ID M2U0B1_COCH5 Unreviewed; 1346 AA.
AC M2U0B1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=COCHEDRAFT_1145245 {ECO:0000313|EMBL:EMD87511.1};
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD87511.1, ECO:0000313|Proteomes:UP000016936};
RN [1] {ECO:0000313|EMBL:EMD87511.1, ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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}.
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DR EMBL; KB445582; EMD87511.1; -; Genomic_DNA.
DR STRING; 701091.M2U0B1; -.
DR eggNOG; KOG0435; Eukaryota.
DR HOGENOM; CLU_004427_3_0_1; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000016936; 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 CDD; cd03062; TRX_Fd_Sucrase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR009737; Aim32/Apd1-like.
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; IPR036249; Thioredoxin-like_sf.
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; PF06999; Suc_Fer-like; 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; SSF52833; Thioredoxin-like; 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:UP000016936}.
FT DOMAIN 53..256
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 265..460
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 475..639
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 793..922
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1346 AA; 149299 MW; 58153F94657B9D97 CRC64;
MQGRLLQSVG WQRALRRPAL HHYTRITSSR WAGTRNTKNR ADDVRLESLT AKWQPRWDEL
SSKWHKLRTS DRGNAYVLPM FPYPSGTLHL GHLRVYTISD VLARFKHMQG YKVLHPIGWD
AFGLPAENAA IERGVHPEKW TLLNIEAMKT QMEQMGGRWD WDAEIRTCDP AFYKHTQRIF
LMLHDHGLAY QAESLVNYDP VDKTVLANEQ VDANGCSWRS GAKVEKVMLK QWFLKIKEFQ
EPLLKDLDAL ATHDRWPEKV LAMQRNWIGK SEGAKLWFDI ISTGSSVSFE PVDVFTTRAD
TLFGVQYIAL SLSHPVVQKL AAQDESLRAF IERAKDLPPD TKEGFLLRSI VARNPLGHVR
GTAGPTIPVY VAPYVLDDYG SGAIMGVPGH DTRDHAFWRT NVGDEPIRLV VSTKKDDLPF
PIVPRSGRDI PVTERGFVAA DIENFGGMPS KQAAREVVQA IINTGKQAEI TATWRLRDWL
ISRQRYWGAP IPIIHCDSCG AVPVPEKDLP VQLPDLPDSF FQGRKGNPLE EDDTWKKATC
PKCGSAAERE TDTMDTFMDS SWYFFRFLDP KNDGALVDPV KANSGMPVDL YIGGVEHAIL
HLLYARFISK FLATTPTWPK GYLTNGEPFT RLITQGMVHG ETFTDPENGR FLRPDEVDLT
NPSKPLIKAT GQAPNVSYEK MSKSKYNGVD PGATIAKYGA DATRAHMLFQ APVGDVLEYD
EKKITGVQRW LHRVVKLAGA SWLPDDEVES FVIPSNIDEN LLVILQNLSG LEDPKAASRE
TLISTLKPDE AQLWIKTQQT IASVTESYSQ TYSLNTIVSD LMTLTNTIWD APHASPTTSY
LKWYSIAHLI RMLAPIAPGV AEESWHLLTT CTASQESNID IPTVFATGFP HADLAIIPLL
TTTRKCVVQV DGKRKFEVDI AKLPASIDSK DSKAVARFVL AELLKMEAGK EWFDRETGKI
WKASASDQAS EEFDGVVPQG WKVIAVNGGA LCNFVAPRKP KGEKTGSSTK KMAFARLPRA
LTPRATRAFS TTRLRLQSSS IPYTPTCPSP TCECASAPKD LDIDRKTPLL NTMAPYSEQV
VFCTGKDDWV SNIEQEEGET GKFVQGLKSV IGKGAPGFDP FTNILITASS LPKSSTPNAT
TALLFPSFKR IQNLPNTPSS LSNFATAYLK AKSLHPMHTN LSAAQKANLT RDESKAASLP
EAQDITKPTV FICGHGGRDQ RCGILGPLLQ SAFRSEFQRR GLDADVGLIS HIGGHKYAGN
VIMYVPPSME GNELGGAGVW YGRVGPEHVE GLVDETFVRG RVITELLRGG VMQDGRNIGR
MVEAQMKKDS GEEDDGVLKL KARARG
//
