HAMAP rule MF_02075
General rule information
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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
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Identifier, protein and gene names
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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
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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 | 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 | |
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 | 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 | |
SUBUNIT | Homodimer. |
SUBCELLULAR LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily. |
Keywords
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Aminoacyl-tRNA synthetase | |
ATP-binding | |
Cytoplasm | |
Ligase | |
case <OC:Archaea> | |
Magnesium | |
Metal-binding | |
end case | |
Nucleotide-binding | |
Protein biosynthesis |
Gene Ontology
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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
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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
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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 | 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
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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. |