ID   A0A165DCY7_9APHY        Unreviewed;       960 AA.
AC   A0A165DCY7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE            EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN   ORFNames=LAESUDRAFT_703211 {ECO:0000313|EMBL:KZT04593.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT04593.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT04593.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT04593.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV427635; KZT04593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165DCY7; -.
DR   STRING; 1314785.A0A165DCY7; -.
DR   InParanoid; A0A165DCY7; -.
DR   OrthoDB; 382728at2759; -.
DR   Proteomes; UP000076871; 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:KZT04593.1};
KW   Ligase {ECO:0000313|EMBL:KZT04593.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT   DOMAIN          295..598
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   960 AA;  109145 MW;  AD980479F0B1CCE5 CRC64;
     MSSIKKVIHR ARNSISSGHC SSPVRELDDD AHNRHASNGH AHVDDTNADC PTAAQRQQAH
     EPDKPHHTQR PSTEMRRRRM SFTEQKVERH MERKEIDKRE AAERKERQKH AHDEDPLRDN
     YGDLPMNMSQ NLSETRLSSL IAVNDMEQGT HVTFRARVHH IRPLGSKIVF IIFRSQLSTL
     QGVLAEEEYK VSQNMIHWAE GLNRETVVLV EGMVQNPPED QSEVKSARVK SREVKVEKLY
     VVAGPTSPPP FQVEDVSRAE KVYHQEDAHF SRVNQKTRLL NRVLDLRSPT NQAIFRIRAG
     VGTLFREYLL ERNFLEIQSS KFQKTSTESG AAVFKVDYFR RPAFLAQSPQ LAKQMCIAGD
     MERVFEIGPV FRAENSNTHR HLTEFTGLDL EMQFESHYHE VLDTIDELLK YIIKGVQKRY
     REEIETVKLQ FPHDDLVILD ETPRLRFADG IRMLKESGWK EEDGSEPSEW ADLSTKAEQR
     LGVLMKAKYG ADYYILDKFP LEVRPFYTMP DPQDHRLSNS FDIFLRGEEI LSGGQRIHVA
     PMLEERMRAV GIDPDSMKDY VDGFRWGCPP HGGGGIGLER VVMLFLKLGD IRYASLFPRD
     PRSFPANGQD LAEASMSAAT HMILHGPEAT TFKEGYPHGD MPLLQDLIAK YGDSTNTSWI
     DPAWTVWRDP ATGAAVGYIP QNEFAVAFGN PLCEHKQMGR VVQAYVKYVE EKNLKPVWCC
     IDKECERIVA EDMGWSAIIA VAEERLNPIE VDPAANDKTV RRKIHKAERD GVKIVEVEGG
     MDPKTREKLE ERCKEWAENR KGTQIHLTGV RPFDDMKHRK YFYAVDKDGK PCAMVVLAQL
     APTHGFQIKW SLEFPGAPLG AIEYILTHVI KKLGDAGLRS ATFGAGATER LQRVDNLGGF
     RVRTLEKTYN GIASTFHLSG KGDFRAKFGI HQEPMFICYP KGGLGMKGIE AIMAALQMPK
//