ID E8T3R2_THEA1 Unreviewed; 917 AA.
AC E8T3R2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN OrderedLocusNames=Theam_1356 {ECO:0000313|EMBL:ADU97319.1};
OS Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1).
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Thermovibrio.
OX NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU97319.1, ECO:0000313|Proteomes:UP000006362};
RN [1] {ECO:0000313|EMBL:ADU97319.1, ECO:0000313|Proteomes:UP000006362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15698 / JCM 12110 / HB-1
RC {ECO:0000313|Proteomes:UP000006362};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C., Woyke T.;
RT "Complete sequence of chromosome of Thermovibrio ammonificans HB-1.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363035}.
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DR EMBL; CP002444; ADU97319.1; -; Genomic_DNA.
DR RefSeq; WP_013538105.1; NC_014926.1.
DR AlphaFoldDB; E8T3R2; -.
DR STRING; 648996.Theam_1356; -.
DR KEGG; tam:Theam_1356; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_0; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000006362; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 11..214
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 220..407
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 420..536
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 674..713
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 756..880
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 39..49
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 675..679
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 917 AA; 104739 MW; CA35D345ABBFD91C CRC64;
MKYNPQEIEI KWQKRWEEEG VFRSSVSDKK KFYCLEMFPY PSGKIHMGHV RNYSIGDVIA
RFKRLAGFNV LHPMGWDAFG LPAENAAIKS GVHPREWTLS NIENMKEELK RLGFSYDWER
EVTTCSPEYY RWNQWIFLKM LEKGIAYRAK ASVNWCPSCQ TVLANEQVDE EGRCWRCGTT
VEQREIDSWF LKITDYAEEL LRDLELLKGH WPDPVITMQR NWIGKSVGAR VKFEVPEKGE
TIEVFTTRPD TLFGVTYVVL APEHPLTLKL AEGTSQEEAV KAFVEKMKRT EKRKRSTGEL
EKEGVFLGVY AVHPLTGERV PVYTANFVLM DYGTGAVMSV PAHDQRDFEF AKKYGLPVKL
VITPEGEELK PEELQEAYTE PGILVNSGKF SGLKSQKAKS EITKELEKLG KGKRSVQYRL
RDWNISRQRY WGTPIPVVHC PKCGIVPVPQ EELPVKLPEE APLLGEGRSP LERVPEFINT
TCPKCKGPAK RDPDTMDTFF DSSWYFLRYC SPKEENLPFK PEEASYWMAV DQYIGGIEHA
VLHLLYSRFF TKVLRDLGLL KGEGEGEDAA FLSRGEPFKR LLTQGMVNKR WISVKNLLKA
LGLSEESTVG ELVEKLTGQR AELTETVGSL MKRYHITVGD NAVLLLSTEE VSKFLESTPE
EVLKPYEEKF GEVSKMSKSK LNIVNPSDMI AKYGADATRL YVLFAAPPES EFEWKSEGIE
GAYRFLRRLF QFVAERAQEL KAAQALNPEK LSKEGKNLRK KAHQTLKKVT EELSGRFKFN
TAVAAVMELF NRVTSFKPET EADRAALKEA VELTVTMLYP FTPHLSEELW EMLGHKELLA
RSTWPKPDPS ALVEEEVEIP VQVNGKVRAV ISVPVNASEE EVREAVMKEP KVVKAIEGKQ
LVKFIYRPGR IINLVVR
//
