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HAMAP rule MF_02075
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
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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. |