ID A0A2T5LQY9_9EURO Unreviewed; 980 AA.
AC A0A2T5LQY9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=P175DRAFT_0463584 {ECO:0000313|EMBL:PTU18704.1};
OS Aspergillus ochraceoroseus IBT 24754.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU18704.1, ECO:0000313|Proteomes:UP000244073};
RN [1] {ECO:0000313|EMBL:PTU18704.1, ECO:0000313|Proteomes:UP000244073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU18704.1,
RC ECO:0000313|Proteomes:UP000244073};
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA 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.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
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:PTU18704.1}.
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DR EMBL; MSFN02000007; PTU18704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5LQY9; -.
DR VEuPathDB; FungiDB:P175DRAFT_0463584; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000244073; 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; 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}.
FT DOMAIN 99..236
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 286..476
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 490..652
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 692..729
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 797..926
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 70..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 108912 MW; AB00B827FBFC40A9 CRC64;
MQYLARFRLS PSRTPLAPGA WKTNLSRPLP FLGSSCYHRH LASTTTPAKP GRLDLRALDK
KWQAKWQADG AGGVGLTEGG SSHTQGTREP DGSEKPKFYV LSMFPYPSGT LHMGHLRVYT
ISDLLARFYR MRGHEVLHPM GWDAFGLPAE NAAIERGIDP AKWTMDNIAK MKEQLRKIST
SFNWDREIAT CNPEFYEHTQ RLFLRLYEKD LAYQAEAMVN YDPIDKTVLA NEQVDANGFS
WRSGARVEKL KLRQWFFRIT AFKETLLKDL DSLADGWPER VLSMQRNWLG KSYGAKIKFP
LVVEGNGGQH VDIEVFTTRP DTLYGVEYLA LALDHPIVLE AAKKDEGLQK FLQEAASFPP
DSKAGYKLSN VSVTHPLRAI DPESPHIAPS LPVFVAPYVL SDYGEGAVMG VPGHDSRDFL
FFKENANPSS ISLVIEAESG SDSAKPITQE GVLNSRCGKY HGLHSREAGK QIVNDLKATG
GGDFVEQWRL RDWLISRQRY WGAPIPIIHC GDCGPVPVPE KDLPVKLPEI EGDWLKGKRG
NPLEWSEEWV NTQCPSCGGA AKRDTDTMDT FVDSSWYYLR FLDPKNKQEP FSPSVARPVD
IYIGGVEHAI LHLLYARFIY KFLASTDLFP DEARTGAAQE PFKTLLSQGM VHGKTFSEPS
TGRFLLPSEL DLSNPDRPFI KGTAVTPNVS FEKMSKSKQN GVDPTTCAAK HGADAIRAHV
LFSAPVSEVL EWDETKIVGI ERWFGRLWNL VLDAQQSFIS SSPLESGQGD SSAVVDLVAR
LADQLQSLGD NDAEAVLSTH RTICSVTNCI ENNPYGLNTV ISDLTKLTNS LLSSPPTSPL
VLYLTVSSLL RLLAPIAPAL ASECWEILHA AAVPKVSGRV VPAIFDCPWP TPLLSTEQAD
ALSARGGQIV AVQINGKLRF TATVPRPVSP TTTATEEQEW IIRHILETEE GRTWLREKND
WEKRRRVIVV KGGKLVNVVF
//
