Q9U6Y9 · ANM5_DROME
- ProteinProtein arginine N-methyltransferase 5
- Genecsul
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids610 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA) (By similarity).
Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3. Required for arginine symmetrical dimethylation of piwi family proteins, piwi, aub and AGO3, during germline development (PubMed:19377467, PubMed:19959991).
Required during oogenesis for pole cell formation in the pathway controlled by oskar (osk) and for abdominal segments during early embryogenesis. Involved in nanos (nos) and germ cell mRNAs localization
Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3. Required for arginine symmetrical dimethylation of piwi family proteins, piwi, aub and AGO3, during germline development (PubMed:19377467, PubMed:19959991).
Required during oogenesis for pole cell formation in the pathway controlled by oskar (osk) and for abdominal segments during early embryogenesis. Involved in nanos (nos) and germ cell mRNAs localization
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 300 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 303 | L-arginine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI); substrate | ||||
Sequence: F | ||||||
Binding site | 309-310 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: KY | ||||||
Binding site | 368 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 396-397 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DM | ||||||
Active site | 412 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 412 | L-arginine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI); substrate | ||||
Sequence: E | ||||||
Active site | 421 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 421 | L-arginine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI); substrate | ||||
Sequence: E |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | histone arginine N-methyltransferase activity | |
Molecular Function | protein methyltransferase activity | |
Molecular Function | protein-arginine N-methyltransferase activity | |
Molecular Function | protein-arginine omega-N symmetric methyltransferase activity | |
Biological Process | intracellular mRNA localization | |
Biological Process | P granule organization | |
Biological Process | peptidyl-arginine methylation | |
Biological Process | pole plasm assembly | |
Biological Process | pole plasm protein localization | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein arginine N-methyltransferase 5
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9U6Y9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Flies are viable and do not display neuromuscular dysfunctions. Strong synthetic lethal phenotype in the presence of a hypomorphic Smn mutation.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000212340 | 1-610 | Protein arginine N-methyltransferase 5 | |||
Sequence: MNYYVCLHQEGVNSIPKLIEKAFANNYNVVSTSINANMLPFEPHESDPTYPATILSGSDWNSKVIFTMSDVNVDSPNDKLREHAKEVFMRDVAWAEHLQNVGNLMVRLRGPENENLASIVLAKTKDDFPSGNWFIQVPITNPELATFEHRKDATAEEVAEAESNDPWNWWNNLRMVTKHSTKVKVVIELNDADRPSKETVRRWLGEPIEAIIIPSSLFVRNRSNYCVLKKEWQLIVGHFISVRANIIISTNPNDKALCQYADYVNKLINDNCDKHMLNSYENMLEIPLQPLCDNLDTYTYEVFETDPVKYKLYQDAVQAALLDRVSAAEAKTKLTVVMLLGGGRGPLARAVFNAAELTKRKVRLYIIEKNPNAIRTLSNMVKTLWADKDVHIFSKDMRDFSPPELADIMVSELLGSFGDNELSPECLDGALKLLKPDGISIPYKSTSYINPLMSAVLHQNVCQLLPTYPAFDYGYVSLLKNIYHIDEPQALFEFVHPNRAENIDNTRCKTVSFKVNKDCVLHGIGGYFDTHLYKDICLSINPLTHTPGMFSWFPMFFATRPRTLREGQTISIQFWRCVDATKVWYEWQVVNSPDDWEHHNTRGTGYNMRL |
Proteomic databases
Expression
Tissue specificity
Expressed only in ovaries.
Developmental stage
Expressed both maternally and zygotically. Expressed from stage 3 egg chambers onward, becoming restricted to the cortex of the oocytes at stage 10. Evenly distributed in preblastoderm embryos.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 284-587 | SAM-dependent MTase PRMT-type | ||||
Sequence: LEIPLQPLCDNLDTYTYEVFETDPVKYKLYQDAVQAALLDRVSAAEAKTKLTVVMLLGGGRGPLARAVFNAAELTKRKVRLYIIEKNPNAIRTLSNMVKTLWADKDVHIFSKDMRDFSPPELADIMVSELLGSFGDNELSPECLDGALKLLKPDGISIPYKSTSYINPLMSAVLHQNVCQLLPTYPAFDYGYVSLLKNIYHIDEPQALFEFVHPNRAENIDNTRCKTVSFKVNKDCVLHGIGGYFDTHLYKDICLSINPLTHTPGMFSWFPMFFATRPRTLREGQTISIQFWRCVDATKVWYEW | ||||||
Region | 470-610 | Interaction with vls | ||||
Sequence: AFDYGYVSLLKNIYHIDEPQALFEFVHPNRAENIDNTRCKTVSFKVNKDCVLHGIGGYFDTHLYKDICLSINPLTHTPGMFSWFPMFFATRPRTLREGQTISIQFWRCVDATKVWYEWQVVNSPDDWEHHNTRGTGYNMRL |
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9U6Y9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsA
- Length610
- Mass (Da)69,741
- Last updated2005-06-07 v2
- Checksum3531ACE5BEE9713E
Q9U6Y9-2
- Name2
- SynonymsB
- Differences from canonical
- 126-130: Missing
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 39 | in Ref. 2; CAA05712 | ||||
Sequence: L → M | ||||||
Sequence conflict | 78 | in Ref. 2; CAA05712 | ||||
Sequence: D → A | ||||||
Alternative sequence | VSP_014035 | 126-130 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 350-355 | in Ref. 2; CAA05712 | ||||
Sequence: AVFNAA → LFSMTS | ||||||
Sequence conflict | 447 | in Ref. 1; AAF04504 | ||||
Sequence: S → F | ||||||
Sequence conflict | 487-488 | in Ref. 2; CAA05712 | ||||
Sequence: EP → K | ||||||
Sequence conflict | 494 | in Ref. 1; AAF04504 | ||||
Sequence: F → V | ||||||
Sequence conflict | 501-502 | in Ref. 1; AAF04504 | ||||
Sequence: EN → GD | ||||||
Sequence conflict | 507 | in Ref. 2; CAA05712 | ||||
Sequence: R → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF167574 EMBL· GenBank· DDBJ | AAF04504.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ002740 EMBL· GenBank· DDBJ | CAA05712.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF58030.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAM68510.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY122153 EMBL· GenBank· DDBJ | AAM52665.1 EMBL· GenBank· DDBJ | mRNA |