ID A0A2S0KBR8_9ACTN Unreviewed; 960 AA.
AC A0A2S0KBR8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=C6V83_01355 {ECO:0000313|EMBL:AVL99141.1};
OS Gordonia iterans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1004901 {ECO:0000313|EMBL:AVL99141.1, ECO:0000313|Proteomes:UP000239814};
RN [1] {ECO:0000313|EMBL:AVL99141.1, ECO:0000313|Proteomes:UP000239814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co17 {ECO:0000313|EMBL:AVL99141.1,
RC ECO:0000313|Proteomes:UP000239814};
RA Lee S.-S., Kim H.;
RT "Characteristics and genome of n-alkane degrading marine bacteria Gordonia
RT iterans isolated from crude oil contaminated in Tae-an, South Korea.";
RL Submitted (MAR-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:RU363039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP027433; AVL99141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0KBR8; -.
DR KEGG; git:C6V83_01355; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000239814; Chromosome.
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; 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.
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}; Cytoplasm {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:UP000239814}.
FT DOMAIN 70..178
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 300..494
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 810..925
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 732..736
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 735
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 960 AA; 106333 MW; 3B9F51E58BD0C413 CRC64;
MYAGRVSIAE PAPGHRYTAQ TAGEIEAAWQ QYWTENQTFA APNPVGPLAG DFSDFSGSGP
QAPDKLFVQD MFPYPSGSGL HVGHPLGFIA TDVYARFQRM TGKNVLHTMG FDSFGLPAEQ
YAVQTGTHPR TTTEANIERY LAQIRRLGLA HDERRRVATT DVDFYRWTQW IFLQIYNAWF
DEEKNKARPI SELIDEFESG ARTLDDGRAW SELDAAARRE VLDSYRLVYL SDSLVNWCPG
LGTVLANEEV TADGRSERGN FPVFRKNLRQ WMMRITAYAD RLIDDLDLLD WSDKVKTMQR
NWIGRSRGAR VRFPVSPVDT VEVFTTRPDT LFGASYMVLA PEHELVDRIV AEAWPPGVDG
RWTGGAPDPK AAVAAYRASI AAKSDLERQE NKEKTGVFTG AFAVNPLNGE QLPVFIADYV
LIGYGTGAIM AVPAHDERDY EFATAFGLPI REVIGSDAGV AEKAFTGDGP LVNSGFLDGM
GVDEAKAAVV AHLEAQGAGV GTIQYKLRDW LFARQRYWGE PFPIVYDDQG APHALPDSML
PIELPEVADY APVAFDPDDA DSWPSPPLAK ASEWVAVDLD LGDGLKSYTR DTNVMPQWAG
SSWYQLRYID PTNEETLCAK ENEAYWMGPR PELHGPDDPG GLDLYVGGME HAVLHLLYSR
FWHKVLYDLG YVTSSEPYRK LFNQGMIQAY AYTDSRGVYV PAEEVVERPA EGAGQAPRYF
YGDEEVTQEY GKMGKSLKNS VAPDDICRDY GADTLRVYEM AMGPLDQSRP WATKDVVGAQ
RFLQRVWRLV VDEESGGVRV SGDPAPEETL KVLHKTIAGV RDDYDGLRMN TAGAKLIELT
NHLTKSYPGG APRDAVEPLV LMLAPLAPHL AEELWNRLGH NVSLAHGPFP EPDPDLLVED
TLELPVQVKG KVRSRIVVAA DADEATVVAA ALADEKVQGF LDGEPRKVIY VPGRTVNVVP
//
