EF1A_DESMO
ID EF1A_DESMO Reviewed; 438 AA.
AC P41203;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE AltName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tux;
OS Desulfurococcus mucosus (Desulfurococcus mobilis).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=2275;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35582 / DSM 2161 / JCM 9186 / Hvv 3/9;
RX PubMed=7898436; DOI=10.1007/bf00290714;
RA Ceccarelli E., Bocchetta M., Creti R., Sanangelantoni A.M., Tiboni O.,
RA Cammarano P.;
RT "Chromosomal organization and nucleotide sequence of the genes for
RT elongation factors EF-1 alpha and EF-2 and ribosomal proteins S7 and S10 of
RT the hyperthermophilic archaeum Desulfurococcus mobilis.";
RL Mol. Gen. Genet. 246:687-696(1995).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
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|HAMAP-Rule:MF_00118}.
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DR EMBL; X73582; CAA51984.1; -; Genomic_DNA.
DR AlphaFoldDB; P41203; -.
DR SMR; P41203; -.
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; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; IPR005225; Small_GTP-bd_dom.
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 TIGRFAMs; TIGR00231; small_GTP; 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 Protein biosynthesis.
FT CHAIN 1..438
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090976"
FT DOMAIN 6..229
FT /note="tr-type G"
FT REGION 15..22
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 71..75
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 92..95
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 154..157
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 195..197
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 92..96
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 154..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 438 AA; 48737 MW; 4A4955EE6CB39427 CRC64;
MSAPQKPHLN IVIIGHVDHG KSTMTGHILY RLGYFDEKTV KMIEEESKKM GKESFKFAWL
LDRMKEERER GVTISLSYMK FETKKYFFTI IDAPGHRDFV KNMITGASQA DAAILVVSAR
KGEFEAGMSA EGQTREHAIL ARTMGINQLI VAINKMDATE PPYSEKRYNE IKEILGKFLK
GLGYDVSKIP FIPISAWTGE NLIERSPNMP WYNGPTLVEA LDTLEVPPKP INKPLRIPIQ
DVYNISGIGV VPVGRVETGV LKVGDKLVFM PAGLVAEVKT IETHHTKIEK AEPGDNIGFN
VKGVEKKDIK RGDVAGSLDV PPTVADEFTA RIMVMWHPTA IAVGYTPVIH VHTASVACRI
TEIIAKIDPR TGKEIEKNPH FLKQGDIAIV KFKPIKPLVV EKYSDFQGLG RFAMRDMGKT
IGIGQVLEIK PAQVNIKK
