ID   CHI1_HORVU              Reviewed;         318 AA.
AC   P11955;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 4.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=26 kDa endochitinase 1;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. NK 1558; TISSUE=Leaf;
RA   Ignatius S.M.J., Huang J., Muthukrishnan S.;
RL   Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 141-318.
RC   STRAIN=cv. Himalaya;
RA   Swegle M., Huang J.-K., Lee G., Muthukrishnan S.;
RT   "Identification of an endochitinase cDNA clone from barley aleurone
RT   cells.";
RL   Plant Mol. Biol. 12:403-412(1989).
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   -!- INDUCTION: By ethylene.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; U02287; AAA18586.1; -; Unassigned_DNA.
DR   EMBL; X15349; CAA33407.1; -; mRNA.
DR   PIR; S04131; S04131.
DR   PIR; T04403; T04403.
DR   AlphaFoldDB; P11955; -.
DR   SMR; P11955; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   BRENDA; 3.2.1.14; 2687.
DR   ExpressionAtlas; P11955; baseline and differential.
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; 1.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..318
FT                   /note="26 kDa endochitinase 1"
FT                   /id="PRO_0000005296"
FT   DOMAIN          20..59
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        142
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        22..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        31..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        36..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        53..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        98..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        172..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        279..311
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   318 AA;  33402 MW;  42D62B2FE8041954 CRC64;
     MRAFVLFAVV AMAATMAVAE QCGSQAGGAT CPNCLCCSRF GWCGSTPYCG DGCQSQCSGC
     GGGSTPVTPT PSGGGGVSSI VSRALFDRML LHRNDGACQA KGFYTYDAFV AAASAFRGFG
     TTGGTDTRKR EVAAFLAQTS HETTGGWATA PDGAFAWGYC FKQERGATSN YCTPSAQWPC
     APGKSYYGRG PIQLSHNYNY GPAGRAIGVD LLRNPDLVAT DPTVSFKTAM WFWMTAQAPK
     PSSHAVITGQ WSPSGTDRAA GRVPGFGVIT NIVNGGIECG HGQDSRVADR IGFYKRYCDI
     LGVGYGNNLD CYSQRPFA