EF1A_ORYLA
ID EF1A_ORYLA Reviewed; 461 AA.
AC Q9YIC0;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=eef1a; Synonyms=ef1a;
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HNI-I; TISSUE=Liver;
RA Kinoshita M.;
RT "Medaka polypeptide elongation factor 1 alpha.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HNI-1;
RA Kinoshita M.;
RT "Structure and transcription of the gene cording for polypeptide chain
RT elongation factor 1a of medaka Oryzias latipes.";
RL Submitted (DEC-1998) 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 -!- SUBCELLULAR LOCATION: Cytoplasm.
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; AB013606; BAA34370.1; -; mRNA.
DR EMBL; AB020734; BAA78376.1; -; Genomic_DNA.
DR PIR; T51991; T51991.
DR RefSeq; NP_001098132.1; NM_001104662.1.
DR RefSeq; XP_011479259.1; XM_011480957.1.
DR AlphaFoldDB; Q9YIC0; -.
DR SMR; Q9YIC0; -.
DR STRING; 8090.ENSORLP00000009543; -.
DR Ensembl; ENSORLT00000009544; ENSORLP00000009543; ENSORLG00000007614.
DR Ensembl; ENSORLT00020017896; ENSORLP00020028579; ENSORLG00020012076.
DR GeneID; 100049188; -.
DR KEGG; ola:100049188; -.
DR CTD; 100049188; -.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00940000164334; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; Q9YIC0; -.
DR OMA; YNEARFE; -.
DR OrthoDB; 1150082at2759; -.
DR TreeFam; TF300304; -.
DR Proteomes; UP000001038; Chromosome 11.
DR Proteomes; UP000265180; Chromosome 11.
DR Proteomes; UP000265200; Unplaced.
DR Bgee; ENSORLG00000007614; Expressed in gastrula and 14 other tissues.
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; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT CHAIN 2..461
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090897"
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 BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
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 461 AA; 50443 MW; C0199B6194BBDB0A CRC64;
MGKEKIHINI VVIGHVDSGK STSTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA FTLGVKQLIV GVNKMDSTEP PYSQARFEEI QKEVSTYIKK
IGYNPAAVAF VPISGWHGDN MLEASDKMSW FKGWKIERKD GNASGTTLLE ALDAILPPSR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APPNLTTEVK SVEMHHESLP
EAVPGDNVGF NIKNVSVKEI RRGYVAGDSK NDPPKAAASF NAQVIILNHP GQINQGYAPV
LDCHTAHIAC KFNELIEKID RRSGKKLEDN PKFVKSGDAA IVKLIPQKPM VVEPFSNYPP
LGRFAVRDMR QTVAVGVIKA VDTKEISGKT TKAAEKAQKK K
