ID A0A0F4Z863_9PEZI Unreviewed; 1119 AA.
AC A0A0F4Z863;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=TD95_005186 {ECO:0000313|EMBL:KKA26535.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA26535.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA26535.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA26535.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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 -!- 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:KKA26535.1}.
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DR EMBL; LAEV01002143; KKA26535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4Z863; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000033483; 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 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:UP000033483}.
FT DOMAIN 64..130
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 209..794
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 837..970
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 148..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 125155 MW; A05F18BF41B68EF8 CRC64;
MAAPTKAMDG LTISKTKELK GTEKRDKLVA WEKKCQEKWA AEKVFEPNAP SIDEIPLDAM
SPEELREKHP KFFGCMAYPY MNGNLHAGHA FSISKVEFTG MVAAMQGKRA LTPLGFHVSG
MPIKACADKL VNEIRMFGKD FSGYNPDAES ESAPAAPAAS AAPKPKEDVT KFSTKKSKSV
AKTAKMKYQF QIMAASGVPL QEVHKFADVN HWLEFFPPIA RRDLTAFGSR ADWRRSFVTT
TANPYYDSMI RWQMTRLKEL GKIKFGNRYT IYSIKDGQPC LDHDRQSGEG INAQEYTGLK
MRVAQWAPAA QDALAGKLPA DASVFLVAAT LRPETMYGQT NCFVGPDITY GVFKASPTDY
YVVTERAAKN MAYQGLFEKH GEIVKVASLP GPAIIGTLVD APLSQYKQVY VLPMATVKEG
KGTGVVTSVP SDSPDDYINV MDLKKKPEFY GIKPEWIDRD VVPVIETPTY GTACAETLCK
QMKISSPKDT VQLEKAKELA YKAGFYNGTM IVGDFKGQKV EVAKPKVRDQ MIAAGTAFAY
AEPEGKVMSR SGDECIVALM DQWFLDYGEE SWKEQALEWV DNKDGKGLNT FSSEAKNQFQ
SVLGWLNAWA VSRSFGLGSR LPWDESQLVE SLSDSTIYMA YYTLVPFLHK DIFGKEPTEY
NVKPEQMTFA VWDYVFCRTE WSDALETESG IARKTLESMR RSFQYFYPLD MRASGKDLIG
NHLTFFIYNH IALFPQEYWP KGIRANGHLM VNSEKMSKST GNFMTLHDLV AKYGADASRI
ALADAGDGIG DANFEEDVAD NNILRLFNCR EWCEEISKTK KESPDSFRSA DFNDFQDKLF
ANDINAVGRE ILHQYDLTNY KLALKGIYDL FNARDFYREG CTASGIPLHI GLVERWIRTL
ALLLNPLAPH FAEFLWLEIL NQPESIQKQR FPDLPEADVG LTATREYIKN ISSAVNSAEA
AQLKKKAKGK EVAFDPSKPK KLTVYINDKF PEWQQKYIDL LSEMWDPATK SLDEKALMGR
VGKMGEMKKA MPFVQTIKKR LQAGEDALNR GLAFDEAQVL VQMAASLKRS AGLRELQVVR
VVEGTKKGVR VEDGVEVDGL AVSAEGAVPG SPTYFFENI
//