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Entry: A0A2S1YX69_9ACTN
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ID   A0A2S1YX69_9ACTN        Unreviewed;       963 AA.
AC   A0A2S1YX69;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=DDQ41_06450 {ECO:0000313|EMBL:AWK08622.1}, SSP531S_15030
GN   {ECO:0000313|EMBL:GBQ00093.1};
OS   Streptomyces spongiicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1690221 {ECO:0000313|EMBL:AWK08622.1, ECO:0000313|Proteomes:UP000245051};
RN   [1] {ECO:0000313|EMBL:AWK08622.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HNM0071 {ECO:0000313|EMBL:AWK08622.1};
RA   Zhou S., Huang X.;
RT   "Complete genome sequence of the Type Strain of Streptomyces spongiicola
RT   HNM0071, the producer of staurosporine.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GBQ00093.1, ECO:0000313|Proteomes:UP000265354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=531S {ECO:0000313|EMBL:GBQ00093.1,
RC   ECO:0000313|Proteomes:UP000265354};
RA   Dohra H., Kodani S.;
RT   "Whole Genome Shotgun Sequence of Streptomyces spongiicola strain 531S.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP029254; AWK08622.1; -; Genomic_DNA.
DR   EMBL; BGZL01000003; GBQ00093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S1YX69; -.
DR   KEGG; sspo:DDQ41_06450; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000245051; Chromosome.
DR   Proteomes; UP000265354; 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          75..157
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          304..506
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          809..922
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           734..738
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   COMPBIAS        562..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         737
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   963 AA;  106363 MW;  DD0BD889EE4E2AB7 CRC64;
     MSEKNSSPVA SGTDGATSAE AAAPHRYTAA AAADIEARWQ DFWDADGTYE APNPSGDLAG
     DAGVVARPKK FIMDMFPYPS GAGLHVGHPL GYIATDAYAR YQRMTGHNVL HTLGFDAFGL
     PAEQYAVQTG THPRVSTEAN IENMKAQLRR LGLGHDRRRS FATIDPDYYK WTQWIFLRIF
     GSWYDEAAGK ARPIEDLAAQ FESGERATPS GRPWSELSAV ERADVLSGHR LAYASDSPVN
     WCPGLGTVLA NEEVTAEGRS ERGNFPVFKA NLRQWNMRIT AYADRLLDDL DALDWPEAIK
     LQQRNWIGRS EGARVDFPVD GHDHARVTVF TTRPDTVFGA TYMVLAPEHD LIDSVLPAEW
     PEDARGRDAW TGGAATPAEA VAEYRKQAQT KSDVERQTEH KAKTGVFTGA YAVNPVTGAR
     IPVFVADYVL MGYGTGAIMA VPGQDERDWE FAEAFGLPIV RTVRPPEGWE GEAFTGQGPA
     INSSNDEISL DGLEVAEAKA KITEWLVAKG VGEATVNFRL RDWLFSRQRY WGEPFPIVYD
     EDGVAHALPE SMLPLELPEV DDYSPRTFDP DDADTRPETP LSRNAEWVEV ELDLGDGVKR
     YRRETNTMPN WAGSCWYELR YLDPHNADRL VDPAIERYWM GPREGQPHGG VDLYVGGAEH
     AVLHLLYARF WSKVLYDLGH VSSSEPFHKL YNQGMIQAHV YRDARGFPVP AAEVEERDGG
     YVHGGEPVRR ELGKMGKSLK NAVTPDEIAA EYGADTLRLY EMAMGPLDVS RPWDTRAVVG
     QYRLLQRLWR NVVDETTGEV TVVDAEPDEA TLRALHKTVD GVRQDMEAMR FNTAIAKITE
     LNNHLTRTGG PVARSVAERL VLLIAPLAPH IGEELWRRLG HSGSVVHQDF PVADPAYVVD
     ETVTCVVQVK GKVKARLEVS PSIGDAELEA LAVDDPAVVA ALGGAEVRKV IVRAPKLVNI
     VPA
//
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