HAMAP rule MF_00282
General rule information
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Accession | MF_00282 |
Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 38) |
Name | Phe_tRNA_synth_alpha2 |
Scope(s) |
Bacteria Archaea Plastid |
Template(s) | P27002 (SYFB_THETH); O26837 (SYFA_METTH); A5K9S0 (SYFA_PLAVS); Q9Y285 (SYFA_HUMAN); [ Recover all ] |
Triggered by |
HAMAP; MF_00282 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | SYFA |
Protein name | RecName: Full=Phenylalanine--tRNA ligase alpha subunit; EC=6.1.1.20; AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit; Short=PheRS; |
Gene name | Name=pheS; |
Comments
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CATALYTIC ACTIVITY | Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; |
COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per tetramer.; |
SUBUNIT | Tetramer of two alpha and two beta subunits. |
case <OG:Chloroplast> | |
SUBCELLULAR LOCATION | Plastid, chloroplast. |
end case | |
case not <OG:Chloroplast> | |
SUBCELLULAR LOCATION | Cytoplasm. |
end case | |
SIMILARITY | Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily. |
Keywords
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case not <OG:Chloroplast> | |
Cytoplasm | |
end case | |
Aminoacyl-tRNA synthetase | |
ATP-binding | |
Ligase | |
Magnesium | |
Metal-binding | |
Nucleotide-binding | |
Protein biosynthesis |
Gene Ontology
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GO:0005524; Molecular function:ATP binding | |
GO:0000287; Molecular function:magnesium ion binding | |
GO:0004826; Molecular function:phenylalanine-tRNA ligase activity | |
GO:0006432; Biological process:phenylalanyl-tRNA aminoacylation | |
case <OG:Chloroplast> | |
GO:0009507; Cellular component:chloroplast | |
end case | |
case not <OG:Chloroplast> | |
GO:0005737; Cellular component:cytoplasm | |
end case |
Cross-references
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Features
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From: SYFA_THEKO (Q76KA8) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 426 | 426 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="ligand shared with heterodimeric partner" |
E | ||||||||
BINDING | 344 | 344 | /ligand="L-phenylalanine" /ligand_id="ChEBI:CHEBI:58095" |
T | ||||||||
BINDING | 383 | 385 | /ligand="L-phenylalanine" /ligand_id="ChEBI:CHEBI:58095" |
Q-[IVL]-[DE] | ||||||||
BINDING | 424 | 424 | /ligand="L-phenylalanine" /ligand_id="ChEBI:CHEBI:58095" |
[FY] | ||||||||
BINDING | 449 | 449 | /ligand="L-phenylalanine" /ligand_id="ChEBI:CHEBI:58095" |
F |
Additional information
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Size range | 465-553 amino acids |
Related rules |
MF_00281 |
Fusion | Nter: None Cter: None |
Comments | Generally found in archaea, but also present in BORBU and TREPA. Possible wrong starts various sequences |