ID A0A1H7QJM2_9ACTN Unreviewed; 973 AA.
AC A0A1H7QJM2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN04515665_11358 {ECO:0000313|EMBL:SEL47804.1};
OS Blastococcus sp. DSM 46786.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1798227 {ECO:0000313|EMBL:SEL47804.1, ECO:0000313|Proteomes:UP000198952};
RN [1] {ECO:0000313|Proteomes:UP000198952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46786 {ECO:0000313|Proteomes:UP000198952};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOAO01000013; SEL47804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7QJM2; -.
DR STRING; 1798227.SAMN04515665_11358; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000198952; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198952}.
FT DOMAIN 75..156
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 308..513
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 819..935
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 741..745
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 973 AA; 108040 MW; 4322E2C342B9E364 CRC64;
MSQTDSRSTE ATGGGVGGDI PRHRYTPALA QQIELAWQDR WEAEGTFHTP NPVGRLSAGF
ERVADRPKFF AMDMFPYPSG AGLHVGHPLG YLGTDVTSRF RRMDGDNVLH PMGYDAFGLP
AEQYAVQTGQ HPRITTEANI AAISAQLRRL GVDHDQRRTF ATIDPGYYKW TQWIFLQIFG
SWFDADAGRA RRIEELVAEL DAGTREPGEG TNPYGRPWAE LDEVQRGVVV DAHRLAYLHE
APVNWCPGLG TVLSNEEVTP DGRSERGNFP VFRRPLKQWM MRITAYADRL LADLDRLDWS
DSLKLMQRNW IGRSTGARIR FAVAGLAGRV GDGAPIEVFT TRPDTLFGAT YMVLAPEHPL
VGQLTADAWP DGTDPRWTGG AATPAEALRE YQRQASRRSE LDRQDAGREK TGVWLGATAV
NPVNGRDLPV FIADYVLTGY GTGAIMAVPG EDTRDFEFAE AFGLPVVRTV QPPADFEGGA
YTGPGRMINS ANDEISLDGL DKAEAIARVT EWLVAKGSGE ATTTYKLRDW LFSRQRYWGE
PFPIVYDEHD RPVAVPESML PVLLPEVDDY SPKTFDDDDA DSAPEPPLSR ASEWTTVELD
LGDGVKKYRR ETNTMPNWAG SCWYYLRYLD PGDDERMVDP ELERYWMGPR EPGDTGGVDL
YVGGVEHAVL HLLYARFWHK VLHDLGHVSS EEPFRRLVNQ GYISAHAYTD ERGFYVPAAD
VEEKDGRFLY QGAEVNREYG KIGKSLKNMV TPDEMIGAYG ADTFRVYEMS TGPLEQSRPW
ETKAVVGSQR LLQRIWRVVV DEETGAVRAA DVEPAEETLR ALHKAIDGVR DGYATLRFNI
AIARITELTN HLTQAYGSDR PVPRSVAEPL VLLVAPLAPH LAEELWSRLG HDGSSAWAPF
PVADERWLVE DTVQVAVQVN GKVRSQVQVP ADADAAALEA AARADEKIAG HLEGATIRRV
VAVPGRLVNF VLG
//
