SYDND_HALVO
ID SYDND_HALVO Reviewed; 433 AA.
AC O24822;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_02075};
DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_02075};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02075};
DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_02075};
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02075};
DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_02075};
GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_02075};
OS Haloferax volcanii (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=2246;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shinoda H., Ihara H., Ishigami M., Nakano Y., Yamaji R.;
RT "Haloferax volcanii gene for aspartyl tRNA synthetase.";
RL Submitted (JAN-1998) 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:0000255|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:0000255|HAMAP-
CC Rule:MF_02075};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_02075};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02075}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02075}.
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DR EMBL; AB010464; BAA31457.1; -; Genomic_DNA.
DR AlphaFoldDB; O24822; -.
DR SMR; O24822; -.
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 Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 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; PTHR43450; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00458; aspS_nondisc; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..433
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_0000110993"
FT REGION 189..192
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 167
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 211..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 211
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 219..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 359
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 363
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 404..407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT SITE 82
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
SQ SEQUENCE 433 AA; 48691 MW; 71A3C6AE6325EEA7 CRC64;
MRNRTYTADA EPGDTVTVAG WVHEVRDLGG IAFLILRDTS GKIQVKFEKD EMDDDLVETG
LGVHRESVIS VTGEVDEEPR APTGVEVTPE SLDVIAEAEA QLPLDPSGKV DAELSTRLDN
RTLDLRKDEV KAIFEIRAEV QRAVRDKFRD LRATEINTPK IVATGTEGGT ELFPITYFGQ
EAFMNQSPQL FKQLMVGSGL ERVFEVGPIF RAEEHNTPRH LNEATSIDFE SAFIDHTEAM
DVCEAVVTAA YEAVEENCQD ELEALGLEEE FERRPRVPAA HLRGGHRAHQ RTGELDEQLV
WGDDLPTEGE KALGEDVGEH YFITDWPSEI KPFYIKDHDD DETLSTGFDM MHPNMELVSG
GQREHRFDHL VAGFEQQGLD PDAFEYYTKM FKYGMPPHAG FGLGGERLIM TMLGLENIRE
AVLFPRDRQR LSP
