A1KJ66 (SYFA_MYCBP) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 41.
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: Phenylalanine--tRNA ligase alpha chain EC=6.1.1.20 Alternative name(s): Phenylalanyl-tRNA synthetase alpha chain Short name=PheRS | ||||
| Gene names |
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| Organism | Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 410289 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 341 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP MF_00281 |
| Cofactor | Binds 2 magnesium ions per tetramer By similarity. HAMAP MF_00281 |
| Subunit structure | Tetramer of two alpha and two beta chains By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phenylalanyl-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 metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW phenylalanine-tRNA ligase activityInferred from electronic annotation. Source: EC tRNA bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 341 | 341 | Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281 | PRO_1000006861 | |||||
Sites | |||||||||
| Metal binding | 259 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| [1] | "Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed: 17372194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM408590 Genomic DNA. Translation: CAL71675.1. |
| RefSeq | YP_977780.1. NC_008769.1. |
3D structure databases | |
| ProteinModelPortal | A1KJ66. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A1KJ66. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000021497; EBMYCP00000021247; EBMYCG00000021492. |
| GeneID | 4695647. |
| GenomeReviews | Gene locus BCG_1688 in contig AM408590_GR. |
| KEGG | mbb:BCG_1688. |
| PATRIC | 18014164. VBIMycBov80988_1843. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0016. |
| GeneTree | EBGT00050000016426. |
| HOGENOM | HBG284353. |
| OMA | FRASYFP. |
| ProtClustDB | PRK00488. |
Enzyme and pathway databases | |
| BioCyc | MBOV410289:BCG_1688-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00281. Phe_tRNA_synth_alpha1. [Tree] |
| InterPro | IPR006195. aa-tRNA-synth_II. IPR004529. Phe-tRNA-synth_IIc_asu. IPR004188. Phe-tRNA_synth_II_N. IPR022911. Phe_tRNA_synth_alpha1_bac. IPR002319. Phenylalanyl-tRNA_Synthase. IPR010978. tRNA-bd_arm. [Graphical view] |
| KO | K01889. |
| Pfam | PF02912. Phe_tRNA-synt_N. 1 hit. PF01409. tRNA-synt_2d. 1 hit. [Graphical view] |
| SUPFAM | SSF46589. tRNA_binding_arm. 1 hit. |
| TIGRFAMs | TIGR00468. PheS. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYFA_MYCBP | ||||||||
| Accession | Primary (citable) accession number: A1KJ66 | ||||||||
| 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