HAMAP rule MF_01278
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_01278 |
| Accession | MF_01278 |
| Dates | 16-APR-2007 (Created)
03-SEP-2024 (Last updated, Version 22) |
| Name | Ser_tRNA_synth_type2 |
| Scope(s) |
Archaea |
| Template(s) | Q46AN5; Q58477; O30520; O27194; [ Recover all ] |
| Triggered by |
HAMAP; MF_01278 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | SYS2 |
| Protein name | RecName: Full=Type-2 serine--tRNA ligase; EC=6.1.1.11; AltName: Full=Seryl-tRNA synthetase; Short=SerRS; AltName: Full=Seryl-tRNA(Ser/Sec) synthetase; |
| Gene name | Name=serS; |
Comments
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| 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). |
| CATALYTIC ACTIVITY | Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + diphosphate + H(+); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; |
| CATALYTIC ACTIVITY | Reaction=tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + diphosphate + H(+); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; |
| case <FTGroup:1> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=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.; |
| 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. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| DOMAIN | Consists of two distinct domains, a catalytic core and a N- terminal extension that is presumably involved in tRNA binding. |
| SIMILARITY | Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily. |
Keywords
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| Cytoplasm | |
| Aminoacyl-tRNA synthetase | |
| ATP-binding | |
| Ligase | |
| Metal-binding | |
| Nucleotide-binding | |
| Protein biosynthesis | |
| case <FTGroup:1> | |
| Metal-binding | |
| Zinc | |
| end case | |
Gene Ontology
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| GO:0004828; Molecular function:serine-tRNA ligase activity | |
| 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 | |
Cross-references
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| PROSITE | PS50862; AA_TRNA_LIGASE_II; 1; |
| Pfam | PF00587; tRNA-synt_2b; 1; |
| NCBIfam | TIGR00415; SerS_MJ; 1; |
Features
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| From: SYS2_METBF (Q46AN5) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 336 | 338 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R-x-E | ||||||||
| BINDING | 347 | 348 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R-V | ||||||||
| BINDING | 353 | 355 | /ligand="L-serine" /ligand_id="ChEBI:CHEBI:33384" |
R-x-E | ||||||||
| BINDING | 306 | 306 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
C | 1 | |||||||
| BINDING | 355 | 355 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
E | 1 | |||||||
| BINDING | 461 | 461 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
C | 1 | |||||||
| BINDING | 304 | 304 | /ligand="L-serine" /ligand_id="ChEBI:CHEBI:33384" |
A | ||||||||
| BINDING | 336 | 336 | /ligand="L-serine" /ligand_id="ChEBI:CHEBI:33384" |
R | ||||||||
| BINDING | 400 | 400 | /ligand="L-serine" /ligand_id="ChEBI:CHEBI:33384" |
Q | ||||||||
| BINDING | 432 | 432 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
E | ||||||||
| BINDING | 435 | 435 | /ligand="L-serine" /ligand_id="ChEBI:CHEBI:33384" |
N | ||||||||
| BINDING | 468 | 468 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
Additional information
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| Size range | 500-527 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |