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. |