A0A9L0SB67

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000166 nucleotide binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: nucleotide binding: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Reason: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. file:HORSE/DARS2/DARS2-bioinformatics/RESULTS.md The downloaded human Q6PI48 sequence (645 residues) and selected horse A0A9L0SB67 sequence (616 residues) share 90.3% identity among 607 paired residues. Paired coverage is 94.1% of human and 98.5% of horse.
GO:0003676 nucleic acid binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: nucleic acid binding: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Reason: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. file:HORSE/DARS2/DARS2-bioinformatics/RESULTS.md The downloaded human Q6PI48 sequence (645 residues) and selected horse A0A9L0SB67 sequence (616 residues) share 90.3% identity among 607 paired residues. Paired coverage is 94.1% of human and 98.5% of horse.
GO:0004812 aminoacyl-tRNA ligase activity	IEA GO_REF:0000002	MODIFY	Summary: aminoacyl-tRNA ligase activity: The broad ligase activity is correct, but the experimentally established aspartate-tRNA ligase activity identifies both the amino acid and substrate class. Reason: The broad ligase activity is correct, but the experimentally established aspartate-tRNA ligase activity identifies both the amino acid and substrate class. Proposed replacements: aspartate-tRNA ligase activity Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. file:HORSE/DARS2/DARS2-bioinformatics/RESULTS.md The downloaded human Q6PI48 sequence (645 residues) and selected horse A0A9L0SB67 sequence (616 residues) share 90.3% identity among 607 paired residues. Paired coverage is 94.1% of human and 98.5% of horse.
GO:0005524 ATP binding	IEA GO_REF:0000002	ACCEPT	Summary: ATP binding: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. file:HORSE/DARS2/DARS2-bioinformatics/RESULTS.md The downloaded human Q6PI48 sequence (645 residues) and selected horse A0A9L0SB67 sequence (616 residues) share 90.3% identity among 607 paired residues. Paired coverage is 94.1% of human and 98.5% of horse.
GO:0005737 cytoplasm	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: cytoplasm: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Reason: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. file:HORSE/DARS2/DARS2-bioinformatics/RESULTS.md The downloaded human Q6PI48 sequence (645 residues) and selected horse A0A9L0SB67 sequence (616 residues) share 90.3% identity among 607 paired residues. Paired coverage is 94.1% of human and 98.5% of horse.
GO:0006418 tRNA aminoacylation for protein translation	IEA GO_REF:0000002	ACCEPT	Summary: tRNA aminoacylation for protein translation: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. file:HORSE/DARS2/DARS2-bioinformatics/RESULTS.md The downloaded human Q6PI48 sequence (645 residues) and selected horse A0A9L0SB67 sequence (616 residues) share 90.3% identity among 607 paired residues. Paired coverage is 94.1% of human and 98.5% of horse.
GO:0016874 ligase activity	IEA GO_REF:0000002	MODIFY	Summary: ligase activity: The broad ligase activity is correct, but the experimentally established aspartate-tRNA ligase activity identifies both the amino acid and substrate class. Reason: The broad ligase activity is correct, but the experimentally established aspartate-tRNA ligase activity identifies both the amino acid and substrate class. Proposed replacements: aspartate-tRNA ligase activity Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. file:HORSE/DARS2/DARS2-bioinformatics/RESULTS.md The downloaded human Q6PI48 sequence (645 residues) and selected horse A0A9L0SB67 sequence (616 residues) share 90.3% identity among 607 paired residues. Paired coverage is 94.1% of human and 98.5% of horse.