ID A0A0A0IZD6_9MICO Unreviewed; 971 AA.
AC A0A0A0IZD6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=N802_09805 {ECO:0000313|EMBL:KGN30158.1};
OS Knoellia sinensis KCTC 19936.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385520 {ECO:0000313|EMBL:KGN30158.1, ECO:0000313|Proteomes:UP000030002};
RN [1] {ECO:0000313|EMBL:KGN30158.1, ECO:0000313|Proteomes:UP000030002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 19936 {ECO:0000313|EMBL:KGN30158.1,
RC ECO:0000313|Proteomes:UP000030002};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia sinensis.";
RL Submitted (AUG-2013) 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}.
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:KGN30158.1}.
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DR EMBL; AVPJ01000022; KGN30158.1; -; Genomic_DNA.
DR RefSeq; WP_035919092.1; NZ_AVPJ01000022.1.
DR AlphaFoldDB; A0A0A0IZD6; -.
DR STRING; 1385520.N802_09805; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000030002; 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}.
FT DOMAIN 58..162
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 296..500
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 824..933
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 744..748
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 747
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 971 AA; 108168 MW; A6B22CDA9E23B602 CRC64;
MSETAHRYTA ELADQIELAW QDRWEESGVF NAPNPSGPFA DPEKVASYDG GHMLVLDMFP
YPSGAGLHVG HPLGYIATDV FSRYHRMLGK NVLHCLGMDA FGLPAEQYAV QTGQHPRVTT
EANIVIMKRQ LRRLGLGLDN RRAIRTMDPE YYRWTQWIFL KIFNSWYDRE AVRPDGGLGR
ARPITELIAD FESGARALPD GDERSWSDLS AVERAEVIDS HRLAYASEAP VNWAPGLGSV
VANEEVTNDG RSERGNFPVF KRNLRQWMMR ITDYSDRLAD DLDRVEWPEK VKAMQRNWIG
RSHGARVAFQ VVGAPDGTEP IEVFTTRPDT LFGATFMVLA PEHPLVDSLV PQGEWPAGTN
PTWTGGEATP EASVTAYRLA ASRKSDVERQ MEGKDKTGVF TGAYASNPAT GTEIPIFIAD
YVLMGYGTGA IMAVPGQDER DWHFADVFDL PKIRTVQPTE GHPEDEAFGG EGPAINSAND
TLDLNGKPIA EAKAAMIDWL VAQGFGEATV SYKLRDWLFS RQRYWGEPFP IVFDTDGVAH
GVPESMLPIE LPEVPDYSPR TFDPNDAASE PEPPLGRVRE WVEVELDLGD GRGVQKYRRE
TNTMPNWAGS CWYHLRYLDP ENHDELVSAA TEEYWVGPRE TPVAGAPAGT RDPGGVDLYI
GGVEHAVLHL LYARFWQKVL FDLGHVSSEE PFRTYFSQGY IQAPAYRDDR GQPVEASEVE
ESVGEDGQSA FTWRGQPVTR EFGKIGKSLK NMVSPDDMYA AYGADTLRLY EMGMGPLDQS
KPWDTRAIVG SQRFLQRLWR NVVDEETGEV RVVDEPIDDA TSRILHRTID AVRRDYDELG
FNTAIARLIE FNNALTKLDA VPRAAAEQIV LMVAPLAPHI AEELWSRLGH AESLTHEDFP
VADPALLVED SVTCVVQIKG KVRDRIEVPS DISEDELREK ALALPKVVEA TAGGVRTVIV
RAPKLVNVVP L
//
