ID   A0A165LFJ3_9APHY        Unreviewed;       998 AA.
AC   A0A165LFJ3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE            EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN   ORFNames=DAEQUDRAFT_718124 {ECO:0000313|EMBL:KZT64350.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT64350.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT64350.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT64350.1,
RC   ECO:0000313|Proteomes:UP000076727};
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}.
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; KV429131; KZT64350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165LFJ3; -.
DR   STRING; 1314783.A0A165LFJ3; -.
DR   OrthoDB; 382728at2759; -.
DR   Proteomes; UP000076727; 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:KZT64350.1};
KW   Ligase {ECO:0000313|EMBL:KZT64350.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT   DOMAIN          313..621
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   998 AA;  112983 MW;  655C938FC6C04605 CRC64;
     MASIKKAFHR ARESMSSRSS LRAKSPEPTK ASPTTGNGHA QPPLNGSAKT NGALATTEVD
     DTNAEGMTAA QRQQEEEARI PETHKQKRSS SESTSRRLSF TEEKVQRAKE RHKHDELEEM
     ERKERRKRLH DGDPLRDHYG DLPLNMSNAQ YTPDLTSLIS VVETPEGEHV KFRARIHHIR
     PLGSKIVFLI FRSQLTTLQG VLTEEEGMVS QNMVRWAEGL NRESIVLVEG MVQKPGDGQE
     EVHSTRVHNH EVKVEKLFVV TSPSSTLPFQ VEDAARPEEY YRREGSHFPR INQKTRLANR
     ALDLRSPVNQ AIFRIRSGVC TLFREYLLAH RFLEIQSSKF QESGTESGAA VFKVDYFRRP
     AFLAQSPQLA KQMCIAADME RVFEIGPVFR AENSNTHRHL TEFTGLDLEM QFDHHYHEVL
     DMLDGMLKHI FRGLQERFKD EACALHIEAV KTQFPHDDLV ILDETPRIRF ADGIKMLRED
     GYKDDDGDEP SEFEDLTTNA ERRLGQLVKE KYGADYYILD KFPLEVRPFY TMPDPEDGKL
     SNSFDIFLRG EEILSGGQRI HVASMLEERM RMADVEPDQA KDYVNGFRWG CPPHGGGGIG
     LERIVMLFLK LGDIRYSSLL PRDPRSFART GQDLAEMSMA AATRQILHGP EASTYQEGIP
     HGDLPPLADL VAKYGDSTST SWVDPSWTVW RDLRTGAAVG YLPQNGFAMT FGNPLCDEKQ
     VPGVIDRYLK FLRGENLKPV WCCIDHDVER ILASDLGWSA IIAVSEERLN PTEVDPASND
     KTVRRKIHRA EREGVKVIDV EGEPDERVHE MLEKKCKQWE ESRKGTQIHL TGLRPWDDMK
     HRKYYYALDK EGNCCAMVVL AQLATTRGFQ IKWALEFPDA PLGAIEYILS HVIKELGDAG
     VTSATFGAGA IDRLQRVENV GGLRIRTLEK TYNGLSSTFN LGGKGDFRQK FGVQQEPLYI
     CYRKGGLGVK GVEALMNALQ RPKPSDLPAD KQEVKTSN
//