Reviewed,
UniProtKB/Swiss-Prot P50475 (SYAC_RAT)
Last modified
November 3, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alanyl-tRNA synthetase, cytoplasmic EC=6.1.1.7 Alternative name(s): Alanine--tRNA ligase Short name=AlaRS | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 968 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). |
| Subunit structure | Monomer. |
| Subcellular location | Cytoplasm Potential. |
| Domain | The C-terminal 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 Potential. |
| 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 RNA-binding tRNA-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | alanyl-tRNA aminoacylation Ref.2 Inferred from direct assay. Source: RGD |
| Cellular component | cytoplasm Ref.2 Inferred from direct assay. Source: RGD |
| Molecular function | ATP binding Ref.2 Inferred from physical interaction. Source: RGD alanine-tRNA ligase activity Ref.2Inferred from direct assay. Source: RGD amino acid binding Ref.2Inferred from physical interaction. Source: RGD tRNA binding Ref.2Inferred from physical interaction. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 968 | 968 | Alanyl-tRNA synthetase, cytoplasmic | PRO_0000075284 | |||||
Regions | |||||||||
| Region | 1 – 497 | 497 | Catalytic By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
| Modified residue | 19 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 555 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 578 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 580 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 876 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 459 | 1 | G → E AA sequence Ref.2 | ||||||
| Sequence conflict | 474 – 476 | 3 | RAK → ARA AA sequence Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "Alanyl-tRNA synthetase from Escherichia coli, Bombyx mori and Ratus ratus. Existence of common structural features." Dignam J.D., Dignam S.S., Brumley L.L. Eur. J. Biochem. 198:201-210(1991) [PubMed: 2040280] [Abstract] Cited for: PROTEIN SEQUENCE OF 456-476. Tissue: Liver. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 600-968. Tissue: Thymus. |
| [4] | Maurya D.K., Bhargava P. Submitted (JAN-2009) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| CH473972 Genomic DNA. Translation: EDL92558.1. BC098738 mRNA. Translation: AAH98738.1. | |
| IPI | IPI00363563. |
| PIR | S16073. |
| RefSeq | NP_001093987.1. |
| UniGene | Rn.8645 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 292023. |
Organism-specific databases | |
| RGD | 1304832. Aars. |
Phylogenomic databases | |
| HOVERGEN | P50475. |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.7. 248. |
Gene expression databases | |
| Genevestigator | P50475. |
Family and domain databases | |
| InterPro | IPR002318. Ala-tRNA-synth_IIc. IPR018165. Ala-tRNA-synth_IIc_cons-reg. IPR018164. Ala-tRNA-synth_IIc_N. IPR003156. Pesterase_DHHA1. IPR012947. tRNA_SAD. [Graphical view] |
| Pfam | PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view] |
| PRINTS | PR00980. TRNASYNTHALA. |
| TIGRFAMs | TIGR00344. alaS. 1 hit. |
| PROSITE | PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYAC_RAT | ||||||||
| Accession | Primary (citable) accession number: P50475 Secondary accession number(s): A6IZ80, Q4G057 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


