ID C5C5X3_BEUC1 Unreviewed; 846 AA.
AC C5C5X3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 100.
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 OrderedLocusNames=Bcav_4090 {ECO:0000313|EMBL:ACQ82331.1};
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Beutenbergia.
OX NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ82331.1, ECO:0000313|Proteomes:UP000007962};
RN [1] {ECO:0000313|EMBL:ACQ82331.1, ECO:0000313|Proteomes:UP000007962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC {ECO:0000313|Proteomes:UP000007962};
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
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}.
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DR EMBL; CP001618; ACQ82331.1; -; Genomic_DNA.
DR RefSeq; WP_015884568.1; NC_012669.1.
DR AlphaFoldDB; C5C5X3; -.
DR STRING; 471853.Bcav_4090; -.
DR KEGG; bcv:Bcav_4090; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000007962; 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; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 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; 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; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_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}; Reference proteome {ECO:0000313|Proteomes:UP000007962}.
FT DOMAIN 48..192
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 232..385
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 418..620
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 732..805
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 696..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 52..62
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 581..585
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 846 AA; 91209 MW; 85279856836ADCF7 CRC64;
MSASTDQTTA TDAAAARTAV EHHWQGVWER LGLFTARDDG SAERRYLVTM FPYPSGDLHM
GHGEVFALAD VLARYWRMRG YDVLFPIGWD SFGLPAENAA IRRGESPAVY TSDNIATQAA
SIRRYGVSFD WTRRFHTSDP EFYRWNQWIF LRMVEQGLAY RAASSVNWCP QDGTVLANEQ
VVSGRCERCG TPVVRRDLVQ WFFRITDYAD RLLDDMALLE GRWPDRVLTM QRNWIGRSTG
ARVRFAVVGP VPPEGSDDGV PAAREGAAPS DVVVFTTRPD TVPGVTFLAV APDSDLADRL
CAPEQRAAFE AYRELVRAAT EIERQATDRP KTGVPLGASV RHPVTGAVVP VWAADYVLPG
YGTGVVMGVP AHDERDAAFA QVHGVGVGDA SLMPELDPAR PGAFDGVAWA EPAVSYRLRD
WLLSRQRYWG TPIPIVHCGA CGEVPVPDDE LPVVLPDLRG ADLTPRGVSP LAAASEWVDV
PCPRCGGPGR RDTDTMDTFV DSSWYFLRYL SPTFTGGPFD AEDARRWMPA VRYVGGVEHA
TGHLLYARFM QKVLRDLGLV DDVEPFAAVT NQGQVINEGR AMSKSLGNGV ELAEQLDAYG
SDAVRLTMVF AGPPEEDIDW ADLSPAGAER FLARALRLAR DVTSSPGADP AGGSATLRRV
THRTVRDVEG LLEGLRFNVV VARVMELVNA ARRTLDGAAG GGRSASGGGR PEAGGGREGD
DGGPGDALTG AADPAVREAA EVAAILLSLV APYTAEEMWA ALGRGPSVAA APWPEVDPAL
LVESTTVAIV QVDGRVRDRL DVPLDVSDDE LLGLAAASPA VERALAGRAV TRTIVRAPGL
VNLVTR
//
