ID A0A1A8ZMT0_9ACTN Unreviewed; 428 AA.
AC A0A1A8ZMT0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=GA0070611_2927 {ECO:0000313|EMBL:SBT45130.1};
OS Micromonospora auratinigra.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=261654 {ECO:0000313|EMBL:SBT45130.1, ECO:0000313|Proteomes:UP000199385};
RN [1] {ECO:0000313|Proteomes:UP000199385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44815 {ECO:0000313|Proteomes:UP000199385};
RA Varghese N.;
RL Submitted (JUN-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 -!- 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}.
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DR EMBL; LT594323; SBT45130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8ZMT0; -.
DR STRING; 261654.GA0070611_2927; -.
DR PATRIC; fig|261654.4.peg.2977; -.
DR OrthoDB; 9802326at2; -.
DR Proteomes; UP000199385; Chromosome i.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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 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 ECO:0000313|EMBL:SBT45130.1};
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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02075};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02075};
KW Reference proteome {ECO:0000313|Proteomes:UP000199385}.
FT DOMAIN 146..428
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 187..190
FT /note="Aspartate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 165
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 208..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 208
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 216..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 354
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 358
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 399..402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT SITE 79
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
SQ SEQUENCE 428 AA; 46170 MW; 758AC2D64CB4C5E1 CRC64;
MKRILSSQLS HHVGESVRIA GWVHRRRLLK SVAFLIVRDA AGLGQVVVTD PQARAAVEAL
PEETVVEVVG TVVANPTAPA GVELTDPTVR PLGPPAVPPP FDLYRPTLTA TLPTQLDHAP
TALRHPTRSA ALRISAAAVA GFRAGLDARG FVEIHTPKVV ASSTESGANV FALDWFGRPA
YLAQSPQFYK QLMVGVFERV YEVGPVFRAE PHDTVRHLAQ YTSLDVELGF VADHRDVMAV
LRDTLATMLD AVTERAGAAL ATLAVAPPPV PAEIPAVHFT EALKIAGAPA DESDLAPAHE
RALGEWARAE HGSDFLFVTG YPMAKRPFYT HPDPARPAHS NGFDLLFRGV ELVTGGQRLH
RHEDYLAALA ARGEPVEPYA GYLDAFRHGM PPHGGFAIGL ERFVARLTGA ANVREVTAFP
RDLHRLTP
//
