A0A0C3RR82 · PGMA1_PHLG1
- ProteinMethyltransferase/ribosomally synthesized type II borosin cyclic peptide precursor pgiMA1
- GenepgiMA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids556 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities (PubMed:31117659).
Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM) (PubMed:31117659).
The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product (By similarity).
Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM) (PubMed:31117659).
The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product (By similarity).
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 74 | |||||
Sequence: R | ||||||
Active site | 78 | |||||
Sequence: Y | ||||||
Active site | 100 | |||||
Sequence: Y | ||||||
Binding site | 100 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 102 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 105 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 174 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 212 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 243 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 244 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: T |
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 | |
---|---|---|
Molecular Function | methyltransferase activity | |
Biological Process | methylation |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMethyltransferase/ribosomally synthesized type II borosin cyclic peptide precursor pgiMA1
- Alternative names
- Cleaved into 13 chains
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Phanerochaetaceae > Phlebiopsis
Accessions
- Primary accessionA0A0C3RR82
Proteomes
PTM/Processing
Features
Showing features for chain, peptide, modified residue, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458519 | 1-386 | N-methyltranferase pgiM1 | |||
Sequence: MSSASSDSNTGSLTIAGSGIASVRHMTLETLAHVQEADIVFYVVADPVTEAYIKKNARGPCKDLEVLFDKDKVRYDTYVQMAETMLNAVREGQKVLGIFYGHPGVFVSPSRRALSIARKEGYQAKMLPGISSEDYMFADLEFDPAVHGCCAYEATQLLLREVSLDTAMSNIIWQVGGVGVSKIDFENSKVKLLVDRLEKDFGPDHHVVHYIGAVLPQSATVQDVLKISDLRKEEIVAQFNSCSTLYVPPLTHANKFSGNMVKQLFGQDVTEVSSALCPTPKWAAGSHLGDVVEYGPREKAAVDALVEHTVPADYRVLGGSLAFQQFMIDLALRPAIQANYKENPRALVDATKGLTTVEQAALLLRQPGAVFGVMKLRASEVANEQG | ||||||
Peptide | PRO_0000458520 | 387-399 | Ribosomally synthesized type II borosin core peptide pgiA1-I | |||
Sequence: HPVAPASLDHVAF | ||||||
Peptide | PRO_0000458521 | 400-412 | Ribosomally synthesized type II borosin core peptide pgiA1-II | |||
Sequence: TAPSPASLDHVAF | ||||||
Peptide | PRO_0000458522 | 413-425 | Ribosomally synthesized type II borosin core peptide pgiA1-III | |||
Sequence: SAPNPASLDHVAF | ||||||
Modified residue | 421 | N-methylaspartate | ||||
Sequence: D | ||||||
Peptide | PRO_0000458523 | 426-438 | Ribosomally synthesized type II borosin core peptide pgiA1-IV | |||
Sequence: IAPTPASLDHVAF | ||||||
Modified residue | 434 | N-methylaspartate | ||||
Sequence: D | ||||||
Peptide | PRO_0000458524 | 439-451 | Ribosomally synthesized type II borosin core peptide pgiA1-V | |||
Sequence: SAPTPASLDHVSF | ||||||
Modified residue | 447 | N-methylaspartate | ||||
Sequence: D | ||||||
Peptide | PRO_0000458525 | 452-464 | Ribosomally synthesized type II borosin core peptide pgiA1-VI | |||
Sequence: GTPTSASLDHVAF | ||||||
Modified residue | 460 | N-methylaspartate | ||||
Sequence: D | ||||||
Peptide | PRO_0000458526 | 465-477 | Ribosomally synthesized type II borosin core peptide pgiA1-VII | |||
Sequence: EAPVPASLDHVAF | ||||||
Modified residue | 473 | N-methylaspartate | ||||
Sequence: D | ||||||
Peptide | PRO_0000458527 | 478-490 | Ribosomally synthesized type II borosin core peptide pgiA1-VIII | |||
Sequence: AAPVPASLDHVAF | ||||||
Modified residue | 486 | N-methylaspartate | ||||
Sequence: D | ||||||
Peptide | PRO_0000458528 | 491-503 | Ribosomally synthesized type II borosin core peptide pgiA1-IX | |||
Sequence: AAPTPASLDHVAF | ||||||
Modified residue | 499 | N-methylaspartate | ||||
Sequence: D | ||||||
Peptide | PRO_0000458529 | 504-516 | Ribosomally synthesized type II borosin core peptide pgiA1-X | |||
Sequence: AAPTPASLDHVAF | ||||||
Modified residue | 512 | N-methylaspartate | ||||
Sequence: D | ||||||
Peptide | PRO_0000458530 | 517-529 | Ribosomally synthesized type II borosin core peptide pgiA1-XI | |||
Sequence: AVPVPASLDHIAF | ||||||
Modified residue | 525 | N-methylaspartate | ||||
Sequence: D | ||||||
Peptide | PRO_0000458531 | 530-542 | Ribosomally synthesized type II borosin core peptide pgiA1-XII | |||
Sequence: SVPTPASLDHVAF | ||||||
Modified residue | 538 | N-methylaspartate | ||||
Sequence: D | ||||||
Propeptide | PRO_0000458532 | 543-556 | ||||
Sequence: AVPVPDHVAGIPCM |
Post-translational modification
PgiMA1 automethylates at Asp-421, Asp-434, Asp-447, Asp-460, Asp-473, Asp-486, Asp-499, Asp-512, Asp-525 and Asp-538 before being processed, probably by the M64 family peptidase found in the genes surrounding PgiMA1, to release methylated peptides which then undergos macrocyclization with the N-terminus of the modified core peptides (PubMed:31117659).
Peptide backbone alpha-N-methylations change the physicochemical properties of amide bonds to provide structural constraints and other favorable characteristics including biological membrane permeability to peptides (Probable)
Peptide backbone alpha-N-methylations change the physicochemical properties of amide bonds to provide structural constraints and other favorable characteristics including biological membrane permeability to peptides (Probable)
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-250 | Methyltransferase domain | ||||
Sequence: MSSASSDSNTGSLTIAGSGIASVRHMTLETLAHVQEADIVFYVVADPVTEAYIKKNARGPCKDLEVLFDKDKVRYDTYVQMAETMLNAVREGQKVLGIFYGHPGVFVSPSRRALSIARKEGYQAKMLPGISSEDYMFADLEFDPAVHGCCAYEATQLLLREVSLDTAMSNIIWQVGGVGVSKIDFENSKVKLLVDRLEKDFGPDHHVVHYIGAVLPQSATVQDVLKISDLRKEEIVAQFNSCSTLYVPPL | ||||||
Region | 251-377 | Clasp domain | ||||
Sequence: THANKFSGNMVKQLFGQDVTEVSSALCPTPKWAAGSHLGDVVEYGPREKAAVDALVEHTVPADYRVLGGSLAFQQFMIDLALRPAIQANYKENPRALVDATKGLTTVEQAALLLRQPGAVFGVMKLR | ||||||
Region | 378-386 | Precursor leader | ||||
Sequence: ASEVANEQG |
Domain
Within the homodimer, the clasp domain wraps around the adjacent subunit to position the core peptide into the other subunit's active site for iterative intermolecular methylation.
Sequence similarities
In the N-terminal section; belongs to the precorrin methyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length556
- Mass (Da)59,109
- Last updated2023-09-13 v2
- ChecksumC0B8974EBDFCEC5C
Sequence caution
Keywords
- Technical term