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
//