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Reviewed, UniProtKB/Swiss-Prot Q06350 (CHI2_YEAST)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Sporulation-specific chitinase 2
    EC=3.2.1.14
Gene names
Name: CTS2
Ordered Locus Names: YDR371W
ORF Names: D9481.7
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

Subcellular location

Secreted Potential.

Miscellaneous

Present with 3050 molecules/cell in log phase SD medium. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Chain35 – 511477Sporulation-specific chitinase 2
PRO_0000011937

Sites

Active site2231Proton donor By similarity

Amino acid modifications

Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Glycosylation4721N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q06350-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 238FF79963BF0D63

FASTA51159,118
        10         20         30         40         50         60 
MVGHSAQHRS KSSLVSHLLI LLIFITIIIE MCLYNKIFKN QRSDDIRDNF NNGGHRVPSN 

        70         80         90        100        110        120 
VQNHGTHIRD EAFISGVYYS NWSPYKPRFH FPHDINLKQV SHIYYAFFKI NSRTGGIENT 

       130        140        150        160        170        180 
DSWSDLEMNL YKSLAIKNSE LIKESSNNSV QNILPLGCIG ELFYLKNTCS DKKFKVIMSI 

       190        200        210        220        230        240 
GGWSDSENFK IIIKDDKLLQ NFVDSSVETM FRLGFDGIDL DWEFPGNNES EPRGYLKLVR 

       250        260        270        280        290        300 
MLRLKLNSLE SQIFGKRTED HFQLSIAAPA FKDKLFYLPI TEIDQYVDYW NMMTYDYYGS 

       310        320        330        340        350        360 
WSETTGYHSN LFSETELNGN FAMHYMIDRF GVNSRKLVLG MAAYGRSFHI KDNKFEPFNQ 

       370        380        390        400        410        420 
NTVLINKIFK GVGKPTKEID KADGKEGIWP YKNLPKIGTI EQYDPKYVSA YCFDEKNSIF 

       430        440        450        460        470        480 
ISYDNTKSVK TKAEYVTHNN LGGGFWWESC GEAYANESRS LINAFNEGLH FNVSSKPSIF 

       490        500        510 
QDVRVKKYYL NKYGDGGFLS PYLKHLDSRK Q 

« Hide

References

[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

U28373 Genomic DNA. Translation: AAB64807.1.
PIRS61166.
RefSeqNP_010659.1.

3D structure databases

HSSPHSSP built from PDB template 1LL7 based on UniProtKB P54196.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5251N.
IntActQ06350. 2 interactions.

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Proteomic databases

PeptideAtlasQ06350.

Genome annotation databases

EnsemblYDR371W. Saccharomyces cerevisiae. [Contig view]
GeneID851977.
GenomeReviewsGene locus YDR371W in contig Z71256_GR.
KEGGsce:YDR371W.
NMPDRfig|4932.3.peg.1428.

Organism-specific databases

CYGDYDR371w.
SGDS000002779. CTS2.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMQ06350.
OMAQ06350. ERIVNCY.

Enzyme and pathway databases

BRENDA3.2.1.14. 250.

Gene expression databases

ArrayExpressQ06350.
GermOnlineYDR371W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
ProDomPD000471. Chitinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00636. Glyco_18. 1 hit.
[Graphical view]
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio970115.

Entry information

Entry nameCHI2_YEAST
AccessionPrimary (citable) accession number: Q06350
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

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