A0A6I3PSU1 · A0A6I3PSU1_9FIRM
- ProteinProtein-arginine kinase
- GenemcsB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids329 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic activity
- ATP + L-arginyl-[protein] = ADP + H+ + N(omega)-phospho-L-arginyl-[protein]
Activity regulation
Appears to be allosterically activated by the binding of pArg-containing polypeptides to the pArg-binding pocket localized in the C-terminal domain of McsB.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | creatine kinase activity | |
Molecular Function | protein kinase activity | |
Biological Process | phosphocreatine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein-arginine kinase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Ruminococcus
Accessions
- Primary accessionA0A6I3PSU1
Proteomes
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-235 | Phosphagen kinase C-terminal | ||||
Sequence: EVISTRVRLARNLKDYPFPCRLSEQGRKKVIEKVTSAIRDSNSSIASDFNLIKLDDLTEAQGVSLVERHLVSPEFISETEGRALLLSKDESMSIMINEEDHIRLQVITDGLSLEQAYDTADKLDTLLDENLEFAFDDKLGYLTQCPTNLGTGMRASVMLHLPALEKSRTIGRIAGNLSKLGLTIRGAYGEGSEPSGSLYQLSNQVTLGISEKAAIENLENITKQLVSQEQQA | ||||||
Motif | 316-321 | RDXXRA motif of the pArg binding pocket involved in allosteric regulation | ||||
Sequence: RDIERA |
Sequence similarities
Belongs to the ATP:guanido phosphotransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length329
- Mass (Da)36,279
- Last updated2020-08-12 v1
- Checksum66A5517736D12237