ID   CHI4_BRANA              Reviewed;         268 AA.
AC   Q06209;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   16-JUN-2009, entry version 76.
DE   RecName: Full=Basic endochitinase CHB4;
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 [MRNA].
RC   STRAIN=cv. Bienvenu;
RX   MEDLINE=93004480; PubMed=1391771; DOI=10.1007/BF00014495;
RA   Rasmussen U., Bojsen K., Collinge D.B.;
RT   "Cloning and characterization of a pathogen-induced chitinase in
RT   Brassica napus.";
RL   Plant Mol. Biol. 20:277-287(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 101-115 AND 253-267.
RC   STRAIN=cv. Bienvenu; TISSUE=Cotyledon;
RA   Rasmussen U., Giese H., Mikkelsen J.D.;
RT   "Induction and purification of chitinase in Brassica napus L. spp.
RT   oleifera infected with Phoma lingam.";
RL   Planta 187:328-334(1992).
CC   -!- FUNCTION: Defense against chitin containing fungal pathogens.
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-
CC       glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- INDUCTION: By infection with the fungal pathogen Phoma lingam.
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; X61488; CAA43708.1; -; mRNA.
DR   PIR; S25311; S25311.
DR   HSSP; P02877; 1HEV.
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:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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:0006952; P:defense response; 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   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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Plant defense; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    268       Basic endochitinase CHB4.
FT                                /FTId=PRO_0000005291.
FT   DOMAIN       25     59       Chitin-binding type-1.
FT   REGION       71    268       Catalytic.
FT   COMPBIAS     60     70       Gly/Pro-rich (hinge region).
FT   CARBOHYD    265    265       N-linked (GlcNAc...) (Potential).
FT   DISULFID     27     35       By similarity.
FT   DISULFID     29     41       By similarity.
FT   DISULFID     34     48       By similarity.
FT   DISULFID     52     57       By similarity.
FT   DISULFID     92    137       By similarity.
FT   DISULFID    150    159       By similarity.
FT   DISULFID    236    268       By similarity.
SQ   SEQUENCE   268 AA;  28733 MW;  066BAC7BC699A0D6 CRC64;
     MALTKLSLVL FLCFLGLYSE TVKSQNCGCA PNLCCSQFGY CGSTDAYCGT GCRSGPCRSP
     GGTPSPPGGG SVGSIVTQAF FNGIINQAGG GCAGKNFYTR DSFINAANTF PNFANSVTRR
     EIATMFAHFT HETGHFCYIE EINGASRDYC DENNRQYPCA PGKGYFGRGP IQLSWNYNYG
     ACGQSLNLNL LGQPELVSSN PTVAFRTGLW FWMNSVRPVL NQGFGATIRA INGMECNGGN
     SGAVNARIRY YRDYCGQLGV DPGPNLSC
//