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HAMAP rule MF_02006
General rule information
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Accession | MF_02006 |
Dates | 24-APR-2006 (Created)
1-JUN-2023 (Last updated, Version 25) |
Name | Tyr_tRNA_synth_type1 |
Scope(s) |
Bacteria |
Template(s) | P0AGJ9 (SYY_ECOLI); P00952 (SYY_GEOSE); P41256 (SYY_ACIFR); Q57834 (SYY_METJA); [ Recover all ] |
Triggered by |
HAMAP; MF_02006 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | SYY |
Protein name | RecName: Full=Tyrosine--tRNA ligase; EC=6.1.1.1; AltName: Full=Tyrosyl-tRNA synthetase; Short=TyrRS; |
Gene name | Name=tyrS; |
Comments
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FUNCTION | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). |
CATALYTIC ACTIVITY | Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L- tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1; |
SUBUNIT | Homodimer. |
SUBCELLULAR LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. |
Keywords
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case <FT:7> | |
Acetylation | |
end case | |
Aminoacyl-tRNA synthetase | |
ATP-binding | |
Cytoplasm | |
Ligase | |
Nucleotide-binding | |
Protein biosynthesis |
Gene Ontology
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GO:0004831; Molecular function:tyrosine-tRNA ligase activity |
GO:0005524; Molecular function:ATP binding |
GO:0006437; Biological process:tyrosyl-tRNA aminoacylation |
GO:0005737; Cellular component:cytoplasm |
Cross-references
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PROSITE | PS00178; AA_TRNA_LIGASE_I; 1; |
PROSITE | PS50889; S4; 1; |
Pfam | PF01479; S4; 1; |
Pfam | PF00579; tRNA-synt_1b; 1; |
PRINTS | PR01040; TRNASYNTHTYR; 1; |
NCBIfam | TIGR00234; TyrS; 1; |
Features
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From: SYY_ECOLI (P0AGJ9) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
MOTIF | 42 | 51 | /note="'HIGH' region" | [PCATI]-[TS]-[AGES]-x-[SA]-[LMI]-[HT]-[ILVA]-G-[HNSG] | ||||||||
MOTIF | 235 | 239 | /note="'KMSKS' region" | K-[FMILY]-G-K-[ST] | ||||||||
BINDING | 37 | 37 | /ligand="L-tyrosine" /ligand_id="ChEBI:CHEBI:58315" |
Y | ||||||||
BINDING | 175 | 175 | /ligand="L-tyrosine" /ligand_id="ChEBI:CHEBI:58315" |
Y | ||||||||
BINDING | 179 | 179 | /ligand="L-tyrosine" /ligand_id="ChEBI:CHEBI:58315" |
Q | ||||||||
BINDING | 238 | 238 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
K | ||||||||
case <OC:Escherichia> or <OC:Shigella> | ||||||||||||
MOD_RES | 144 | 144 | /note="N6-acetyllysine" | K | ||||||||
end case |
Additional information
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Size range | 391-471 amino acids |
Related rules |
MF_02007 MF_02008 |
Fusion | Nter: None Cter: None |
Comments | Some species have a second copy of TyrRS in another subfamily (MF_02007). Shorter sequences in second copy of STRT1 and STRT2; sequences not included in alignment and not taken into account in size range. |