ID A0A136J885_9PEZI Unreviewed; 993 AA.
AC A0A136J885;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=Micbo1qcDRAFT_133579 {ECO:0000313|EMBL:KXJ93266.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ93266.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) 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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; KQ964248; KXJ93266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136J885; -.
DR STRING; 196109.A0A136J885; -.
DR InParanoid; A0A136J885; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000070501; 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 Gene3D; 3.40.50.620; HUPs; 2.
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 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 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|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:UP000070501}.
FT DOMAIN 79..215
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 288..472
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 486..655
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 684..736
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 793..930
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 993 AA; 110289 MW; E7E54F0636499609 CRC64;
MLLSIRAACR PRLMLQRLPA ACPRLSVIPR FYATGLDLPS LDQKWRGRWH DPKLHAAAKT
PGSSVSANAP GATTKDNMYI LAMFPYPSGK LHLGHLRVYT IADVVTRFRK LQGRNVMMPM
GWDAFGLPAE NAAIERGIDP AEWTTQNMAR MKEQLGLMNA SFDWSRELAT CDPGFYKHTQ
SLFLLLRRNG LVSRKKATVN WDPVEKTVLA NEQVDADGRS WRSGAIVEQR DLEQWFFHIT
RFKEALLRDL KALGENEAWP ERVLAMQENW LGLTKGAHYV FPAHAPMGLQ LHVPLEGGQR
YLENFKIYTT RPETIFAAQF IAISPKSAEA AALAEEDARL AEFIARVKDL PHDSMEGYEV
KTVTATNPLA QVPGMPVSYH EKLPVFVAAY VRGDYETGAL MGVPAHDSRD MAFWKQHKPA
EPVKHALAPT KNGEAEAQAD KVFTEPGYMT SLAGDLAGTP SDEAAEAIVK KISTVSKDTQ
LKESWKIRDW LISRQRYWGT PIPIVHCQSC GEVPVPEEQL PVELPKVDHH WAGGHTGNPL
ERATEWVNTD CPKCHGPAKR DTDTMDTFVD SSWYYMRFAD PHNSEMPVSQ AAAKQSLPVD
VYIGGVEHAI LHLLYARFFY KAVMGTLFPS SVATTDLYDS THEPFKRLIT QGMVHGKTFT
DPETGRFLKP DEVDLTTNPS RPTVISTGQE ARSSFEKMSK SKHNGVDPTD FIGQYGADAT
RAHMLFQAPV AEVLNWDEDK IAGVTRWIGK LHGFVKALAP AAPSAPTRDF DPRTYFSKRS
SHPIEQWEAD ARVWAATQRA IASTTLAYEK VYSLNTVVST LMSLTNTLTA ERSLASDVMQ
VAATSALLRL MAPIAPAVAE ECWSVLFPQE QSIFPSRHGG SGEEEAVLVD KWPVTDGTLP
LVEPKTRSCA VQVNGKLRCV VKIPATTAEE IPESEFQTWV TEEIYKSPEA QSKLVDGNDI
RRATRLYTAA TGAMVNFIIP GAKKAKKGKG AKE
//
