| General information | | DisProt: | DP00726 | | Name: | Tyrosine--tRNA ligase | | Synonym(s): | SYY_MIMIV
Tyrosyl-tRNA synthetase
TyrRS
| | First appeared in release: | Release 6.00 (07/01/2012) | | UniProt: | Q5UPJ7 | | UniGene: | | | SwissProt: | SYY_MIMIV | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Acanthamoeba polyphaga mimivirus (APMV) | | Sequence length: | 346 | | Percent disordered: | 12% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MENTDHTNNE HRLTQLLSIA EECETLDRLK QLVDSGRIFT AYNGFEPSGR IHIAQALITV - 60
MNTNNIIECG GQMIIYIADW FAKMNLKMNG DINKIRELGR YFIEVFKACG INLDGTRFIW - 120
ASEFIASNPS YIERMLDIAE FSTISRVKRC CQIMGRNESD CLKASQIFYP CMQAADVFEL - 180
VPEGIDICQL GIDQRKVNML AIEYANDRGL KIPISLSHHM LMSLSGPKKK MSKSDPQGAI - 240
FMDDTEQEVS EKISRAYCTD ETFDNPIFEY IKYLLLRWFG TLNLCGKIYT DIESIQEDFS - 300
SMNKRELKTD VANYINTIID LVREHFKKPE LSELLSNVKS YQQPSK
|
| Functional narrative |
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) (By similarity).
CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). Kinetic parameters: KM=0.5 uM for tRNA-Tyr;
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
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|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered w/ Residual Structure | | Name: | Alpha-helix 7, extended (A7) | | Location: | 130 - 149 | | Length: | 20 | | Region sequence: |
SYIERMLDIAEFSTISRVKR | | Modification type: | Complex
| | PDB: | 2J5B:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-tRNA binding
| Detection methods:
- X-ray crystallography (298 K; pH: 5.5; TyrRS protein (14 mg/mL in Tris) 2 uL; Tris (pH 7.4) 20 mM; Tyrosinol 1 mM; ATP 1 mM; Sodium citrate buffer pH 5.5 (with 8% PEG 4000 w/v & 15% MPD v/v) 0.1 M; KCl 0.1 M; MgCl2 1 mM)
| References:
- Abergel C, Rudinger-Thirion J, Giegé R, Claverie JM. "Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS." J. Virol.. 2007; 81(22): 12406-17. PubMed: 17855524
| Comments:According to Abergel et al (2007), A7 is a 20-residue extended alpha-helix which differs from the conserved motif of a 14-residue helix followed by a 90-degree turn and a 9-residue helix. The authors also describe aa R149 as involved in recognition of the RNA acceptor stem.
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| Region 2 | | Type: | Disordered | | Name: | variable loop | | Location: | 150 - 166 | | Length: | 17 | | Region sequence: |
CCQIMGRNESDCLKASQ | | Modification type: | Complex
| | PDB: | 2J5B:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-tRNA binding
| Detection methods:
- X-ray crystallography (298 K; pH: 5.5; ATP 1 mM; KCl 0.1 M; MgCl2 1 mM; Sodium citrate buffer pH 5.5 (with 8% PEG 4000 w/v & 15% MPD v/v) 0.1 M; Tris (pH 7.4) 20 mM; Tyrosinol 1 mM; TyrRS protein (14 mg/mL in Tris) 2 uL)
| References:
- Abergel C, Rudinger-Thirion J, Giegé R, Claverie JM. "Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS." J. Virol.. 2007; 81(22): 12406-17. PubMed: 17855524
| Comments:
|
| Region 3 | | Type: | Disordered | | Name: | KMSKS region | | Location: | 230 - 234 | | Length: | 5 | | Region sequence: |
KMSKS | | Modification type: | Complex
| | PDB: | 2J5B:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-tRNA binding
| Detection methods:
- X-ray crystallography (298 K; pH: 5.5; ATP 1 mM; KCl 0.1 M; MgCl2 1 mM; Sodium citrate buffer pH 5.5 (with 8% PEG 4000 w/v & 15% MPD v/v) 0.1 M; Tris (pH 7.4) 20 mM; Tyrosinol 1 mM; TyrRS protein (14 mg/mL in Tris) 2 uL)
| References:
- Abergel C, Rudinger-Thirion J, Giegé R, Claverie JM. "Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS." J. Virol.. 2007; 81(22): 12406-17. PubMed: 17855524
| Comments:Abergel et al (2007) discuss the high conservation of the KMSKS motif and note that "this loop [is] often disordered in ATP-free TyrRS structures." Additionally, aa K233 participates in ATP binding.
|
| Comments |
AV sent 6-26-2012 (PMID: 17855524) [AV rec'd 07/18/2012]
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