ID A0A182UK78_9DIPT Unreviewed; 990 AA.
AC A0A182UK78;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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};
OS Anopheles melas.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC021929-PA, ECO:0000313|Proteomes:UP000075902};
RN [1] {ECO:0000313|Proteomes:UP000075902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEC021929-PA}
RP IDENTIFICATION.
RC STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC021929-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
CC -!- SIMILARITY: Belongs to the GPSM family.
CC {ECO:0000256|ARBA:ARBA00006600}.
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DR AlphaFoldDB; A0A182UK78; -.
DR STRING; 34690.A0A182UK78; -.
DR EnsemblMetazoa; AMEC021929-RA; AMEC021929-PA; AMEC021929.
DR VEuPathDB; VectorBase:AMEC021929; -.
DR Proteomes; UP000075902; Unassembled WGS sequence.
DR GO; GO:0030695; F:GTPase regulator activity; IEA:InterPro.
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; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03044; BMT2; 1.
DR InterPro; IPR021867; Bmt2/SAMTOR.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45954; LD33695P; 1.
DR PANTHER; PTHR45954:SF1; LD33695P; 1.
DR Pfam; PF02188; GoLoco; 3.
DR Pfam; PF13489; Methyltransf_23; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 3.
DR SMART; SM00390; GoLoco; 3.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50877; GOLOCO; 3.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03044};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03044}; TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03044}.
FT REPEAT 409..442
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 747..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03044"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03044"
SQ SEQUENCE 990 AA; 110325 MW; C15F8C8F1FF282D8 CRC64;
MNVNRASDDD GDGSGGRVAQ NINYTRGAEQ LELSGLIKSV HQRLRDSAKQ QDPEAVWKEH
VRDAGLLKSY AEAMHKLATC YWDRTMEVSC KRSNSRIEWV VASCRSYFHG ATPLLYLFRE
KDDKVMQAID GIGHQPDHRP YTIDRIRLLD VGSCYDPFAC FPDFDVTAID IAPACASVWH
CDFLEAEILK SLTEPLVSVE HRLIEAFPSE YYDAIVFSLL LEYLPSPDQR LRCCRKAYEL
LKPEGILLII TPDSRHQGAN AKLMKNWRYT LGLMGFGRIK IEKLEHVTCM VFRKCIFPAV
SKRWCDIHWE AYMQPVLNIP QDFNETKVDV REQEGEMEVC RTEEDEGEIR EAFAGAENLS
SDQNNDGSSM CLELALEGER LCKSGDCRAG VAFFQAAIQA GTDDLRTLSA IYSQLGNAYF
YLGDYTKAMQ YHKHDLTLAR SMNDRLGEAK SSGNLGNTLK VMGRFDEAAI FCQRHLAIAR
VLEDRLSEGR ALYNLGNVYH AKGKQLGQKD PGDFSAEVQD SLLKAVDFYQ QNLRLMRELG
DRGAQGRACG NLGNTYYLLG QFETAIEHHQ ERLRIAREFG DKAAERRANS NLGNSHIFLG
HFEQAANHYK RTLSLAIELG ERAVEAQACY SLGNTYTLLR DFPTAIDYHQ RHLAIAQELG
DRIGEARACW SLGNAHTSIG NHEKALHYAN SHYLLAKELG DMVGESTARM NMADLRKILG
LPELETNVEA AQPVELGGAH TVPHAATAKA PTDGVGDSES GSLHHHTHHG QQVHVAAAAK
VASLAASKQH RLRRQSMEQL DLIKLTPDGK KLAQHNVQEN QTSNAQVPPS QPSKVKKNEN
SFKSNDEDFF DLLTRSQSKR MDDQRCTLKV SCGNVLLEMI AHFQSERMDE QRALLPGLKR
ISLGNANNMS RPTNNNESGP GSTTPEDPVE LGTPPDDAFL DMLMRCQGSR IEEQRSELPT
PNITLDAEAT EGQVVAPASV ASNSGATCLG
//
