Reviewed,
UniProtKB/Swiss-Prot Q81KS9 (SYY1_BACAN)
Last modified
November 3, 2009.
Version 46.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Tyrosyl-tRNA synthetase 1 EC=6.1.1.1 Alternative name(s): Tyrosine--tRNA ligase 1 Short name=TyrRS 1 | ||||||
| Gene names |
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| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1392 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 418 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
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). HAMAP MF_02006 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. Contains 1 S4 RNA-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding RNA-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | tyrosyl-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 RNA bindingInferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 418 | 418 | Tyrosyl-tRNA synthetase 1 HAMAP MF_02006 | PRO_0000234667 | |||||
Regions | |||||||||
| Domain | 352 – 418 | 67 | S4 RNA-binding | ||||||
| Motif | 39 – 48 | 10 | "HIGH" region HAMAP MF_02006 | ||||||
| Motif | 230 – 234 | 5 | "KMSKS" region HAMAP MF_02006 | ||||||
Sites | |||||||||
| Binding site | 34 | 1 | Tyrosine By similarity | ||||||
| Binding site | 169 | 1 | Tyrosine By similarity | ||||||
| Binding site | 173 | 1 | Tyrosine By similarity | ||||||
| Binding site | 233 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| AE016879 Genomic DNA. Translation: AAP28595.1. AE017334 Genomic DNA. Translation: AAT34029.1. AE017225 Genomic DNA. Translation: AAT56853.1. | |
| RefSeq | NP_847109.1. YP_021554.1. YP_030803.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2TS1 based on UniProtKB P00952. |
| SMR | Q81KS9. Positions 1-319. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1084086. 2818653. 2850360. |
| GenomeReviews | Gene locus BA_4911 in contig AE016879_GR. Gene locus BAS4556 in contig AE017225_GR. Gene locus GBAA_4911 in contig AE017334_GR. |
| KEGG | ban:BA4911. bar:GBAA4911. bat:BAS4556. |
| TIGR | BA_4911. GBAA_4911. |
Phylogenomic databases | |
| HOGENOM | Q81KS9. |
| OMA | PGYVPNT. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS4556-MON. BANT261594:GBAA4911-MON. |
| BRENDA | 6.1.1.1. 267517. |
Family and domain databases | |
| HAMAP | MF_02006. [Tree] |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ib. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA_bd. IPR002307. Tyr-tRNA-synth_Ib_bac/mito. [Graphical view] |
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| PANTHER | PTHR11766. Tyr_tRNA-synt_1b. 1 hit. |
| Pfam | PF01479. S4. 1 hit. PF00579. tRNA-synt_1b. 1 hit. [Graphical view] |
| PRINTS | PR01040. TRNASYNTHTYR. |
| SMART | SM00363. S4. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00234. tyrS. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50889. S4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYY1_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81KS9 Secondary accession number(s): Q6HS85, Q6KLI4 | ||||||||
| 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


