ID   CHI1_THECC              Reviewed;         321 AA.
AC   Q41596;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 74.
DE   RecName: Full=Endochitinase 1;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHIA1;
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Snyder-Leiby T.E., Furtek D.B.;
RT   "A genomic clone from Theobroma cacao L. with high similarity to plant
RT   class I endochitinase sequences.";
RL   (er) Plant Gene Register PGR95-056.
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: Vacuole (By similarity). Note=Vacuolar and
CC       protoplast (By similarity).
CC   -!- INDUCTION: In response to infection, elicitor, ethylene, wounding.
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; U30324; AAA80656.1; -; Genomic_DNA.
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; 18928.
DR   GO; GO:0005773; C:vacuole; 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   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; Plant defense;
KW   Polysaccharide degradation; Signal; Vacuole.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    321       Endochitinase 1.
FT                                /FTId=PRO_0000005329.
FT   DOMAIN       22     64       Chitin-binding type-1.
FT   REGION       65     98       Hinge.
FT   REGION       99    321       Catalytic.
FT   DISULFID     24     39       By similarity.
FT   DISULFID     33     45       By similarity.
FT   DISULFID     38     52       By similarity.
FT   DISULFID     58     62       By similarity.
FT   DISULFID     93    156       By similarity.
FT   DISULFID    167    175       By similarity.
FT   DISULFID    274    306       By similarity.
SQ   SEQUENCE   321 AA;  34848 MW;  E87DBFBC8D7A2ADB CRC64;
     MSFRALSVFS LFLSYLILGS AEQCGRQAGG ALCPGGLCCS QFGWCGNTDD YCKKENGCQS
     QCSGSGGDTG GLDSLITRER FDQMLLHRND GGCPARGFYT YDAFIAAAKS FPAFATTGDD
     ATRKREVAAF LAQTSHETTG GAGWAAPDGP YTWGYCYNRE LNPADYCQWD PNYPCAPGKQ
     YFGRGPMQLT WNYNYGQCGR AIGVDLLNNP DLLATDPTIS FKSAFWFWMT PQSPKPSCHD
     VIIGAWSPSG SDQAAGRVPG FGLITNIING GLECGQGWNA KVEDRIGFYK RYCDTLGVGY
     GNNLDCYNQR SYNNGPSVDS M
//