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Database: UniProt
Entry: A0A395ICR4_ASPHC
LinkDB: A0A395ICR4_ASPHC
Original site: A0A395ICR4_ASPHC 
ID   A0A395ICR4_ASPHC        Unreviewed;       683 AA.
AC   A0A395ICR4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Aspartyl-tRNA synthetase {ECO:0000313|EMBL:RAL15964.1};
GN   ORFNames=BO97DRAFT_383846 {ECO:0000313|EMBL:RAL15964.1};
OS   Aspergillus homomorphus (strain CBS 101889).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL15964.1, ECO:0000313|Proteomes:UP000248961};
RN   [1] {ECO:0000313|EMBL:RAL15964.1, ECO:0000313|Proteomes:UP000248961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL15964.1,
RC   ECO:0000313|Proteomes:UP000248961};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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; KZ824270; RAL15964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395ICR4; -.
DR   STRING; 1450537.A0A395ICR4; -.
DR   VEuPathDB; FungiDB:BO97DRAFT_383846; -.
DR   OrthoDB; 1046261at2759; -.
DR   Proteomes; UP000248961; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   CDD; cd04321; ScAspRS_mt_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; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
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   Pfam; PF01336; tRNA_anti-codon; 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:RAL15964.1}; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248961}.
FT   DOMAIN          224..652
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   683 AA;  75497 MW;  19D933B28A328562 CRC64;
     MFLSRAVRCP PQLRASYVEI SNYFRGRRPA FNRTFYAHSS PLRAPHGIQP PPEQSDADKS
     ASAALASFKK SIEFPSPTYD FETFLRTAQP GQEVVLQGYV SSRRELSSKL AFIRLRDPTL
     KHSVQVVSTQ KSGTFAAAKA VRTHSPVVIK GTVQKKQAKD AEMAEKDPWE IVLTEIQALN
     EFPKDIVLTG EHAHPPKHRH LQLRSSDELR DALRFRAEAR NVCRQELEQA RPGFVEIETP
     MLFKSTPEGA REFLVPSRKR GLAYALPQSP QQYKQILMAS GIPRYFQFAR CFRDEDLRAD
     RQPEFTQLDL EMSFATGNDV MQVVEGVIRR LWSELMPEPA PSGPFRRMPY QEAMSRYGSD
     KPDTRYGMEI SRIDYLLPVD LVQKITPLTD PVVEVFRLEG NDNDPAATQE FITRFLDSPE
     GAPFNENPDG GPGIFVVDAK KPLSGLQPFG FEAAEHLETT LGIEHGDLVV IQARAQGSLT
     GGSTALGNLR RALHAAAVAT GFKPAPPGFE FMWVVDFPLF TPAAEDSAEE PGQGGAAGFS
     ATHHPFTAPK SAADVDLLTS ADPTQATADH YDLVVNGVEL GGGSRRIHDA AVQEFVFRHV
     LRMPDHRIAD FAHLLEALRA GCPPHAGFAL GFDRLVAVML GKESVRDVIA FPKIGKTGED
     PMVKAPSPIS EEAAKIYHLS VKE
//
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