ID A0A0G1U5T9_9BACT Unreviewed; 434 AA.
AC A0A0G1U5T9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Aspartate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02075};
DE EC=6.1.1.12 {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};
GN Name=aspS {ECO:0000256|HAMAP-Rule:MF_02075};
GN ORFNames=UY19_C0014G0057 {ECO:0000313|EMBL:KKU89457.1};
OS Candidatus Wolfebacteria bacterium GW2011_GWA2_47_9b.
OC Bacteria; Candidatus Wolfebacteria.
OX NCBI_TaxID=1619005 {ECO:0000313|EMBL:KKU89457.1, ECO:0000313|Proteomes:UP000033882};
RN [1] {ECO:0000313|EMBL:KKU89457.1, ECO:0000313|Proteomes:UP000033882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a
CC two-step reaction: L-aspartate is first activated by ATP to form Asp-
CC AMP and then transferred to the acceptor end of tRNA(Asp).
CC {ECO:0000256|HAMAP-Rule:MF_02075}.
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; 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02075}.
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:KKU89457.1}.
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DR EMBL; LCPB01000014; KKU89457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1U5T9; -.
DR PATRIC; fig|1619005.3.peg.796; -.
DR Proteomes; UP000033882; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
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 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 ECO:0000313|EMBL:KKU89457.1};
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}.
FT DOMAIN 132..434
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 209..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 209
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 360
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 364
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 405..408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
SQ SEQUENCE 434 AA; 49455 MW; 3F61E12108B72C70 CRC64;
MERIHSTAIG GRVGQTVKLA GWAQAIRDQG GIMFIVLRDI TGTAQLVISG ELLEAARSIQ
LESVIEVVGQ VATETKSHSG VEIQVSELTI LSMAEPELPI PVVEKSDAPT DQQIRLDWRF
LDIRKPEKAL LFKVWTELER SFIEYCTEQE YIEIHSPKLM STPSEGGAEL FEVQYFERKA
YLAQSPQFYK QMAMAGGFEK VFEIGPVFRA EPSSTPRHAT EFNGFDLEKS FITSHQDIIQ
EEERLIVHAL TNIKTKYGEE IKRLYQRDVH IPVIPFPQLT VAQAKEILGK LGITSEKEGD
LSPEEEREIS KYIKETHGHE FVFITEYPAS VRAFYHMRLE DKPDITKSFD LLWNGIEITT
GAQREHRLEI LIRQAKEKGI GTESLQFYFD FFKYGCPPHG GFGAGPERMI MKLFGLDSIR
EASYIYRGMK RLTP
//
