QTVAVGVIKG VTKDDGSSGK VTKSAQKKK