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Annotation rule MF_00044
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General rule information [?]

Accession MF_00044
Dates 1-JUN-2001 (Created)
27-OCT-2018 (Last updated, Version 38)
Name Asp_tRNA_synth_type1
Scope
Bacteria
Archaea
Templates P21889 (SYD_ECOLI); P36419 (SYD_THETH); Q5SKD2 (SYD_THET8); P56459 (SYDND_HELPY); Q51422 (SYDND_PSEAE); Q9RUN7 (SYD_DEIRA); O84546 (SYDND_CHLTR): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

case <FTTag:NonDiscr1_bact> or <FTTag:NonDiscr2_bact>
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:NonDiscr1_bact> or <FTTag:NonDiscr2_bact>
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
Subunit Homodimer.
Subcellular location Cytoplasm.
Similarity Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.

Keywords [?]

Cytoplasm
Aminoacyl-tRNA synthetase
Protein biosynthesis
Ligase
ATP-binding
Nucleotide-binding

Gene Ontology [?]

GO:0004815; Molecular function: aspartate-tRNA ligase activity.
GO:0005524; Molecular function: ATP binding.
GO:0006422; Biological process: aspartyl-tRNA aminoacylation.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF02938; GAD; 1;
PF00152; tRNA-synt_2; 1;
PF01336; tRNA_anti-codon; 1;
PRINTS PR01042; TRNASYNTHASP; 1;
TIGRFAMs TIGR00459; aspS_bact; 1;
PROSITE PS50862; AA_TRNA_LIGASE_II; 1;

Features [?]

From: SYD_THETH (P36419)
Key     From     To       Description   Tag   Condition   FTGroup
NP_BIND     223     225       ATP     R-x-E  
NP_BIND     528     531       ATP     G-x-x-R  
REGION     201     204       Aspartate     Q-x-x-K  
BINDING (Optional)     177     177       Aspartate     E  
BINDING (Optional)     223     223       Aspartate     R  
BINDING (Optional)     232     232       ATP     Q  
BINDING (Optional)     442     442       Aspartate     H  
BINDING (Optional)     476     476       ATP     E  
BINDING (Optional)     483     483       Aspartate     R  
From: SYDND_PSEAE (Q51422)
SITE (Optional)     31     31       Important for tRNA non-discrimination   NonDiscr1_bact   H  
SITE (Optional)     82     82       Important for tRNA non-discrimination   NonDiscr2_bact   G  

Additional information [?]

Size range 430-700 amino acids
Related rules MF_02075 (SYD)
Fusion Nter: <Unknown>; Cter: None
Comments This subfamily contains most bacterial aspartate--tRNA ligases and eukaryotic mitochondrial aspartate--tRNA ligases. See MF_02075 for type 2 subfamily. Unknown N-terminal domain in MAGSA.


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