ID A0AAJ0FTE6_9HYPO Unreviewed; 1134 AA.
AC A0AAJ0FTE6;
DT 24-JUL-2024, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
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 Name=CDC60_2 {ECO:0000313|EMBL:KAK2597965.1};
GN ORFNames=QQS21_005881 {ECO:0000313|EMBL:KAK2597965.1};
OS Conoideocrella luteorostrata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Conoideocrella.
OX NCBI_TaxID=1105319 {ECO:0000313|EMBL:KAK2597965.1, ECO:0000313|Proteomes:UP001251528};
RN [1] {ECO:0000313|EMBL:KAK2597965.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ARSEF 14590 {ECO:0000313|EMBL:KAK2597965.1};
RA Barrett H., Lovett B., Macias A.M., Stajich J.E., Kasson M.T.;
RT "Conoideocrella luteorostrata (Hypocreales: Clavicipitaceae), a potential
RT biocontrol fungus for elongate hemlock scale in United States Christmas
RT tree production areas.";
RL Submitted (JUN-2023) 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:KAK2597965.1}.
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DR EMBL; JASWJB010000103; KAK2597965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAJ0FTE6; -.
DR Proteomes; UP001251528; 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 CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR FunFam; 3.90.740.10:FF:000001; Leucine--tRNA ligase, cytoplasmic; 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; 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 ECO:0000313|EMBL:KAK2597965.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KAK2597965.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP001251528}.
FT DOMAIN 66..137
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 230..802
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 844..971
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 993..1048
FT /note="Leucine--tRNA ligase RagD-binding"
FT /evidence="ECO:0000259|Pfam:PF24810"
SQ SEQUENCE 1134 AA; 126929 MW; A817EF6A28A19CA4 CRC64;
MATASVPKAM EALTISKTKE LKGTEKRDSL IAVEKKYQQK WKDDRVFETD APTTAEVPLH
SISAAELREK VPKFFGCMAY PYMNGTLHAG HTFSASKVEF ATGVARMQGK RALFPMGFHC
TGMPIKACAD KLINEIGKFG KDFSGYNEED EAAAAAAAAA AAVEVKPATK QAKEDITKFT
TNKSKANAKT VKMKYQFQIM QAIGIPKEEI HQFADPQYWL KFFPPLTIRD LTSFGCRIDW
RRSFVTTDAN PYYDAFVRWQ MNRLRELNKI KFGKRYTIYS IKDGQPCMDH DRSEGEAVNP
QEYTAIKLKV LEWAPKAAEA VKSKIPSNAD VFLVPATLRP ETMYGQTCCF VGPKITYGLF
KAGENSYYVV TDRAARNMAY QGILAQEGVV EKAGEIQGSD IVGTLVNAPL SMHKEGVRVL
PMESVLPTKG TGVVSCVPSD SPDDFATISD LAKKADYYGI TKEWAELEII PIIETPSYGD
LCAPFLVKKL KIASPKDTKP LEEAKELAYK EGYYQGVLKV GDFKGEKVES AKPKVRTQMI
DAGEAFAYSE PERKVVSRSG DDCIVSLMDQ WYLDYGEESW KETALKWVEN ADGKGLNTWA
PETKNSFEGV LNWLNQWACA RTYGLGSKLP WDPQFLVESL SDSTIYMAYY TVAHWLHKDM
FGREKGIGNV GPEQMTDEVW DYLFCRRDMA DEVLNKSKIS KATLESMRRE FEYFYPLDVR
SSGKDLIPNH LTFFLYIHLA IFPPEYWPRG IRANGHLMLN GEKMAKSTGN FMTLRELVDK
YGADASRIAI ADAGDGVSDA NFEEDVADNN ILRLFNLREW CEEMVREQNE LRSGETNSFQ
DALFNNEMSG TAHEAVEQYA QTNYKLALKA ALYELTGARD FYREACAAAG IKMHKDLVFK
YIEMQALLMA VITPHWSEYI WLEVLKKDST IHNAAFPKAP AVDASLSAKR DYVRNTASNV
NSAEGLQLKK KAKGKEVSFD PKQPKKLTIY MSEKFPAWQA KYIDLLKEMW DPATKSVNDK
ELNGKIAKMG EMKKAMGFVQ TLKKRLQAGE PAGVVLEQKL AFDEKETLGQ MMQGLKKTAG
LVACDVLIVQ EGGKKGVNLE DGKEVDITMP LAENAVPGQP TFFFENVTAA AAAA
//
