CHI2_GOSHI
ID CHI2_GOSHI Reviewed; 302 AA.
AC Q39785;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Endochitinase 2;
DE EC=3.2.1.14;
DE Flags: Precursor; Fragment;
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Stoneville 887; TISSUE=Leaf;
RA Levorson J.P., Chlan C.A.;
RT "Cloning of an ethylene-responsive chitinase from cotton.";
RL (er) Plant Gene Register PGR97-034(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 112-205.
RC STRAIN=cv. Stoneville 887; TISSUE=Leaf;
RA Levorson J.P., Chlan C.A.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; U78888; AAB68047.1; -; mRNA.
DR EMBL; U57408; AAB01339.1; -; Genomic_DNA.
DR PIR; T10810; T10810.
DR AlphaFoldDB; Q39785; -.
DR SMR; Q39785; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR Proteomes; UP000189702; Genome assembly.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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 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; Reference proteome.
FT CHAIN 1..295
FT /note="Endochitinase 2"
FT /id="PRO_0000005294"
FT PROPEP 296..302
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005295"
FT DOMAIN <1..42
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT ACT_SITE 117
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 3..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 12..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 17..31
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 36..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 73..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 148..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 255..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT NON_TER 1
SQ SEQUENCE 302 AA; 32262 MW; F6BD0C9AB6BC1870 CRC64;
EQCGRQAGGA LCPGGLCCSQ FGWCGSTADY CTVPGCQSQC SGSGPAPGPG GLTNLISRET
FNQMLLHRND GACPARGFYT YDAFIAAARS FPAFATTGDQ ATRKREIAAF LAQTSHETTG
GAGWAAPDGP YAWGYCYNRE LNPPSSYCAS DPNYPCAPGK QYFGRGPMQL SWNYNYGQCG
RAIGVDLLNN PDLLSSDPTI SFKSAFWFWM TPQSPKPSCH NVIIGAWSPS SSDRAAGRAT
GYGVITNIIN GGLECGKGWN AQVEDRIGFY KRYCDILGVS YGNNLDCYNQ SPFGNGVSVD
SM