ID A0A0Q9C895_9CELL Unreviewed; 986 AA. AC A0A0Q9C895; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 22-FEB-2023, entry version 34. 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=ASE27_09785 {ECO:0000313|EMBL:KRD36750.1}; OS Oerskovia sp. Root918. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Oerskovia. OX NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD36750.1, ECO:0000313|Proteomes:UP000051694}; RN [1] {ECO:0000313|EMBL:KRD36750.1, ECO:0000313|Proteomes:UP000051694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root918 {ECO:0000313|EMBL:KRD36750.1, RC ECO:0000313|Proteomes:UP000051694}; RA Gilbert D.G.; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRD36750.1, ECO:0000313|Proteomes:UP000051694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root918 {ECO:0000313|EMBL:KRD36750.1, RC ECO:0000313|Proteomes:UP000051694}; RA Schulze-Lefert P.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-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: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:KRD36750.1}. 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; LMJG01000013; KRD36750.1; -; Genomic_DNA. DR RefSeq; WP_056650735.1; NZ_LMJG01000013.1. DR AlphaFoldDB; A0A0Q9C895; -. DR EnsemblBacteria; KRD36750; KRD36750; ASE27_09785. DR Proteomes; UP000051694; 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 PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 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 TIGRFAMs; TIGR00396; leuS_bact; 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:UP000051694}. FT DOMAIN 80..182 FT /note="Methionyl/Leucyl tRNA synthetase" FT /evidence="ECO:0000259|Pfam:PF09334" FT DOMAIN 320..524 FT /note="Leucyl-tRNA synthetase editing" FT /evidence="ECO:0000259|Pfam:PF13603" FT DOMAIN 837..945 FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase FT anticodon-binding" FT /evidence="ECO:0000259|Pfam:PF08264" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 576..603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 758..762 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049" FT COMPBIAS 582..596 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 761 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049" SQ SEQUENCE 986 AA; 109285 MW; 4725E564F4918329 CRC64; MSTPENPAPE NPAESAHTAP AASLETTSHR YTPALAQDIE LRWQDAWEER GTFFAANPSG HLTDGEGRHA DGRSPYFIMD MFPYPSGAGL HVGHPLGYIA TDVVGRFRRM CGDNVLHALG YDAFGLPAEQ FAVQTGQHPR VTTEANMANM KRQLRRLGLG HDSRRSFATI DPEYIRWTQW IFLQIFEAWY DEDAERPDGG TGRARPITEL VAEYAAGTRA VPGHPEGTRW EDLDRVAQRA VIDPQRLAYV SESPVNWAPG LGTVLANEEV TSDGRSERGN FPVFQRSLRQ WNMRITAYAD RLADDLDLID WPEKVKSMQR NWIGRSEGAT VRFAIDGAIG GSSPVGDVEV FTTRPDTLFG ATFMVVSPEH PLLDEVPAEW PDGTHDVWTG GHATPIDAVA AYRKEAAAKT AVERQADAGK KTGVFTGHLA VNPVNGVLIP VFTADYVLMG YGTGAIMAVP GGDERDHAFA EAFELPVVRT VAAPEDHEGA WTGDGEIVNS SNDEISLDGL SVPDAKRAMI EWLEAKGIGS GTVTYRLRDW LFSRQRYWGE PFPIVYDEND QPIALPDSLL PVNLPEVPDY SPRTYEPDDA DSSPEPPLGR NEDWVNVTLD LGDGPKTYRR DTNTMPNWAG SCWYYLRYLD PADTEHMASP ELEKYWTGPG HNATAGPAGG VDLYVGGVEH AVLHLLYARF WHKVLLDLGH VTSTEPFHKL FNQGYVQAYA YTDSRGAYVP AEEVVEESSG DEVRYLWKGE PVNREYGKMG KSLKNVVTPD DMYEAYGADT FRVYEMSMGP LDLSRPWDTR AVVGSQRFLQ RLWRNVVSED SGETTVSEEP AEVATLRLVH RTIADVRVEM EHMRSNTAIA KLIALNNHLT GLDRVPREAI EPLILMVAPI APHIAEELWS RLGHPQSLAH EPFPVALDEY LVEDTVTCVV QVQGKVRSRL EVSPSIGDDE LRELALADAN VQRTLDGRGI RTVIVRAPKL VNVVPA //