Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P30584 (CHSA_EMENI)

Last modified October 13, 2009. Version 61. 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 A
    EC=2.4.1.16
Alternative name(s):
    Chitin-UDP acetyl-glucosaminyl transferase A
    Class-II chitin synthase A
Gene names
Name: chsA
Synonyms: chs2
ORF Names: AN7032
OrganismEmericella nidulans (Aspergillus nidulans) [Complete proteome]
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length1013 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 II subfamily.

Sequence caution

The sequence EAA61678.1 differs from that shown. Reason: Erroneous gene model prediction.

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

chitin biosynthetic process

Inferred from electronic annotation. Source: InterPro

   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10131013Chitin synthase A
PRO_0000193691

Regions

Transmembrane508 – 52821 Potential
Transmembrane646 – 66621 Potential
Transmembrane686 – 70621 Potential
Transmembrane721 – 74121 Potential
Transmembrane759 – 77921 Potential
Transmembrane892 – 91221 Potential
Transmembrane919 – 93921 Potential

Sequences

Sequence LengthMass (Da)Tools
P30584-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: DD5D2E9523B0778A

FASTA1,013113,679
        10         20         30         40         50         60 
MDCQNGRRAN RTVRFARTAE SRYPERYSYE YDPEETLSRA APSMRNAPTI PPPTASGADE 

        70         80         90        100        110        120 
MRYTASRPAS PARPWSPTRA ADWVRPPSAA ASYYERADIN GSPRPGTPSS RYGGSPRRPL 

       130        140        150        160        170        180 
PPAPLFSKPG TTTQDTKIDI GDGEEDPFGG GGRTISSRHG PQGSVQSFTS ESTFIADETD 

       190        200        210        220        230        240 
LEKVDLDEYE EESNETKSMV DPNLHYGPAP EKQSRRGVRN AQMAKKEVQL VNGELILECK 

       250        260        270        280        290        300 
IPTILHSFLP RRDDREFTHM RYTAVTCDPD DFTQRGYKLR QQIGRTMRET ELFICITMYN 

       310        320        330        340        350        360 
EDETHFTRTM HGVMQNISHF CSRSKSRTWG KDGWKKIVVC IISDGRKKVH PRTLNALAAL 

       370        380        390        400        410        420 
GVYQEGIAKN VVNQKQVNAH VYEYTTQVSL DSDLKFKGAE KGIVPCQVIF CLKEHNQKKL 

       430        440        450        460        470        480 
NSHRWFFNAF GRALQPNICI LLDVGTRPEP TALYHLWKAF DQDSNVAGAA GEIKASKGKN 

       490        500        510        520        530        540 
MLGLLNPLVA SQNFEYKMSN ILDKPLESVF GYITVLPGAL SAYRFFALQN DAEGNGPLNQ 

       550        560        570        580        590        600 
YFKGETLHGK DADVFTANMY LAEDRILCWE LVAKREERWV LRFVKSAVGE TDVPDSIPEF 

       610        620        630        640        650        660 
ISQRRRWLNG AFFAAVYSIV NVKQLWKTDH SLARKILLQI ESVYQLLQLI FTYFGLANFY 

       670        680        690        700        710        720 
LAFFFIAGSL TDEKIDPFGH NMGKYIFIVL RYACVLVMCL QFIFSMGNRP QGAKKLYLSS 

       730        740        750        760        770        780 
MIVYSIVMAY TAFCTLYLIV LELMAKTGHD VPITMSDTLF VNIVVSLLST VGLYFFTSFM 

       790        800        810        820        830        840 
YLDPWHMFTS SAQYFALLPS YICTLQCYAF CNTHDVTWGT KGDNTINTDL GTARIINGSI 

       850        860        870        880        890        900 
VEVEMPSEQL DIDSGYDAAL RNLRDRLEVP DPGVSESQQQ EDYYRAVRTY MVSVWMVANV 

       910        920        930        940        950        960 
VLAMAVSEVY GVGSSGTNVY LAIILWSVAV LAIIRAIGST AYAVLYLIQK LVEGKAKFQA 

       970        980        990       1000       1010 
GNIASANASA AGSSLGTKSN VSYGSKGLNM TDRINETKWA ISRGMQKAMF WKK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of two chitin synthase genes from Aspergillus nidulans."
Yanai K., Kojima N., Takaya N., Horiuchi H., Ohta A., Takagi M.
Biosci. Biotechnol. Biochem. 58:1828-1835(1994) [PubMed: 7765508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FGSC 89.
[2]"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.
[3]"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 303-491.

Cross-references

Sequence databases

D21268 Genomic DNA. Translation: BAA04806.1.
AACD01000117 Genomic DNA. Translation: EAA61678.1. Sequence problems.
M82939 Genomic DNA. Translation: AAA33303.1.
PIRJC2314.
RefSeqXP_664636.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Genome annotation databases

GeneID2870113.
KEGGani:AN7032.2.

Family and domain databases

InterProIPR004834. Chitin_synth.
IPR013616. Chitin_synth_N.
[Graphical view]
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 nameCHSA_EMENI
AccessionPrimary (citable) accession number: P30584
Secondary accession number(s): Q5AXE8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: October 13, 2009
This is version 61 of the entry and version 2 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