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Annotation rule MF_02075
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General rule information [?]

Accession MF_02075
Dates 29-SEP-2016 (Created)
20-NOV-2019 (Last updated, Version 4)
Name Asp_tRNA_synth_type2
Scope
Bacteria
Archaea
Templates Q52428 (SYD_THEKO); O07683 (SYDND_HALSA); Q5SIC2 (SYDND_THET8); O26328 (SYDND_METTH); Q8Q0R2 (SYDND_METMA); Q9RVH4 (SYDND_DEIRA): [Recover all]

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
aspS

Comments [?]

case <FTTag:NonDiscr_arch>
Function Aspartyl-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 RHEA:18349: ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
EC 6.1.1.23
else
Function Catalyzes 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 RHEA:19649: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
EC 6.1.1.12
end case
case <OC:Archaea>
Cofactor Mg(2+)
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
Subunit Homodimer.
Subcellular location Cytoplasm.
Similarity Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.

Keywords [?]

case <OC:Archaea>
end case

Gene Ontology [?]

GO:0004815; Molecular function: aspartate-tRNA ligase activity.
GO:0005524; Molecular function: ATP binding.
case <OC: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;
PF01336; tRNA_anti-codon; 1;
PRINTS PR01042; TRNASYNTHASP; 1;
TIGRFAMs TIGR00458; aspS_nondisc; 1;

Features [?]

From: SYD_THEKO (Q52428)
Key     From     To       Description   Tag   Condition   FTGroup
NP_BIND     214     216       ATP     R-x-E  
NP_BIND (Optional)     222     224       ATP     [RK]-H-[LV]  
NP_BIND     409     412       ATP     G-x-x-R  
REGION     192     195       Aspartate     Q-x-x-K  
BINDING     170     170       Aspartate     E  
BINDING     214     214       Aspartate     R  
BINDING     361     361       ATP     E  
BINDING (Optional)     364     364       Aspartate     [ST]  
BINDING     368     368       Aspartate     R  
case <OC:Archaea>
METAL     361     361       Magnesium 2     E  
METAL     361     361       Magnesium 3     E  
METAL     364     364       Magnesium 2     [ST]  
SITE (Optional)     85     85       Important for tRNA discrimination   Discr_arch   K  
end case
From: SYDND_DEIRA (Q9RVH4)
SITE (Optional)     77     77       Important for tRNA non-discrimination   NonDiscr_arch   P  

Additional information [?]

Size range 400-620 amino acids
Related rules MF_00044 (SYDND)
Fusion 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.