A6QPU5 (SYDM_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 42.
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: Aspartate--tRNA ligase, mitochondrial EC=6.1.1.12 Alternative name(s): Aspartyl-tRNA synthetase Short name=AspRS | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 651 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Catalytic activity | ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aspartate-tRNA ligase activityInferred from electronic annotation. Source: EC nucleic acid bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 44 | 44 | Mitochondrion Potential | ||||||
| Chain | 45 – 651 | 607 | Aspartate--tRNA ligase, mitochondrial | PRO_0000327860 | |||||
Amino acid modifications | |||||||||
| Modified residue | 232 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 379 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 624 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thymus. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC149492 mRNA. Translation: AAI49493.1. |
| IPI | IPI00867017. |
| RefSeq | NP_001095692.1. NM_001102222.1. |
| UniGene | Bt.103622. |
3D structure databases | |
| ProteinModelPortal | A6QPU5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A6QPU5. |
Proteomic databases | |
| PRIDE | A6QPU5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 538772. |
| KEGG | bta:538772. |
Organism-specific databases | |
| CTD | 55157. |
Phylogenomic databases | |
| eggNOG | maNOG04388. |
| GeneTree | ENSGT00550000074971. |
| HOVERGEN | HBG055815. |
| InParanoid | A6QPU5. |
| OrthoDB | EOG4M91R5. |
Family and domain databases | |
| InterPro | IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR004524. Asp-tRNA-synth_IIb_bac/mt. IPR002312. Asp/Asn-tRNA-synth_IIb. IPR004115. GAD_dom. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view] |
| Gene3D | G3DSA:3.30.1360.30. GAD_dom. 1 hit. G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. |
| KO | K01876. |
| PANTHER | PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF5. AspS_bac. 1 hit. |
| Pfam | PF02938. GAD. 1 hit. PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view] |
| PRINTS | PR01042. TRNASYNTHASP. |
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. SSF55261. SSF55261. 1 hit. |
| TIGRFAMs | TIGR00459. AspS_bact. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYDM_BOVIN | ||||||||
| Accession | Primary (citable) accession number: A6QPU5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with