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O14321 (ERG6_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sterol 24-C-methyltransferase erg6

EC=2.1.1.41
Alternative name(s):
Delta(24)-sterol C-methyltransferase erg6
Ergosterol biosynthesis protein 6
Gene names
Name:erg6
ORF Names:SPBC16E9.05
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. Involved in the biosynthesis or ergosterol which is important for plasma membrane structure and function and for localization of plasma membrane proteins. Ref.5

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.

Subcellular location

Nucleus. Endoplasmic reticulum Probable Ref.4.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Sterol 24-C-methyltransferase erg6
PRO_0000124797

Sequences

Sequence LengthMass (Da)Tools
O14321 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: FA4D3D82A1CE03D6

FASTA37842,867
        10         20         30         40         50         60 
MSSTALLPPN TDQVLSRRLH GKAAEKKTGL AAIASKDVDE QSRKLQEYFE FWDRNHENES 

        70         80         90        100        110        120 
EEDRARRIDG YKSVVNSYYD LATDLYEYGW SQSFHFSRFY KGEAFAQSIA RHEHYLAYRM 

       130        140        150        160        170        180 
GIKPGSRVLD VGCGVGGPAR EITEFTGCNL VGLNNNDYQI SRCNNYAVKR NLDKKQVFVK 

       190        200        210        220        230        240 
GDFMHMPFED NTFDYVYAIE ATVHAPSLEG VYGEIFRVLK PGGVFGVYEW VMSDDYDSSI 

       250        260        270        280        290        300 
PKHREIAYNI EVGDGIPQMV RKCDAVEAIK KVGFNLLEED DLTDHDNPDL PWYYPLTGDI 

       310        320        330        340        350        360 
TKCQNIWDVF TVFRTSRLGK LVTRYSVQFL EKIGVAAKGT SKVGDTLAIA QKGLIEGGET 

       370 
HLFTPMFLMI AKKPETDA 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-378.
Strain: PR745.
[3]Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 55-63.
[4]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Multiple functions of ergosterol in the fission yeast Schizosaccharomyces pombe."
Iwaki T., Iefuji H., Hiraga Y., Hosomi A., Morita T., Giga-Hama Y., Takegawa K.
Microbiology 154:830-841(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAB16897.1.
D89131 mRNA. Translation: BAA13793.2.
PIRT39579.
T42375.
RefSeqNP_595787.1. NM_001021688.2.

3D structure databases

ProteinModelPortalO14321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276160. 1 interaction.
MINTMINT-4672270.
STRING4896.SPBC16E9.05-1.

Proteomic databases

MaxQBO14321.
PaxDbO14321.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC16E9.05.1; SPBC16E9.05.1:pep; SPBC16E9.05.
GeneID2539602.
KEGGspo:SPBC16E9.05.

Organism-specific databases

PomBaseSPBC16E9.05.

Phylogenomic databases

eggNOGCOG0500.
HOGENOMHOG000171097.
KOK00559.
OMAFHFCRFS.
OrthoDBEOG7DVDMW.
PhylomeDBO14321.

Enzyme and pathway databases

UniPathwayUPA00768; UER00760.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025810. ERG6.
IPR013216. Methyltransf_11.
IPR029063. SAM-dependent_MTases-like.
IPR013705. Sterol_MeTrfase_C.
[Graphical view]
PfamPF08241. Methyltransf_11. 1 hit.
PF08498. Sterol_MT_C. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 2 hits.
PROSITEPS51685. SAM_MT_ERG6_SMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800759.

Entry information

Entry nameERG6_SCHPO
AccessionPrimary (citable) accession number: O14321
Secondary accession number(s): P78782
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways