ID A0A0M0J2M0_9EUKA Unreviewed; 924 AA.
AC A0A0M0J2M0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN ORFNames=Ctob_000193 {ECO:0000313|EMBL:KOO20799.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO20799.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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:KOO20799.1}.
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DR EMBL; JWZX01003412; KOO20799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0J2M0; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000037460; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 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; 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; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 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|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..924
FT /note="leucine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005601477"
FT DOMAIN 85..286
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 295..495
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 636..717
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 774..886
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 924 AA; 101631 MW; 0E89CB6BCABBAFA3 CRC64;
MRLVRSVSLV SLIGTAASTS VRSLASLPQT SAVAAWTGSV RRATAVHRAQ LQHVCMQATG
APAAMAEQQI APAKGGYDHT TIEPKWQDYW DEHDTFATLR REGKEKKYVL DMFPYPSGAG
LHVGHPEGYT ASDIMARYWR MCDYDVLHPM GWDAFGLPAE QHAINTGTRP EETTKANIAN
FKRQLRSLGF SYDWKRELAT TDIGYVKWTQ WIFLQLFKKD LAVQSEVRVN WCAELGTVLA
NEEVIDGKSE RGGFPVMRMP LRQWVLRITE YAEQLAADLA TEGIEWPEGT MTMQKTWIGR
SEGAEITFEV EGASASTPQT IDVFTTRPDT LMGATYAVIA PEHPLAAAQL AAADKGGSDD
ATAAALRAYV KAAAGRSDLD RSTAKVKSGV WSGLHVKHPL TGKALPLWVA DYVLAGYGTG
AVMAVPAHDE RDFEFAKAFN LPIVQVVAPS VGAPSLDFGA EGAAAYTELG VCVNSGEGLD
GLSTLDAKTA MIAKLTTLGK GKGKITYKLR DWVFSRQRYW GEPIPIYFPV TVHEAGGDPR
KGDPHTIDYN TPIPVPESEL PVALPDIEDF KPGSDPQGVL AKAEVAHWRY FQKEGKWYAR
ETNTMPQWAG SCWYYLRFAD PANGAAAWSP EAEKAWLPVD LYVGGAEHAV LHLLYARFWH
KVLFDLGLVT TKEPFKKLVH QGMILGEDGE KMSKSRGNVV NPDDIVMQYG GDAMRLYEMF
MGPLEAVKPW QTEQISGVVR FQNRVYALAA KHAAAAGEET ILPGTMTEET ARLMHQTVRK
VTLDIEAMSF NTAISQMMVF SNHLQSLSTP PPTEALTKLT LLLAPFSPHL SEEIWQTLLG
HPESVSFATW PTYDEKMCEV TTVTLGVQVN GKVRSEITLE KTADADEAKA AALADEKVQK
AIGDKEVKKF VYVPGRILNF VLGK
//
