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HAMAP rule MF_02075

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General rule information [?]

Accession MF_02075
Dates 29-SEP-2016 (Created)
1-JUN-2023 (Last updated, Version 7)
Name Asp_tRNA_synth_type2
Scope(s) Bacteria
Archaea
Template(s) Q52428 (SYD_THEKO); O07683 (SYDND_HALSA); Q5SIC2 (SYDND_THET8); O26328 (SYDND_METTH); Q8Q0R2 (SYDND_METMA); Q9RVH4 (SYDND_DEIRA); [ Recover all ]
Triggered by HAMAP; MF_02075 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTTag:Discr_arch>
Identifier SYD
Protein name RecName: Full=Aspartate--tRNA(Asp) ligase;
                 EC=6.1.1.12;
AltName: Full=Aspartyl-tRNA synthetase;
                 Short=AspRS;
AltName: Full=Discriminating aspartyl-tRNA synthetase;
                 Short=D-AspRS;
else case <FTTag:NonDiscr_arch>
Identifier SYDND
Protein name RecName: Full=Aspartate--tRNA(Asp/Asn) ligase;
                 EC=6.1.1.23;
AltName: Full=Aspartyl-tRNA synthetase;
                 Short=AspRS;
AltName: Full=Non-discriminating aspartyl-tRNA synthetase;
                 Short=ND-AspRS;
else
Identifier SYD
Protein name RecName: Full=Aspartate--tRNA ligase;
                 EC=6.1.1.12;
AltName: Full=Aspartyl-tRNA synthetase;
                 Short=AspRS;
end case
Gene name Name=aspS;

Comments [?]

case <FTTag:NonDiscr_arch>
FUNCTIONAspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
CATALYTIC ACTIVITY Reaction=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L- aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710, Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; EC=6.1.1.23;
else
FUNCTIONCatalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp).
CATALYTIC ACTIVITY Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L- aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660, Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; EC=6.1.1.12;
end case
case <OC:Archaea>
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 3 Mg(2+) cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.;
end case
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.

Keywords [?]


Gene Ontology [?]

GO:0004815; Molecular function:aspartate-tRNA ligase activity
GO:0005524; Molecular function:ATP binding
case <OCellular component:Archaea>
GO:0000287; Molecular function:magnesium ion binding
end case
GO:0006422; Biological process:aspartyl-tRNA aminoacylation
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

PROSITE PS50862; AA_TRNA_LIGASE_II; 1;
Pfam PF00152; tRNA-synt_2; 1;
Pfam PF01336; tRNA_anti-codon; 1;
PRINTS PR01042; TRNASYNTHASP; 1;
NCBIfam TIGR00458; aspS_nondisc; 1;

Features [?]

From: SYD_THEKO (Q52428)
Key From To Description Tag Condition FTGroup
BINDING 214 216 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
R-x-E
BINDING 222 224 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[RK]-H-[LV]
BINDING 409 412 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
G-x-x-R
REGION 192 195 /note="Aspartate" Q-x-x-K
BINDING 170 170 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"
E
BINDING 214 214 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"
R
BINDING 361 361 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
E
BINDING 364 364 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"
[ST]
BINDING 368 368 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"
R
case <OC:Archaea>
BINDING 361 361 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
E
BINDING 361 361 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="3"
E
BINDING 364 364 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
[ST]
SITE 85 85 /note="Important for tRNA discrimination" Discr_arch K
end case
From: SYDND_DEIRA (Q9RVH4)
Key From To Description Tag Condition FTGroup
SITE 77 77 /note="Important for tRNA non-discrimination" NonDiscr_arch P

Additional information [?]

Size range 400-620 amino acids
Related rules MF_00044
Fusion Nter: None Cter: 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.



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