ID A0A2V1HN86_9MICO Unreviewed; 856 AA.
AC A0A2V1HN86;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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=DDQ50_10100 {ECO:0000313|EMBL:PVZ94093.1};
OS Amnibacterium flavum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Amnibacterium.
OX NCBI_TaxID=2173173 {ECO:0000313|EMBL:PVZ94093.1, ECO:0000313|Proteomes:UP000244893};
RN [1] {ECO:0000313|EMBL:PVZ94093.1, ECO:0000313|Proteomes:UP000244893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8JJ-5 {ECO:0000313|EMBL:PVZ94093.1,
RC ECO:0000313|Proteomes:UP000244893};
RA Tuo L.;
RT "Amnibacterium sp. M8JJ-5, whole genome shotgun sequence.";
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: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:PVZ94093.1}.
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DR EMBL; QEOP01000002; PVZ94093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1HN86; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000244893; 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; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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:UP000244893}.
FT DOMAIN 24..224
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 236..444
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 457..656
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 694..813
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 55..65
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 618..622
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 856 AA; 95664 MW; B90BDC8EF4CB7EBC CRC64;
MSLTPGPDRD EPGVAGFSEV QDKWQRVWEE TKPFATATAA SGDSRPRKYI LDMFPYPSGD
LHMGHAEAYA LGDVIARYWR QQGFNVLHPI GWDSFGLPAE NAAIKRGVDP REWTYANIAQ
QRESMRRYAP SFDWDRVLHT SDPEYYKWNQ WLFLKMYERG LAYRKDSWVN WDPVDQTVLA
NEQVLPDGTS ERSGAIVVKK KLTQWYLRIT AYADRLLDDL NQLEGSWPSK VIAMQRNWIG
RSTGADIDFA VEGRTEPVTV YTTRPDTLYG ATFMVVAPDS DLAAELVAGS DDAEIRERFQ
DYLQRVQKST EIERLTVDRE KTGVFTGRYA INPLNGERLP IWAADYVLSD YGQGAIMAVP
AHDQRDLDFA RAFDLPVRVV VDTTQPVTGA IRIIPEDGEL PVLDEMDPGT TGVALSGEGR
LINSGQFNGF SKVNAIARVI AHLEAQGVGR KAKNYRLRDW LISRQRYWGT PIPIVYDEDG
NEIPVPEDQL PVALPPSEGL DLKPKGTSPL GGATEWVQTE IDGKPVRRDT DTMDTFVDSS
WYFLRFLSPN DPDKAFDPSE VDKWAPVDQY VGGVTHAILH LLYARFITKV LFDMGYVNFT
EPFTALLNQG MVLMDGSAMS KSKGNLVRLS DQLDEFGVDA VRLTMAFAGP PEDDIDWADV
SPAGSAKFLA RALRVARDVD SSPDVVWKNG DDRLRRQTHR LWADAPGLIE AFKFNVLVAR
IMELTNATRK VIDSGAGPTD PAVREAAEAI ALTLSLFTPY TAEEMWEILG YPPSVALYGW
RKPDPTLLVD ESVTAIMQVD GKVRDRLEVS PKIGGEELEK LARASVAVTR SIGDREVVNV
IVRAPRLVNI ATKPVS
//
