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   25-MAY-2022, entry version 122.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bienvenu;
RX   PubMed=1391771; DOI=10.1007/bf00014495;
RA   Rasmussen U., Bojsen K., Collinge D.B.;
RT   "Cloning and characterization of a pathogen-induced chitinase in Brassica
RT   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. oleifera
RT   infected with Phoma lingam.";
RL   Planta 187:328-334(1992).
CC   -!- FUNCTION: Defense against chitin-containing fungal pathogens.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
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. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X61488; CAA43708.1; -; mRNA.
DR   PIR; S25311; S25311.
DR   RefSeq; NP_001302855.1; NM_001315926.1.
DR   AlphaFoldDB; Q06209; -.
DR   SMR; Q06209; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   EnsemblPlants; CDX83475; CDX83475; GSBRNA2T00139054001.
DR   GeneID; 106388328; -.
DR   Gramene; CDX83475; CDX83475; GSBRNA2T00139054001.
DR   KEGG; bna:106388328; -.
DR   OMA; HASHETR; -.
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:UniProtKB-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   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 2.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF57016; SSF57016; 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; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..268
FT                   /note="Basic endochitinase CHB4"
FT                   /id="PRO_0000005291"
FT   DOMAIN          25..59
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   REGION          71..268
FT                   /note="Catalytic"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        29..41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        34..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        52..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        92..137
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        150..159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        236..268
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
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