ID A0A291GQB2_9MICO Unreviewed; 986 AA.
AC A0A291GQB2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=CFK38_13245 {ECO:0000313|EMBL:ATG52377.1};
OS Brachybacterium vulturis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=2017484 {ECO:0000313|EMBL:ATG52377.1, ECO:0000313|Proteomes:UP000218165};
RN [1] {ECO:0000313|Proteomes:UP000218165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VM2412 {ECO:0000313|Proteomes:UP000218165};
RA Tak E.J., Bae J.-W.;
RT "Brachybacterium sp. VM2412.";
RL Submitted (SEP-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; CP023563; ATG52377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291GQB2; -.
DR KEGG; brz:CFK38_13245; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000218165; Chromosome.
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:UP000218165}.
FT DOMAIN 63..169
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 319..524
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 833..947
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 755..759
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 758
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 986 AA; 109633 MW; 6AB4700CC3F01805 CRC64;
MSEAPHRYTA AVADEIERRW QQRWDEDGTF HADNPVGALR GSAESLEEAA ATSGGAAAEK
MYIMDMFPYP SGAGLHVGHP LGYIATDVVA RHQRMLGKNV LYTMGYDAFG LPAEQYAVQT
GTHPRTTTEA NIATMRRQLH RLGLSHDPRR SLSTTDPEFV KWTQWIFLRI FDSWYDPEAP
NTDGDAGRAR PIAELRDALR AGAVDPFVLA DRQGIELPAE WTDRSAAEVP AASAEEIAQL
ADSFRLTYIS ETPVNWCPGL GTVLANEEVT AEGRSERGNF PVFTRRLRQW NMRITVYADR
LLEDLDRVDW PESIRAMQRN WIGRSHGAQV TFRASGLEDG GEASFDVFTT RADTLFGATF
CVLSPEHALL ADGAALPEQW PAGTREAWTG GAPGPRAAVA AYQARAASMD EDERTADDRE
KTGVFTGLFA TNPMDGRELP VFTADYVLTG YGTGAIMAVP AEDARDFEFS ARFDLPVIRT
VRPPADFEGG AWTGEGEKIN SASAGLDLNG LDKDEAKQRA TAYAEEQGFG RARTTYRLRD
WLFSRQRYWG EPFPIVYDPD APEVPIPLPD SMLPVDLPEV ADFSPTTFDP TDADTEPQTP
LSRATEWAEV ELDLGQGPKR YLRETNSMPQ WAGSSWYHLR YIDPTEDEVL VRPENEKYWL
GAREDGGVGG VDLYVGGAEH AVLHLLYARF WHKVLFDRGD VSSQEPFHRL FNQGYIQAFA
YTDARGVHVP AEEVVAEPDG TFTYLGESVT QEYGKMGKSL KNAVAPDDMY EEYGADTLRV
YEMSMGPLDL SRPWETRAVV GSQRFLQRLW RLVVDEETGR LTLSDDPADL ATLQATHRAI
DGVVRDMERM HFNTAIAKLI ELVNQLTKRL IATGSAPREA VEPLVLMVAP FAPHLAEELW
TRLGHTGSIS RVAYPIADPE LLKAERVTCV VQVKGKVRHR IEVDPEISEA DLEAAVMAEA
RVQELLEGQS VRKLIIRAPK IVNIVV
//
