ID A0A2J5HPS4_9EURO Unreviewed; 997 AA.
AC A0A2J5HPS4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=BDW42DRAFT_173349 {ECO:0000313|EMBL:PLN79244.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN79244.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) 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; KZ559563; PLN79244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J5HPS4; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000235023; 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; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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 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; 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|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}.
FT DOMAIN 91..228
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 278..480
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 494..658
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 806..937
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 63..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 110925 MW; 757EB7E22DB06EC2 CRC64;
MNSLFRPRMS PPRAVFAQGR WRCGLRPCRL PAPIRFATTS TPGSVSKKLD LLAIDRKWQE
KWKSDGVSPP EAPVTEQGMG GDATEKKPKS YVLSMFPYPS GTLHMGHLRV YTISDVLSRF
YRMRGHEVIH PMGWDAFGLP AENAAIERGI NPAEWTKENI TKMKEQLRSI SASFDWDREL
ATCAPEFYEH TQRIFLMLYK QGLAYQAEAL VNYDPVDKTV LANEQVDANG FSWRSGAKVE
QLNLKQWFFR ITAFKEALLK DLDSLSGGWP DRVVSMQRNW LGKSYGAKVK FPVSVGEGGG
AQCDINVFTT RPDTLYGVEY LALSLNHPIV QAAAQDDTGL RKFLEEAASL PPDSKVGYQL
PTVSATNPLH IIDKETPHIA RGLPVFVAPY VLGDYGEGAV MGVPGHDSRD LAFFKENMNP
EEIAIVVQPE RPTETKEANP GVVSASKAEA FTQEGFLTSR CWKYQGLHSR EASEQIVKDL
IRVEHGDFVE QWRLRDWLIS RQRYWGTPIP IIHCGDCGSV PVPDDQLPIE LPKIEGEWLK
GKRGNPLESN EEWVQTECPK CGGPARRDTD TMDTFVDSSW YYLRYLDPAN KAAPFSPSKV
RPVDVYIGGV EHAILHLLYA RFIYKFLSQS GLFPEISHAG SLAGPAEPFK TLLSQGMVHG
KTFSDPSTGR FLHPSEVDLS NPERPLIKGT EITPNVSFEK MSKSKYNGVD PTSCTSTYGA
DATRAHVLFS APVSEVLEWD EEKIVGIERW FKRVWKVVLD TNERFASDPA SLRINGSDLM
APSHHAIPLP SSLESLGDND MNAVLSTHRT ISSITHCIEH NPYGLNTVIS DLTKLTNTLS
SSAPDSPQIL YLCLSSLLRL LAPVAPGLSS ESWEILNRAV LGDTAASVPT IFDCPWPTPL
LSPEQAEALS TRGGQTVAVQ INGKLRFSVT IPRRLSATTT PADSGRNGGP TAEEQAWIID
RLLDTEEGRV WLREKNDWEK RRRVIVVKGG KLVNVVF
//
