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Database: UniProt
Entry: A0A0F0ICH0_ASPPU
LinkDB: A0A0F0ICH0_ASPPU
Original site: A0A0F0ICH0_ASPPU 
ID   A0A0F0ICH0_ASPPU        Unreviewed;       988 AA.
AC   A0A0F0ICH0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=P875_00138147 {ECO:0000313|EMBL:KJK64437.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK64437.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK64437.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) 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}.
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:KJK64437.1}.
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DR   EMBL; JZEE01000510; KJK64437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0ICH0; -.
DR   STRING; 1403190.A0A0F0ICH0; -.
DR   Proteomes; UP000033540; 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; 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-RELATED; 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:UP000033540}.
FT   DOMAIN          58..259
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          273..476
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          490..654
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          800..936
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   988 AA;  110421 MW;  4F906FA4F2455932 CRC64;
     MLSLSRLRLG PTRTFLAQAR WKLGCRLHSV PALTRFATTV TPKANTRKLD LPAIDRKWQE
     KWHSEKSNLP SIASETKGNT EKPKSYILSM FPYPSGTLHM GHLRVYTISD VLARFYRMRG
     HEVLHPMGWD AFGLPAENAA IERGIDPAEW TKDNIARMKE QLRSISTSFD WDRELATCAP
     EFYEHTQRIF LMLYKKGLAY QAEALVNYDP VDKTVLANEQ VDANGFSWRS GAKVEKLNLK
     QWFFRITDFK EALLNDLDSL AGGWPERVLS MQRNWLGKSN GAKVKFPIAA EGIGCGSTEI
     DVFTTRPDTL YGVEYLALSL NHPIVLAAAE TDSKLRKFLD EAASLPPDSK TGYKLSTVTA
     SHPLHIIDRE SPHVARRLPI FAAPYVLSDY GEGAVMGVPG HDSRDLAFFK ENVQPESIPV
     VIEPHRASDA ESGASAGHLP AGDMKAYTHE GFLNSRCWKY QGLHSSEAGQ QIINDLRAVG
     HGDTVEQWRL RDWLISRQRY WGTPIPIIHC GDCGPVPVPD DQLPVKLPKI EGDWLKGKRG
     NPLESSDEWV HTECPRCQGP AKRDTDTMDT FVDSSWYFLR FLDSANRRQP FSPSSARPVD
     VYIGGVEHAI LHLLYARFIY KFLAKSDLFP EIAHVGDVSG PLEPFKTLLS QGMVHGKTYS
     EPSTGRFLHP SEMDLSSPDK PVIKGTQITP NVSFEKMSKS KHNGVDPTAC ALKYGADATR
     AHVLFSAPVS EVLEWDETKI VGVERWLGRV WKLVQDAQQT LASSSYTFNP DELMLSNHAT
     ALPHSPQNLS DNDADAVLFT HRTILSVTSC IENNPYGLNT VISDLTKLTN SLSSSTPSSP
     QVLYLCISSL LRLLAPIAPA LASESWETLN EPIIGRYPRN ESIDNAYDVP PIFDCPWPTA
     LLTSEQADIL SARGGQTVAV QINGKLRFTV TVPRQLSPTT GESSEQDFII NRILETDEGR
     TWLREKNDWE KRRRVIVVKG GKLVNIVF
//
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