ID A0A0R2S3L9_9FLAO Unreviewed; 941 AA.
AC A0A0R2S3L9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=ABR84_03650 {ECO:0000313|EMBL:KRO67824.1};
OS Cryomorphaceae bacterium BACL21 MAG-121220-bin10.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655592 {ECO:0000313|EMBL:KRO67824.1, ECO:0000313|Proteomes:UP000051758};
RN [1] {ECO:0000313|EMBL:KRO67824.1, ECO:0000313|Proteomes:UP000051758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL21 MAG-121220-bin10 {ECO:0000313|EMBL:KRO67824.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:RU363035}.
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:KRO67824.1}.
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DR EMBL; LICC01000003; KRO67824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2S3L9; -.
DR STRING; 1655592.ABR84_03650; -.
DR Proteomes; UP000051758; 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 CDD; cd00812; LeuRS_core; 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; IPR002300; aa-tRNA-synth_Ia.
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; PF00133; tRNA-synt_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 39..179
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 278..459
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 710..741
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 791..903
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 714..718
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 717
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 941 AA; 107446 MW; 044E24EABC97989E CRC64;
MSNYPFRTLE EKWQNYWAKH QTFKAEQQAD LPKFYVLDMF PYPSGAGLHV GHPLGYIASD
IYARYMRHKG FNVLHPQGYD SFGLPAEQYA IQTGQHPKKT TQENIARYRE QLDKMGFSFD
WSREVRTSNA DYYRWTQWIF MQLFDSWYDL EHQKARPIDT LVAHFEANGT HGICAVCDDN
ALSFAADQWK AMSWEQQQKH LLHYRMTYLA ESEVNWCPNL GTVLANDEII NGVSERGGHP
VVRKKMKQWS MRISAYAQRL IDGLEAIDWP QPLKEAQRNW IGRSQGASVV FSVQGHDQEI
DVFTTRPDTI FGVSFLTLAP EHELVDKIVT PDQKEAVAQY ILATAQRSER ERMADVKTIS
GVFTGAYAAH PLTNEPIPIW IGDYVLAGYG TGAVMAVPCG DQRDYDFAKH FDLPIPNIFA
DVDLSEQAYT LKDPCIIAAS DFLNGLTYQK ASQKAIEALE QNGRGSGKIN YRLRDAVFSR
QRYWGEPFPV YYKQGLPQMI PVEALPLKLP EVDAYLPTQG GDPPLGRASD WAWNTDSQQV
VSLDLVNHTN VFPLELNTMP GWAGSSWYFF RYMDPHNSQE FAGHQALNYW QQVDLYIGGS
EHATGHLLYS RFWVKFLFDR GFVSVDEPFK KLINQGMILG ESAFVHRDDS GRNFLSANQI
NTAQTQPIHV DVSFVTPSND LDIEAFRRWR PEYQTATFTT EQDGSFKVTR EVEKMSKSKF
NVVNPDDICD QYGADTLRMY EMFLGPLEQA KPWSTAGITG VHGFLKKFWR LYHSGKDGAF
KVEESKPSPE ALKALHKTIK KVTEDIENFS FNTSVSTFMI NANELTSMAC SDRQILEPLL
ILIEPYAPHI AEELWQKMGH LRSISREPFP VFDPQFLVES SKAYPISFNG KTRFTLELSM
DLTPQEIEDI VMAHEKTQEQ LEGRVPKKVI VVPGKIVNIV G
//
