ID A0A1S8W4K9_9FUNG Unreviewed; 628 AA.
AC A0A1S8W4K9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=BSLG_01543 {ECO:0000313|EMBL:OON09402.1};
OS Batrachochytrium salamandrivorans.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON09402.1, ECO:0000313|Proteomes:UP000189906};
RN [1] {ECO:0000313|EMBL:OON09402.1, ECO:0000313|Proteomes:UP000189906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS {ECO:0000313|EMBL:OON09402.1,
RC ECO:0000313|Proteomes:UP000189906};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000225};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OON09402.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LYON01000149; OON09402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8W4K9; -.
DR STRING; 1357716.A0A1S8W4K9; -.
DR VEuPathDB; FungiDB:BSLG_01543; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000189906; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04320; AspRS_cyto_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR43450; ASPARTYL-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 Ligase {ECO:0000313|EMBL:OON09402.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189906}.
FT DOMAIN 323..628
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 628 AA; 71100 MW; FA1AC9E067DBB4C1 CRC64;
MARVVWAIAQ RQAGSIARVF GSCSLASAHR KTQVCLSASL FMSKRSTCQD FICSIFQCSP
QLQQQRQIHS GTVGRIDSTI NTEMAEEPPR SEDIANKMED MVLGEDGKPL SKAAIKKLEK
QREKDLKKAE VAARLAAEKA ARDAASPDYS VEFYGKLPMN QSATRLNEER TSISSIGERH
VGKTLLVSAR VQTSRPTGSK MLFLTLRQGT FTLQTIMTVD AESVSKQMLK FSTGITPESL
VLVSGEVTKV DVLITGCTVQ EYELKIRKIF VVSEASRLPF TLEDATRPDS DFTEDSGFSK
INLDTRLDNR VIDLRTTTNQ AIFRIQAGVS RFFRDFLDNK DFVEIHTPKL IAAASEGGAN
VFRVSYFKES GFLAQSPQLY KQMMVCADFE RVYEIGPVFR AENSQTHRHM TEFMGLDMEM
AFQEHYHEVL DVLDGLFVRI FDGLKEKFQQ ELATIQSQYP FDEFKYLPKS LRLEFPEAIQ
MLRDANVEIG DFDDFNTAQE RLLGKLVREK YNTDFFILDK FPLAVRPFYT MPDPQRPGYS
NSYDFFIRGE EIMSGAQRIH DPSYLKERAE EHGVDISTIQ PYIDAFKYGA PPHAGGGIGL
ERVVMLYLDL GNIRKTSLFP RDPKRLTP
//
