ID A0A1E3ICD9_9TREE Unreviewed; 887 AA.
AC A0A1E3ICD9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=L203_04362 {ECO:0000313|EMBL:ODN86244.1};
OS Cryptococcus depauperatus CBS 7841.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN86244.1, ECO:0000313|Proteomes:UP000094043};
RN [1] {ECO:0000313|EMBL:ODN86244.1, ECO:0000313|Proteomes:UP000094043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN86244.1,
RC ECO:0000313|Proteomes:UP000094043};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN86244.1}.
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DR EMBL; AWGK01000018; ODN86244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3ICD9; -.
DR STRING; 1295531.A0A1E3ICD9; -.
DR VEuPathDB; FungiDB:L203_04362; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000094043; 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; 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; 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:ODN86244.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094043}.
FT DOMAIN 239..545
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 101847 MW; 92CC567D91F8268B CRC64;
MTTEPTQPSN PLAKLGQAIK SRLPNGKQEQ EDDNGSDHDQ IQIEREQRKQ QEMQEQKEKQ
MRLQREAEEL RQRRLEADLR AQQEDDPETR ASYGKLEDLE EITPLEDIVQ LPAGTRVTTR
VRIHTQRDIS SHINFVILRH RGYLIQGLLP DGTSEHMIKW VQHLPDESIV QVTGTLQNPP
QPITSNVDTP LEIIIESIHL VEASYDIPFS LSRGFRPPQN TRLNNRTLDL RHPTNQAIFK
IRSKVLKVFR DTLEDLSFLE INTPKLQPAA TESGAEVFRV NYFGRKAFLA QSPQLMKQMA
ISADFGRVYE IGPVFRAENS NTHRHLTEYT GLDIEMLIEK DYHEVFQVVD IVLKNIFKTL
TNMKTELGRV LEHFLYEDLQ WLDETLILPF HEAIQMLRDD GRDVEEEDLS TPDEIRLGQI
IKEKYKTDYY AIDRFPISAR PFYTANDGEA TNSFDLFIRG QEICTGGQRI NDSEKLRQSM
YDSGIDPREM QEYLSAFDWG MPPHGGAGLG LERIVTFFLN LPDVRLATLY HRDPHSLPVS
PAYLPHPEAD TTKPTDPSNP PPVEMLIANY GDAANTSWLD DRFEIWHDEE TGAAVGYSKQ
DSKFCMITGD PLCAEKQKKE VTKRFIDFVQ RVIKLRPVWM LVSETMEEIL AEEHGWRALS
CTQEQRSDSD KADLSLIHNS KQKKGVFKVR EIEPKEDIIR RIDDRIEDWK SGRNEKGKQI
RLTEVAPWKD MEHRRYFIAE SHHEEDQIIK EDDNSAKIKG NPSIDTLVVL TRLAPSKGYQ
LKWALDFPGA PHDAIECTVQ AALSAVPGEP VTFGTAVSER LVQKHGISET RARFMEKTYK
GIVKSLALDK KAGFREKFGV TGDLTYICYP KGGVKPYELK DIVKFFE
//
