Q9UY36 (SYA_PYRAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 77.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Alanine--tRNA ligase EC=6.1.1.7 Alternative name(s): Alanyl-tRNA synthetase Short name=AlaRS | ||||||
| Gene names |
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| Organism | Pyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 272844 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus |
Protein attributes
| Sequence length | 914 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP MF_00036_A |
| Catalytic activity | ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A |
| Subcellular location | |
| Domain | Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity. HAMAP MF_00036_A |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW tRNA bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 914 | 914 | Alanine--tRNA ligase HAMAP MF_00036_A | PRO_0000075271 | |||||
Sites | |||||||||
| Metal binding | 613 | 1 | Zinc By similarity | ||||||
| Metal binding | 617 | 1 | Zinc By similarity | ||||||
| Metal binding | 717 | 1 | Zinc By similarity | ||||||
| Metal binding | 721 | 1 | Zinc By similarity | ||||||
Sequences
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References
| [1] | "An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi." Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P. Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GE5 / Orsay. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ248288 Genomic DNA. Translation: CAB50576.1. |
| PIR | B75017. |
| RefSeq | NP_127346.1. NC_000868.1. |
3D structure databases | |
| ProteinModelPortal | Q9UY36. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBPYRT00000003041; EBPYRP00000002972; EBPYRG00000003041. |
| GeneID | 1495969. |
| GenomeReviews | Gene locus PYRAB16720 in contig AL096836_GR. |
| KEGG | pab:PAB1245. |
| NMPDR | fig|272844.1.peg.1779. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000022658. |
| HOGENOM | HBG392147. |
| OMA | MFTNSGM. |
| PhylomeDB | Q9UY36. |
| ProtClustDB | PRK13902. |
Enzyme and pathway databases | |
| BioCyc | PABY272844:PAB1245-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00036_A. Ala_tRNA_synth_A. [Tree] |
| InterPro | IPR002318. Ala-tRNA-synth_IIc. IPR018162. Ala-tRNA-synth_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR022429. Ala-tRNA_synth_arc. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view] |
| KO | K01872. |
| PANTHER | PTHR11777:SF6. PTHR11777:SF6. 1 hit. |
| Pfam | PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view] |
| PRINTS | PR00980. TRNASYNTHALA. |
| SMART | SM00863. tRNA_SAD. 1 hit. [Graphical view] |
| SUPFAM | SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit. |
| TIGRFAMs | TIGR03683. A-tRNA_syn_arch. 1 hit. TIGR00344. AlaS. 1 hit. |
| PROSITE | PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYA_PYRAB | ||||||||
| Accession | Primary (citable) accession number: Q9UY36 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with