Reviewed,
UniProtKB/Swiss-Prot Q7WP45 (SYM_BORBR)
Last modified
February 9, 2010.
Version 43.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Methionyl-tRNA synthetase EC=6.1.1.10 Alternative name(s): Methionine--tRNA ligase Short name=MetRS | ||||
| Gene names |
| ||||
| Organism | Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 518 [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 |
| Gene Ontology (GO) | |
| Biological process | methionyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP methionine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP tRNA bindingInferred from electronic annotation. Source: UniProtKB-KW zinc ion 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 | Methionyl-tRNA synthetase HAMAP MF_00098 | PRO_0000139106 | |||||
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: RB50 / ATCC BAA-588 / NCTC 13252. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX640439 Genomic DNA. Translation: CAE31339.1. |
| RefSeq | NP_887389.1. |
3D structure databases | |
| SMR | Q7WP45. Positions 2-560, 581-691. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2662481. |
| KEGG | bbr:BB0840. |
| NMPDR | fig|257310.1.peg.836. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG721667. |
| OMA | SAYQPEQ. |
| PhylomeDB | Q7WP45. |
Enzyme and pathway databases | |
| BioCyc | BBRO257310:BB0840-MONOMER. |
| BRENDA | 6.1.1.10. 413. |
Family and domain databases | |
| HAMAP | MF_00098. Met_tRNA_synth_type1. [Tree] |
| InterPro | IPR015413. aa-tRNA-synt_I. IPR001412. aa-tRNA-synth_I_CS. IPR002304. Met-tRNA-synth_Ia. IPR004495. Met-tRNA-synth_Ia_bsu_C. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR014729. Rossmann-like_a/b/a_fold. IPR002547. tRNA-bd_dom. IPR014758. tRNA-synt_met_N. 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. 1 hit. |
| Pfam | PF09334. tRNA-synt_1g. 1 hit. PF01588. tRNA_bind. 1 hit. [Graphical view] |
| PRINTS | PR01041. TRNASYNTHMET. |
| 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_BORBR | ||||||||
| Accession | Primary (citable) accession number: Q7WP45 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


