ID   EF1A_METS5              Reviewed;         435 AA.
AC   A4YCR6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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}; OrderedLocusNames=Msed_0041;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP94218.1; -; Genomic_DNA.
DR   RefSeq; WP_011921187.1; NC_009440.1.
DR   AlphaFoldDB; A4YCR6; -.
DR   SMR; A4YCR6; -.
DR   STRING; 399549.Msed_0041; -.
DR   EnsemblBacteria; ABP94218; ABP94218; Msed_0041.
DR   GeneID; 5105180; -.
DR   GeneID; 59456527; -.
DR   KEGG; mse:Msed_0041; -.
DR   eggNOG; arCOG01561; Archaea.
DR   HOGENOM; CLU_007265_3_5_2; -.
DR   OMA; AIRDMGM; -.
DR   Proteomes; UP000000242; Chromosome.
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; 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   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..435
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000337604"
FT   DOMAIN          4..229
FT                   /note="tr-type G"
FT   REGION          13..20
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          69..73
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          90..93
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          152..155
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          193..195
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         90..94
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         152..155
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   435 AA;  48394 MW;  1BC99833EDF570FA CRC64;
     MSQKPHLNLI VIGHVDHGKS TLVGRLLMDR GFLDEKTIKE AEEAAKKLGK ESEKYAFLLD
     RLKEERERGV TINLTFMRFE TKKYFFTIID APGHRDFVKN MITGASQADA AILAVSARKG
     EFESGMSLEG QTREHIILAK TMGLNQVIVA ITKMDVAEPP YDQKRYNEIK ETIEKFMKSF
     GFDMSKVKFI PIVSITGENV TKRSENMKWY NGPTLEEALD MLEIPPKPVD KPLRLPIQEV
     YSISGVGTVP VGRVESGVMK VGDKIVFMPA GKSAEVRSIE THHTKLEKAE PGDNIGFNVR
     GIDKKDVKRG DVVGHTTNPP TVAEEFTARV IVVWHPTALA VGYTPVVHVH TASIACRVSE
     IVARLDPKTG KEAEKNPQFI KQGESAIVKF KPIKPLCVEK FSDFPPLGRF AMRDMGKTVG
     VGVINDVKPS KIEIK