ID A0A1W5CXH0_9LECA Unreviewed; 679 AA.
AC A0A1W5CXH0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Aspartyl-trna synthetase {ECO:0000313|EMBL:SLM35536.1};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM35536.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) 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; FWEW01000736; SLM35536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5CXH0; -.
DR OrthoDB; 1046261at2759; -.
DR Proteomes; UP000192927; 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 PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:SLM35536.1}; 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 226..662
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 524..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 74869 MW; 0C3F9CC3AF172404 CRC64;
MSRYQGSSAL APTGALQASI KGKVQDAVLL GDQTITVVEA CIKLHLLARI HCNASNGLSF
LKIQFPAATH EIKALSEPNF HNGESVILHG YLGTRADLSR NLCFVPLLDK ELRYSVQIVS
AAKSSTGEIR PAHGILKVLE PNTPVVVRGL LKPRVPPTSK GPGDVQKIKT VEIELRAVQS
LNDFPKDIIV TPDTEFPLEQ RHLQIRSDEE LRGALAFRAS AANTCRDELI NKYGFLEVET
PLLFKSTPEG AREFIVPTRR KGLAYALPQS PQQFKQILMA SGIPKYFQLA KCFRDEGMRA
DRQPEFTQLD LEVSFATGDN VMNCIEGLIL RLWKDLLQIT LSSPFPRMAY QEAMKRYGSD
KPDIRLGTLI SKVDYLLPAD LVQKISPLTD PIVEAIRFRI DDDYDPTETR SFISKFMESP
EATTFNENPE GGPGIFIHDS RKPLQGLQPL GFEAAEAIDK LFGAREGDLV VLQAREKAPF
SGGSTKLGDL RLALHKEAVK QGLMQPPTGF APLWITDFPL FSPSKSSEPG QGGRAGLAST
HHPFTSPKSS DDVDLLLSDP SKVVGEHYDL VINGVELGGG SRRIHDAKVQ EFIMKDILKM
SPERLAEFSH LLEVLRAGCP PHAGIALGFD RLITVMLGKE SVRDVIAFPK SGKGEDALTR
SPGMMSEEVL ETYHLRLRE
//
