ID E4ZST8_LEPMJ Unreviewed; 683 AA.
AC E4ZST8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Similar to aspartyl-tRNA synthetase {ECO:0000313|EMBL:CBX94526.1};
GN ORFNames=LEMA_P120170.1 {ECO:0000313|EMBL:CBX94526.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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DR EMBL; FP929123; CBX94526.1; -; Genomic_DNA.
DR RefSeq; XP_003837970.1; XM_003837922.1.
DR AlphaFoldDB; E4ZST8; -.
DR STRING; 985895.E4ZST8; -.
DR EnsemblFungi; CBX94526; CBX94526; LEMA_P120170.1.
DR GeneID; 13291047; -.
DR eggNOG; KOG2411; Eukaryota.
DR HOGENOM; CLU_014330_2_1_1; -.
DR InParanoid; E4ZST8; -.
DR OMA; YQLDVEM; -.
DR OrthoDB; 1046261at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070146; P:mitochondrial aspartyl-tRNA aminoacylation; IEA:EnsemblFungi.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:CBX94526.1}; 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:UP000002668}.
FT DOMAIN 237..653
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 683 AA; 76294 MW; 0B84D19D5EA5C237 CRC64;
MSLRHASRHV ASRATCLRSS YSEISRFCRT RQLGIVQVRV EGWKKGVGRC FSQSIVRSDG
IEPDEQLRKT LDDFKTSLRP SWPHEGGVWT PEILEKIPLG SEFTLVGYLG SRRDVSQKLS
FTMLRNENLS WCVQLVSSTS TTEAEAHARL RSLKNWTPVV VTGILKERQP PKQATHQGMK
LVGTREIAVT HVEPINEVSK DLIITEETVF GPDQRHLQLR ADSRLRNNIF LRDRAGRAAR
KVLAENNLVE VETPILFKST PEGAREFLVP TRQKGLAYAL PQSPQQYKQI LMASGITKYF
QFARCFRDED LRADRQPEFT QLDMEMAFAG EEDVMNTIEL LLADLWDKMD LGSIPTKFQR
MTYEEAMSSY GSDKPDLRYE AKANLIGKIT PLQDPIVEAV KIPVSSDPKT TRKFVSSFLD
SPDGKNFLEN PNGQPGIFIG DLSQPMQGLG PLGYQYVMEG PEALAVENGE LLVLQARPNA
PLSGGSTALG NLRLALYKAA ISQDLIEAPA ADDFRFLWIT DFPLFTPSND SDPGQGGTAG
FSSTHHPFTA PKTPADVELL LTAPEKAKAA HYDIVLNGVE LGGGSRRIHN AAVQEFIFRD
ILKMKYERIE DFRHLLDVLR SGCPPHAGIA LGWDRLMAVM TGTESVRDVI VFPKSGKGED
LLVKSPNCVT REQWDTYHLS VKE
//
