Reviewed,
UniProtKB/Swiss-Prot Q1L6A3 (PYLS_METTE)
Last modified
June 16, 2009.
Version 17.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Pyrrolysyl-tRNA synthetase EC=6.1.1.26 Alternative name(s): Pyrrolysine--tRNA ligase Short name=PylRS | ||
| Gene names |
| ||
| Organism | Methanosarcina thermophila | ||
| Taxonomic identifier | 2210 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina |
Protein attributes
| Sequence length | 478 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the attachment of pyrrolysine to tRNA(Pyl). Pyrrolysine is a lysine derivative encoded by the termination codon UAG By similarity. |
| Catalytic activity | ATP + L-pyrrolysine + tRNA(Pyl) = AMP + diphosphate + L-pyrrolysyl-tRNA(Pyl). HAMAP MF_01573 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Gene Ontology (GO) | |
| Biological process | tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA ligase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 478 | 478 | Pyrrolysyl-tRNA synthetase HAMAP MF_01573 | PRO_0000260454 | |||
Sequences
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References
| [1] | "The substrate specificity of pyrrolysyl-tRNA synthetase." Polycarpo C., Ambrogelly A., Herring S., Soell D.G. Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| DQ017250 Genomic DNA. Translation: AAY81923.1. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.26. 8918. |
Family and domain databases | |
| HAMAP | MF_01573. [Tree] |
| InterPro | IPR018150. aa-tRNA-synt_II-like. IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR012739. PylS. [Graphical view] |
| PANTHER | PTHR22594. aa-tRNA-synt_II. 1 hit. |
| Pfam | PF00587. tRNA-synt_2b. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02367. PylS. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYLS_METTE | ||||||||
| Accession | Primary (citable) accession number: Q1L6A3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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