ID   EF1A_METAR              Reviewed;         426 AA.
AC   Q0W8G2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=UNCMA_28450;
GN   ORFNames=LRC365;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; AM114193; CAJ35331.1; -; Genomic_DNA.
DR   RefSeq; WP_012037160.1; NC_009464.1.
DR   AlphaFoldDB; Q0W8G2; -.
DR   SMR; Q0W8G2; -.
DR   STRING; 351160.LRC365; -.
DR   EnsemblBacteria; CAJ35331; CAJ35331; LRC365.
DR   GeneID; 5144924; -.
DR   KEGG; rci:LRC365; -.
DR   PATRIC; fig|351160.9.peg.2918; -.
DR   eggNOG; arCOG01561; Archaea.
DR   OMA; AIRDMGM; -.
DR   OrthoDB; 13117at2157; -.
DR   Proteomes; UP000000663; 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; 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; Reference proteome.
FT   CHAIN           1..426
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_1000015784"
FT   DOMAIN          5..221
FT                   /note="tr-type G"
FT   REGION          14..21
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          70..74
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          91..94
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          146..149
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          185..187
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         146..149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   426 AA;  46833 MW;  15F26646E6247A6A CRC64;
     MAATKPHINL AVIGHIDHGK STLVGRLLFE TGAVPAHIIE QYKKEAESKG KGTFEFAWVM
     DSLKEERERG ITIDIAHRRF DTEKYYFTVV DCPGHRDFVK NMITGASQAD AAILVCAAPD
     GVMQQTKEHI FLSKTLGINQ LIIAVNKMDA INYDQKRYNE VKEEVSKILR MIGFKPDQIP
     FIPTSAFKGT NIAKHAEETP WYTGVTILEA LNALKEPEKP TQLPLRVPIQ DVYTISGIGL
     VPVGRVETGI MKKGDKVIFR PGIDGVGHAG EVKSIEMHHE EIPQALPGDN IGFNVRGIEK
     NLIRRGDVCG HVDKQPTVAV EFKAQVVVLQ HPSAITAGYT PVFHCHTAQV ACTLTQILAT
     LDPKTGGVKE QNPPFIKTGD AAIVLIRPTR PLVIEKVKEI PQLGRFAIRD MGQTVAAGVV
     MDITPK