ID A0A1C8ZWL1_9CREN Unreviewed; 429 AA.
AC A0A1C8ZWL1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000256|HAMAP-Rule:MF_02075};
DE EC=6.1.1.23 {ECO:0000256|HAMAP-Rule:MF_02075};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075};
DE Short=AspRS {ECO:0000256|HAMAP-Rule:MF_02075};
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075};
DE Short=ND-AspRS {ECO:0000256|HAMAP-Rule:MF_02075};
GN Name=aspS {ECO:0000256|HAMAP-Rule:MF_02075};
GN ORFNames=BFU36_05010 {ECO:0000313|EMBL:AOL17674.1};
OS Sulfolobus sp. A20.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1891280 {ECO:0000313|EMBL:AOL17674.1, ECO:0000313|Proteomes:UP000094286};
RN [1] {ECO:0000313|Proteomes:UP000094286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A20 {ECO:0000313|Proteomes:UP000094286};
RA Dai X.;
RT "Genome sequencing of Sulfolobus sp. A20 from Costa Rica and comparative
RT analyses of central carbon, nitrogen and sulfur metabolism in various
RT Sulfolobus strains.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since
CC it is able to aspartylate not only its cognate tRNA(Asp) but also
CC tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first
CC activated by ATP to form Asp-AMP and then transferred to the acceptor
CC end of tRNA(Asp/Asn). {ECO:0000256|HAMAP-Rule:MF_02075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710,
CC Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.23; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02075};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02075};
CC Note=Binds 3 Mg(2+) cations per subunit. The strongest magnesium site
CC (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water
CC molecules complete its coordination sphere. {ECO:0000256|HAMAP-
CC Rule:MF_02075};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312, ECO:0000256|HAMAP-
CC Rule:MF_02075}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02075}.
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DR EMBL; CP017006; AOL17674.1; -; Genomic_DNA.
DR RefSeq; WP_069284599.1; NZ_CP017006.1.
DR AlphaFoldDB; A0A1C8ZWL1; -.
DR STRING; 1891280.BFU36_05010; -.
DR GeneID; 28695195; -.
DR KEGG; sula:BFU36_05010; -.
DR OrthoDB; 5908at2157; -.
DR Proteomes; UP000094286; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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 InterPro; IPR004365; NA-bd_OB_tRNA.
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 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|HAMAP-Rule:MF_02075};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02075};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02075, ECO:0000313|EMBL:AOL17674.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02075};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02075};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02075};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02075}.
FT DOMAIN 134..429
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 189..192
FT /note="Aspartate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 167
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 210..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 210
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 355
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 359
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 400..403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT SITE 82
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
SQ SEQUENCE 429 AA; 48974 MW; E874F2213F3DD53C CRC64;
MFRTHFISEL NDNLDGKEVK LAGWVHNIRN LGGKVFLILR DKSGTVQVVV EKSSKAYEVL
NQLSLESAIS ITGSVKKDER APNGIEVHAK EISIISVSKS PLPLDVSGKV KADIDTRLRE
RLLDLRRPEM QAVLKIQSVA VKSFRETLYK NGFIEVFTPK IIASATEGGA QLFPVMYFGK
DAFLAQSPQL YKELLAGAIE RVFEIAPAWR AEESDTPYHL SEFISMDVEM AFADYNQVMQ
LIEQIMYNMI NDVKRECEKE LKVLNHTLPD VALPLRRITY SEAIEILQNK GLNIKFGDDI
GTPELRLLNE EIKENLYFII DWPWLSRPFY TKQKSDNPQL SESFDLIYKW LEIASGSSRN
YIREVLENSL KVRGLNPTSF EFFLKWFDYG MPPHAGFGMG LARVMLMLTG LQSVKEVVPF
PRDKKRLTP
//
