Q5RGQ2 · ANM8B_DANRE
- ProteinProtein arginine N-methyltransferase 8-B
- Geneprmt8b
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids419 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA).
Catalytic activity
- L-arginyl-[protein] + S-adenosyl-L-methionine = H+ + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 111 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 120 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 144 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 144-147 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GSGT | ||||||
Binding site | 166 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 195 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 210 | |||||
Sequence: E | ||||||
Active site | 219 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | plasma membrane | |
Molecular Function | arginine N-methyltransferase activity | |
Molecular Function | histone methyltransferase activity | |
Molecular Function | identical protein binding | |
Molecular Function | protein-arginine omega-N asymmetric methyltransferase activity | |
Molecular Function | protein-arginine omega-N monomethyltransferase activity | |
Molecular Function | S-adenosyl-L-methionine binding | |
Molecular Function | S-adenosylmethionine-dependent methyltransferase activity | |
Biological Process | chordate embryonic development | |
Biological Process | chromatin remodeling | |
Biological Process | dendrite morphogenesis | |
Biological Process | midbrain-hindbrain boundary development | |
Biological Process | neuron development | |
Biological Process | peptidyl-arginine methylation | |
Biological Process | protein homooligomerization | |
Biological Process | protein methylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein arginine N-methyltransferase 8-B
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ5RGQ2
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000378153 | 2-419 | Protein arginine N-methyltransferase 8-B | |||
Sequence: GLRHSSRCLLLRRKMAEAESTEQQQQKHKQPQHQQQQSISSIPSSQSLQPSPLPKPVTSVHHVPPHPPHTPHVSALSACPGRGKMAKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHIFKDKIVLDVGSGTGILSMFAAKAGAKHVYGIECSSISEYSEKIIKSNHLDSVITILKGKVEETELPVDQVDIIISEWMGYCLFYESMLNTVIYARDKWLKPGGFMFPDRATLYVVAIEDRQYKDFKIHWWENVYGFDMTCIRNVAMMEPLVDIVDPKQVVTNSCLVKEVDIYTVKTEDLSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKTGFSTAPDAPSTHWKQTVFYLEDYLTVRRGEEILGSITVRPNENNERDLDFTFELDFKGQLCDAAISHDYKMR | ||||||
Modified residue | 83 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 98 | Asymmetric dimethylarginine | ||||
Sequence: R |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer. Tetramer; individual homodimers associates to form a homotetramer. Homooctamer; individual homodimers associates to form a homooctamer and homooligomerization is required for proper localization to the cell membrane.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-79 | Disordered | ||||
Sequence: MGLRHSSRCLLLRRKMAEAESTEQQQQKHKQPQHQQQQSISSIPSSQSLQPSPLPKPVTSVHHVPPHPPHTPHVSALSA | ||||||
Compositional bias | 11-27 | Basic and acidic residues | ||||
Sequence: LLRRKMAEAESTEQQQQ | ||||||
Compositional bias | 28-55 | Polar residues | ||||
Sequence: KHKQPQHQQQQSISSIPSSQSLQPSPLP | ||||||
Compositional bias | 58-72 | Pro residues | ||||
Sequence: VTSVHHVPPHPPHTP | ||||||
Domain | 98-402 | SAM-dependent MTase PRMT-type | ||||
Sequence: RDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHIFKDKIVLDVGSGTGILSMFAAKAGAKHVYGIECSSISEYSEKIIKSNHLDSVITILKGKVEETELPVDQVDIIISEWMGYCLFYESMLNTVIYARDKWLKPGGFMFPDRATLYVVAIEDRQYKDFKIHWWENVYGFDMTCIRNVAMMEPLVDIVDPKQVVTNSCLVKEVDIYTVKTEDLSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKTGFSTAPDAPSTHWKQTVFYLEDYLTVRRGEEILGSITVRPNENNERDLDFTFELD |
Domain
The N-terminal region (1-60) inhibits the arginine N-methyltransferase activity.
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT8 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length419
- Mass (Da)48,222
- Last updated2009-06-16 v2
- Checksum63111344E2BC7D17
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8M9Q5Y0 | A0A8M9Q5Y0_DANRE | prmt8b | 418 | ||
A0A2R8Q6G4 | A0A2R8Q6G4_DANRE | prmt8b | 420 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-27 | Basic and acidic residues | ||||
Sequence: LLRRKMAEAESTEQQQQ | ||||||
Compositional bias | 28-55 | Polar residues | ||||
Sequence: KHKQPQHQQQQSISSIPSSQSLQPSPLP | ||||||
Compositional bias | 58-72 | Pro residues | ||||
Sequence: VTSVHHVPPHPPHTP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX784029 EMBL· GenBank· DDBJ | CAI20944.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BC162920 EMBL· GenBank· DDBJ | AAI62920.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC162940 EMBL· GenBank· DDBJ | AAI62940.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |