ID   EF1A_CENSY              Reviewed;         436 AA.
AC   A0RUM4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=CENSYa_0406;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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; DP000238; ABK77041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RUM4; -.
DR   SMR; A0RUM4; -.
DR   STRING; 414004.CENSYa_0406; -.
DR   EnsemblBacteria; ABK77041; ABK77041; CENSYa_0406.
DR   KEGG; csy:CENSYa_0406; -.
DR   PATRIC; fig|414004.10.peg.366; -.
DR   HOGENOM; CLU_007265_3_5_2; -.
DR   OMA; AIRDMGM; -.
DR   Proteomes; UP000000758; 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..436
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000337600"
FT   DOMAIN          8..232
FT                   /note="tr-type G"
FT   REGION          17..24
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          74..78
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          95..98
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          157..160
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          196..198
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         95..99
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         157..160
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   436 AA;  47810 MW;  629E539F22ED8B39 CRC64;
     MTAHMADKPH LNMIVTGHID NGKSTTMGHF LMDLGVVDER TIAQHAEESE KTGKGDTFKY
     AWVMDNIKDE RERGITIDLA FQKFETPKYF FTLIDAPGHR DFIKNMITGA SEADCAILVL
     SAKEGETDTA IAAGGQAREH AFLLKTLGVN QLIVAVNKMD DSKYSEEAYK KTVEKGEGLV
     KSVGYKLENV PFIPVSGWKG DNLVKRSENM PWYKGKTLLE SFDDFKMAEK PVGKPLRVPI
     QDVYTITGVG TVPVGRVETG TMKPGDKIVV MPSGAQGEIK SIETHHTEMP SAEAGDNIGF
     NLRGIEKKDI KRGDVLGDPA NPPKVAKEFL AQIIVIHHPT ALAPGYTPVM HCHTAQVAAI
     MSEFVSKINP ATGAVEEENP KFLKVGDSAI IKIRPVRPTP IETFKEFPEM GRFALRDMGA
     TIAAGIVKEI TEEHKV