ID   O65331_ELAUM            Unreviewed;       317 AA.
AC   O65331;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   SubName: Full=Basic chitinase {ECO:0000313|EMBL:AAC16011.1};
DE            EC=3.2.1.14 {ECO:0000313|EMBL:AAC16011.1};
OS   Elaeagnus umbellata (Autumn olive) (Elaeagnus crispa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Elaeagnaceae; Elaeagnus.
OX   NCBI_TaxID=43233 {ECO:0000313|EMBL:AAC16011.1};
RN   [1] {ECO:0000313|EMBL:AAC16011.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Root nodule {ECO:0000313|EMBL:AAC16011.1};
RA   Kim H.-B., An C.-S.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAC16011.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Root nodule {ECO:0000313|EMBL:AAC16011.1};
RX   PubMed=11952123; DOI=10.1094/MPMI.2002.15.3.209;
RA   Kim H.B., An C.S.;
RT   "Differential expression patterns of an acidic chitinase and a basic
RT   chitinase in the root nodule of Elaeagnus umbellata.";
RL   Mol. Plant Microbe Interact. 15:209-215(2002).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000256|ARBA:ARBA00009373}.
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DR   EMBL; AF061806; AAC16011.1; -; mRNA.
DR   AlphaFoldDB; O65331; -.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008843; F:endochitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-ARBA.
DR   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd06921; ChtBD1_GH19_hevein; 1.
DR   FunFam; 3.30.60.10:FF:000001; Basic endochitinase; 1.
DR   FunFam; 3.30.20.10:FF:000001; Endochitinase (Chitinase); 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 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   PANTHER; PTHR22595:SF79; CHITINASE 12; 1.
DR   PANTHER; PTHR22595; CHITINASE-RELATED; 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   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 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   Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW   ProRule:PRU00261};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR001060-2};
KW   Glycosidase {ECO:0000313|EMBL:AAC16011.1};
KW   Hydrolase {ECO:0000313|EMBL:AAC16011.1};
KW   Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..317
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004159663"
FT   DOMAIN          23..64
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-1"
FT   DISULFID        26..41
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        35..47
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        40..54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        58..62
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        89..152
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
FT   DISULFID        163..171
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
FT   DISULFID        270..302
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
SQ   SEQUENCE   317 AA;  34692 MW;  642BD761E1073F7D CRC64;
     MKLWVVTIIV SSLLFFTIQR SRAEQCGNQA GGKVCPGGQC CSQYGWCGTT DEYCKKGCQS
     KCGGASGIES VISSNIFNQM LKHRNDGACK AKGFYTYDAF IKAAKAFPNF GTTGNDATRK
     KEIAAFFGQT SHETTGWDGP SAPDGPYAWG YCYVREQNPS AYCSPNPTYP CASGKQYYSR
     GPMQLSWNYN YGQCGRAIGV DLLRNPDLVA TDPVVSFKTA IWFWMTPQSP KPSCHDVITG
     RWKPSGADQS AGRVAGYGTI TNIINGGLEC GKGRNPQVED RIGFYKRYCD ILKVGYGNNL
     DCYNQRPFGS GLLVDTM
//