ID A0A2T0S9M5_9ACTN Unreviewed; 940 AA.
AC A0A2T0S9M5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CLV70_105261 {ECO:0000313|EMBL:PRY30091.1};
OS Pseudosporangium ferrugineum.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Pseudosporangium.
OX NCBI_TaxID=439699 {ECO:0000313|EMBL:PRY30091.1, ECO:0000313|Proteomes:UP000239209};
RN [1] {ECO:0000313|EMBL:PRY30091.1, ECO:0000313|Proteomes:UP000239209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45348 {ECO:0000313|EMBL:PRY30091.1,
RC ECO:0000313|Proteomes:UP000239209};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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:PRY30091.1}.
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DR EMBL; PVZG01000005; PRY30091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0S9M5; -.
DR Proteomes; UP000239209; 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}; Reference proteome {ECO:0000313|Proteomes:UP000239209}.
FT DOMAIN 68..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 296..488
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 793..905
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 542..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 715..719
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT COMPBIAS 543..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 718
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 940 AA; 105320 MW; C45D4481A8EAF4D4 CRC64;
MVTMSESETN ADVPPYRYTA AMAAEIEPRW QEFWAENGTF YAPNPVGELA DPSHPRAGAP
KLHVQDMFPY PSGAGLHVGH PLGYIGTDSY TRYKRMAGFN VLHPMGFDAF GLPAEQYAVQ
TGTHPRTTTE ANVERYRGQL RRLGLAYDDR RSVATTDPEY YRWTQWIFLQ VFNSWFDPEL
RRARPIDELV AEFEAGTREV PGGRDWSALS AVERRQVIND FRLAYVSEAP VNWCPGLGTV
LANEEVTPDG RSERGNYPVF QRSLKQWKMR ITAYGDRLVE DLDALDWPEP VKLMQRNWIG
RSRGAHVDFP VGDDVITVFT TRPDTLFGAT YMVLAPEHEL VDRIVPAEWP DGTNPAWTGG
AAAPAEAVRA YRAAAAAKTE EERTDAKEKT GVFTGAFAVN PVNGARIPVF VADYVLAGYG
TGAIMAVPGQ DERDWAFAEI FQLPIIRTVA APEGFEGAYT GEGPAINSDW LNGMEVAEAK
AAMIAWLEEH GHGRGATTFR LRDWLFSRQR YWGEPFPIVY DETGLPIALP ESMLPVELPE
VDDFSPRTFD PDDAESEPET PLSRKKDWVQ VELDLGDGPK TYTRETNTMP QWAGSCWYEL
RYLDPHNDKV LVDPENEAYW MGPQRPGDPG GVDLYVGGVE HAVLHLLYAR FWHKVLYDLG
HVSSFEPFRR LFNQGYIQAY AYRDARGVIV PAEEVVERGG KYYYGDQEVA REYGKMGKSL
KNVVTPDEMS EQYGADTFRV YEMAMGPLDV SRPWETRAVV GSQRFLQRVW RLVVDEETGA
VRVSDTPLDE KTRRALHRTI AGVREDMDEL RFNTAIAKLI QLTNTLTPLE TTSREAVEPL
VLMMSPFAPH LAEELWRKLG HDGTLAYADF PVADPAQLVA ESITYPVQIN GKVRGRVEVA
PDTAEDSVRE AALAAVADAL AGRDPRKVIV VPGRLVSVVV
//
