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Reviewed, UniProtKB/Swiss-Prot P78611 (CHSD_EMENI)

Last modified October 13, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    Chitin synthase D
    EC=2.4.1.16
Alternative name(s):
    Chitin-UDP acetyl-glucosaminyl transferase D
    Class-V chitin synthase D
Gene names
Name: chsD
Synonyms: chsE
ORF Names: AN1555
OrganismEmericella nidulans (Aspergillus nidulans) [Complete proteome]
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length1184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Plays a major role in cell wall biogenesis.

Catalytic activity

UDP-N-acetyl-D-glucosamine + (1,4-(N-acetyl-beta-D-glucosaminyl))(n) = UDP + (1,4-(N-acetyl-beta-D-glucosaminyl))(n+1).

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the chitin synthase family. Class V subfamily.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionchitin synthase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11841184Chitin synthase D
PRO_0000193693

Regions

Transmembrane221 – 24121 Potential
Transmembrane476 – 49621 Potential
Transmembrane1039 – 105921 Potential
Transmembrane1073 – 109321 Potential
Transmembrane1097 – 111721 Potential

Experimental info

Sequence conflict6061L → S in BAA11866. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P78611-1 [UniParc].

Last modified May 26, 2009. Version 3.
Checksum: BC1676F95F17004B

FASTA1,184133,531
        10         20         30         40         50         60 
MSLPQRPGKT SPRREETSAF REPSRRRRRE SDSLSNNDPT SPRHHRHHRS HSSRHQHDID 

        70         80         90        100        110        120 
EERAEEGGIR RKRSLVKPER GRMDPSHPNY LYRQKTQNMP TYNPMTGNEP LIHEEGEAET 

       130        140        150        160        170        180 
NSTPSMDSKR KDALYGAHGN VNKPMERVPT RHRSKKRKGS RKISKREAAA EKRRRKAMEQ 

       190        200        210        220        230        240 
VRPPSLWTTY CSVITFWAPD FVLKCFGMPQ KAQRSAWREK IGLISIILMI AAFVGFLTFG 

       250        260        270        280        290        300 
FTATVCGTPP TRLKINEIGS GYMIFHGQAY DLTKSTHPAA AGIPDMTNVL YDLPHKYGGQ 

       310        320        330        340        350        360 
DGSFFFQEVN GACKGLITRT ENSDIPTNSN GDLAWYFPCH AFNQDGSSEP NTTVSYYNGW 

       370        380        390        400        410        420 
ACHTSGSARK SFYSLKNSGD VYFTWEDTKN TSRKLAVYSG NVLDLNLLNW FDDTQVNYPT 

       430        440        450        460        470        480 
KFKDLRDNDD IRGVDLTYYF QTGEDKQIGK CLSQIIKVGS IDTDTVGCIA SQVVLYVSLI 

       490        500        510        520        530        540 
FILSIVIVKF AFALLFQWFL APRFAAQKTS MGAVDSKARN QQIEDWSNDI YRPGPRLADP 

       550        560        570        580        590        600 
VPGDRMSKRA SFLPTTSRFS SPYTVSNGGK QKPQWVTMAS QNSTTRLVPP ASGTTPSIYR 

       610        620        630        640        650        660 
QSHNGLGNVS VDNSRLNPSA SRTSLVQDSR YSTVIPDSEG IGSAGYVHEL VVPQPPPDWQ 

       670        680        690        700        710        720 
PYGFPLAHAM CLVTCYSEGE EGIRTTLDSI ALTDYPNSHK SIVVICDGII KGKGEEFSTP 

       730        740        750        760        770        780 
DIVLRMMRDP IIPPEEVEAF SYVAVATGSK RHNMAKVYAG FYDYGEHSII PVEKQQRVPM 

       790        800        810        820        830        840 
MIIVKCGTPA EATAAKPGNR GKRDSQIILM SFLQKVMFDE RMTELEYEMF NGLLHVTGIP 

       850        860        870        880        890        900 
PDFYEVVLMV DADTKVFPDS LTHMISAMVK DPEVMGLCGE TKIANKTDSW VTMIQVFEYF 

       910        920        930        940        950        960 
VSHHQSKAFE SVFGGVTCLP GCFSMYRIKA PKGGQNYWVP ILANPDIVEH YSENVVDTLH 

       970        980        990       1000       1010       1020 
KKNLLLLGED RYLSTLMLRT FPKRKQIFVP QAVCKTVVPD KFMVLLSQRR RWINSTVHNL 

      1030       1040       1050       1060       1070       1080 
MELVLVRDLC GTFCFSMQFV IFVELVGTVV LPAAISFTIY VVVSSIIKQP VQIIPLVLLA 

      1090       1100       1110       1120       1130       1140 
LILGLPGVLV VVTAHRLVYV LWMLVYLISL PIWNFVLPTY AYWKFDDFSW GDTRKTAGEK 

      1150       1160       1170       1180 
DKGHEDGEGE FDSSKITMKR WRDFEKGMSM LTVLHDARTA NDIY 

« Hide

References

« Hide 'large scale' references
[1]"The Aspergillus nidulans genes chsA and chsD encode chitin synthases which have redundant functions in conidia formation."
Motoyama T., Fujiwara M., Kojima N., Horiuchi H., Ohta A., Takagi M.
Mol. Gen. Genet. 251:442-450(1996) [PubMed: 8709948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FGSC 89.
[2]Erratum
Motoyama T., Fujiwara M., Kojima N., Horiuchi H., Ohta A., Takagi M.
Mol. Gen. Genet. 253:520-528(1997) [PubMed: 9037115] [Abstract]
[3]Motoyama T., Fujiwara M., Kojima N., Horiuchi H., Ohta A., Takagi M.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"The chsD and chsE genes of Aspergillus nidulans and their roles in chitin synthesis."
Specht C.A., Liu Y., Robbins P.W., Bulawa C.E., Iartchouk N., Winter K.R., Riggle P.J., Rhodes J.C., Dodge C.L., Culp D.W., Borgia P.T.
Fungal Genet. Biol. 20:153-167(1996) [PubMed: 8810520] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FGSC 4.
[5]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC 4.

Cross-references

Sequence databases

D83246 Genomic DNA. Translation: BAA11866.2.
U52362 Genomic DNA. Translation: AAA97482.1.
AACD01000025 Genomic DNA. Translation: EAA64262.1.
PIRJC6079.
RefSeqXP_659159.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Genome annotation databases

GeneID2875763.
KEGGani:AN1555.2.

Family and domain databases

InterProIPR004835. Chitin_synth_fng.
IPR001199. Cyt_B5.
[Graphical view]
PfamPF03142. Chitin_synth_2. 1 hit.
PF00173. Cyt-b5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHSD_EMENI
AccessionPrimary (citable) accession number: P78611
Secondary accession number(s): Q00744, Q5BD25
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 26, 2009
Last modified: October 13, 2009
This is version 56 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

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