ID G3YFV8_ASPNA Unreviewed; 1126 AA.
AC G3YFV8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=ASPNIDRAFT_52554 {ECO:0000313|EMBL:EHA18526.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA18526.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA18526.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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 -!- 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:EHA18526.1}.
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DR EMBL; ACJE01000021; EHA18526.1; -; Genomic_DNA.
DR AlphaFoldDB; G3YFV8; -.
DR STRING; 380704.G3YFV8; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1169124; -.
DR HOGENOM; CLU_004174_1_1_1; -.
DR Proteomes; UP000009038; 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; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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; TIGR00395; leuS_arch; 1.
DR PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 68..142
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 223..802
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 840..965
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1126 AA; 126786 MW; 34CAE64B88978058 CRC64;
MAAAAAAASA AALEQGTKNT MKLENTEKRD TLIALEKKYQ AQWKANKVFE VDAPSETEVP
FGSMSAAELR EKHPKFFGTM AYPYMNGTLH AGHSFTASKV EFMTGVARME GKRALFPLGF
HCTGMPIKAC ADKLRDEVAK FGKNFEGYSE ESEEQDKAAV AAPTQEVKAE QEKFSGKKSK
AAAKTVKMKY QFQIMLAIGI PIEEIHKFAD AAHWLQHFPP LAIRDLDSLG ARVDWRRQFV
TTDANPYYDA FVRWQMNRLH ELGKIQYGNR YTIYSPKDGQ PCMDHDRTEG EGIGPQEYTA
MKLKVKEWAP EIAELVKGKI EDDANVYFVP ATLRPETMYG QTCCFLGPKI TYGLYKVKEK
EYFVVTKRAA WNMAFQGYFS DGEKFLKSQD QLPLVVEAPG TAFVGTLVNA PLSFHTEGVR
ILPMEGVSAS KGTGVVTSVP SDSPDDYATL MDLAKKPEYY GIKKEWAELE IFPLIETPTY
GNLTAPALVK QLKINSPKDV NQLAQAKELA YGEAFYKGTM IVGEYKGQPV SAVKEKIRKS
LYESGDAFPF ADPMGKVVSR SGDDCVVAYL GQWFLNYGEN DAEWQKTTLN HVVNTLNTYS
NETKNGFEKN LSWLNRWACA RTYGLGSKLP WDKQFLVESL SDSTVYMAYY TIAHYLHGDR
YGKEPGSLNV KAEQMIDEVW DYIFTRRELS DELVSKSGIS KEALQKMRRE FEYWYPLDVR
VSGKDLIQNH LTFFLYIHVA LFPPEYWPRG VRANGHLLLN GEKMSKSTGN FLTLKDAVDK
FGADATRIAF ADAGDGIEDA NFEETVANSN ILRLHTLKDW MEEVVKDETL RTGPADAFWD
KLFDNELNGL VRETKKHYQD TNFKLALKSG LYDLVSARDF YREATTTAGI GMHRDVVLRY
IELQALMMAV IAPHWSEHIW LEILKKPSTI HHARFPEVPE LSLELSAALD YARSTTSSIT
SAEANFVKKL SKGKQTAFDP RKPKKLSIYA AKKFPVWQEK YIDLVREAFD AVSISFNDKE
LNAKVGKLGE MKKAMPFVQR LKKRLVVDKE VPETVFDRKL PFDEFAVLSE MVPAIKRVTG
AKELEIVAVD EGGKTGEVVG TGEKREGLQA ENAVPGQPSF NFANIE
//
