PROSITE logo
Black ribbon
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.
Amos Bairoch

ProRule PRU00892


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00892
General rule information [?]

Accession PRU00892
Dates 25-NOV-2011 (Created)
03-SEP-2024 (Last updated, Version 23)
Data class Domain;
Predictors PROSITE; PS51559; SAM_RMT2
Name Arginine and arginine-like N-methyltransferase.
Function Guanidinoacetate N-methyltransferase (EC 2.1.1.2) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to guanidinoacetate to form creatine and S-adenosyl-L-homocysteine.
Scope(s) Eukaryota
Example(s) P10868;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Chordata> and <Length>=210> and <Length<=280>
Protein name + RecName: EC=2.1.1.2;
else
Protein name + RecName: EC=2.1.1.-;
end case

Comments [?]

case <OC:Chordata> and <Length>=210> and <Length<=280>
CATALYTIC ACTIVITY Reaction=guanidinoacetate + S-adenosyl-L-methionine = creatine + S- adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:10656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57742, ChEBI:CHEBI:57856, ChEBI:CHEBI:57947, ChEBI:CHEBI:59789; EC=2.1.1.2;
end case
SIMILARITYBelongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.

Keywords [?]

Methyltransferase
S-adenosyl-L-methionine
Transferase

Gene Ontology [?]

case <OCellular component:Chordata> and <Length>=210> and <Length<=280>
GO:0030731; Molecular function:guanidinoacetate N-methyltransferase activity
else case (<OCellular component:Fungi> or <OC:Viridiplantae>) and <Length>=315> and <Length<=540>
GO:0019702; Molecular function:protein arginine N5-methyltransferase activity
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0008757; Molecular function:S-adenosylmethionine-dependent methyltransferase activity
end case
GO:0032259; Biological process:methylation
GO:0046500; Biological process:S-adenosylmethionine metabolic process

Features [?]

From: PS51559
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="RMT2 #"
BINDING 69 74 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 [FH]-G-[LM]-[AGS]-[IL]-[AFISV]
BINDING 90 92 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 E-[ACP]-[HN]
BINDING 117 118 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 W-[EQ]
case <OC:Chordata> and <Length>=210> and <Length<=280>
BINDING 169 170 /ligand="guanidinoacetate"
/ligand_id="ChEBI:CHEBI:57742"		 L-T
end case
BINDING 20 20 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 [FWY]
case <OC:Chordata> and <Length>=210> and <Length<=280>
BINDING 41 41 /ligand="guanidinoacetate"
/ligand_id="ChEBI:CHEBI:57742"		 M
BINDING 45 45 /ligand="guanidinoacetate"
/ligand_id="ChEBI:CHEBI:57742"		 E
end case
BINDING 49 49 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 [MS]
case <OC:Chordata> and <Length>=210> and <Length<=280>
BINDING 137 137 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 D
BINDING 137 137 /ligand="guanidinoacetate"
/ligand_id="ChEBI:CHEBI:57742"		 D
else
BINDING 137 137 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 D
end case

Additional information [?]

Size range unlimited amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

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 [?]