ID G9FLF9_9HYPO Unreviewed; 228 AA.
AC G9FLF9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE Flags: Fragment;
GN Name=chi18-5 {ECO:0000313|EMBL:AEV54225.1};
OS Trichoderma ghanense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=65468 {ECO:0000313|EMBL:AEV54225.1};
RN [1] {ECO:0000313|EMBL:AEV54225.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 28019 {ECO:0000313|EMBL:AEV54225.1}, and GJS 95-137
RC {ECO:0000313|EMBL:AEV54230.1};
RA Ismaiel A.A., Samuels G.J.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV54225.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 28019 {ECO:0000313|EMBL:AEV54225.1}, and GJS 95-137
RC {ECO:0000313|EMBL:AEV54230.1};
RX PubMed=22405896; DOI=10.1016/j.fgb.2012.02.004;
RA Druzhinina I.S., Komon-Zelazowska M., Ismaiel A., Jaklitsch W., Mullaw T.,
RA Samuels G.J., Kubicek C.P.;
RT "Molecular phylogeny and species delimitation in the section
RT Longibrachiatum of Trichoderma.";
RL Fungal Genet. Biol. 49:358-368(2012).
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; JN175496; AEV54225.1; -; Genomic_DNA.
DR EMBL; JN175501; AEV54230.1; -; Genomic_DNA.
DR AlphaFoldDB; G9FLF9; -.
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 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}.
FT DOMAIN 1..228
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEV54225.1"
FT NON_TER 228
FT /evidence="ECO:0000313|EMBL:AEV54225.1"
SQ SEQUENCE 228 AA; 24704 MW; 3B73266F7B1B9527 CRC64;
FMKDWGFDGI DIDWEYPADS TQASNMILLL KEVRSQLDAY AAQYAPGYHF LLSIAAPAGE
VNYSVLRLAD LGQVLDYVNL MAYDYAGSWS NASGHDANLY PNPQNPNATP FNTDVAVKAY
IKGGVPANKI VLGMPIYGRS FEATSGIGQP FSGIGSGSWE NGVWDYKALP KAGATVQYDD
VAKASYSYDP SSKELISFDT PDVINTKVSY LKSLGLGGSM FWEASADK
//