ID E8UQV2_THEBF Unreviewed; 816 AA.
AC E8UQV2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=Thebr_2003 {ECO:0000313|EMBL:ADV80522.1};
OS Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 /
OS AKO-1) (Thermoanaerobacter finnii).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV80522.1, ECO:0000313|Proteomes:UP000002062};
RN [1] {ECO:0000313|EMBL:ADV80522.1, ECO:0000313|Proteomes:UP000002062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43586 / DSM 3389 / AKO-1
RC {ECO:0000313|Proteomes:UP000002062};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacter brockii finnii Ako-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:RU363039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR EMBL; CP002466; ADV80522.1; -; Genomic_DNA.
DR RefSeq; WP_012269682.1; NC_014964.1.
DR AlphaFoldDB; E8UQV2; -.
DR KEGG; tbo:Thebr_2003; -.
DR HOGENOM; CLU_004427_0_0_9; -.
DR Proteomes; UP000002062; 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 HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 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.
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}; Cytoplasm {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 40..185
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 218..399
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 412..603
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 659..779
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 575..579
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 816 AA; 94568 MW; 18F25A72D9A5C5A5 CRC64;
MAYSVEIDRK WQKRWEETKL YKFNPKNVDK KLYCLEMFSY PSGAKLHVGH WYNYGPTDSW
ARMKRMQGWE VFHPMGFDAF GLPAENYAIK TGIHPYDSTM ENIRTMEKQL KEMGATFDWD
YEVITCLPEY YKWTQWIFLK LFEAGLAYRK KAPVNWCPSC QTVLANEQVI DGKCERCGTE
VTKKDLTQWF FKITAYAEEL LEKLDELDWP EKTKIMQRNW IGKSDGAEIE FKVAGKDLTF
KVFTTRADTL YGATYVVIAP EHEIVDLITT EEYKQAVEEY KEYARKQSEI ERLSTEKEKT
GVFTGAYAIH PLTGEKLPIW IADYVLATYG TGCVMAVPAH DKRDYEFATK YNLPIKRVIK
GIGDVEDSLP FDEYGVLVDS GEFAGLKSEE ARIKIVEKLK QEGRAEFKVN YRLRDWLVSR
QRYWGAPIPV IHCERCGIVP VPEEDLPVLL PYDVEFAPTG ESPLKKHEGF MNVTCPKCGG
KALRDPDTLD TFVDSSWYFL RYPDNKNDKE PFNKEWINKM LPVDKYVGGA EHATMHLLYA
RFVTKALRDL GYLDFDEPFK SLVHQGTILG PDGSRMSKSK GNVISPDEYI KEYGSDVFRL
YLMFGFAYSE GGPWNDDGIK AIARFVNRVE RFIDKFIETR NNPGKIKDDM GKDEKELNYV
RHYAIKGVTE DAERFQFNTA IARIMELVNA LYKYEADVEV KNIKFYEEVV ADLIKLLAPF
APHFSEEMWE KLGYEYSVFN QKWPEWDEKA LQRDVVEIAV QVNGKVRGRL EVPSKATDEE
IEKLALSDKN VKAYVDGKEI KKVIVVKNRL VNIVVK
//
