Q7W0F7 (SYM_BORPE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 54.
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: Methionine--tRNA ligase EC=6.1.1.10 Alternative name(s): Methionyl-tRNA synthetase Short name=MetRS | ||||
| Gene names |
| ||||
| Organism | Bordetella pertussis | ||||
| Taxonomic identifier | 520 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 692 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation By similarity. HAMAP MF_00098 |
| Catalytic activity | ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). HAMAP MF_00098 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_00098 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00098 |
| Subcellular location | |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily. Contains 1 tRNA-binding domain. |
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 Reference proteome |
| Gene Ontology (GO) | |
| Biological process | methionyl-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 methionine-tRNA ligase activityInferred from electronic annotation. Source: EC 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 – 692 | 692 | Methionine--tRNA ligase HAMAP MF_00098 | PRO_0000139110 | |||||
Regions | |||||||||
| Domain | 586 – 692 | 107 | tRNA-binding | ||||||
| Motif | 12 – 22 | 11 | "HIGH" region HAMAP MF_00098 | ||||||
| Motif | 341 – 345 | 5 | "KMSKS" region HAMAP MF_00098 | ||||||
Sites | |||||||||
| Metal binding | 143 | 1 | Zinc By similarity | ||||||
| Metal binding | 146 | 1 | Zinc By similarity | ||||||
| Metal binding | 156 | 1 | Zinc By similarity | ||||||
| Metal binding | 159 | 1 | Zinc By similarity | ||||||
| Binding site | 344 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX640411 Genomic DNA. Translation: CAE40559.1. |
| RefSeq | NP_879070.1. NC_002929.2. |
3D structure databases | |
| ProteinModelPortal | Q7W0F7. |
| SMR | Q7W0F7. Positions 135-161. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2664345. |
| GenomeReviews | Gene locus BP0180 in contig BX470248_GR. |
| KEGG | bpe:BP0180. |
| NMPDR | fig|257313.1.peg.150. |
| PATRIC | 21153366. VBIBorPer7866_0190. |
Phylogenomic databases | |
| HOGENOM | HBG721667. |
| OMA | EEKTRNV. |
| PhylomeDB | Q7W0F7. |
| ProtClustDB | PRK00133. |
Enzyme and pathway databases | |
| BioCyc | BPER257313:BP0180-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00098. Met_tRNA_synth_type1. [Tree] |
| InterPro | IPR015413. aa-tRNA-synt_I. IPR001412. aa-tRNA-synth_I_CS. IPR004495. Met-tRNA-synth_Ia_bsu_C. IPR014758. Met-tRNA_synth. IPR023458. Met-tRNA_synth_1. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR014729. Rossmann-like_a/b/a_fold. IPR002547. tRNA-bd_dom. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view] |
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. |
| KO | K01874. |
| Pfam | PF09334. tRNA-synt_1g. 1 hit. PF01588. tRNA_bind. 1 hit. [Graphical view] |
| PRINTS | PR01041. TRNASYNTHMET. |
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit. |
| TIGRFAMs | TIGR00398. MetG. 1 hit. TIGR00399. MetG_C_term. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50886. TRBD. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYM_BORPE | ||||||||
| Accession | Primary (citable) accession number: Q7W0F7 | ||||||||
| 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