ID A0A318KRC9_9NOCA Unreviewed; 948 AA.
AC A0A318KRC9;
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=DFR70_104561 {ECO:0000313|EMBL:PXX65497.1};
OS Nocardia tenerifensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=228006 {ECO:0000313|EMBL:PXX65497.1, ECO:0000313|Proteomes:UP000247569};
RN [1] {ECO:0000313|EMBL:PXX65497.1, ECO:0000313|Proteomes:UP000247569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44704 {ECO:0000313|EMBL:PXX65497.1,
RC ECO:0000313|Proteomes:UP000247569};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-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:PXX65497.1}.
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DR EMBL; QJKF01000004; PXX65497.1; -; Genomic_DNA.
DR RefSeq; WP_040739958.1; NZ_QJKF01000004.1.
DR AlphaFoldDB; A0A318KRC9; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000247569; 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}.
FT DOMAIN 60..167
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 290..482
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 797..910
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 719..723
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 722
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 948 AA; 105356 MW; C63550E230EB3CA7 CRC64;
MQDTRATDSD VPEHRYNAEL AGRIERRWQR TWSERGTFHA PNPVGPLAGA TPPDKLFVQD
MFPYPSGAGL HVGHPLGYIA TDVFARYHRM HGRNVLHALG YDAFGLPAEQ YAVQTGAHPR
DTTESNITTM QRQLDRLGLG HDRRRSFATT DPEYYRWTQW IFLRIYNAWY DTELDRARPI
GELIDQFASG TRPAPDGKDW ASMTAAERAA VIDSYRLVYQ TDSMVNWCPG LGTVLSNEEV
TAEGRSERGN FPVFRKRLWQ WMMRITAYSD RLVDDLERLD WPENVKAMQR NWIGRSRGAQ
VRFDADGEQI EVFTTRPDTL FGATYVVLAP EHELVDTLTA AAWPEGTDAR WTNEGAATPA
EAVAAYRKSI AAKSDLERQE NKEKTGVFLG SYATNPANGA PMPIFIADYV LSGYGTGAIM
AVPGHDQRDW DFATALGLPI KEVVAGGDLA VSAYTGDGAI VNSDYLNGLS IEEAKATVIA
RLEADGHGKG TIQYKLRDWL FARQRYWGEP FPIVYDEDGA PHALPESMLP VRLPEMDDFA
PVTFDPNDAN SEPSPPLAKA TDWVEVELDL GDGPKRYRRD TNVMPNWAGS SWYQLRYADP
TNSAAFCAKE NEQYWLGPRT GEHGPHDPGG VDLYVGGVEH AVLHLLYARF WQKVLFDLGD
VSGYEPYRRL FNQGYIQAYA YTDERGAYVP AAEVIERDGA FFWTDATGAE VRVNQEYGKI
GKSLKNAISP DEMCDLYGAD TFRFYEMSMG PLDTSRPWAT KDVVGAHRFL QRVWRLVVDE
ETGGLRVTEA EPAQDTLRLL HKTIAGVDED LAALRDNTAG AKLIELTNHL TKTYPDGAPR
TVVEPLVLML APLSPHIAEE LWERLGHTES LAHGPFPVAD PALLIDESVE YPIQVNGKVR
SRIQVPAGAD NAAIEAAALA DEKIAAALGG AAPRKLIVVP GRLVNIVA
//
