ID   CHID_SOLLC              Reviewed;         246 AA.
AC   Q05537;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Basic endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Fragment;
GN   Name=CHI14;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Moneymaker;
RX   PubMed=8400122; DOI=10.1007/bf00028974;
RA   Danhash N., Wagemakers C.A.M., van Kan J.A.L., de Wit P.J.G.M.;
RT   "Molecular characterization of four chitinase cDNAs obtained from
RT   Cladosporium fulvum-infected tomato.";
RL   Plant Mol. Biol. 22:1017-1029(1993).
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 {ECO:0000305}.
CC   -!- INDUCTION: By fungal infection.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; Z15138; CAA78843.1; -; mRNA.
DR   PIR; S37341; S37341.
DR   RefSeq; NP_001266258.1; NM_001279329.2.
DR   AlphaFoldDB; Q05537; -.
DR   SMR; Q05537; -.
DR   STRING; 4081.Solyc02g061770.2.1; -.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   PaxDb; Q05537; -.
DR   PRIDE; Q05537; -.
DR   GeneID; 544146; -.
DR   KEGG; sly:544146; -.
DR   eggNOG; KOG4742; Eukaryota.
DR   InParanoid; Q05537; -.
DR   OrthoDB; 1132954at2759; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q05537; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
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:0050832; P:defense response to fungus; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   SUPFAM; SSF53955; SSF53955; 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; Disulfide bond; Glycosidase;
KW   Hydrolase; Plant defense; Polysaccharide degradation; Reference proteome;
KW   Secreted.
FT   CHAIN           <1..246
FT                   /note="Basic endochitinase"
FT                   /id="PRO_0000124827"
FT   ACT_SITE        70
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        26..88
FT                   /evidence="ECO:0000250"
FT   DISULFID        100..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        207..239
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   246 AA;  26686 MW;  03FAA833109F6DB8 CRC64;
     LSQNISSLIS KNLFERILVH RNDRACGAKG FYTYEAFITA TKTFAAFGTT GDTNTRNKEI
     AAFLAQTSHE TTGGWATAPD GPYSWGYCYN REQGSPGDYC ASSQQWPCAP GKKYFGRGPI
     QISYNYNYGA AGSAIGVNLL NNPDLVANDA VVSFKTALWF WMTAQQPKPS AHDVITGRWS
     PSVADSAPGR VPGFGVITNI INGGMECNSG SNALMDNRIG FYRRYCQILG VDPGNNLDCA
     NQRPFG