Q2L008 (PIMT_BORA1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 47.
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: Protein-L-isoaspartate O-methyltransferase EC=2.1.1.77 Alternative name(s): L-isoaspartyl protein carboxyl methyltransferase Protein L-isoaspartyl methyltransferase Protein-beta-aspartate methyltransferase Short name=PIMT | ||||
| Gene names |
| ||||
| Organism | Bordetella avium (strain 197N) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 360910 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › ![]() |
Protein attributes
| Sequence length | 264 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins By similarity. HAMAP-Rule MF_00090 |
| Catalytic activity | S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester. HAMAP-Rule MF_00090 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | protein repair Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Inferred 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 – 264 | 264 | Protein-L-isoaspartate O-methyltransferase HAMAP-Rule MF_00090 | PRO_0000351818 | |||||
Sites | |||||||||
| Active site | 112 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction." Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M. J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 197N. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM167904 Genomic DNA. Translation: CAJ49589.1. |
| RefSeq | YP_786496.1. NC_010645.1. |
3D structure databases | |
| ProteinModelPortal | Q2L008. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 360910.BAV1980. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6265723. |
| KEGG | bav:BAV1980. |
| PATRIC | 21130154. VBIBorAvi43433_1999. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2518. |
| HOGENOM | HOG000257189. |
| KO | K00573. |
| OMA | VRARMVQ. |
| ProtClustDB | CLSK920464. |
Family and domain databases | |
| HAMAP | MF_00090. PIMT. |
| InterPro | IPR000682. PCMT. [Graphical view] |
| PANTHER | PTHR11579. PTHR11579. 1 hit. |
| Pfam | PF01135. PCMT. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00080. pimt. 1 hit. |
| PROSITE | PS01279. PCMT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PIMT_BORA1 | ||||||||
| Accession | Primary (citable) accession number: Q2L008 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
