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Database: UniProt
Entry: A0A1H6A4B3_9ACTN
LinkDB: A0A1H6A4B3_9ACTN
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ID   A0A1H6A4B3_9ACTN        Unreviewed;       815 AA.
AC   A0A1H6A4B3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ORFNames=SAMN05444920_1021010 {ECO:0000313|EMBL:SEG43190.1};
OS   Nonomuraea solani.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEG43190.1, ECO:0000313|Proteomes:UP000236732};
RN   [1] {ECO:0000313|EMBL:SEG43190.1, ECO:0000313|Proteomes:UP000236732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEG43190.1,
RC   ECO:0000313|Proteomes:UP000236732};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNVT01000002; SEG43190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6A4B3; -.
DR   Proteomes; UP000236732; Unassembled WGS sequence.
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; 3.10.20.590; -; 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; 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-RELATED; 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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000236732}.
FT   DOMAIN          42..183
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          222..405
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          420..620
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          657..776
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           582..586
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         585
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   815 AA;  90922 MW;  35A05A6055CE4172 CRC64;
     MSEYDPQALQ AKWQQRWEEQ DTFRASEDPA DPRERRYMLD MFPYPSGDLH MGHGEVFAIG
     DVVARYWMQQ GYNVLHPIGW DSFGLPAENA AIKRNAHPAE WTYANIETQA NSFRRYGIAF
     DWSRRLHTSD PDYYRWNQWL FNRFFERGLA YRKGGLVNWC PNDQTVLANE QVVAGKCERC
     GADVIRRELT QWYFKITDYA QRLLDDMAQL DGWPERLLTM QRNWIGRSEG ADVLFEIEGR
     DEPVHVYTTR PDTLFGATFF VVAVDAALAA EIVTDEQRAA YEAYRAETAK LSDIERLATD
     KEKTGVFLGR YAINPVNGER IPVWAADYVL ADYGHGAIMA VPAHDQRDLD FALKFELPVK
     VVVHTGLADP GETGEATPGE GVLVNSGPLD GLDKTEAIAK IIEVLEVDGR GTGAVNFRLR
     DWLLSRQRYW GTPIPIIHCP DCGEVPVPDE QLPVTLPDLR GEALAPKGVS PLASATEWVN
     VECPKCSGPA KRDTDTMDTF VDSSWYFLRY CSPGFNDGPF DVEQVRKWGP IDQYVGGIEH
     AVLHLLYSRF FTKVLHDMGM VDFSEPFLRM LNQGQVINGG KAMSKSLGNG VDLGKQIDDF
     GVDAVRLTMV FAGPPEDDID WADVSPAASQ KFLARALRVM SEVTSEPGVS FDDGDPELRK
     VTHHTIDEAT KLVDSYRFNV AVARMMELTS AARKAIDTGR GPADPAVREA AETLAILLSL
     VAPYTAEEGW ERLGRTGSVS FGGWPVADPA LLVQESVTCV VQVAGKVRDR LEVPPGIGED
     ELRELALASE KVASYLRGTP RKVIVRAPKL VNIVP
//
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