ID A0A161V5X9_9MICO Unreviewed; 858 AA.
AC A0A161V5X9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:KZE95522.1};
GN ORFNames=AVP42_00282 {ECO:0000313|EMBL:KZE95522.1};
OS Agromyces sp. NDB4Y10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1775951 {ECO:0000313|EMBL:KZE95522.1, ECO:0000313|Proteomes:UP000185889};
RN [1] {ECO:0000313|EMBL:KZE95522.1, ECO:0000313|Proteomes:UP000185889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NDB4Y10 {ECO:0000313|EMBL:KZE95522.1,
RC ECO:0000313|Proteomes:UP000185889};
RA Adelskov J., Patel B.K.;
RT "Draft genome sequence of Agromyces sp. NDB4Y10 isolated from a newly
RT drilled coal seam bore well.";
RL Submitted (JAN-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:RU363035}.
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:KZE95522.1}.
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DR EMBL; LQGY01000004; KZE95522.1; -; Genomic_DNA.
DR RefSeq; WP_067945390.1; NZ_LQGY01000004.1.
DR AlphaFoldDB; A0A161V5X9; -.
DR STRING; 1775951.AVP42_00282; -.
DR PATRIC; fig|1775951.3.peg.284; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000185889; 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; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 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:UP000185889}.
FT DOMAIN 27..221
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 234..444
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 459..660
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 699..817
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 54..64
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 622..626
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 858 AA; 95130 MW; 13146AEAA2EF7D08 CRC64;
MAHEQDTPET ADAGTYDFAA IQAKWSPVWE ELQPFRAAQP GDTRPRKYIL DMFPYPSGDL
HMGHAEAFGF GDAAARYWRH QGFDVLHPIG WDSFGLPAEN AAIKRGADPK AWTYANIEQQ
KRSFKQYAPS FDWSRELHTS DPEYYKWNQW LFLKLYEKGI AYRKAGQVNW CPNDQTVLAN
EQVVDGHCER CGSVVTKKAL TQWYFRVTDY ADRLLDDLNQ LEGKWPGKVI TMQRNWIGRS
SGADVDFAIE GRDEPVTVFT TRPDTLYGAT FMVVAPDSAL AAELVEGASD DVRARFEQYL
ESVRAESDID RLATDRPKTG VFLDRYATNP LTGERLPIWA ADYVLADYGH GAIMAVPAHD
QRDLDFARAF ELPVRVVVDT NAPVTGVIPV IPVDDQGVPL PLEDLPELDP ASTGVALTGE
GRLMNSGPLN GLSKSNAIRR AIEILEERGL GRAAKNYRLR DWLISRQRYW GTPIPIIHCE
QCGEVPVPES DLPVRLPDAA GLDLRPKGSS PLGAAEEWAS VTCPNCGGDA RRDSDTMDTF
VDSSWYFLRY LNPNDDDRAF DPAEAEKWMP VDQYVGGVEH AILHLLYARF FTKVLFDLGY
LGFTEPFTSL LNQGMVIMDG HKMSKSKGNL VEFASELSAH GADALRVTMA FAGPPEDDID
WADVSPVGAA KFLARAWRIS GEVASSPDVE WKTGDPALRR ITHRLLADAP GLAESFKFNV
IVARLMELVN ATRKAIDSGA GPADAAVREA AEVTAMILDL FAPYTAEDMW QRLGYEPTVA
NVVWRKADPA LLVEESVTAI VQVDGKVRDR IEVSPKIGAD ELESLARASD AVTRSVAGRE
IANVIVRAPK LVNIATRR
//
