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Database: UniProt
Entry: A0A0F4Z863_9PEZI
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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
//
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