ID   CHI2_BRANA              Reviewed;         322 AA.
AC   Q09023;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Endochitinase CH25;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94143492; PubMed=8310072; DOI=10.1104/pp.101.4.1403;
RA   Hamel F., Bellemare G.;
RT   "Nucleotide sequence of a Brassica napus endochitinase gene.";
RL   Plant Physiol. 101:1403-1403(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Westar;
RX   PubMed=7548207; DOI=10.1016/0167-4781(95)00099-3;
RA   Hamel F., Bellemare G.;
RT   "Characterization of a class I chitinase gene and of wound-inducible,
RT   root and flower-specific chitinase expression in Brassica napus.";
RL   Biochim. Biophys. Acta 1263:212-220(1995).
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-
CC       glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
CC   -!- TISSUE SPECIFICITY: High expression in roots, moderate in floral
CC       tissues and low in stems and leaves.
CC   -!- INDUCTION: In roots by wounding and ethephon.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily.
CC   -!- SIMILARITY: Contains 1 chitin-binding type-1 domain.
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DR   EMBL; M95835; AAA32986.1; -; Genomic_DNA.
DR   PIR; S59953; S59953.
DR   HSSP; P23951; 1CNS.
DR   SMR; Q09023; 21-311.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   BRENDA; 3.2.1.14; 393.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR001002; Chitin_bd_1.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   Gene3D; G3DSA:3.30.60.10; Chitin_bd_1; 1.
DR   PANTHER; PTHR22595; Glyco_hydro_19_cat; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   ProDom; PD000609; Chitin_binding_1; 1.
DR   ProDom; PD354900; Glyco_hydro_19; 1.
DR   SMART; SM00270; ChtBD1; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
DR   PROSITE; PS00774; CHITINASE_19_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Signal.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    322       Endochitinase CH25.
FT                                /FTId=PRO_0000005290.
FT   DOMAIN       21     62       Chitin-binding type-1.
FT   DISULFID     23     38       By similarity.
FT   DISULFID     32     44       By similarity.
FT   DISULFID     37     51       By similarity.
FT   DISULFID     56     60       By similarity.
FT   DISULFID     92    154       By similarity.
FT   DISULFID    166    174       By similarity.
FT   DISULFID    273    305       By similarity.
SQ   SEQUENCE   322 AA;  34816 MW;  E62EE4B17211DBCD CRC64;
     MKSCLLLFLI FSFLLSFSLA EQCGRQAGGA LCPNGLCCSE FGWCGDTEAY CKQPGCQSQC
     GGTPPGPTGD LSGIISRSQF DDMLKHRNDN ACPARGFYTY DAFINAAKSF PGFGTTGDTA
     TRKKEIAAFF GQTSHETTGG WATAPDGPYS WGYCFKQEQN PSSNYCSPSA EWPCASGKSY
     YGRGPMQLSW NYNYGQCGRA IGSDLLNNPD LVSNDPVIAF KAAIWFWMTP QSPKPSCHAV
     IVGQWQPSDA DRAAGRVPGY GVITNIINGG LECGRGQDAR VADRIGFYQR YCNILGVNPG
     GNLDCYNQRS FASVNFFLDA AI
//