AC   MF_03044;
DC   Protein; auto
TR   HAMAP; MF_03044; -; 1; level=0
XX
Names: BMT2
XX
case <OC:Saccharomyces>
ID   BMT2
DE   RecName: Full=25S rRNA (adenine(2142)-N(1))-methyltransferase;
DE            EC=2.1.1.286;
DE   AltName: Full=Base MethylTransferase of 25S RNA;
else case <OC:Fungi>
ID   BMT2
DE   RecName: Full=25S rRNA adenine-N(1) methyltransferase;
DE            EC=2.1.1.-;
else case <OC:Metazoa>
ID   SAMTR
DE   RecName: Full=S-adenosylmethionine sensor upstream of mTORC1;
DE   AltName: Full=Probable methyltransferase BMT2 homolog;
DE            EC=2.1.1.-;
else
ID   BMT2
DE   RecName: Full=Probable methyltransferase BMT2 homolog;
DE            EC=2.1.1.-;
end case
case <OC:Saccharomycotina>
GN   Name=BMT2;
else case <OC:Vertebrata>
GN   Name=BMT2; Synonyms=SAMTOR;
end case
XX
case <OC:Saccharomyces>
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       specifically methylates the N(1) position of adenine 2142 in 25S rRNA.
CC       N(1)-methyladenine(2142) in 25S rRNA is present in helix 65, a region
CC       that accounts for most of the intersubunit surface of the large
CC       subunit.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(2142) in 25S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(1)-methyladenosine(2142) in 25S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43784, Rhea:RHEA-COMP:10691, Rhea:RHEA-COMP:10692,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.286;
else case <OC:Fungi>
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       specifically methylates the N(1) position of an adenine present in
CC       helix 65 in 25S rRNA.
else case <OC:Vertebrata>
CC   -!- FUNCTION: S-adenosyl-L-methionine-binding protein that acts as an
CC       inhibitor of mTORC1 signaling via interaction with the GATOR1 and
CC       KICSTOR complexes. Acts as a sensor of S-adenosyl-L-methionine to
CC       signal methionine sufficiency to mTORC1: in presence of methionine,
CC       binds S-adenosyl-L-methionine, leading to disrupt interaction with the
CC       GATOR1 and KICSTOR complexes and promote mTORC1 signaling. Upon
CC       methionine starvation, S-adenosyl-L-methionine levels are reduced,
CC       thereby promoting the association with GATOR1 and KICSTOR, leading to
CC       inhibit mTORC1 signaling. Probably also acts as a S-adenosyl-L-
CC       methionine-dependent methyltransferase.
CC   -!- SUBUNIT: Interacts with the GATOR1 complex; interaction is disrupted
CC       when @gn(BMT2/SAMTOR) binds S-adenosyl-L-methionine. Interacts with the
CC       KICSTOR complex; interaction is disrupted when @gn(BMT2/SAMTOR) binds
CC       S-adenosyl-L-methionine.
else case <OC:Metazoa>
CC   -!- FUNCTION: S-adenosyl-L-methionine-binding protein that acts as an
CC       inhibitor of mTORC1 signaling. Acts as a sensor of S-adenosyl-L-
CC       methionine to signal methionine sufficiency to mTORC1. Probably also
CC       acts as a S-adenosyl-L-methionine-dependent methyltransferase.
else
CC   -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase.
end case
case <OC:Fungi>
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
end case
CC   -!- SIMILARITY: Belongs to the BMT2 family.
XX
DR   Pfam; PF11968; DUF3321; 1; trigger=no
XX
case <OC:Fungi>
KW   Nucleus
end case
KW   Methyltransferase
KW   S-adenosyl-L-methionine
KW   Transferase
XX
case <OC:Fungi>
GO   GO:0005730; C:nucleolus
GO   GO:0016433; F:rRNA (adenine) methyltransferase activity
else
GO   GO:0008168; F:methyltransferase activity
end case
XX
FT   From: SAMTR_HUMAN (Q1RMZ1)
FT   BINDING         172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: G
FT   BINDING         190
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: D
XX
Size: 270-672;
Related: None;
Template: P38278; Q1RMZ1; Q9W138;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.12 2022/11/19
//