ID D7E750_METEZ Unreviewed; 421 AA.
AC D7E750;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|HAMAP-Rule:MF_00118};
DE Short=EF-1-alpha {ECO:0000256|HAMAP-Rule:MF_00118};
DE AltName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN OrderedLocusNames=Metev_0774 {ECO:0000313|EMBL:ADI73674.1};
OS Methanohalobium evestigatum (strain ATCC BAA-1072 / DSM 3721 / NBRC 107634
OS / OCM 161 / Z-7303).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanohalobium.
OX NCBI_TaxID=644295 {ECO:0000313|EMBL:ADI73674.1, ECO:0000313|Proteomes:UP000000391};
RN [1] {ECO:0000313|EMBL:ADI73674.1, ECO:0000313|Proteomes:UP000000391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1072 / DSM 3721 / NBRC 107634 / OCM 161 / Z-7303
RC {ECO:0000313|Proteomes:UP000000391};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Anderson I.,
RA Woyke T.;
RT "Complete sequence chromosome of Methanohalobium evestigatum Z-7303.";
RL Submitted (JUN-2010) 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:0000256|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|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:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC Rule:MF_00118}.
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DR EMBL; CP002069; ADI73674.1; -; Genomic_DNA.
DR RefSeq; WP_013194242.1; NC_014253.1.
DR AlphaFoldDB; D7E750; -.
DR STRING; 644295.Metev_0774; -.
DR GeneID; 9346398; -.
DR KEGG; mev:Metev_0774; -.
DR HOGENOM; CLU_007265_3_5_2; -.
DR OrthoDB; 371718at2157; -.
DR Proteomes; UP000000391; 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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 NCBIfam; TIGR00483; EF-1_alpha; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00118}; Nucleotidyltransferase {ECO:0000313|EMBL:ADI73674.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00118}; Reference proteome {ECO:0000313|Proteomes:UP000000391};
KW Transferase {ECO:0000313|EMBL:ADI73674.1}.
FT DOMAIN 5..219
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 146..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 421 AA; 46374 MW; 32708CBB48F61926 CRC64;
MADEKPHMNL AIIGHIDHGK STLVGRLMYE TGAIPQHIID KNREKAKEQG KETFAFAWIM
DSLKEERDRG ITIDIAHKRF DTDKYYFTIV DCPGHRDFVK NMITGASQAD AAVLSVAAPD
GVMDQTKEHV FLSRTLGIND LIVAVNKMDD INYDEKRYEE VKNQVSELLK MVGFKPDDVT
FVPTSAYLGD NVAKLSENTP WYNGPTILEA LNNLTPPEKA DKLPLRIPVQ DVYTISGIGT
VPVGRVETGV MKKGDQVTFM PSGKTGEVKS IEMHHEEVPQ ATPGDNIGWS VRGLGKGDAR
RGDVAGHKDN PPTVANEFTA QIVVLQHPSA ITVGYTPVFH AHTAQIACTF ISLDKKMDPK
SGQVKEENPT FLKSGDSAIV TLKPTRPMII EPVKEIPHMG RFAIRDMGKT IAAGMCMSVN
Q
//
