ID A0A2G1X1Y6_9EURY Unreviewed; 421 AA.
AC A0A2G1X1Y6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=DJ68_14085 {ECO:0000313|EMBL:PHQ45221.1};
OS Halorubrum sp. C3.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1483399 {ECO:0000313|EMBL:PHQ45221.1, ECO:0000313|Proteomes:UP000225238};
RN [1] {ECO:0000313|EMBL:PHQ45221.1, ECO:0000313|Proteomes:UP000225238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:PHQ45221.1,
RC ECO:0000313|Proteomes:UP000225238};
RX PubMed=24782836; DOI=10.3389/fmicb.2014.00140;
RA Fullmer M.S., Soucy S.M., Swithers K.S., Makkay A.M., Wheeler R.,
RA Ventosa A., Gogarten J.P., Papke R.T.;
RT "Population and genomic analysis of the genus Halorubrum.";
RL Front. Microbiol. 5:140-140(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHQ45221.1}.
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DR EMBL; NHOB01000855; PHQ45221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1X1Y6; -.
DR Proteomes; UP000225238; Unassembled WGS sequence.
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 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00118}.
FT DOMAIN 4..220
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 90..94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 145..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 421 AA; 45700 MW; 8C0B050D6739A5A4 CRC64;
MSDKPHQNLA IIGHVDHGKS TLVGRLLFET GSVPEHVIEQ HREEAEEKGK GGFEFAYVMD
NLAEERERGV TIDIAHQEFD TDEYYFTIVD CPGHRDFVKN MITGASQADN AVLVVAADDG
VAPQTREHVF LARTLGINEL IIGVNKMDLV DYSEDSYKEV ISEVEDLLNQ VRFATDDTTF
VPISAFEGDN VAEASENTDW YDGPTLLESL NDLPEAEPPT DAPLRLPIQD VYTISGIGTV
PVGRVETGIL NTGDNVSFQP SDVGGEVKTV EMHHEEVPKA EPGDNVGFNV RGIGKDDIRR
GDVCGPADDP PSVAETFKAQ VVVMQHPSVI TAGYTPVFHA HTAQVACTIE SIDQKIDPSS
GEVAEENPDF IKSGDAAVVT VRPQKPLSIE PSGEIPELGS FAIRDMGQTI AAGKVLEVNE
R
//
