C3HP06 (C3HP06_BACTU) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 19.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Alanine--tRNA ligase HAMAP MF_00036 EC=6.1.1.7 HAMAP MF_00036 Alternative name(s): Alanyl-tRNA synthetase HAMAP MF_00036 | ||||
| Gene names |
| ||||
| Organism | Bacillus thuringiensis serovar pulsiensis BGSC 4CC1 EMBL EEM87717.1 | ||||
| Taxonomic identifier | 527028 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 880 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP MF_00036 |
| Catalytic activity | ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00036. |
| Domain | Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity. HAMAP MF_00036 |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. HAMAP MF_00036 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis HAMAP MF_00036 |
| Cellular component | Cytoplasm HAMAP MF_00036 |
| Ligand | ATP-binding HAMAP MF_00036 Metal-binding HAMAP MF_00036 Nucleotide-binding RNA-binding Zinc HAMAP MF_00036 tRNA-binding HAMAP MF_00036 |
| Molecular function | Aminoacyl-tRNA synthetase HAMAP MF_00036 EMBL EEM87717.1 Ligase |
| Gene Ontology (GO) | |
| Biological process | alanyl-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 alanine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP tRNA bindingInferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Metal binding | 567 | 1 | Zinc By similarity HAMAP MF_00036 | ||||||
| Metal binding | 571 | 1 | Zinc By similarity HAMAP MF_00036 | ||||||
| Metal binding | 669 | 1 | Zinc By similarity HAMAP MF_00036 | ||||||
| Metal binding | 673 | 1 | Zinc By similarity HAMAP MF_00036 | ||||||
Sequences
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References
| [1] | "Annotation of the Bacillus thuringiensis BGSC 4CC1 genome." Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., Willner K., Zwick M.E. Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: BGSC 4CC1 EMBL EEM87717.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ACNJ01000087 Genomic DNA. Translation: EEM87717.1. |
3D structure databases | |
| ProteinModelPortal | C3HP06. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000183595; EBBACP00000178897; EBBACG00000184047. |
| PATRIC | 28947894. VBIBacThu66700_5683. |
Family and domain databases | |
| HAMAP | MF_00036_B. Ala_tRNA_synth_B. [Tree] |
| InterPro | IPR002318. Ala-tRNA-synth_IIc. IPR018162. Ala-tRNA-synth_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR023033. Ala_tRNA_synth_euk/bac. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view] |
| PANTHER | PTHR11777:SF6. PTHR11777:SF6. 1 hit. |
| Pfam | PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view] |
| PRINTS | PR00980. TRNASYNTHALA. |
| SMART | SM00863. tRNA_SAD. 1 hit. [Graphical view] |
| SUPFAM | SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit. |
| TIGRFAMs | TIGR00344. AlaS. 1 hit. |
| PROSITE | PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | C3HP06_BACTU | ||||||||
| Accession | Primary (citable) accession number: C3HP06 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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