Q06752 (SYC_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 103.
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: Cysteine--tRNA ligase EC=6.1.1.16 Alternative name(s): Cysteinyl-tRNA synthetase Short name=CysRS | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 466 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). HAMAP-Rule MF_00041 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Metal-binding Nucleotide-binding Zinc |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cysteinyl-tRNA aminoacylation Inferred from sequence or structural similarity. Source: RefGenome |
| Cellular_component | cytosol Inferred from sequence or structural similarity. Source: RefGenome |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP cysteine-tRNA ligase activityInferred from sequence or structural similarity. Source: RefGenome zinc ion bindingInferred 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 – 466 | 466 | Cysteine--tRNA ligase HAMAP-Rule MF_00041 | PRO_0000159352 | |||||
Regions | |||||||||
| Motif | 31 – 41 | 11 | "HIGH" region HAMAP-Rule MF_00041 | ||||||
| Motif | 266 – 270 | 5 | "KMSKS" region HAMAP-Rule MF_00041 | ||||||
Sites | |||||||||
| Metal binding | 29 | 1 | Zinc By similarity | ||||||
| Metal binding | 209 | 1 | Zinc By similarity | ||||||
| Metal binding | 234 | 1 | Zinc By similarity | ||||||
| Metal binding | 238 | 1 | Zinc By similarity | ||||||
| Binding site | 269 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 270 | 1 | Phosphoserine Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis." Gagnon Y., Breton R., Putzer H., Pelchat M., Grunberg-Manago M., Lapointe J. J. Biol. Chem. 269:7473-7482(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [3] | "A mutant cysteinyl-tRNA synthetase affecting timing of chromosomal replication initiation in B. subtilis and conferring resistance to a protein kinase C inhibitor." Seror S.J., Casaregola S., Vannier F., Zouari N., Dahl M., Boye E. EMBO J. 13:2472-2480(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [4] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [5] | "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, MASS SPECTROMETRY. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L14580 Genomic DNA. Translation: AAA21798.1. D26185 Genomic DNA. Translation: BAA05328.1. X73989 Genomic DNA. Translation: CAA52167.1. AL009126 Genomic DNA. Translation: CAB11870.1. |
| PIR | C53402. |
| RefSeq | NP_387975.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | Q06752. |
| SMR | Q06752. Positions 3-464. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU00940. |
PTM databases | |
| PhosSite | P0802198. |
Proteomic databases | |
| PaxDb | Q06752. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB11870; CAB11870; BSU00940. |
| GeneID | 936859. |
| KEGG | bsu:BSU00940. |
| PATRIC | 18971697. VBIBacSub10457_0097. |
Organism-specific databases | |
| GenoList | BSU00940. [Micado] |
Phylogenomic databases | |
| eggNOG | COG0215. |
| HOGENOM | HOG000245250. |
| KO | K01883. |
| OMA | DFDALNM. |
| ProtClustDB | PRK00260. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU00940-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.50.620. 1 hit. |
| HAMAP | MF_00041. Cys_tRNA_synth. |
| InterPro | IPR015803. Cys-tRNA-ligase. IPR015273. Cys-tRNA-synt_Ia_DALR. IPR024909. Cys-tRNA/MSH_ligase. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view] |
| PANTHER | PTHR10890. PTHR10890. 1 hit. |
| Pfam | PF09190. DALR_2. 1 hit. PF01406. tRNA-synt_1e. 1 hit. [Graphical view] |
| PRINTS | PR00983. TRNASYNTHCYS. |
| SMART | SM00840. DALR_2. 1 hit. [Graphical view] |
| SUPFAM | SSF47323. tRNAsyn_1a_bind. 1 hit. |
| TIGRFAMs | TIGR00435. cysS. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYC_BACSU | ||||||||
| Accession | Primary (citable) accession number: Q06752 | ||||||||
| 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 |
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with
