ID A0A239VJL1_9MICO Unreviewed; 968 AA.
AC A0A239VJL1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ECO:0000313|EMBL:SNV22322.1};
GN ORFNames=SAMEA4475696_01485 {ECO:0000313|EMBL:SNV22322.1};
OS Dermatophilus congolensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Dermatophilus.
OX NCBI_TaxID=1863 {ECO:0000313|EMBL:SNV22322.1, ECO:0000313|Proteomes:UP000242637};
RN [1] {ECO:0000313|EMBL:SNV22322.1, ECO:0000313|Proteomes:UP000242637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13039 {ECO:0000313|EMBL:SNV22322.1,
RC ECO:0000313|Proteomes:UP000242637};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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; LT906453; SNV22322.1; -; Genomic_DNA.
DR RefSeq; WP_028327694.1; NZ_LT906453.1.
DR AlphaFoldDB; A0A239VJL1; -.
DR STRING; 1121387.GCA_000429885_02151; -.
DR GeneID; 63459697; -.
DR KEGG; dco:SAMEA4475696_1485; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000242637; Chromosome 1.
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:UP000242637}.
FT DOMAIN 60..163
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 295..499
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 821..927
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 740..744
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 743
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 968 AA; 107839 MW; 5114075CD2E2FE7C CRC64;
MSESASGAGY RYTAEVADRI ERHWQDVWET EGTYAAANPA GPWADSQAAK REPLYVLDMF
PYPSGAGLHV GHPLGYIATD AFARFQRMTG KNVLHTLGYD AFGLPAEQYA IQTGQHPRVT
TENNIANMRR QLRRLGLGHD TRRSVATTDV EFYRWTQWIF LQLFNAWFDP QAPNASNGKG
KARPISELEA EFADGTRPTP DGRPWGELAR HEQREILDQY RLAYVSSAPV NWCPGLGTVL
ANEEVTAEGR SDIGNYPVFK RNMRQWMMRI TTYADRLLED LDRVDWPEPV KLMQRNWIGR
STGATVRFDV PAAEGATEQV EVFTTRPDTL FGATFMVLAP EHPLVEKIVP ATWPEGTKQA
WKAGAATPSE GVSAYIAAAA SKTEMERQAE GKEKTGVFTG AFAINPVDGR ALPVFIADYV
LMGYGTGAIM AVPAEDERDF AFASAFDIDV IRTIEPPAGH PEDQPYTGDG VKINSTGEGI
DLNGMSVPQA KAAMITHLEA QGIGEGTTTY KLRDWLFSRQ RYWGEPFPIV YDEFDQPVAV
PESMLPVQLP EVDDYSPQKL EPEDETSQPV PPLARAEEWA NVQLDLGDGP KMYRRELNVM
PQWAGSCWYE MRYLDPANTE RFVDPQVERY WMGPRATPVE GAPAGLPDVG GVDLYVGGVE
HAVLHLLYAR FWHKVLFDLG HTSSAEPFRR LYNQGYIQAY AFRDQRGQIV PAAEITESVQ
QDGTTAYLWN GQEVVREYGK MGKSLKNVVS PDEMYDQYGA DTFRVYEMSM GPLEASKPWE
TRAVVGSQRF LQRVWRNVID EETGEVVVVD EPMDEDTARA MARAVQGVRA DYAGLRFNTA
IAKLIEFNNV LTKLAHTPRE AAETLVVMLA PVAPHIAEEL WHRLGHSDSV VYAQFPEADE
ALLAAASVTA VIQVLGKVRA RIEVDPSICE ADLEKAAFAE PRIAELIEGK TVRKVIVRAP
NLVNIVAQ
//
