| General information | | DisProt: | DP00514 | | Name: | Seryl-tRNA synthetase | | Synonym(s): | SYS_THET2
EC 6.1.1.11
Seryl-tRNA(Ser/Sec) synthetase
Serine--tRNA ligase
SerRS
| | First appeared in release: | Release 3.4 (08/15/2006) | | UniProt: | P34945 | | UniGene: | | | SwissProt: | SYS_THET2 | | TrEMBL: | | | NCBI (GI): | 47606770 | | Source organism: | Thermus thermophilus | | Sequence length: | 421 | | Percent disordered: | 31% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MVDLKRLRQE PEVFHRAIRE KGVALDLEAL LALDREVQEL KKRLQEVQTE RNQVAKRVPK - 60
APPEEKEALI ARGKALGEEA KRLEEALREK EARLEALLLQ VPLPPWPGAP VGGEEANREI - 120
KRVGGPPEFS FPPLDHVALM EKNGWWEPRI SQVSGSRSYA LKGDLALYEL ALLRFAMDFM - 180
ARRGFLPMTL PSYAREKAFL GTGHFPAYRD QVWAIAETDL YLTGTAEVVL NALHSGEILP - 240
YEALPLRYAG YAPAFRSEAG SFGKDVRGLM RVHQFHKVEQ YVLTEASLEA SDRAFQELLE - 300
NAEEILRLLE LPYRLVEVAT GDMGPGKWRQ VDIEVYLPSE GRYRETHSCS ALLDWQARRA - 360
NLRYRDPEGR VRYAYTLNNT ALATPRILAM LLENHQLQDG RVRVPQALIP YMGKEVLEPC - 420
G
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| Functional narrative |
Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
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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.
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| Region 1 | | Type: | Disordered | | Name: | flexible arm | | Location: | 1 - 111 | | Length: | 111 | | Region sequence: |
MVDLKRLRQEPEVFHRAIREKGVALDLEALLALDREVQELKKRLQEVQTERNQVAKRVPK
APPEEKEALIARGKALGEEAKRLEEALREKEARLEALLLQVPLPPWPGAPV | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-tRNA binding
| Detection methods:
- High relative B-factor
- X-ray crystallography
| References:
- Biou V, Yaremchuk A, Tukalo M, Cusack S. "The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)." Science. 1994; 263(5152): 1404-10. PubMed: 8128220
- Fujinaga M, Berthet-Colominas C, Yaremchuk AD, Tukalo MA, Cusack S. "Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution." J Mol Biol. 1993; 234(1): 222-33. PubMed: 8230201
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | coiled coil domain of the flexible arm | | Location: | 36 - 89 | | Length: | 54 | | Region sequence: |
EVQELKKRLQEVQTERNQVAKRVPKAPPEEKEALIARGKALGEEAKRLEEALRE | | Modification type: | Complex
| | PDB: | 1SER:A, 1SER:B | | 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
| References:
- Biou V, Yaremchuk A, Tukalo M, Cusack S. "The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)." Science. 1994; 263(5152): 1404-10. PubMed: 8128220
- Cusack S, Yaremchuk A, Tukalo M. "The crystal structure of the ternary complex of T.thermophilus seryl-tRNA synthetase with tRNA(Ser) and a seryl-adenylate analogue reveals a conformational switch in the active site." EMBO J. 1996; 15(11): 2834-42. PubMed: 8654381
| Comments:
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| Region 3 | | Type: | Disordered | | Name: | motif 2 loop | | Location: | 258 - 267 | | Length: | 10 | | Region sequence: |
EAGSFGKDVR | | Modification type: | Complex
| | PDB: | 1SRY:A, 1SRY:B | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-tRNA binding
Substrate/ligand binding
| Detection methods:
- X-ray crystallography
- High relative B-factor
| References:
- Biou V, Yaremchuk A, Tukalo M, Cusack S. "The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)." Science. 1994; 263(5152): 1404-10. PubMed: 8128220
- Cusack S, Yaremchuk A, Tukalo M. "The crystal structure of the ternary complex of T.thermophilus seryl-tRNA synthetase with tRNA(Ser) and a seryl-adenylate analogue reveals a conformational switch in the active site." EMBO J. 1996; 15(11): 2834-42. PubMed: 8654381
- Fujinaga M, Berthet-Colominas C, Yaremchuk AD, Tukalo MA, Cusack S. "Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution." J Mol Biol. 1993; 234(1): 222-33. PubMed: 8230201
| Comments:
|
| Region 4 | | Type: | Disordered | | Name: | | | Location: | 360 - 368 | | Length: | 9 | | Region sequence: |
ANLRYRDPE | | Modification type: | Complex
| | PDB: | | | 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
| References:
- Biou V, Yaremchuk A, Tukalo M, Cusack S. "The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)." Science. 1994; 263(5152): 1404-10. PubMed: 8128220
| Comments:
|
| Region 5 | | Type: | Disordered | | Name: | | | Location: | 420 - 421 | | Length: | 2 | | Region sequence: |
CG | | Modification type: | | | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography
- High relative B-factor
| References:
- Fujinaga M, Berthet-Colominas C, Yaremchuk AD, Tukalo MA, Cusack S. "Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution." J Mol Biol. 1993; 234(1): 222-33. PubMed: 8230201
| Comments:
|
| References |
- Belrhali H, Yaremchuk A, Tukalo M, Larsen K, Berthet-Colominas C, Leberman R, Beijer B, Sproat B, Als-Nielsen J, Grübel G, et al. "Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate." Science. 1994; 263(5152): 1432-6. PubMed: 8128224
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