Q0W2W0 (PIMT_UNCMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 50.
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 |
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| Organism | Uncultured methanogenic archaeon RC-I [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 351160 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanocellales › Methanocellaceae › Methanocella › ![]() |
Protein attributes
| Sequence length | 188 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 – 188 | 188 | Protein-L-isoaspartate O-methyltransferase HAMAP-Rule MF_00090 | PRO_0000351974 | |||||
Sites | |||||||||
| Active site | 33 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere." Erkel C., Kube M., Reinhardt R., Liesack W. Science 313:370-372(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM114193 Genomic DNA. Translation: CAJ37283.1. |
| RefSeq | YP_686609.1. NC_009464.1. |
3D structure databases | |
| ProteinModelPortal | Q0W2W0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 351160.RCIX2158. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAJ37283; CAJ37283; RCIX2158. |
| GeneID | 5143578. |
| KEGG | rci:RCIX2158. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2518. |
| HOGENOM | HOG000257189. |
| KO | K00573. |
| OMA | RILFSAC. |
| ProtClustDB | CLSK2789256. |
Family and domain databases | |
| HAMAP | MF_00090. PIMT. Divergent sequence. |
| 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PIMT_UNCMA | ||||||||
| Accession | Primary (citable) accession number: Q0W2W0 | ||||||||
| 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
