ID A0A0L6WWJ9_9AGAR Unreviewed; 678 AA.
AC A0A0L6WWJ9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Aspartyl-tRNA synthetase {ECO:0000313|EMBL:KNZ79930.1};
GN ORFNames=J132_08588 {ECO:0000313|EMBL:KNZ79930.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ79930.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) 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; KQ412282; KNZ79930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6WWJ9; -.
DR STRING; 1306850.A0A0L6WWJ9; -.
DR OrthoDB; 1046261at2759; -.
DR Proteomes; UP000053712; 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; 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; 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:KNZ79930.1}; 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:UP000053712}.
FT DOMAIN 176..659
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 678 AA; 75453 MW; F51A298E52C73597 CRC64;
MAPCGGASGA AAFPPLSVLS HCAPYPSRTH TCGSLTARDE GARVVLTGWI LPERKGKRMS
FYPLKDSYGT TQLIVDHSEG APDLSALAKI PVESSVLIEG TVLLRPPNAR RPVISCPKGP
TGEIDVQVEK FTVLNTARSL PFVPSNPHNV ANDDVRARYR YLDLRRTVLS ENIKKRSKVA
QTVREVLHQR DFVEVETPVL LRSSPEGARE FLVPTRITKP NGSGIGNANP TFYALQQSPQ
QPKQLLICSG GVDRYFQLAK CFRDEDGRKD RQPEFTQIDL EMSFVSWGPH ESREVQSSNV
WRIGGSEVRD MVETLIQQIW QQVEGISLPS NFPVMTYHEA MTRVSLRSLF TTSELVTIYA
QFGSDKPDTR FGLEVSDITH LLPEKQRSLF EDNMEILEMI AVRKSGEAQF LGASRVCKPD
STAECITVTN RTLNSWLSGA TTHASLKELT SEEISYINEK LQLVPGDDVW LARRSRIAKG
GSTALGAVRL RISEIAQARN DFVITTTPHI LWITEFPLFT QADADKDFLA KGRWSSTHHP
FTAPMWQDID AMYRGDIEAV RGQHYDLVLN GVEIGGGSVR VHDAIMQDFI FTHILKLNEA
EKEPFQHLLH ALQCGAPPHG GIALGFDRMM AMLCHTQSIR DVIAFPKTAT GTDFLFRSPA
PISDEVLFQY GIQPRSTT
//