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| HAMAP annotation rule: MF_01278 |
| Accession | MF_01278 |
| Dates | 16-APR-2007 (Created) 25-NOV-2009 (Last updated, Version 9) |
| Data class | Protein |
| Predictors | HAMAP; MF_01278; [distribution of match scores in UniProtKB];[seed alignment for MF_01278] |
| Names | Ser_tRNA_synth_type2 |
| Identifier | SYS2 |
| Protein name |
|
| Gene name | serS |
FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also 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) (By similarity).
CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).
CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).
case <FTGroup:1>
COFACTOR: Binds 1 Zn(2+) ion per subunit. This ion is coordinated with 2 cysteines, 1 glutamate and a water molecule that dissociates from the zinc ion to allow the coordination of the amino group of the serine substrate, which is essential for catalysis (By similarity).
end case
PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
DOMAIN: Consists of two distinct domains, a catalytic core and a N-terminal extension that is presumably involved in tRNA binding (By similarity).
SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily.
| PROSITE |
PS50862; AA_TRNA_LIGASE_II; 1; |
| Pfam |
PF00587; tRNA-synt_2b; 1; |
| TIGRFAMs |
TIGR00415; serS_MJ; 1; |
Cytoplasm,
Aminoacyl-tRNA synthetase,
ATP-binding,
Ligase,
Metal-binding,
Nucleotide-binding,
Protein biosynthesis.
case <FTGroup:1>
end case
GO:0004828; Molecular function: serine-tRNA ligase activity.
GO:0005524; Molecular function: ATP binding.
GO:0005524; Molecular function: ATP binding.
case <FTGroup:1>
GO:0008270; Molecular function: zinc ion binding.
end case
GO:0016260; Biological process: selenocysteine biosynthetic process.
GO:0006434; Biological process: seryl-tRNA aminoacylation.
GO:0005737; Cellular component: cytoplasm.
GO:0006434; Biological process: seryl-tRNA aminoacylation.
GO:0005737; Cellular component: cytoplasm.
| From: SYS2_METBF (Q46AN5) | ||||||||||
| Key | From | To | Description | Condition | FTGroup | |||||
| NP_BIND | 336 | 338 | ATP (By similarity) | R-x-E | ||||||
| NP_BIND | 347 | 348 | ATP (By similarity) | R-V | ||||||
| REGION | 353 | 355 | Serine binding (By similarity) | R-x-E | ||||||
| METAL | 306 | 306 | Zinc; catalytic (By similarity) | C | 1 | |||||
| METAL | 355 | 355 | Zinc; catalytic (By similarity) | E | 1 | |||||
| METAL | 461 | 461 | Zinc; catalytic (By similarity) | C | 1 | |||||
| BINDING | 304 | 304 | Serine; via carbonyl oxygen (By similarity) | A | ||||||
| BINDING | 336 | 336 | Serine (By similarity) | R | ||||||
| BINDING (Optional) | 400 | 400 | Serine (By similarity) | Q | ||||||
| BINDING (Optional) | 432 | 432 | ATP (By similarity) | E | ||||||
| BINDING (Optional) | 435 | 435 | Serine (By similarity) | N | ||||||
| BINDING | 468 | 468 | ATP (By similarity) | R | ||||||
| Size range: | 500-527 amino acids |
| Related UniRules: | None |
| Template: | Q46AN5 (SYS2_METBF); Q58477 (SYS2_METJA); O30520 (SYS2_METMP); O27194 (SYS2_METTH): [Recover all] |
| Scope: | Archaea |
| Fusion: | Nter: None; Cter: None |
| Duplicate: | None |
| Plasmid encoded: | None |
| Comments: | There are two distinct types of seryl-tRNA synthetase, as differentiated by primary sequence analysis, three-dimensional structure and substrate recognition mechanism: type 1 (MF_00176) is found in the majority of organisms (prokaryotes, eukaryotes and archaea) whereas type 2 (MF_01278) is confined to some methanogenic archaea. METBF (Methanosarcina barkeri) possesses two seryl-tRNA synthetases, one of each type. |
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