AC   MF_02075;
DC   Protein; auto
TR   HAMAP; MF_02075; -; 1; level=0
XX
Names: Asp_tRNA_synth_type2
XX
case <FTTag:Discr_arch>
ID   SYD
DE   RecName: Full=Aspartate--tRNA(Asp) ligase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
DE   AltName: Full=Discriminating aspartyl-tRNA synthetase;
DE            Short=D-AspRS;
else case <FTTag:NonDiscr_arch>
ID   SYDND
DE   RecName: Full=Aspartate--tRNA(Asp/Asn) ligase;
DE            EC=6.1.1.23;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
DE   AltName: Full=Non-discriminating aspartyl-tRNA synthetase;
DE            Short=ND-AspRS;
else
ID   SYD
DE   RecName: Full=Aspartate--tRNA ligase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
end case
GN   Name=aspS;
XX
case <FTTag:NonDiscr_arch>
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).
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;
else
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   -!- 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;
end case
case <OC:Archaea>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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.;
end case
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 2 subfamily.
XX
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no
DR   Pfam; PF00152; tRNA-synt_2; 1; trigger=no
DR   Pfam; PF01336; tRNA_anti-codon; 1; trigger=no
DR   PRINTS; PR01042; TRNASYNTHASP; 1; trigger=no
DR   NCBIfam; TIGR00458; aspS_nondisc; 1; trigger=no
XX
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Cytoplasm
KW   Ligase
case <OC:Archaea>
KW   Magnesium
KW   Metal-binding
end case
KW   Nucleotide-binding
KW   Protein biosynthesis
XX
GO   GO:0004815; F:aspartate-tRNA ligase activity
GO   GO:0005524; F:ATP binding
case <OC:Archaea>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0006422; P:aspartyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYD_THEKO (Q52428)
FT   BINDING         214..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R-x-E
FT   BINDING         222..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: [RK]-H-[LV]
FT   BINDING         409..412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-x-x-R
FT   REGION          192..195
FT                   /note="Aspartate"
FT   Condition: Q-x-x-K
FT   BINDING         170
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: E
FT   BINDING         214
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: R
FT   BINDING         361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: E
FT   BINDING         364
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Optional; Condition: [ST]
FT   BINDING         368
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: R
case <OC:Archaea>
FT   BINDING         361
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         361
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT   Condition: E
FT   BINDING         364
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: [ST]
FT   SITE            85
FT                   /note="Important for tRNA discrimination"
FT   Tag: Discr_arch; Optional; Condition: K
end case
FT   From: SYDND_DEIRA (Q9RVH4)
FT   SITE            77
FT                   /note="Important for tRNA non-discrimination"
FT   Tag: NonDiscr_arch; Optional; Condition: P
XX
Size: 400-620;
Related: MF_00044;
Template: Q52428; O07683; Q5SIC2; O26328; Q8Q0R2; Q9RVH4;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: This subfamily contains archaeal aspartate--tRNA ligases, some
 bacterial aspartate--tRNA ligases and eukaryotic cytoplasmic
 aspartate--tRNA ligases.
 See MF_00044 for type 1 subfamily.
XX
# Revision 1.7 2023/06/01
//