ID   EF1A_PYRAE              Reviewed;         444 AA.
AC   O93729;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=PAE3000;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Fitz-Gibbon S., Choi A.J.;
RT   "Pyrobaculum aerophilum putative elongation factor EF-1alpha.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; U94347; AAD09252.1; -; Genomic_DNA.
DR   EMBL; AE009441; AAL64600.1; -; Genomic_DNA.
DR   PIR; T44963; T44963.
DR   AlphaFoldDB; O93729; -.
DR   SMR; O93729; -.
DR   STRING; 178306.PAE3000; -.
DR   EnsemblBacteria; AAL64600; AAL64600; PAE3000.
DR   KEGG; pai:PAE3000; -.
DR   PATRIC; fig|178306.9.peg.2251; -.
DR   eggNOG; arCOG01561; Archaea.
DR   HOGENOM; CLU_007265_3_5_2; -.
DR   InParanoid; O93729; -.
DR   OMA; AIRDMGM; -.
DR   Proteomes; UP000002439; 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..444
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090987"
FT   DOMAIN          15..238
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;  48809 MW;  39FF970B660E655D CRC64;
     MPSIILPPKP TALQKPHINL AVVGHVDNGK STLVGRLLYE TGYVDEKALK EIEEMAKKIG
     KEDFAFAWIL DRFKEERERG VTIEATHVGF ETNKLFITII DLPGHRDFVK NMIVGASQAD
     AALFVISARP GEFEAAIGPQ GQGREHLFLI RTLGVQQIVV AVNKMDVVNY DQKRYEQVKA
     EVSKLLKLLG YDPSKIHFIP VSAIKGDNIK TKSSNTPWYT GPTLLEVFDS FQPPQRPVDK
     PLRMPIQDVF TITGAGTVVV GRVETGVLKV GDRVVIVPPA KVGDVRSIET HHMKLEQAQP
     GDNIGVNVRG IAKEDVKRGD VLGKPDNVPT VAEEIVARIV VLWHPTAIGP GYAPVMHIHT
     ATVPVQITEL VSKLDPRTGQ AVEQKPQFIK QGDVAIVKIK PLKPVVAEKF SDFPPLGRFA
     LRDMGRTIAA GQILEVKPAQ VQIK