ID   A0A0A1T252_9HYPO        Unreviewed;       891 AA.
AC   A0A0A1T252;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE            EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN   ORFNames=VHEMI00521 {ECO:0000313|EMBL:CEJ80332.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ80332.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ80332.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000001; CEJ80332.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1T252; -.
DR   STRING; 1531966.A0A0A1T252; -.
DR   HOGENOM; CLU_004553_0_0_1; -.
DR   OrthoDB; 382728at2759; -.
DR   Proteomes; UP000039046; 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   Ligase {ECO:0000313|EMBL:CEJ80332.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039046}.
FT   DOMAIN          264..572
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   891 AA;  100042 MW;  B16E774309E09311 CRC64;
     MPSSSTPGAA TPNTIASAFG MPRSNSPAGS NRFPRRISPN QTSNTTPASS IDFDRLSLEQ
     REQLRLQGGS MSSSQVNTPA SPIHTEATRR ILAGLNDGFG GSGSNSPRGS MDSVRSTSSA
     DWPVHPNELT TIGQLDTLPI GTSVNFRARI YTQRQLSKAL DFLLLRDQTH SVQGVIARHD
     TDLISWVQKL PPESLVQVAG TLKQPPEPIR SATQSSIEID IEAIHLVNLA QHTPWNNYKP
     PETLRNRMSS RILDLRHPSN HALFRIRSLV MRKFRETLEE QGFLEINTPK LQPAATESGA
     AVFKVNYFGR NAFLAQSPQL AKQMSVSADF GRVFEIGPVF RAENSNTHRH LTEYTGLDIE
     MAIENDYHEV IAVLDDFLKS VFKAVYAMPE IEQVKKRWPS KEFKWLDETL ILDFTEGIQM
     LRDDGRDVPM EDLSTPDEMR LGELVLEKYG TDYYVLDRFP TSARPFYTYK DPEDPNFTRS
     FDIFIRGQEI CSGGQRIHNA QELRDNLAAA GIAEEGMEDY LTAFDLGAPP HAGAGLGLER
     IVAWMLEIGD VRYASLFHRD PKSLPERKPG LPHPEADTTK HLATPPQIEK LIANYGDASN
     TSWLDERFLI WRHETGAAIG YVKHGKFAMV TGDPLCDSSQ YKDVCQSFVK FVTQDLKLVP
     MWMLVSFDVQ KILGRDLGWR TLSCTEEQRI NADKHVTSTD PAKARRVERE GVKIHEVKVD
     ADFISRVDPE IQAWKDNRKG KQVHLTEVRP WVDQAHRRYF VAEKDGKVQC LVVLAKLSPK
     HGWQVKWALD FPGAVNGAIE VLIEHVFSAI TGQVTFGVGA SQKFKPGEHL NGIRAKFLAT
     TYNTIVNRLG LLRKTGFRNK FGALGEDVYI CYPRHGVGLR DLQQVVKFFQ D
//