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P30583 (CHSC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chitin synthase C
EC=2.4.1.16
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase C
Class-I chitin synthase C
Gene names
Name:chsC
Synonyms:chs1
ORF Names:AN4566
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length918 AA.
Sequence statusComplete.
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 I subfamily.

Sequence caution

The sequence BAA75501.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAA60909.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

chitin biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionchitin synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Chitin synthase C
PRO_0000193690

Regions

Transmembrane605 – 62521Helical; Potential
Transmembrane637 – 65721Helical; Potential
Transmembrane672 – 69221Helical; Potential
Transmembrane715 – 73521Helical; Potential
Transmembrane745 – 76521Helical; Potential
Transmembrane845 – 86521Helical; Potential
Transmembrane890 – 91021Helical; Potential

Experimental info

Sequence conflict281 – 2822SK → RS in BAA75501. Ref.1
Sequence conflict6751L → F in BAA75501. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P30583 [UniParc].

Last modified November 16, 2011. Version 3.
Checksum: CF13A026D13AEAC4

FASTA918104,831
        10         20         30         40         50         60 
MSYNRLGDPY GDDRDARSPI MNPSSLSNRS PSPGRPLDGY QLSDAPYGHH HHIEMPSSDR 

        70         80         90        100        110        120 
LAEQPTYSVE RIPQSYGHNE AYEAQHQHYP GYEYSVDPEA HHDAYYTQPY QPTVTPGHDD 

       130        140        150        160        170        180 
YDLGQYPGHQ HSYQDDEPIL QPEDPFQAQN PYSDDYQEDM TIAPTPSPAP LRRWKTVKEV 

       190        200        210        220        230        240 
QLFQGNLVLD CPIAPKLLNQ IPHAENGQRD EFTHMRYSAA TCDPKDFFEE RFTLRQKLFA 

       250        260        270        280        290        300 
KPRHTELFIV VTMYNEDDFL FARTMVGVFK NIEHMCSRTR SKTWGKDAWK KIVVCVISDG 

       310        320        330        340        350        360 
RAKINPRTRA VLAGLGCYQD GIAKQQVNGK DVTAHIYEYT TQVGMELKGN QVHLKPRSGV 

       370        380        390        400        410        420 
PVQMIFCLKE KNQKKINSHR WFFQAFGRVL DPNICVLLDA GTQPGKDSIY RLWKAFDVEP 

       430        440        450        460        470        480 
MCGGACGEIK VMLDHGKKLF NPLVAGQNFE YKLSNILDKP LESAFGFISV LPGAFSAYRY 

       490        500        510        520        530        540 
IALQNDKNGQ GPLERYFLGE KMHGANAGIF TANMYLAEDR ILCFEIVTKR NCRWLLQYVK 

       550        560        570        580        590        600 
SSTGETDVPD QMAEFILQRR RWLNGSFFAA VYAITHFYQL WRSDHSFIRK FMLLIETIYQ 

       610        620        630        640        650        660 
TINMLFAWFG IGNFFLVFHI LTTYLGDADL LGTAGKVLGV VFEWLYLATL VTCFVLSLGN 

       670        680        690        700        710        720 
RPGGSNKLYM TMVYLWVFIM IYLAFAAVFV TVRSIQEEVK DGSFTFSTLF TNSTFFSIIV 

       730        740        750        760        770        780 
SLGSTYVMWF IASIIFMDPW HMFTCFIQYI LLTPTYINVL NIYAFCNTHD ITWGTKGDDK 

       790        800        810        820        830        840 
AEKLPSANLK PGGKVDVNIP QDDGDLNAQY EAELMKFAQK PPKEIKTISE EERQADYYKG 

       850        860        870        880        890        900 
FRSSVVLVWV FCNFALGAVV LSSAGLDRFS DDAEAAETDR NNRAMIYMAV VLWSVAGLSI 

       910 
FKFLGAMWFL VVRMFRGV

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a chitin synthase gene (chsC) of Aspergillus nidulans."
Motoyama T., Kojima N., Horiuchi H., Ohta A., Takagi M.
Biosci. Biotechnol. Biochem. 58:2254-2257(1994) [PubMed: 7765719] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FGSC 89.
[2]Horiuchi H.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"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 A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[5]"Classification of fungal chitin synthases."
Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J., Robbins P.W.
Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992) [PubMed: 1731323] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 258-446.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB023911 Genomic DNA. Translation: BAA75501.1. Sequence problems.
AACD01000078 Genomic DNA. Translation: EAA60909.1. Sequence problems.
BN001303 Genomic DNA. Translation: CBF77244.1.
M82938 Genomic DNA. Translation: AAA33302.1.
PIRA59054.
RefSeqXP_662170.1. XM_657078.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2872365.
KEGGani:AN4566.2.

Phylogenomic databases

OrthoDBEOG4GMZ52.
PhylomeDBP30583.

Family and domain databases

InterProIPR004834. Chitin_synth.
IPR013616. Chitin_synth_N.
[Graphical view]
KOK00698.
PfamPF01644. Chitin_synth_1. 1 hit.
PF08407. Chitin_synth_1N. 1 hit.
[Graphical view]
ProDomPD002998. Chitin_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameCHSC_EMENI
AccessionPrimary (citable) accession number: P30583
Secondary accession number(s): C8V7X5, O94165, Q5B4G4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 16, 2011
Last modified: January 25, 2012
This is version 70 of the entry and version 3 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents