ID M2SPZ8_COCSN Unreviewed; 1162 AA.
AC M2SPZ8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=COCSADRAFT_76405 {ECO:0000313|EMBL:EMD69313.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD69313.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD69313.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
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:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
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:RU363039}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB445637; EMD69313.1; -; Genomic_DNA.
DR RefSeq; XP_007694675.1; XM_007696485.1.
DR AlphaFoldDB; M2SPZ8; -.
DR STRING; 665912.M2SPZ8; -.
DR GeneID; 19140561; -.
DR KEGG; bsc:COCSADRAFT_76405; -.
DR eggNOG; KOG0437; Eukaryota.
DR HOGENOM; CLU_004174_1_1_1; -.
DR OMA; KFIEWQF; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000016934; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039};
KW Reference proteome {ECO:0000313|Proteomes:UP000016934}.
FT DOMAIN 91..146
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 729..812
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 871..983
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1162 AA; 130725 MW; E91DEC2AB03CDE0E CRC64;
MAETTKSSET PKSAVAATLE QLKPQEAESK TLKIENTDKR DTLIAEEKKY QKSWEEQGIF
NPDAPSLEEE PFDTTTPDQL HEKFPKWLGC FAYPYMNGTL HAGHGFTASK VEFTAGFQKM
LGKRVLFPLG WHVTGMPIKA CADKLVREVE MFGQNFERCP VEDVVETAVS EPPAPTQAET
KTDITKFKAQ KGKAAAKTVK TKYQFQIMLA QGIPLEEIHK FSDPYHWIEF FPPLAKRDLT
AFGARIDWRR QFVTTDANPY YDSFVAWQMR RLKAMGKIIF AKRYTVYSPK DGQACMDHDR
QSGEGVTVQE YTALKMKVVK WADSAKTHIA SLPEGASCYF VPATLRPETM YGQTSCFVGP
SINYSLVKIN DSEYFVLSER AARNMSYQGT TAKWGEYSII ATFPGKDVIG TIVNAPLSVH
KEVYILPMET VKDTKGTAVV TCVPSDSPDD YITSFDLAKK ADYYGIQKEW VKFDNLLGII
ETPTYGNLTA QKLVEEMKIQ SPKDSAKLAE AKEKAYKEGF YKGKMVYGDF AGKPVEEAKL
LVRKQLIDSG VAFPYAEPDG KVISRSGDDC VAALLDQWYM NYGTAANGGD GEWAEKVRSH
IEGELNLYYP EAKNQFLRVV DWLGIWACAR SYGLGTKVPW DPSVMVESLS DSTIYQAYYS
FAHLLHKDMF GKEPGPLGVK PDQMTDEAWD YVFALRDRSD VPQSTIPKQA LETMRRHFDY
WYPLDQRSSG KDLIQNHLTM NLYVHAAIFP KENWPRSFRV NGHLLLNGDK MSKSTGNFLT
IAGAVQKFGA DATRIALADA GDEISDANFE ETVANSNILK LFELRKWCED LMNEAIYVPD
AAAYMEKRAN ERVKNADVIQ RQSGSERLLF DKMFDNEMNV LVHEAFGHYS NTSYKLALKS
GFYDFTSARD FYREATKAAG IGMHQDLVKK FIELQALLLT PLAPHWAEYI WLEVLKNKET
IQNALWPKVP ESDPSLTAAR EFVRTTQTNI TSAEGNAIKK LSKGKAATFD PKKEKKIIIF
SAQEWPAWQK KYIDMLRDAA TIDIKAISKS IDKSESKKAM PFINGLKRRL DNGEPKEVVL
NRELAFDELS TLRVMVPGLK QTIQKCVDVE IIVVSEGGKD GTVIKEDGSK GETRSELPPQ
AATAEPGSPS FAFENVESVP VR
//
