ID C3YFS7_BRAFL Unreviewed; 463 AA.
AC C3YFS7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN Name=LOC118404505 {ECO:0000313|RefSeq:XP_035659512.1};
GN ORFNames=BRAFLDRAFT_122567 {ECO:0000313|EMBL:EEN60732.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN60732.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN60732.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN60732.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
RN [2] {ECO:0000313|RefSeq:XP_035659512.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035659512.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035659512.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|RuleBase:RU000325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249,
CC ECO:0000256|RuleBase:RU000325}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG666510; EEN60732.1; -; Genomic_DNA.
DR RefSeq; XP_002604722.1; XM_002604676.1.
DR RefSeq; XP_035659512.1; XM_035803619.1.
DR STRING; 7739.C3YFS7; -.
DR KEGG; bfo:118404505; -.
DR eggNOG; KOG0052; Eukaryota.
DR InParanoid; C3YFS7; -.
DR OMA; QICNGYT; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000001554; Chromosome 17.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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 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:SF170; ELONGATION FACTOR 1-ALPHA 2; 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 3: Inferred from homology;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|RefSeq:XP_035659512.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|RefSeq:XP_035659512.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554}.
FT DOMAIN 5..242
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 463 AA; 50607 MW; 292ACAD37FFB6856 CRC64;
MGKEKIHINI VVIGHVDSGK STSTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETTKYYVTVI DAPGHRDFIK NMITGTSQAD CAVLIVAAGT
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSADRFTEI TKEVSTYIKK
VGYNPKAVAF VPISGWHGDN MLEPSEKMGW YKGWAIERKE GNASGKTLFE ALDSILPPKR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILKPGVVVTF APVNLTTEVK SVEMHHESLP
EALPGDNVGF NVKNVSVKEI KRGMVAGDSK NDPPKEAESF TAQVIVMNHP GEIHNGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDN PKMVKSGDAA IVEMTPSKPM CVETFSEYPP
LGRFAVRDMK QTVAVGVIKA VKKTDRAGKT TKAAQKATGG KKK
//
