NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9593144 [NCBI, ExPASy, EBI, Israel, Japan]
Jensen-Pergakes K.L., Kennedy M.A., Lees N.D., Barbuch R., Koegel C., Bard M.;
"Sequencing, disruption, and characterization of the Candida albicans sterol methyltransferase (ERG6) gene: drug susceptibility studies in erg6 mutants.";
Antimicrob. Agents Chemother. 42:1160-1167(1998).

Comments

FUNCTION: Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 5-alpha-cholesta-8,24-dien-3-beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5-alpha-cholest-8-en-3-beta-ol.
PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from zymosterol: step 1/5 .
SIMILARITY: Belongs to the methyltransferase superfamily. ERG6 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF031941; AAC26626.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O74198.

Organism-specific databases

CGD

CAL0006397; ERG6.

Family and domain databases

InterPro

IPR013216; Methyltransf_11.
IPR013705; Sterol_MeTrfase_C.
Graphical view of domain structure.

Pfam

PF08241; Methyltransf_11; 1.
PF08498; Sterol_MT_C; 1.
Pfam graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Lipid synthesis; Methyltransferase; S-adenosyl-L-methionine; Steroid biosynthesis; Sterol biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 376`	`376`		`Sterol 24-C-methyltransferase.`	`PRO_0000124789`

Sequence information

Length: 376 AA [This is the length of the unprocessed precursor]

Molecular weight: 43086 Da [This is the MW of the unprocessed precursor]

CRC64: 369D094AFCDED0A0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSPVQLAEKN YERDEQFTKA LHGESYKKTG LSALIAKSKD AASVAAEGYF KHWDGGISKD 

        70         80         90        100        110        120 
DEEKRLNDYS QLTHHYYNLV TDFYEYGWGS SFHFSRYYKG EAFRQATARH EHFLAHKMNL 

       130        140        150        160        170        180 
NENMKVLDVG CGVGGPGREI TRFTDCEIVG LNNNDYQIER ANHYAKKYHL DHKLSYVKGD 

       190        200        210        220        230        240 
FMQMDFEPES FDAVYAIEAT VHAPVLEGVY SEIYKVLKPG GIFGVYEWVM TDKYDETNEE 

       250        260        270        280        290        300 
HRKIAYGIEV GDGIPKMYSR KVAEQALKNV GFEIEYQKDL ADVDDEIPWY YPLSGDLKFC 

       310        320        330        340        350        360 
QTFGDYLTVF RTSRIGRFIT TESVGLMEKI GLAPKGSKQV THALEDAAVN LVEGGRQKLF 

       370 
TPMMLYVVRK PLEKKD

O74198 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools