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Database: UniProt
Entry: A0A0Q2LT11_MYCGO
LinkDB: A0A0Q2LT11_MYCGO
Original site: A0A0Q2LT11_MYCGO 
ID   A0A0Q2LT11_MYCGO        Unreviewed;       957 AA.
AC   A0A0Q2LT11;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=AO501_18995 {ECO:0000313|EMBL:KQH78954.1};
OS   Mycobacterium gordonae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH78954.1, ECO:0000313|Proteomes:UP000051677};
RN   [1] {ECO:0000313|EMBL:KQH78954.1, ECO:0000313|Proteomes:UP000051677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH78954.1,
RC   ECO:0000313|Proteomes:UP000051677};
RA   Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA   Chernousova L.;
RT   "Mycobacterium gordonae draft genome assembly.";
RL   Submitted (OCT-2015) 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}.
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:KQH78954.1}.
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DR   EMBL; LKTM01000135; KQH78954.1; -; Genomic_DNA.
DR   RefSeq; WP_055578139.1; NZ_LKTM01000135.1.
DR   AlphaFoldDB; A0A0Q2LT11; -.
DR   STRING; 1778.A9W97_04760; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000051677; 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   Gene3D; 3.40.50.620; HUPs; 3.
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; 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; 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:UP000051677}.
FT   DOMAIN          66..173
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          296..493
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          808..920
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          546..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           728..732
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         731
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   957 AA;  105642 MW;  359B73DC7B0DFBA8 CRC64;
     MTESPTAGPD ADAPRYRYTA ELAAGLERTW QDNWAQLGTF NVPNPVGSLA PADGSTVPAD
     KLFVQDMFPY PSGEGLHVGH PLGYIATDVY ARYYRMLGRN VLHALGFDAF GLPAEQYAVQ
     TGTHPRTRTE ANVVNFQRQL GRLGLGHDSR RSFSTTDVEF YKWTQWIFLQ IYNAWFDPAA
     DRARPISELI AEFDSGARVL DDGRQWAQLS AGERADVVDG YRLVYRADSM VNWCPGLGTV
     LANEEVTADG RSDRGNFPVF RKRLRQWMMR ITAYSDRLLN DLESLDWPDQ VKTMQRNWIG
     RSTGATALFA ATRPDGSAAD IEVFTTRPDT LFGATYLVLA PEHELVDEVV AAGWPEGVPE
     AWTYGGATPA DSVAAYRRAI AAKSDLERQE SREKTGVFLG SYATNPANGE SVPIFIADYV
     LAGYGTGAIM AVPGHDQRDW DFARQFGLPI VEVIAGGDVS QAAHSGDGVL VNSGFLDGKS
     VADAKQAMTQ RLESEGRGRA RIQFKLRDWL FARQRYWGEP FPIVYDADGR AHGIDEAALP
     VELPDVPDYS PVSFDPDDAD SEPSPPLAKA TDWVHVELDL GDGLKPYTRD TNVMPQWAGS
     SWYELRYTDP HNSERFCAKE NEAYWMGPRP AEHGPGDPGG VDLYVGGAEH AVLHLLYCRF
     WHKVLYDLGH VSSWEPYRKL VNQGYIQAFA YTDARGSYVP AEEVIERDGG FVYPGPDGEI
     QVFQEFGKIG KSLKNSISPD EMCDAYGADT LRVYEMSMGP LEASRPWATK DVVGAHRFLQ
     RVWRLVIDED TGETRVADAD PAAETQRVLH RTIAGVSEDY AALRNNTAAA KLIEYTNHLT
     KQYRGEVPRA AVEPLVLMLA PLAPHMAEEL WLRLGHTTSL AHGPFPVADP AFLVDDTVEY
     PVQVNGKVRG RVVVASDAAT DAVQAAALAD EKVQAFLDGA TPRKVIVVPG RMVNLVV
//
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