ID A0A0D0CI52_9AGAR Unreviewed; 1098 AA.
AC A0A0D0CI52;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
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=GYMLUDRAFT_1022253 {ECO:0000313|EMBL:KIK54628.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK54628.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK54628.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK54628.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) 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};
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DR EMBL; KN834814; KIK54628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0CI52; -.
DR HOGENOM; CLU_004174_1_1_1; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000053593; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593}.
FT DOMAIN 59..122
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 211..774
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 814..934
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 135..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 123422 MW; E80977AF32DC7E1A CRC64;
MSTTAETSQT IELAQTGKRD HLKALEKKYQ QQWQDQHVFE VNAPSPADIQ SLSQAEIMQK
YPKWFGNFPY PYMNGSLHLG HAFTISKIEF AAGYQRMLGK RVLFPHGFHV TGLPIKASAD
KLVREIELFG ENFERYVEPE PEPEEPASSQ GTAGASTADK SKGKKGKLAA KSSGHKYQFQ
ILLSIGVPRE DIKKFADPMH WLVHFPPIAI EDHNAFGSRI DWRRRFLTTK ANPYYDAFVR
WQVNKLYKMG KIKFGERYTI YSPKDGQPCM DHDRQDGEGV GPQEYTAIKS QVIEWSPAAK
EIVESKIGGR KVYMVAATLR PETMYGQTNC FVGTSIKYGI FAVNDQEAYL ITYRAARNMT
FQGVNEPRGS IEQLVEIEGA KLVGTKINAP FSVNPEIYVL PMDNVLATKG TGVVTSVPSD
SPHDYATLMD LRKKAEYYKI DPAWASIDPV PVISTPTYGD LTAPAIVKQL KIQSQKDVKQ
LEDAKEIAYK EGFYNGTMLV GEFKGQSVQD AKGKVRDSMI QAGLAFAYAE PEGHVTSRSG
DECVVALMDQ WYLDYGEPVW RAQVEKHVAS MELYGPETRN AFAKTLAWLN QWACARTYGL
GSEMPWDPQF LVESLSDSTI YMAYYTVAQL LHENSIDGSN PGPLGITPDQ MTDEVWEYVF
CDGPWPSPAP LPKEKADALK HEFNYFYPFD IRSSGKDLIN NHLSFALYNH VAIFAPNKWP
LSIRTNGHLM LNGAKMSKST GNFLTLRDAV NKFGADACRL ALADAGDGIE DANFDEMNGN
ANILRVHTLL GWCEEMMKEE ANLRSGPRNY HDDVFENEVN DLINITQGHY EALNFKDALK
YGFYELQSAR DWYREVTSDV GMHVDLVRYW IEISVLLVAP IAPHFAEHVY LSILQKPTSI
QLARWPTPAK PVDRTLIEVG QYMRGTVKMI RDAETSLLKM LNKNKGKGKG VNAPFDPKQP
KSVRVYVATA FPAWQESCVQ AIKDAYDSES DKVDDAKVRT LLTESGLIKN KMAMPFVQAF
KKRMAEFGAK TAFRRTLPFS ETAVLKELLP YLKKTLNLVD AEILSVDEGY AKEGEVGYTK
SIIDSSEPGS PAFEYRNV
//
