ID   CHI2_YEAST              Reviewed;         511 AA.
AC   Q06350;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=Sporulation-specific chitinase 2;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CTS2; OrderedLocusNames=YDR371W; ORFNames=D9481.7;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-
CC       glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- MISCELLANEOUS: Present with 3050 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily.
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DR   EMBL; U28373; AAB64807.1; -; Genomic_DNA.
DR   PIR; S61166; S61166.
DR   RefSeq; NP_010659.1; -.
DR   HSSP; P54196; 1LL7.
DR   DIP; DIP:5251N; -.
DR   IntAct; Q06350; 2.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PeptideAtlas; Q06350; -.
DR   Ensembl; YDR371W; Saccharomyces cerevisiae.
DR   GeneID; 851977; -.
DR   GenomeReviews; Z71256_GR; YDR371W.
DR   KEGG; sce:YDR371W; -.
DR   NMPDR; fig|4932.3.peg.1428; -.
DR   CYGD; YDR371w; -.
DR   SGD; S000002779; CTS2.
DR   HOGENOM; Q06350; -.
DR   OMA; Q06350; ERIVNCY.
DR   BRENDA; 3.2.1.14; 250.
DR   NextBio; 970115; -.
DR   ArrayExpress; Q06350; -.
DR   GermOnline; YDR371W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0004568; F:chitinase activity; IEA:EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cel...; IEA:UniProtKB-KW.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR001223; Glyco_hydro18cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR013781; Glyco_hydro_sg_catalytic.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   ProDom; PD000471; Chitinase_II; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   PROSITE; PS01095; CHITINASE_18; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Complete proteome;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Secreted; Signal; Sporulation.
FT   SIGNAL        1     34       Potential.
FT   CHAIN        35    511       Sporulation-specific chitinase 2.
FT                                /FTId=PRO_0000011937.
FT   ACT_SITE    223    223       Proton donor (By similarity).
FT   CARBOHYD    147    147       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    228    228       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    456    456       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    472    472       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   511 AA;  59118 MW;  238FF79963BF0D63 CRC64;
     MVGHSAQHRS KSSLVSHLLI LLIFITIIIE MCLYNKIFKN QRSDDIRDNF NNGGHRVPSN
     VQNHGTHIRD EAFISGVYYS NWSPYKPRFH FPHDINLKQV SHIYYAFFKI NSRTGGIENT
     DSWSDLEMNL YKSLAIKNSE LIKESSNNSV QNILPLGCIG ELFYLKNTCS DKKFKVIMSI
     GGWSDSENFK IIIKDDKLLQ NFVDSSVETM FRLGFDGIDL DWEFPGNNES EPRGYLKLVR
     MLRLKLNSLE SQIFGKRTED HFQLSIAAPA FKDKLFYLPI TEIDQYVDYW NMMTYDYYGS
     WSETTGYHSN LFSETELNGN FAMHYMIDRF GVNSRKLVLG MAAYGRSFHI KDNKFEPFNQ
     NTVLINKIFK GVGKPTKEID KADGKEGIWP YKNLPKIGTI EQYDPKYVSA YCFDEKNSIF
     ISYDNTKSVK TKAEYVTHNN LGGGFWWESC GEAYANESRS LINAFNEGLH FNVSSKPSIF
     QDVRVKKYYL NKYGDGGFLS PYLKHLDSRK Q
//