HAMAP rule MF_02075
General rule information
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Accession | MF_02075 |
Dates | 29-SEP-2016 (Created) 19-NOV-2022 (Last updated, Version 6) |
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] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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case <FTTag:Discr_arch>
Identifier |
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Protein name |
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else case <FTTag:NonDiscr_arch>
Identifier |
|
Protein name |
|
else
Identifier |
|
Protein name |
|
end case
Gene name |
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Comments
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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
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case <OC:Archaea>
end case
Gene Ontology
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GO:0004815; Molecular function: aspartate-tRNA ligase activity.
GO:0005524; Molecular function: ATP binding.
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.
GO:0005737; Cellular component: cytoplasm.
Cross-references
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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
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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 (Optional) | 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 | 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 (Optional) | 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>
end case
From: SYDND_DEIRA (Q9RVH4) | ||||||||||||
SITE (Optional) | 77 | 77 | Important for tRNA non-discrimination | NonDiscr_arch | P |
Additional information
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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. |