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Database: UniProt
Entry: A0A8H7DGZ3_9AGAR
LinkDB: A0A8H7DGZ3_9AGAR
Original site: A0A8H7DGZ3_9AGAR 
ID   A0A8H7DGZ3_9AGAR        Unreviewed;      1139 AA.
AC   A0A8H7DGZ3;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 13.
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=MSAN_00393200 {ECO:0000313|EMBL:KAF7375069.1};
OS   Mycena sanguinolenta.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Mycenaceae; Mycena.
OX   NCBI_TaxID=230812 {ECO:0000313|EMBL:KAF7375069.1, ECO:0000313|Proteomes:UP000623467};
RN   [1] {ECO:0000313|EMBL:KAF7375069.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=160909Yilan {ECO:0000313|EMBL:KAF7375069.1};
RA   Tsai I.J.;
RT   "Mycena genomes resolve the evolution of fungal bioluminescence.";
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC         diphosphate; 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:ARBA00047469};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594}.
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:KAF7375069.1}.
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DR   EMBL; JACAZH010000002; KAF7375069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8H7DGZ3; -.
DR   OrthoDB; 10249672at2759; -.
DR   Proteomes; UP000623467; Unassembled WGS sequence.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase 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   FunFam; 3.90.740.10:FF:000001; Leucine--tRNA ligase, cytoplasmic; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; IPR055416; RBD_LARS1.
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; PF24810; RBD_LARS1; 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   3: Inferred from homology;
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:UP000623467}.
FT   DOMAIN          95..163
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          250..813
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          852..974
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          1008..1072
FT                   /note="Leucine--tRNA ligase RagD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF24810"
SQ   SEQUENCE   1139 AA;  128481 MW;  63523176ABEF1E44 CRC64;
     MTHRVLDSTH RYINARRFGQ IVTIFRTLQK TLVFSRPLCN MATDTKIELV QTGKRDHLIQ
     LEKKYQALWA QEKVFEVNAP DAADVRGLSP AQIHEKHPKW LGTYPYPYMN GSLHLGHAFT
     SSKIEFAAGY QRMLGKRVLY PHGFHVTGLP IKASADKLIR EMEMFGSDFE NFEAVQQKLD
     EEAEEKEKVD VVKDGPVDKS KGKKGKLAAK STGHVYQFQI LQSIDIPTAD IKKFADPLHW
     LTHFPPIAIE DHTAFGSRID WRRKFLTTPA NPYYDAFVRW QMNKLHKLGK IKFGERYTIY
     SPKDGQPCMD HDRSDGEALG PQEYTAVKME VAEWGAAAKN TIEGHVGGRK VFLVAATLRP
     ETMYGQTNCF VGTAIKYGVF AMSDTEAFVC TYRAARNMAF QGISKTRGDI NQLLEIDGTK
     LVGTRVKAPF AINPEVYVLP MDNVLPTKGT GVVTSVPSDS PDDCATLADL VKKPAFYSIE
     PAWAAIEPVP VISTLDYGDM IAPALLKSMK IQSQKDTKQL AEAKEIAYKE GFYNGVMLVG
     EFKGMKVEEA KPKVRERMIE AGLAMAYAEP EGLIISRSTD ECVVALMDQW YLDYGEAGWR
     AETERLLKGM ELYQPETRHS FEKTLAWLNQ WACARTYGLG SQLPWDPHFL VESLSDSTIY
     MSYYTVAQLL HDNSIDGSVP GPLGITPDQM TDEIWEYVFC DGPFPSSSPL PREKADALKH
     EFNYFYPMDI RSSAKDLVPN HLTFCLYNHV ALFPEDKWPR SMRTNGHLLL NGKKMSKSTG
     NSLSLREAIA KFGADSTRLA LADAGDGVED ANFDEKSANA NILRVHTLVQ WCEEMVKDEA
     NLRHGPKNLY HDRVFEQEIN DLINITQSHY EAMNYKDALK YGFYEMQTCR DWYREVTSDV
     GMHADLVMYW IRVAALVVSS IAPHFSEHIY STLLKSPTSI QRALWPTPSA PVDVAVIESG
     AYLRGTIKTI RDAETTLVKM LSKTKGKGAK DGKATYDPKK PKSIRVYVAT TFPEWQEMCV
     NVVKESYDTA TDKVDDAKVR GLLTERGLIK DKRAMPFVQD FKKRMAQFGA QTVFRRTLPF
     SERDVLPEII PYLKRSMSLV DVEVYSIEDA LAKQGEDGFT KAIIESSEPG NPAVEYRNV
//
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