ID   SAMTR_XENLA             Reviewed;         400 AA.
AC   Q66J91; Q6GN88;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=S-adenosylmethionine sensor upstream of mTORC1 {ECO:0000255|HAMAP-Rule:MF_03044};
DE   AltName: Full=Probable methyltransferase BMT2 homolog {ECO:0000255|HAMAP-Rule:MF_03044};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03044};
GN   Name=bmt2 {ECO:0000255|HAMAP-Rule:MF_03044};
GN   Synonyms=samtor {ECO:0000255|HAMAP-Rule:MF_03044};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_03044}.
CC   -!- SUBUNIT: Interacts with the GATOR1 complex; interaction is disrupted
CC       when bmt2/samtor binds S-adenosyl-L-methionine. Interacts with the
CC       KICSTOR complex; interaction is disrupted when Bmt2/samtor binds S-
CC       adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_03044}.
CC   -!- SIMILARITY: Belongs to the BMT2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03044}.
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DR   EMBL; BC073627; AAH73627.1; -; mRNA.
DR   EMBL; BC081015; AAH81015.1; -; mRNA.
DR   RefSeq; NP_001087629.1; NM_001094160.1.
DR   AlphaFoldDB; Q66J91; -.
DR   DNASU; 447453; -.
DR   GeneID; 447453; -.
DR   CTD; 447453; -.
DR   Xenbase; XB-GENE-6078535; bmt2.L.
DR   OMA; DNHWTKK; -.
DR   OrthoDB; 836637at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 447453; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_03044; BMT2; 1.
DR   InterPro; IPR021867; Bmt2/SAMTOR.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR21008; PTHR21008; 1.
DR   Pfam; PF11968; Bmt2; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..400
FT                   /note="S-adenosylmethionine sensor upstream of mTORC1"
FT                   /id="PRO_0000321543"
FT   BINDING         168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
FT   BINDING         186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
SQ   SEQUENCE   400 AA;  45750 MW;  06E2CE90CCB70D71 CRC64;
     MEAVLPSRCN REDVPGKARA ERFVSGFPSV CEQKTEQEKL SGVVKRVHLD LRKKYRKAGD
     FEKIWLEHCK DDGRLCEYAV AMKALADNHW AKKCEGEGRI EWCLGVCQEY FFNGGKKKAL
     EKDAKRDALN KLQSSSHAEA GVSDFGVPSI KPLNDEYMTG KIRLLDVGSC YNPFLKYEDF
     LAVGIDIVPA VETVFKCDFL NLQIQRPLQL APDAIDAFLK QLSSPIDYLP TELFHVIVFS
     LLLSYFPSPY QRWICCKKAH ELLTLNGLLL IITPDSSHQN RHAVMMKSWK IAIESLGFRR
     MTYSKFSHMH LMAFRKTSLK TTSDLLTRNY PDMLYIPQDF NYDGEEDHFS PCCARSELED
     EQLACGFTEL PDTPYDSDSG ESHNSTMPFY EFEDPILLLT