ID E6JB61_9ACTN Unreviewed; 1030 AA.
AC E6JB61;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 ECO:0000313|EMBL:EFV91144.1};
GN ORFNames=ES5_12365 {ECO:0000313|EMBL:EFV91144.1};
OS Dietzia cinnamea P4.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV91144.1, ECO:0000313|Proteomes:UP000004165};
RN [1] {ECO:0000313|EMBL:EFV91144.1, ECO:0000313|Proteomes:UP000004165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4 {ECO:0000313|EMBL:EFV91144.1,
RC ECO:0000313|Proteomes:UP000004165};
RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT survival in complex tropical soil habitats and biotechnology potential.";
RL Antonie Van Leeuwenhoek 101:289-302(2012).
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:EFV91144.1}.
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DR EMBL; AEKG01000308; EFV91144.1; -; Genomic_DNA.
DR AlphaFoldDB; E6JB61; -.
DR Proteomes; UP000004165; 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; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 2.
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 80..185
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 335..384
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 422..551
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 875..994
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 793..797
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 796
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 1030 AA; 112572 MW; 67A321776CD8FED7 CRC64;
MSSSDQSATG VQPETAGASG SGTQPETGPA HRYGAALAGE IESRWQREWS ERGTFEAPNP
VGPLAAPDGE LPADKLFVQD MFPYPSGAGL HVGHPLGYIA TDVFARYNRM LGTNVLHTLG
YDAFGLPAEQ YAVQTGQHPR VTTESNIANM ERQLGRLGLG HDRRRVFATT DTDFYRWTQW
IFLQIHGSWY DPDAPARTID GGDHPTRTGR ARPIAELVEQ FASGARPLAA GLPADLAADL
AGRTWGELTR AEQEKVLDAH RLVYLSDSTV NWCPGLGTVL ANEEVTAEGR SERGNFPVFR
KNLSQWMMRI TAYADRLVDD LDRLDWTDKV KSMQRNWIGR SQGARVRFAV ADQSIEVFTT
RPDTLFGATY MVLSPEHPLV DELAGPFWPE VPAGAPGSAP GESTPGALDP RWTGGHSSPA
EAVFAYRRAA SMKSELERQE NKDKTGVFTG AYAVNPVNGE QVPVFVADYV LMGYGTGAIM
AVPGHDARDH EFALAFGLPI RQVVAPADGR ELDVQAEAYA GDGVAVNSTN DEGLSLDGLG
VDEAKAATIA WLEGEGTGEG TVQYKLRDWL FARQRYWGEP FPVVYDSDGV PHALPEEMLP
VELPEVEDYK PVSFDSDDAD SVPSPPLAKA TEWMTVELDL GDGLKTYTRD ANVMPNWAGS
SWYQLRYIDP TNSEQLCAIE NERYWTGPRP EIHGAGDPGG VDLYVGGVEH AVLHLLYSRF
WHKVLFDLGH VTSEEPYRRL FNQGYIQAFA YTDSRGVYVP AAEVTERDGK FYWTDASAGA
DATEIEVFQE YGKMGKSLKN SVSPDEICDS YGADTLRVYE MSMGPLDTSR PWATKDVVGA
HRFLQRLWRV VIDESTGEVR VTDTDSTDSA PGEDVLKALH RTIAGVRDDY AGLRDNTAIA
KLIEYVNTLT KAYPTEGPGA PRSVVEPLVL MVAPVAPHLA EELWARLGHT GSLAHGPFPE
YDESYLVEDS VEYPVQIKGK VRSRITVPAD ASPVDVEAAA LADAKVQENL GGAAPKKVIV
VPGKMVNIVP
//
