ID E2APD2_CAMFO Unreviewed; 344 AA.
AC E2APD2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=S-adenosylmethionine sensor upstream of mTORC1 {ECO:0000256|HAMAP-Rule:MF_03044};
DE AltName: Full=Probable methyltransferase BMT2 homolog {ECO:0000256|HAMAP-Rule:MF_03044};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03044};
GN ORFNames=EAG_06935 {ECO:0000313|EMBL:EFN64706.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN64706.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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.
CC {ECO:0000256|HAMAP-Rule:MF_03044}.
CC -!- SIMILARITY: Belongs to the BMT2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03044}.
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DR EMBL; GL441512; EFN64706.1; -; Genomic_DNA.
DR RefSeq; XP_011261660.1; XM_011263358.2.
DR AlphaFoldDB; E2APD2; -.
DR STRING; 104421.E2APD2; -.
DR EnsemblMetazoa; XM_011263358.3; XP_011261660.1; LOC105254588.
DR GeneID; 105254588; -.
DR KEGG; cfo:105254588; -.
DR InParanoid; E2APD2; -.
DR OMA; ASIMKNW; -.
DR OrthoDB; 3669878at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03044; BMT2; 1.
DR InterPro; IPR021867; Bmt2/SAMTOR.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21008:SF0; S-ADENOSYLMETHIONINE SENSOR UPSTREAM OF MTORC1; 1.
DR PANTHER; PTHR21008; UNCHARACTERIZED; 1.
DR Pfam; PF11968; Bmt2; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03044}; Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03044};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03044}.
FT BINDING 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03044"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03044"
SQ SEQUENCE 344 AA; 40058 MW; E0E5D3018AC8146D CRC64;
MATEEHKRLA DIVKGTHALL RVECHQYGSE IAWKRHVARN DVLQEYAVSM QKLATTYWAD
NNLKNGTYCR MEWIKTQCKE YFLHGDKKKY DKREQDINAK MALKKLDVEN RTRESDLVED
QLVNSHERRI SVLDVGSCYN PLNVDDAFDV TAIDLIPATG GVFRCDFLNI AIGREKILSG
DTREIHQLPA NSFHAVVFSL LLEYLPCPKQ RYICCRNAYD VLKVGGLLII VSPDSKHVGA
NARLMKSWRY TLSRLGFMRI KYEKLRHIHC LAFRKCACKD VAMRWCELQR FSEDDRRYMS
ETEIFIPQDF QTICPDEKLE KLHEYDKTDL ASIFSELPFD ETAI
//
