ID D7DAE6_STAHD Unreviewed; 438 AA.
AC D7DAE6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=Shell_1657 {ECO:0000313|EMBL:ADI32742.1};
OS Staphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 /
OS P8).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=591019 {ECO:0000313|EMBL:ADI32742.1, ECO:0000313|Proteomes:UP000002573};
RN [1] {ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Anderson I.J., Woyke T.;
RT "Complete sequence of Staphylothermus hellenicus DSM 12710.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI32742.1, ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RX PubMed=22180806; DOI=10.4056/sigs.2054696;
RA Anderson I., Wirth R., Lucas S., Copeland A., Lapidus A., Cheng J.F.,
RA Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Pati A., Mikhailova N., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Staphylothermus hellenicus P8.";
RL Stand. Genomic Sci. 5:12-20(2011).
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; CP002051; ADI32742.1; -; Genomic_DNA.
DR RefSeq; WP_013143939.1; NC_014205.1.
DR AlphaFoldDB; D7DAE6; -.
DR STRING; 591019.Shell_1657; -.
DR GeneID; 9234950; -.
DR KEGG; shc:Shell_1657; -.
DR eggNOG; arCOG01561; Archaea.
DR HOGENOM; CLU_007265_3_5_2; -.
DR OrthoDB; 371718at2157; -.
DR Proteomes; UP000002573; 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:ADI32742.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00118}; Transferase {ECO:0000313|EMBL:ADI32742.1}.
FT DOMAIN 5..228
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 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 438 AA; 48781 MW; 9EEE4CDD9EB17952 CRC64;
MSSEKPHLNL VVIGHVDHGK STLVGHILYR LGLIDQKTIQ MLEEEAKKRG KESFKYAWLL
DKLKEERERG VTIALTYMKF ETRKYIFTII DAPGHRDFVK NMITGASQAD AALLVVSARK
GEFEAGMSPE GQTREHAILA KTMGINQLIV AVNKMDATEP PWSQKRYEQI KTVLGKFLKS
LGYDISKIPF IPVSAWTGDN LIERSPNMPW YNGPTLVEAL DSLEPPPKPI DKPLRIPIQD
VYAISGVGTV PVGRVETGVL KVGDRVVFMP PAKVGEVRSI ETHHVRIEKA EPGDNIGFNV
RGVSKRDIRR GDVTGHPDNP PTVAEEFTAR VFIIWHPTAV TVGYTPVIHI HTASVASRIV
EIKAKLDPRT GKVVEENPQF LKMGDAAIVR FKPIKPLVVE KYSDFPPLGR FAMRDMGKTI
GIGIVVDVKP MKIEIKTK
//
