ID   EF1A_PYRAR              Reviewed;         444 AA.
AC   A4WKK8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Pars_1362;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-2007) 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       {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; CP000660; ABP50925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WKK8; -.
DR   SMR; A4WKK8; -.
DR   STRING; 340102.Pars_1362; -.
DR   EnsemblBacteria; ABP50925; ABP50925; Pars_1362.
DR   KEGG; pas:Pars_1362; -.
DR   HOGENOM; CLU_007265_3_5_2; -.
DR   OMA; AIRDMGM; -.
DR   PhylomeDB; A4WKK8; -.
DR   Proteomes; UP000001567; 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.
FT   CHAIN           1..444
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000337609"
FT   DOMAIN          15..236
FT                   /note="tr-type G"
FT   REGION          24..31
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          80..84
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          101..104
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          163..166
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          202..204
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         24..31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         101..105
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         163..166
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   444 AA;  48886 MW;  5A53D805E63C630E CRC64;
     MPSIILPPKP TALQKPHINL AVVGHVDNGK STLVGRLLYE TGYVDEKGFK EIEEMAKKMG
     KEDFAFAWIL DRFKEERERG VTIEATHVGF ETNKLFITII DLPGHRDFVK NMIVGASQAD
     AALFVISARP GEFETAIGPQ GQGREHLFLI RTLGIQQLVV AVNKMDVVNY DQKRYEQVKS
     EVSKLLKLLG YDPSKIHFVP VSAVKGDNVR TKSSNTPWYN GPTLLEVLDT FQPPPRPTDK
     PLRLPIQDVF SITGAGTVVV GRVETGVLKA GDRVVVVPPA KVGDVRSIET HHMKLEQAQP
     GDNVGVNVRG INKEDVKRGD VLGKVDNIPT VTEEIIARIV VLWHPTAIGP GYAPVMHIHT
     ATVPVQITEL ISKLDPRTGQ AVEQKPQFIK QGDVAIVKIK PLKPVVAEKF SDFPPLGRFA
     LRDMGRTIAA GQILEVKPAQ VQIK