ID A0A0L0LLW0_9BACT Unreviewed; 443 AA.
AC A0A0L0LLW0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 ECO:0000313|EMBL:KND50940.1};
GN ORFNames=AB202_00850 {ECO:0000313|EMBL:KND50940.1};
OS Parcubacteria bacterium C7867-007.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659201 {ECO:0000313|EMBL:KND50940.1, ECO:0000313|Proteomes:UP000037534};
RN [1] {ECO:0000313|EMBL:KND50940.1, ECO:0000313|Proteomes:UP000037534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-007 {ECO:0000313|EMBL:KND50940.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(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:KND50940.1}.
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DR EMBL; LFCQ01000003; KND50940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LLW0; -.
DR STRING; 1659201.AB202_00850; -.
DR PATRIC; fig|1659201.3.peg.163; -.
DR Proteomes; UP000037534; 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 CDD; cd04317; EcAspRS_like_N; 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; IPR047089; Asp-tRNA-ligase_1_N.
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:KND50940.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02075};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02075}.
FT DOMAIN 137..431
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 193..196
FT /note="Aspartate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 170
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 214..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 214
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 222..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 365
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 369
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 410..413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
SQ SEQUENCE 443 AA; 50323 MW; 50EF8F3D84D6916B CRC64;
MERTLIGELS SKAGETITIN GSVDVRRDQG KLVFFDFRDR SGTVQGVVLP GNEVLMEIAK
TVRNEFIVSV SGIVNKRPEK NIQADKQNGD IELEIKEIEV LSSADILPFE LDAELNLDTY
LDYLPLTLRT KRARAIFKVQ SEIARSYRAF LNSEGFIEFQ APKLIGDDAE GSGEVFEVPY
FYGKTAHLAT SPQLYKQIMV GALERVFSIG IVFRAEKHST ARHLNEYTSM DVEMGYITDH
RDVMKMENRL MQYIAADLQK NCSAEFTLLG AEVPVVPDEI PSMKLRAAQE LIFKETGKDN
RNEPDLEPED ERWLCEWSKK VHDSDFVFVT HYPVSKRPMY TTEDQTDPGF TNGFDLLFRG
VEITTGGQRR HEYQNLIDGI KMKGLDPEKF SYYLQAFKYG IPPHGGWGMG LERLTAKFLG
LANVKEATLF PRDINRIDTL LSD
//
