ID   W1PRC8_AMBTC            Unreviewed;       681 AA.
AC   W1PRC8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE            EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN   ORFNames=AMTR_s00029p00241780 {ECO:0000313|EMBL:ERN09785.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN09785.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(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; KI392980; ERN09785.1; -; Genomic_DNA.
DR   RefSeq; XP_006848204.1; XM_006848141.2.
DR   AlphaFoldDB; W1PRC8; -.
DR   STRING; 13333.W1PRC8; -.
DR   EnsemblPlants; ERN09785; ERN09785; AMTR_s00029p00241780.
DR   GeneID; 18437945; -.
DR   Gramene; ERN09785; ERN09785; AMTR_s00029p00241780.
DR   KEGG; atr:18437945; -.
DR   eggNOG; KOG0556; Eukaryota.
DR   HOGENOM; CLU_004553_2_1_1; -.
DR   OrthoDB; 382728at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
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; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00458; aspS_nondisc; 1.
DR   PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR43450; ASPARTYL-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   Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT   DOMAIN          383..681
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  78063 MW;  EFD3305C9658F025 CRC64;
     MDVQSQDEVV DEFNNSDSEC NNSDSNKMLP PPEEKFQYRD ELLNYVRNFA MTQGYMITIK
     RSEKDRRVVL GCDRGGTYKS NGYISLQKRK TKSRLISCPF QMLGVKKSDG LWVLKLKNPD
     HNHGPWKDIS SHPFCRRFSE EEILRIKEMN VAGFQPRQIL DALKQSNPNL QAVLTDVYNV
     KGKIRLENRY PIYAPDLSAS NYGDLSIEEF ESKKVGDHER ATIESLSNEL KGKEVWVRAR
     VHSIREVSKN MVFLILKEKW YTLQCVVTVT QGFVSQQMVK YVSALGVDSF VDVYGVVVVP
     GILIKGASQQ VEIQAKKVYC VNRAVQYLPF NLEDAAQSES EFLSVEQAGE QIARVIQETR
     PKHRFLELGT PANQGIFHFK YQIEEVFRHF LSSKGFIGVH TPKLVAGASE GGSSVFKLEY
     KGQPACLAQS PQLHKQMLAG QFSRVFEIGP AFRAEDSYTH RHLCEFISLD VEMEVEKGYF
     ELLDFVDWLF VSIFDELNER CKKELAAINE QYPFEPLKYL RKTLRLTFEE GIQMLREAGI
     EADLLGDLNI ETERKLGQIV RDKFNTDFYI LHRYPLALRP FYTLPCSDNT SFGRSFDVFM
     RGEEIISGGQ RIHIPQLLVY RAKACGIDTN AFSDYLDSFW YGMPAHGGFG CGLERLVMLF
     CGLDDIRKVS AFPRDPYRLT P
//