Q5I0L3 (SYYM_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 58.
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: Tyrosine--tRNA ligase, mitochondrial EC=6.1.1.1 Alternative name(s): Tyrosyl-tRNA synthetase Short name=TyrRS | ||
| Gene names |
| ||
| 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 | 471 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)
| Function | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) By similarity. |
| Catalytic activity | ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the class-I 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 Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | tyrosyl-tRNA aminoacylation 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 tyrosine-tRNA ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 471 | Tyrosine--tRNA ligase, mitochondrial | PRO_0000250721 | ||||||
Regions | |||||||||
| Motif | 76 – 85 | 10 | "HIGH" region | ||||||
| Motif | 275 – 279 | 5 | "KMSKS" region | ||||||
Sites | |||||||||
| Binding site | 278 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 349 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 420 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 429 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "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]. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC088224 mRNA. Translation: AAH88224.1. |
| IPI | IPI00370436. |
| RefSeq | NP_001009627.1. NM_001009627.1. |
| UniGene | Rn.163187. |
3D structure databases | |
| HSSP | HSSP built from PDB template 4TS1 based on UniProtKB P00952. |
| ProteinModelPortal | Q5I0L3. |
| SMR | Q5I0L3. Positions 31-367. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5I0L3. |
Proteomic databases | |
| PRIDE | Q5I0L3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000034902; ENSRNOP00000037398; ENSRNOG00000025252. |
| GeneID | 287924. |
| KEGG | rno:287924. |
| NMPDR | fig|10116.3.peg.7839. |
| UCSC | NM_001009627. rat. |
Organism-specific databases | |
| CTD | 51067. |
| RGD | 1311696. Yars2. |
Phylogenomic databases | |
| eggNOG | roNOG05666. |
| GeneTree | ENSGT00390000013709. |
| HOVERGEN | HBG056052. |
| InParanoid | Q5I0L3. |
| OMA | LVHGQEG. |
| OrthoDB | EOG47H5Q1. |
| PhylomeDB | Q5I0L3. |
Gene expression databases | |
| ArrayExpress | Q5I0L3. |
| Genevestigator | Q5I0L3. |
| GermOnline | ENSRNOG00000025252. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ic. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA-bd. IPR002307. Tyr-tRNA-synth. IPR024088. Tyr-tRNA-synth_bac-type. [Graphical view] |
| Gene3D | G3DSA:3.10.290.10. G3DSA:3.10.290.10. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| KO | K01866. |
| PANTHER | PTHR11766. Tyr_tRNA-synt_1b. 1 hit. |
| Pfam | PF00579. tRNA-synt_1b. 1 hit. [Graphical view] |
| PRINTS | PR01040. TRNASYNTHTYR. |
| TIGRFAMs | TIGR00234. TyrS. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 627220. |
Entry information
| Entry name | SYYM_RAT | ||||||||
| Accession | Primary (citable) accession number: Q5I0L3 | ||||||||
| 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