ID Q9UV47_HYPAT Unreviewed; 415 AA.
AC Q9UV47;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE Flags: Fragment;
OS Hypocrea atroviridis (Trichoderma atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=63577 {ECO:0000313|EMBL:AAF19614.1};
RN [1] {ECO:0000313|EMBL:AAF19614.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM 165779 {ECO:0000313|EMBL:AAF19614.1};
RX PubMed=10830894;
RA Lieckfeldt E., Cavignac Y., Fekete C., Borner T.;
RT "Endochitinase gene-based phylogenetic analysis of Trichoderma.";
RL Microbiol. Res. 155:7-15(2000).
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 V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
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DR EMBL; AF188920; AAF19614.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UV47; -.
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:InterPro.
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; cd06548; GH18_chitinase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 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 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 Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..415
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004334334"
FT DOMAIN 39..402
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT NON_TER 415
FT /evidence="ECO:0000313|EMBL:AAF19614.1"
SQ SEQUENCE 415 AA; 45265 MW; 0A0AEC83879ABDC1 CRC64;
MLGFLGKSVA LLAALQATLI SASPVTANDV SVEKRASGYA NAVYFTNWGI YGRNFQPQNL
VASDITHVIY SFMNFQADGT VVSGDAYADY QKHYDDDSWN DVGNNAYGCV KQLFKLKKAN
RNLKVMLSIG GWTWSTNFPS AASTDANRKN FAKTAITFMK DWGFDGIDVD WEYPADDTQA
TNMVLLLKEI RSQLDAYAAQ YAPGYHFLLS IAAPAGPEHY SFLHMSDLGQ VLDYVNLMAY
DYAGSWSSYS GHDANLFANP SNPNSSPYNT DQAIKDYIKG GVPASKIVLG MPIYGRAFES
TGGIGQTYSG IGSGSWENGI WDYKVLPKAG ATVQYDSVAQ AYYSYDPSSK ELISFDTPDM
INTKVSYLKN LGLGGSMFWE ASADKTGSDS LIGTSHRALG SLDSTQNLLS YPNSQ
//
