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Database: UniProt
Entry: A0A0B1P0U7_UNCNE
LinkDB: A0A0B1P0U7_UNCNE
Original site: A0A0B1P0U7_UNCNE 
ID   A0A0B1P0U7_UNCNE        Unreviewed;      1137 AA.
AC   A0A0B1P0U7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-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=EV44_g0878 {ECO:0000313|EMBL:KHJ30546.1};
OS   Uncinula necator (Grape powdery mildew).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ30546.1, ECO:0000313|Proteomes:UP000030854};
RN   [1] {ECO:0000313|EMBL:KHJ30546.1, ECO:0000313|Proteomes:UP000030854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX   PubMed=25487071;
RA   Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA   Walker M.A., Cantu D.;
RT   "Adaptive genomic structural variation in the grape powdery mildew
RT   pathogen, Erysiphe necator.";
RL   BMC Genomics 15:1081-1081(2014).
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:KHJ30546.1}.
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DR   EMBL; JNVN01004022; KHJ30546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1P0U7; -.
DR   STRING; 52586.A0A0B1P0U7; -.
DR   HOGENOM; CLU_004174_1_1_1; -.
DR   OMA; KFIEWQF; -.
DR   OrthoDB; 5472610at2759; -.
DR   Proteomes; UP000030854; 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   CDD; cd00812; LeuRS_core; 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   ECO:0000313|EMBL:KHJ30546.1}; 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:UP000030854}.
FT   DOMAIN          72..135
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          214..795
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          836..949
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1137 AA;  128929 MW;  AEAA0D0E4B1E967F CRC64;
     MAPIGPAPII METTVMSKTK ELKGTEKRDS LISFEKKYQV EWQTKGIFQA NAPSISQTPL
     HSISPAELRV QYPKFYGTMA YPYMNGTLHA GHSFTVSKIE FAVGFARMQG KRSLFPMGFH
     CTGMPIKASA DKLAAEVAIF GKKFENYKDE EVEIVLKDQT KSDSRREDVT KFTAKKGKAA
     TKAVRMKYQF QIMQAIGIPT EEIHQFAEAD HWLDYFPPLC QRDLTNFGSR IDWRRSMVTT
     DANPFYDAFV RWQMNRLKEL KKIKFGKRYT IYSPKDGQPC MDHDRSEGEA VGPQEYTALK
     LKVLDWAPEA KKIIEGKIPE DADTYFVPAT LRPETMYGQT CCFVGPNIIY GIFRLSSKEF
     FIVTERAARN MAYQGIFPEN GVYEKVGELI GTTCVGTLVH APLSLHKDGV RILPMESVLS
     TKGTGVVTSV PSDSPDDFAT VTDLCKKAEY YGIKKEWVEL EILPIIRTPT YGDRTAEYLV
     KKFKILSPKD TKKLEEAKEL AYKEGYYQGI MLRGDYAGEK VEVAKPKVKQ QLIASGEGFA
     YSEPERKVVS RSGDECCVAL MDQWYIDYGE ESWKQIALRH VGNTDGAGMN TFAQETKNGL
     EGTLNWLNQW ACARSYGLGS KLPWDPQFLV ESLSDSTIYM AYYTIAHYLH SDIFGKSPGL
     ANIKPDQMTD EVFDYIFARR DLTESILLES KIKEEVLASM RREFEYWYPL DVRISGKDLI
     PNHLTFFLYI HLAIFPKEYW PRGIRANGHL LLNGEKMAKS TGNFMTLDDM LKKYGADATR
     IALADAGDGV TDANFEEDVA DNNILRLFTL REWIQEQVKS ASSLRDGAKN DFLDALFENE
     MNTIVCQARQ HYEDTNYKLA LKSALYDFTS ARDFYREYSA AAGVKMHRDL IFKYIELQAL
     LLCVIAPHWA EYIWLEVLHK PCTIQNALFP TVPAPNAALN AEREYVRATG GNVTSAEAAQ
     QKKKSKGRDI GYDPSKPKKL TIYCADSWPA WQEKYIKLVK SHWDLKKKCM LIDDKELNRQ
     VTLMNEIKTN KKVMPFVQSL KKRLITGVED EIQIFERKLP FDEVQTLQNM VSGLKKAASL
     AVIEIIRVSS SDGGKSGLVV SVGDSLMNHY DVRKIENLPI LAQSAVPGIP TFGFENV
//
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