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
//