ID D6N0X8_9HYPO Unreviewed; 394 AA.
AC D6N0X8;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE Flags: Fragment;
OS Trichoderma citrinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1490982 {ECO:0000313|EMBL:ADF57300.1};
RN [1] {ECO:0000313|EMBL:ADF57300.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 593.76 {ECO:0000313|EMBL:ADF57300.1};
RX PubMed=20454524;
RA Ihrmark K., Asmail N., Ubhayasekera W., Melin P., Stenlid J., Karlsson M.;
RT "Comparative molecular evolution of trichoderma chitinases in response to
RT mycoparasitic interactions.";
RL Evol. Bioinform. Online 6:1-26(2010).
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 Evidence={ECO:0000256|ARBA:ARBA00000822};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000256|ARBA:ARBA00025727}.
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; GU186418; ADF57300.1; -; Genomic_DNA.
DR AlphaFoldDB; D6N0X8; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GO; GO:0005576; C:extracellular region; 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:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..394
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003086949"
FT DOMAIN 28..318
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT NON_TER 394
FT /evidence="ECO:0000313|EMBL:ADF57300.1"
SQ SEQUENCE 394 AA; 40465 MW; 9024DA61F5AD8150 CRC64;
MFFSKALAVA GLLATASAAP MEKRAAGGKL VVYWGAEDDT TTLANVCADP SYDIVNLSFL
SRFFAGGGYP ELSLSTLGGP SSAQRSAGAT NLQDGSSLVS AIQACQSSGK LVMISMGGAV
DFSAVSLSSD SQGQQIADTV WNLFLGGTAN PSLRPFGSVK LDGVDLDNET GNPTGYLAMA
QRFKSNFAQD TSKKYYLTAA PQCPFPDASE PLNVCQLADY IWVQFYNNGD CNIGQSGFNN
AVRNWSKSIG NATLFIGALA SGADGDQGFV SASSLLSAYQ GVSNLNLPNI GGIMLWEAQL
AVKDSNFQKT IKAGISSGGG STPPPPPPPP TCSWAGHCAG ASCGSDDDCS DNLTCNSGIC
GTAGSTPPPA TCSWEGHCLG ASCGNDNDCS DPYS
//
