ID   B7FM75_MEDTR            Unreviewed;       610 AA.
AC   B7FM75;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU366043};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU366043};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:ACJ85858.1};
RN   [1] {ECO:0000313|EMBL:ACJ85858.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Moskal W., Chan A., Cheung F., Xiao Y., Town C.D.;
RT   "Medicago truncatula full length cdna cloning project.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU366043}; Single-
CC       pass type II membrane protein {ECO:0000256|RuleBase:RU366043}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008361, ECO:0000256|RuleBase:RU366043}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT053198; ACJ85858.1; -; mRNA.
DR   AlphaFoldDB; B7FM75; -.
DR   ExpressionAtlas; B7FM75; differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR004159; Put_SAM_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10108:SF1119; METHYLTRANSFERASE PMT2-RELATED; 1.
DR   PANTHER; PTHR10108; SAM-DEPENDENT METHYLTRANSFERASE; 1.
DR   Pfam; PF03141; Methyltransf_29; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
PE   2: Evidence at transcript level;
KW   Glycoprotein {ECO:0000256|RuleBase:RU366043};
KW   Membrane {ECO:0000256|RuleBase:RU366043};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU366043};
KW   Signal-anchor {ECO:0000256|RuleBase:RU366043};
KW   Transferase {ECO:0000256|RuleBase:RU366043};
KW   Transmembrane {ECO:0000256|RuleBase:RU366043};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU366043}.
FT   TRANSMEM        15..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366043"
SQ   SEQUENCE   610 AA;  68950 MW;  50CB0D507762D8F3 CRC64;
     MAKPSAADNR TRSSVQIFIV VGLCCFFYIL GAWQRSGFGK GDSIALEITK NNAECDVVPN
     LSFDSHHAGE VSQIDESNSN TKVFKPCEAR YTDYTPCQDQ RRAMTFPREN MNYRERHCPP
     EEEKLHCMIP APKGYVTPFP WPKSRDYVPY ANAPYKSLTV EKAIQNWIQY EGNVFRFPGG
     GTQFPQGADK YIDQLASVIP INDGTVRTAL DTGCGVASWG AYLWSRNVVA MSFAPRDSHE
     AQVQFALERG VPAVIGVFGT IKLPNPSRAF DMAHCSRCLI PWGANDGMYM MEVDRVLRPG
     GYWVLSGPPI NWKVNYKPWQ RPKEELEEEQ RKIEEVAKKL CWEKKSEKAE IAIWQKMTDT
     ESCRSRQDDS SVEFCESSDP DDVWYKKLKA CVTPTPKVSG GDLKPFPDRL YAIPPRVSSG
     SIPGVSSETY QNDNKMWKKH VNAYKKINSL LDSGRYRNIM DMNAGLGSFA AAIHSSKSWV
     MNVVPTIAEK STLGVIYERG LIGIYHDWCE GFSTYPRTYD LIHANGLFSL YQDKCNTEDI
     LLEMDRILRP EGAVIIRDEV DVLIKVKKLI GGMRWNMKLV DHEDGPLVPE KVLIAVKQYW
     VTDGNSTSTQ
//