ID A0A327VGT8_9ACTN Unreviewed; 974 AA.
AC A0A327VGT8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=K377_07756 {ECO:0000313|EMBL:RAJ70921.1};
OS Streptomyces sp. PsTaAH-137.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305830 {ECO:0000313|EMBL:RAJ70921.1, ECO:0000313|Proteomes:UP000249376};
RN [1] {ECO:0000313|EMBL:RAJ70921.1, ECO:0000313|Proteomes:UP000249376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PsTaAH-137 {ECO:0000313|EMBL:RAJ70921.1,
RC ECO:0000313|Proteomes:UP000249376};
RA Currie C.;
RT "Biomass-degrading enzyme discovery via genome sequencing of insect-
RT associated Streptomyces.";
RL Submitted (JUN-2018) 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:RAJ70921.1}.
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DR EMBL; QLLY01000029; RAJ70921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327VGT8; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000249376; 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 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}.
FT DOMAIN 71..175
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 300..511
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 818..935
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 568..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 740..744
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT COMPBIAS 568..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 743
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 974 AA; 107906 MW; F6A1E5D0ECEE3571 CRC64;
MSETNTAAPS EAAVAPHRYT AAMAADIEAR WQDFWDEHGT YEAPNPSGDL AGETDEARAV
AARPKKFIMD MFPYPSGAGL HVGHPLGYIA TDVFARFQRM NGHNVLHTLG FDAFGLPAEQ
YAVQTGTHPR TSTEANMENM KAQLRALGLG HDKRRSFATI DPEYYKWTQW IFLQIFNSWY
DDELKKARPI ADLVQQFATG ERAVPGGGSW SALSEAERAD VLGEYRLAYA SDAPVNWAPG
LGTVLANEEV TADGRSERGN FPVFKAKLRQ WNMRITAYAD RLIDDLDGLD WPEAIKLQQR
NWIGRSEGAR IDFGFDAASA NRDDVITVFS TRQDTLFGAT YMVLAPEHDL VEKITPAAWP
EGTHDVWTGG HATPAEAVAA YRKQAASKSD VERQAEAKDK TGVFTGAYAI NPVSGEQVPV
FIADYVLMGY GTGAIMAVPA HDARDFAFAR AFELPMRCVV QPSDDRGTDT STWDDAFVAY
EAALVNSSND EVALDGLGVA DAKARMTEWL ERKGIGHGTV NFRLRDWLFS RQRYWGEPFP
IVYDEDGIAH PLPESMLPLE LPEVDDYTPR TFDPDDADTE PETPLSRNQD WVNVTLDLGD
GRGPRPFRRE TNTMPNWAGS CWYELRYLDP HNSERLVDPA VEQYWMGPRE GQPTGGVDLY
VGGAEHAVLH LLYARFWSKV LFDLGHISSA EPFHKLFNQG MIQAFVYRDA RGIAVPAAEV
EERDGAYYYQ GEKVSRLLGK MGKSLKNAVT PDEICEEYGA DTLRLYEMAM GPLDVSRPWD
TRAVVGQFRL LQRLWRNIVD ETTGEVTVAD AAEADIDEAT LRALHKAIDG VRGDLEGMRF
NTAIAKVTEL NNHLVKSYAG GALPRSVAER LVLLVAPLAP HVAEELWRKL GRTDSVVHQD
FPVADPAYVV DEAVTCVVQI KGKVKARLEV SPSISDEELE KIALADEKVV AALDGAGIRK
VIVRAPKLVN IVPA
//
