ID A0A081CNZ9_PSEA2 Unreviewed; 748 AA.
AC A0A081CNZ9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 03-MAY-2023, entry version 43.
DE SubName: Full=Aspartyl-tRNA synthetase {ECO:0000313|EMBL:GAK68395.1};
GN ORFNames=PAN0_083d6645 {ECO:0000313|EMBL:GAK68395.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK68395.1};
RN [1] {ECO:0000313|EMBL:GAK68395.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK68395.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF830150; GAK68395.1; -; Genomic_DNA.
DR RefSeq; XP_014653404.1; XM_014797918.1.
DR AlphaFoldDB; A0A081CNZ9; -.
DR GeneID; 26307442; -.
DR HOGENOM; CLU_014330_4_0_1; -.
DR OrthoDB; 1046261at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 2.
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:GAK68395.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053758}.
FT DOMAIN 213..705
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 81928 MW; 053B7601310FFC6C CRC64;
MLAPSARAVQ RIALRARSVR VAAAWPSSAP SRLSLRPYAT THAPASSSPQ QRDQRASENA
FYGAFPARTH VCGELRPEHE DQEVILTGWI QSSRQVSKQL AFFTMFDHSG SVQLKLQPTE
ASPALLESLA AVPSQSAVLI RGRVALRPVQ DSKATMGTGA VEVIPHSFTL LNPATRDLPF
HPSDSLHADG VSTELRARYR YLDLRRPSLA SNIRLRSRIT HAVRNHLYDN GFLEIETPVL
LRSTPEGARE FLVPTRTSSS EPAFYALPQS PQQPKQLLIA SGVTDRYFQI AKCFRDEDGR
KDRQPEFTQI DLEMGFVSGG PESAPAQAAT LLSPVDGGVD QRDAGGAWRI GGHQVRDVIE
RLVSRIWQVA GRGELPTHFP VMSYWTAMTR YGSDKPDLRY DLALHDISSG FVSSTDPAVE
HEPRSMSLEV LPYQVSASGG LSKKELDTLL VGFKGRVERF RIASSENIYE LAALLLKKSA
LTRTFLQELD DVSASEIDVE HLATTLRAAI GDTSDGAVDV FVSLRKDPPE GGSTVLGDVR
KQLAGMLERK GLLKLNGDAF VWITEFPLFT LADEDKNQLA SLSSTTSTTR WQSSHHPFTA
PVAEDIHLLT QDAQDIAKVR GQHYDLVLNG QEIGGGSVRI HSAKLQQTVF QRVLRLDAAE
QGRFAHLIHA LDCGAPPHGG IALGFDRLMA ILCNTDTIRD VIAFPKQSSG IDPLFASPAP
IADPADHQDK TDTLLQMYRL AKASSSKS
//