ID   SMTL3_BOTBR             Reviewed;         392 AA.
AC   H2E7U0;
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 3;
DE            EC=2.1.1.-;
GN   Name=SMT-3;
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; JN828967; AEY68261.1; -; mRNA.
DR   AlphaFoldDB; H2E7U0; -.
DR   SMR; H2E7U0; -.
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..392
FT                   /note="Sterol methyltransferase-like 3"
FT                   /id="PRO_0000421360"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   392 AA;  43903 MW;  ED465F7AABC7D0D2 CRC64;
     MVSELVSMYV PPIVEAAKAV TPWQAAAGVT AAIFIGSYLW HSASLRKQRR TGTADGGLFS
     LTAGGIKKQD VTKLVDSFSQ AYKTEDDGQL TCHHITREQS VEMVNTFYDL ITDLYEWAWD
     TSFHFSCRPR WANFAQAQVL HEWRIANLAN IQPGMKVLDV GTGVGNPGRT IASLSGAQVT
     GVTINAYQVK RALHHTRKAK LEDFYKPVQA DFTDTPFEDD TFDAAFAIEA TCHAPKLEQV
     YKEVYRVLKP GAYFALYDGV TKPNFDPKNE RHVQLMNATV IGNGCPDMRT WKECEEIGKE
     VGFKLHMSYD AGEASRVLHP WWEKLDNFIN TGFAWYGPAS IKLLSKIGFL PRDFTKFIDI
     AAASVFSVKE AGELGIFTPM YVFVWQKPEK TA