Reviewed,
UniProtKB/Swiss-Prot Q81WL6 (SYP1_BACAN)
Last modified
November 3, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Prolyl-tRNA synthetase 1 EC=6.1.1.15 Alternative name(s): Proline--tRNA ligase 1 Short name=ProRS 1 | ||||
| Gene names |
| ||||
| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 566 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 proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS By similarity. |
| Catalytic activity | ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01569 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Domain | Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | prolyl-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 proline-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 – 566 | 566 | Prolyl-tRNA synthetase 1 HAMAP MF_01569 | PRO_0000248642 | |||
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] | "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. |
| [3] | "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. |
Cross-references
Sequence databases | |
|---|---|
| AE016879 Genomic DNA. Translation: AAP27686.1. AE017225 Genomic DNA. Translation: AAT55972.1. AE017334 Genomic DNA. Translation: AAT33071.1. | |
| RefSeq | NP_846200.1. YP_020596.1. YP_029921.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1086582. 2819521. 2852158. |
| GenomeReviews | Gene locus BA_3957 in contig AE016879_GR. Gene locus BAS3670 in contig AE017225_GR. Gene locus GBAA_3957 in contig AE017334_GR. |
| KEGG | ban:BA3957. bar:GBAA3957. bat:BAS3670. |
| TIGR | BA_3957. GBAA_3957. |
Phylogenomic databases | |
| HOGENOM | Q81WL6. |
| OMA | VVSHQLM. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS3670-MON. BANT261594:GBAA3957-MON. |
| BRENDA | 6.1.1.15. 267517. |
Family and domain databases | |
| HAMAP | MF_01569. [Tree] |
| InterPro | IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004154. Anticodon_bd. IPR004500. Pro-tRNA-synth_IIa_bac. IPR002316. Pro-tRNA-synth_IIa_cons-reg. IPR007214. YbaK/aa-tRNA-synth-assoc-reg. [Graphical view] |
| Gene3D | G3DSA:3.40.50.800. Anticodon_bd. 1 hit. |
| Pfam | PF03129. HGTP_anticodon. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF04073. YbaK. 1 hit. [Graphical view] |
| PRINTS | PR01046. TRNASYNTHPRO. |
| TIGRFAMs | TIGR00409. proS_fam_II. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYP1_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81WL6 Secondary accession number(s): Q6HUR7, Q6KNZ8 | ||||||||
| 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


