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Reviewed, UniProtKB/Swiss-Prot Q95ZE3 (CDS1_ENCCU)

Last modified October 13, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphatidate cytidylyltransferase
    EC=2.7.7.41
Alternative name(s):
    CDP-diglyceride pyrophosphorylase
    CDP-diglyceride synthetase
    CDP-diacylglycerol synthase
      Short name=CDS
    CTP:phosphatidate cytidylyltransferase
    CDP-DG synthetase
    CDP-DAG synthase
Gene names
Name: CDS1
Ordered Locus Names: ECU05_1250
OrganismEncephalitozoon cuniculi (Microsporidian parasite) [Complete proteome]
Taxonomic identifier6035 [NCBI]
Taxonomic lineageEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the CDS family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentMembrane
   DomainTransmembrane
   Molecular functionNucleotidyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphatidate cytidylyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Phosphatidate cytidylyltransferase
PRO_0000090721

Regions

Transmembrane49 – 6921 Potential
Transmembrane73 – 9321 Potential
Transmembrane108 – 12821 Potential
Transmembrane141 – 16121 Potential
Transmembrane171 – 19121 Potential
Transmembrane198 – 21821 Potential
Transmembrane237 – 25721 Potential
Transmembrane290 – 31021 Potential

Sequences

Sequence LengthMass (Da)Tools
Q95ZE3-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 34794E225A5D3CFC

FASTA39344,467
        10         20         30         40         50         60 
MAEERKDSEE SPGTYSCSKT LRRRGEITPN GKVRYETTQN KAAGITKTNF FRRLVLSIVM 

        70         80         90        100        110        120 
ISGFCWISVN DKIYSFGLII FLTISIIREI IGITRKSDGR PFHLRTSIIL GLAVPIYSYL 

       130        140        150        160        170        180 
VFPSIMMMYF SRVSKCFLRR LSFVCFYSYV AAFMCFVASL RKGRLKPQLG LFALIHLSTY 

       190        200        210        220        230        240 
TMAIAAKCAI FNLNKGRFWF VFPALLVISN DISAYVVGKS IGKRPLYRLS PKKTLEGFIG 

       250        260        270        280        290        300 
AFIFTTAVGF ALGHLHVNSG FLRDADSEQF QKFMKFTVFG ANVRVQSIYI HIIPFIFVAS 

       310        320        330        340        350        360 
FVAPFSGFLA SALKRAYKKK DFGEAISGHG GIADRMDCQV LIAIFASTYI SSFIYTEERS 

       370        380        390 
VGSVFSLICR NFSHDEIMIL IEMLNRRVES IRK 

« Hide

References

« Hide 'large scale' references
[1]"Encephalitozoon cuniculi (Microspora): characterization of phospholipid metabolic pathway potentially linked to therapeutics."
El Alaoui H., Bata J., Peyret P., Vivares C.P.
Exp. Parasitol. 98:171-179(2001) [PubMed: 11560410] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.
Nature 414:450-453(2001) [PubMed: 11719806] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.

Cross-references

Sequence databases

AJ310088 Genomic DNA. Translation: CAC51023.1.
AL590445 Genomic DNA. Translation: CAD26645.1.
RefSeqNP_597468.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ95ZE3.

Genome annotation databases

GeneID859134.
GenomeReviewsGene locus ECU05_1250 in contig AL590445_GR.
KEGGecu:ECU05_1250.
NMPDRfig|6035.1.peg.615.

Enzyme and pathway databases

BRENDA2.7.7.41. 276319.

Family and domain databases

InterProIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PfamPF01148. CTP_transf_1. 1 hit.
[Graphical view]
PIRSFPIRSF018269. PC_trans_euk. 1 hit.
PROSITEPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDS1_ENCCU
AccessionPrimary (citable) accession number: Q95ZE3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: December 1, 2001
Last modified: October 13, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents