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ProRule PRU00892


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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

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UniProtKB rule member sequences [?]