Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sterol 24-C-methyltransferase

Gene
N/A
Organism
Pneumocystis carinii
Status
Unreviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol.UniRule annotation

Catalytic activityi

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.UniRule annotation

Pathwayi: ergosterol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes ergosterol from zymosterol.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Sterol 24-C-methyltransferase
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
This subpathway is part of the pathway ergosterol biosynthesis, which is itself part of Steroid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes ergosterol from zymosterol, the pathway ergosterol biosynthesis and in Steroid metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMethyltransferasePROSITE-ProRule annotation, Transferase
Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesisUniRule annotation, Sterol metabolism
LigandS-adenosyl-L-methioninePROSITE-ProRule annotation

Enzyme and pathway databases

UniPathwayi
UPA00768;UER00760

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol 24-C-methyltransferaseUniRule annotation (EC:2.1.1.41UniRule annotation)
Alternative name(s):
Delta(24)-sterol C-methyltransferaseUniRule annotation
OrganismiPneumocystis cariniiImported
Taxonomic identifieri4754 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

Structurei

3D structure databases

ProteinModelPortaliQ9C439
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini62 – 357SAM_MT_ERG6_SMTInterPro annotationAdd BLAST296

Sequence similaritiesi

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

Family and domain databases

InterProiView protein in InterPro
IPR013216 Methyltransf_11
IPR030384 MeTrfase_SMT
IPR029063 SAM-dependent_MTases
IPR013705 Sterol_MeTrfase_C
PfamiView protein in Pfam
PF08241 Methyltransf_11, 1 hit
PF08498 Sterol_MT_C, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51685 SAM_MT_ERG6_SMT, 1 hit

Sequencei

Sequence statusi: Complete.

Q9C439-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHGKDAAKER GLLSSFRRIK KPKTERLDSY FGFWGDKCTS EKKNDVHPPE
60 70 80 90 100
RFKFYATLTR HYYSLVTDFY EYGWSISFHF CRLCKNESFS QAIARHEHYI
110 120 130 140 150
ALHAGIREGE TVLDVGCGVG GPDCQISVFT GANIVGLNNN DYQIQRAKYY
160 170 180 190 200
SEKKGLSDKL KFIKGDFMQM PFPENSFDKI YSIEATIHAP SLEGVYSEIY
210 220 230 240 250
RVLKPGGLYA SYEWVMLTEY DENDPEHQQI VYGIEIGDSI PKISKIGEAE
260 270 280 290 300
AALIKVGFEI IHSEELSTKN SPLPWYYYLD GYLKRVRSFR DFISIARMTT
310 320 330 340 350
IGKWLISSFI GLMEFIGLLP KGSKKVNDIL LVAADSLVKA GKKEIFTPMQ

LWVCRKPLV
Length:359
Mass (Da):41,099
Last modified:June 1, 2001 - v1
Checksum:iF24D6B1B97213BFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308162 mRNA Translation: AAK00294.1

Similar proteinsi

Entry informationi

Entry nameiQ9C439_PNECA
AccessioniPrimary (citable) accession number: Q9C439
Entry historyiIntegrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: March 28, 2018
This is version 63 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again