ID B2WCS5_PYRTR Unreviewed; 1041 AA.
AC B2WCS5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=PTRG_07784 {ECO:0000313|EMBL:EDU50703.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU50703.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000225};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312}.
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DR EMBL; DS231622; EDU50703.1; -; Genomic_DNA.
DR RefSeq; XP_001938116.1; XM_001938081.1.
DR AlphaFoldDB; B2WCS5; -.
DR STRING; 426418.B2WCS5; -.
DR EnsemblFungi; EDU50703; EDU50703; PTRG_07784.
DR GeneID; 6346058; -.
DR eggNOG; KOG0556; Eukaryota.
DR HOGENOM; CLU_004553_1_2_1; -.
DR InParanoid; B2WCS5; -.
DR OMA; KYSLDFP; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04320; AspRS_cyto_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR024320; LPG_synthase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF2; ASPARTATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09924; LPG_synthase_C; 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:0000313|EMBL:EDU50703.1};
KW Ligase {ECO:0000313|EMBL:EDU50703.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT DOMAIN 375..678
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1041 AA; 116723 MW; E42C060A8156475E CRC64;
MSSLKKALDK LKPTKNGHSP SDDEKGGVKS PTSLNSHARA QSPSATSHSS ATLGNSRASG
DFKRSELASP TESRSSIDQP RGSLSGLLHR RTESPNRAGA TKTARSGSLS THSPMRAVKE
KLHIGNDSSD EDAPLNRQGE PMSRGQLRKH ERQAQQEERH KQNMEKEAEL ERRRKEMEQQ
ALTELTPEQR AIYGILPPNG YAGEWKHESR HKIQDFSAKD IGKEVVFRAR IHHLRKMSSK
FVFLMFRQQL ATIQGVLVEH ADISKYMLYW AEHLDAETVV LVKGILQEPK AKQGEVLGAT
IHDVEVSVHA LHVEASVTDH LPFNVNEAEV TQAEVDAELA KEDHKEGHTR VKIADRTRLN
NRVIDLRTTA SQGIFRIQSG ICRLFRNQLD SEGFIEIHTP KLQGGATESG ASVFKIDYFG
RGAFLAQSPQ LAKQMAISAD FGKVYEIGAV FRAENSNTYR HLTEYTGLDL EMQIDEHYHE
VLRVLDRTFK AIFKGIYEQY RPEIEVIKKH FPHEDLVWLD ETPIIPFADA VRMLNESGWR
DDDGNELDVN EDLGTRDEVQ LGRVIKQKLG TDYYILDKFP ANARPFYAMN DPNNPNVTNS
FDIFCRGQEI LSGGQRIHDA DMLLEKMRKL KVDPSSMEEY IQGFQWGAPP HGGGGIGLER
ILMLMMSLGN IRHASMFPRD PKSLPEKAVI KQLRHPEAST MHPPWEGQDR AVAKIDLQPI
EKLIANYGDA TNTSWLEPRT EIWRDENTGA AVGFVPQDGF AITVGDPLCH ESQYLKTMAA
YLKYIKKERN LKPLWLLVGA AAEEVLATKF NWRTFSVTGE QRVDPAHNPA DKDSDVQRKI
RHAEKEGVKI ADYKIGSPPP PEIKQKVDAR VEDWLKNRKG KQVHLTNIHP WQDEEHRQYH
IATTSDGTIA AFVAMAQLSP DHGWQVKYSL DFPGAPGGSI EYIVTHALKQ VAAEGATSVT
FGGGASSKFS PGHNVKGTRV KVLSRAYHAI ATELKLTNKT EFREKLGAVD DPSYICYPPH
GLGPMAVKAI LNFFSDDDDN N
//
