ID   SMTL2_BOTBR             Reviewed;         389 AA.
AC   H2E7T9;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Sterol methyltransferase-like 2;
DE            EC=2.1.1.-;
GN   Name=SMT-2;
OS   Botryococcus braunii (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Elliptochloris clade; Botryococcus.
OX   NCBI_TaxID=38881;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=22241476; DOI=10.1074/jbc.m111.316059;
RA   Niehaus T.D., Kinison S., Okada S., Yeo Y.S., Bell S.A., Cui P.,
RA   Devarenne T.P., Chappell J.;
RT   "Functional identification of triterpene methyltransferases from
RT   Botryococcus braunii race B.";
RL   J. Biol. Chem. 287:8163-8173(2012).
CC   -!- FUNCTION: Unable to convert squalene, botryococcene, cycloartenol,
CC       zymosterol or lanosterol to mono-, di-, tri- or tetramethylated
CC       derivatives. {ECO:0000269|PubMed:22241476}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Erg6/SMT family. {ECO:0000255|PROSITE-ProRule:PRU01022}.
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DR   EMBL; JN828966; AEY68260.1; -; mRNA.
DR   AlphaFoldDB; H2E7T9; -.
DR   SMR; H2E7T9; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR030384; MeTrfase_SMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR013705; Sterol_MeTrfase_C.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   Pfam; PF08498; Sterol_MT_C; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Methyltransferase; Microsome; S-adenosyl-L-methionine; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..389
FT                   /note="Sterol methyltransferase-like 2"
FT                   /id="PRO_0000421359"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   389 AA;  42725 MW;  1E4B0E66C06A64DB CRC64;
     MAAELIKEYV PIVSEYAPGL IEGLLSWKGA VGLVAATGIG YVLIIQRLQN TSATKNLWGL
     TGGGVQAKDV SKVADVYDKS YGKEGDGSLT LHHLDKKESV AVVDTFYNLV TDGYEACWDT
     SFHFSPRPRF TNFRTAQILH EARIGYMARI QPGFKVLDCG CGIGNPGRTV AALTGAHVTG
     ITINEYQVKR ALYHTKKAGL TGLFTPVQGD FTDMPFADKT FDAAFAIEAT CHAPKLEQVY
     GEIFRVLKPG AFFAVYEAVT TDKFDPANKR HVEIINSLVY GNGIPDMRTW KQAEEAGKNV
     GFKLCCAFDA GAASPVALPW WERVKDMINW GVVKYTKAAC LALDSLRLLP KDYWKVANMV
     GDSLPDLVES GETGIFTPMY LLVWQKPEE