ID N1JQ86_BLUG1 Unreviewed; 1028 AA.
AC N1JQ86;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=BGHDH14_bgh00671 {ECO:0000313|EMBL:CCU82855.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU82855.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU82855.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU82855.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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:CCU82855.1}.
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DR EMBL; CAUH01007132; CCU82855.1; -; Genomic_DNA.
DR AlphaFoldDB; N1JQ86; -.
DR STRING; 546991.N1JQ86; -.
DR EnsemblFungi; BLGH_04306-mRNA-1; BLGH_04306-mRNA-1; BLGH_04306.
DR eggNOG; KOG0435; Eukaryota.
DR HOGENOM; CLU_004427_0_0_1; -.
DR InParanoid; N1JQ86; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000015441; 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; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
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; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000015441}.
FT DOMAIN 82..269
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 274..466
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 480..603
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 807..956
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1028 AA; 116081 MW; AC6236FACD16F894 CRC64;
MIELMHSIIR RCATRLLASN ASLQCRCFGQ KSQTAFNEQF QPELNLVELD NKWQRIWRTR
QLKNYTQNPT SCPSTGGKAA FQKKYILPMF PYPSGDLHLG HLRVYTISDV LARFYRMNGY
NVIHPIGWDA FGLPAENAAL ERGIDPKNWT KRNIDRMRAQ IIAMNGQWDW NRELATCDPS
FYKHTQKLFT LLYKAGLAYR AESSVNYDPV DQTVLANEQV DSNGCSWRSG AKVEKRRLNQ
WFFKISEYRQ QLLDDLEQLK IEKSWPENIL AMQKNWLGKS EGARIKFSVI ANDLDAGTDV
EVFTTRPDTL PQVRYLALAT THPLVLRLAA VDSELQAFLD TVPAMSSDTK VGYILSGVKA
LNPLAQEKSF PEATRVPLPI YVAPYVLGDY GDGAIMGVPG HDSRDHDFWN TNCPEDPVNY
VISKSIDEST IGLPLTVHSS DGHVTDKNRP YTNLTSPEAS TKILDILNDS GRGFKADAWK
IRDWLVSRQR YWGTPIPIVH CESCGSVPVP DDELPVKLPE SARYWDGDKP GNPLEKDYDW
INTKCPKCGS MAKRDTDTMD TFVDSSWYFM RYLDPHNIDE MFSPELANEN LPVDIYVGGV
EHAILHLLYA RFISKFISNT YLWPSGSKRS GEPFSVMLAQ GMVHGKTYAD PNNGKFLKPF
EVNLEDPQNP IVISTGKTAT CSFQKMSKSK YNGVDPGICR DKYGADAMRA HILFQAPVTE
VLEWDEKKIS GINRWLRRLY NFIFKSHGNL IKARSHEGLD GICPRDIFEG KKQQPKNVKM
NEGSTNVVAT VAIELQNMGH ESEHLRKLWR TVQFTISKVT ISLSKTHSLN TVISDLMVLT
NTIIENSVES NKPGEPDCVP SSIHSIVIYW SLEILLKMMA PITPAFAEEC WAMLQFKSTT
SQAINNLTGI PNEDIGKSIF SEPFPIVDGT MQKLGPSTQP CAVQINGRLR AVFQIPICPE
GLTSDEVREW ITNEIIAADE SQRNLTEASP DTHVKCNSKA TKLPSDLNIR HAKKVFVVKK
GKMINYII
//
