We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU01018
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01018
General rule information
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| Accession | PRU01018 |
| Dates | 08-AUG-2024 (Created)
08-AUG-2024 (Last updated, Version 3) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51681; SAM_MT_NNMT_PNMT_TEMT |
Name | NNMT, PNMT, TEMT and homologues. |
| Function | Function: Nicotinamide N-methyltransferase (EC 2.1.1.1) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to nicotinamide to form 1-methylnicotinamide and S-adenosyl-L-homocysteine. Phenylethanolamine N-methyltransferase (EC 2.1.1.28) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to phenylethanolamine to form N-methylphenylethanolamine and S-adenosyl-L homocysteine. Amine N-methyltransferase (EC 2.1.1.49) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to an amine to form a methylated amine and S-adenosyl-L-homocysteine. Thioether S-methyltransferase (EC 2.1.1.96) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to dimethyl sulfide to form trimethylsulfonium and S-adenosyl-L-homocysteine. |
| Scope(s) |
Eukaryota Metazoa |
| Example(s) | P40261; |
Propagated annotation
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Identifier, protein and gene names
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| Protein name | + RecName: EC=2.1.1.-; |
Comments
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| SIMILARITY | Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family. |
Keywords
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Gene Ontology
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| GO:0008757; Molecular function:S-adenosylmethionine-dependent methyltransferase activity |
| GO:0032259; Biological process:methylation |
| GO:0046500; Biological process:S-adenosylmethionine metabolic process |
Features
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| From: PS51681 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 13 | 13 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
Y | ||||||||
| BINDING | 18 | 18 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
Y | ||||||||
| BINDING | 55 | 56 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
G-[SA] | ||||||||
| BINDING | 61 | 61 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
Y | ||||||||
| BINDING | 77 | 77 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
D | ||||||||
| BINDING | 82 | 82 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
N | ||||||||
| BINDING | 134 | 135 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
[DN]-[VA] | ||||||||
| BINDING | 155 | 155 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
[TFLAV] | ||||||||
Additional information
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| Size range | 251-260 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Eukaryota [14] All [ 14 ]
- Retrieve set of proteins with 3D structure for this domain