ID EF1A_DANRE Reviewed; 462 AA.
AC Q92005;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 158.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68104};
GN Name=eef1a; Synonyms=ef1a;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7918652; DOI=10.1016/0167-4781(94)90081-7;
RA Nordnes S., Krauss S., Johansen T.;
RT "cDNA sequence of zebrafish (Brachydanio rerio) translation elongation
RT factor-1 alpha: molecular phylogeny of eukaryotes based on elongation
RT factor-1 alpha protein sequences.";
RL Biochim. Biophys. Acta 1219:529-532(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RA Gao D., Li Z.F., Murphy T., Sauerbier A., Sauerbier W.;
RT "Zebrafish translation elongation factor 1 alpha: sequence of a cDNA clone
RT from a neurulation stage embryonic library.";
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9003448; DOI=10.1016/s0167-4781(96)00179-0;
RA Gao D., Li Z.F., Murphy T., Sauerbier W.;
RT "Structure and transcription of the gene for translation elongation factor
RT 1 subunit alpha of zebrafish (Danio rerio).";
RL Biochim. Biophys. Acta 1350:1-5(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Translation elongation factor that catalyzes the GTP-
CC dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of
CC ribosomes during the elongation phase of protein synthesis. Base
CC pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP
CC hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its
CC accommodation into the ribosome. The growing protein chain is
CC subsequently transferred from the P-site peptidyl tRNA to the A-site
CC aa-tRNA, extending it by one amino acid through ribosome-catalyzed
CC peptide bond formation. {ECO:0000250|UniProtKB:P68104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P68104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P68104};
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; X77689; CAA54771.1; -; mRNA.
DR EMBL; L23807; AAA50025.1; -; mRNA.
DR EMBL; L47669; AAB50569.1; -; Genomic_DNA.
DR EMBL; AY422992; AAQ97968.1; -; mRNA.
DR EMBL; BC064291; AAH64291.1; -; mRNA.
DR PIR; S50143; S50143.
DR RefSeq; NP_571338.1; NM_131263.1.
DR AlphaFoldDB; Q92005; -.
DR SMR; Q92005; -.
DR IntAct; Q92005; 1.
DR MINT; Q92005; -.
DR STRING; 7955.ENSDARP00000148761; -.
DR PaxDb; 7955-ENSDARP00000006339; -.
DR GeneID; 30516; -.
DR KEGG; dre:30516; -.
DR AGR; ZFIN:ZDB-GENE-990415-52; -.
DR CTD; 100360413; -.
DR ZFIN; ZDB-GENE-990415-52; eef1a1l1.
DR eggNOG; KOG0052; Eukaryota.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; Q92005; -.
DR OMA; QICNGYT; -.
DR OrthoDB; 5477300at2759; -.
DR PhylomeDB; Q92005; -.
DR PRO; PR:Q92005; -.
DR Proteomes; UP000000437; Chromosome 19.
DR Bgee; ENSDARG00000020850; Expressed in gastrula and 46 other cell types or tissues.
DR ExpressionAtlas; Q92005; baseline and differential.
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; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; ISS:UniProtKB.
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 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 NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF271; ELONGATION FACTOR 1-ALPHA; 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 Cytoplasm; Elongation factor; GTP-binding; Hydrolase; Methylation;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT CHAIN 2..462
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090896"
FT DOMAIN 5..242
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000255"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000255"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000255"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000255"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68105"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68105"
FT BINDING 194..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68105"
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|UniProtKB:P68104"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
SQ SEQUENCE 462 AA; 50048 MW; B007B4088B8901F3 CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAGGV
GEFEAGISKN GQTREHALLA FTLGVKQLIV GVNKMDSTEP PYSQARFEEI TKEVSAYIKK
IGYNPASVAF VPISGWHGDN MLEASSNMGW FKGWKIERKE GNASGTTLLD ALDAILPPSR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APANVTTEVK SVEMHHESLT
EATPGDNVGF NVKNVSVKDI RRGNVAGDSK NDPPMEAANF NAQVIILNHP GQISQGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDN PKALKSGDAA IVEMVPGKPM CVESFSTYPP
LGRFAVRDMR QTVAVGVIKS VEKKIGGAGK VTKSAQKAAK TK
//
