ID G7X7K0_ASPKW Unreviewed; 676 AA.
AC G7X7K0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Aspartyl-tRNA synthetase {ECO:0000313|EMBL:GAA82778.1};
GN ORFNames=AKAW_00893 {ECO:0000313|EMBL:GAA82778.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA82778.1};
RN [1] {ECO:0000313|EMBL:GAA82778.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA82778.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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DR EMBL; DF126448; GAA82778.1; -; Genomic_DNA.
DR AlphaFoldDB; G7X7K0; -.
DR STRING; 1033177.G7X7K0; -.
DR VEuPathDB; FungiDB:AKAW_00893; -.
DR eggNOG; KOG2411; Eukaryota.
DR InParanoid; G7X7K0; -.
DR Proteomes; UP000006812; 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 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; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00459; aspS_bact; 1.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-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 Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:GAA82778.1}; 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}.
FT DOMAIN 222..660
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 523..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 76147 MW; 9DB32A4146E71281 CRC64;
MYLARAVRCP PHLRATYVEI SNYFRGRQLG RLSALQAHSP PVRSFHEFSE KHRSNVTSSE
FLDKFKQSME FPQTPLDIDT LYSHDHEGQS VLLHGYLDKR DDMGKELSFA RFYDHTMGRT
IQLLSNSQSN TLPQLKKISR GSPVVVRGTV KRRVTKTAEE ERTDYLEIAL ESIQPLNEFP
REIVLFGKNI VHPPKHRHLQ LRSDKELRDA LRFRAQARNV CRETLEQLKP AFVEIETPLL
FKSTPEGARE FIVPTRKKGK AYALPQSPQQ YKQILMASGI PRYFQFARCF RDEDLRADRQ
PEFTQLDLEM AFAAGQDVMA VVEELIRGLW GNMMPEPVPS GLFRRMTYQE AMTRYGSDKP
DTRHGMEIHR VEHLLPADLV SKITPLTDPI VEAFKMDTVE QLPSATREFV SRFFDSTEGE
PFNKNPDGAP GIFIYDEGQP LKGLGPLGFE AAEKIQEMLD LSHGDLLILQ ARPQAPFAGG
ATQLGSIRRA MAAASIAEDL REAPPGFEFL WIVDFPLFSP TDASEPGQGG TAGLSATHHP
FTAPKTSSDV DLLSQDPTKA LADHYDLVVN GVELGGGSRR IHCALTQNYI FKEILKMPKE
RIDEFQHLLN ALWAGCPPHA GFALGFDRLI TVMLGKESVR DVIAFPKIGK KGEDAMVKAP
GKISEEVARL YNIKLK
//
