Reviewed,
UniProtKB/Swiss-Prot P23920 (SYM_BACST)
Last modified
June 16, 2009.
Version 71.
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 | Bacillus stearothermophilus (Geobacillus stearothermophilus) | ||||
| Taxonomic identifier | 1422 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus |
Protein attributes
| Sequence length | 649 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). HAMAP MF_01228 |
| Cofactor | Binds 1 zinc ion per subunit. HAMAP MF_01228 |
| Subunit structure | Homodimer. HAMAP MF_01228 |
| Subcellular location | |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2A 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 |
| 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 – 649 | 649 | Methionyl-tRNA synthetase HAMAP MF_01228 | PRO_0000139210 | |||||
Regions | |||||||||
| Domain | 555 – 647 | 93 | tRNA-binding | ||||||
| Motif | 13 – 23 | 11 | "HIGH" region HAMAP MF_01228 | ||||||
| Motif | 298 – 302 | 5 | "KMSKS" region HAMAP MF_01228 | ||||||
Sites | |||||||||
| Metal binding | 128 | 1 | Zinc By similarity | ||||||
| Metal binding | 131 | 1 | Zinc By similarity | ||||||
| Metal binding | 145 | 1 | Zinc By similarity | ||||||
| Metal binding | 148 | 1 | Zinc By similarity | ||||||
| Binding site | 301 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Methionyl-tRNA synthetase from Bacillus stearothermophilus: structural and functional identities with the Escherichia coli enzyme." Mechulam Y., Schmitt E., Panvert M., Schmitter J.-M., Lapadat-Tapolsky M., Meinnel T., Dessen P., Blanquet S., Fayat G. Nucleic Acids Res. 19:3673-3681(1991) [PubMed: 1852609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 1518. |
Cross-references
Sequence databases | |
|---|---|
| X57925 Genomic DNA. Translation: CAA40999.1. | |
| PIR | S16682. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1MKH based on UniProtKB Q9V011. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.10. 266715. |
Family and domain databases | |
| HAMAP | MF_01228. Fused. [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. IPR014729. Rossmann-like_a/b/a_fold. IPR014758. tRNA-synt_met_N. IPR002547. tRNA_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_BACST | ||||||||
| Accession | Primary (citable) accession number: P23920 | ||||||||
| 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


