ID   SMTL1_BOTBR             Reviewed;         389 AA.
AC   H2E7T8;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Sterol methyltransferase-like 1;
DE            EC=2.1.1.-;
GN   Name=SMT-1;
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; JN828965; AEY68259.1; -; mRNA.
DR   AlphaFoldDB; H2E7T8; -.
DR   SMR; H2E7T8; -.
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 1"
FT                   /id="PRO_0000421358"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   389 AA;  43399 MW;  8EA21BC25F5E74A4 CRC64;
     MASELFATYY PRVVEAAQQL APWQIAAGVT AAVVIGGYIW IITELRSPRR TGTSLFKLSG
     GGIKKHDVAK FMDGYEKSYK TQEDGALTWH HISKEDSVKM VNTFYDLVTD AYEWAWDISF
     HFSCRPVWAN FAQAQVLHEC RIANLARIQP GMKVIDVGTG VGNPGRTIAS LTGAHVTGVT
     INAYQIKRAL HHTKKAGLLD MYKPVQADFT DMPFADESFD AAFAIEATCH APKLEQVYAE
     VYRVLKPGAY FAVYEAVSKP NFDPKNKRHV EIINSLVYGN GIPDMRTWKE AEEAGKKVGF
     KLHFSYDAGE ASSVLAPWWE RPRNLVNTGV IAYTKFAIKV CDKIGILPRD YAKFAKCVGD
     CIPDAVESGE LGIFTPMYVY VWQKPEKST