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Database: UniProt
Entry: A0A0L6X157_9AGAR
LinkDB: A0A0L6X157_9AGAR
Original site: A0A0L6X157_9AGAR 
ID   A0A0L6X157_9AGAR        Unreviewed;       394 AA.
AC   A0A0L6X157;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Chitinase A1 {ECO:0000313|EMBL:KNZ81552.1};
GN   ORFNames=J132_00518 {ECO:0000313|EMBL:KNZ81552.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ81552.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   EMBL; KQ412189; KNZ81552.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6X157; -.
DR   STRING; 1306850.A0A0L6X157; -.
DR   OrthoDB; 3203764at2759; -.
DR   Proteomes; UP000053712; Unassembled WGS sequence.
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:SF406; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_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   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   Reference proteome {ECO:0000313|Proteomes:UP000053712}.
FT   DOMAIN          1..377
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   394 AA;  43266 MW;  5D2C747096774603 CRC64;
     MAYYPDWVDI RPEDVPFHLF DWIDFAFALP TNSMGLTWDN PDSAPEKLHQ LVSRAHSCGT
     KVKLSVGGWT GSKYFSSAVR TQKARDLFAN SIYDVYNEFN LDGIDLDWEY PGRGGADGNE
     IDPDDSSNFL LFLQKLRSVL PADTCITAAV QTVPFMDAQG EPMKDLKPFA ALLNWTMLMN
     YDVWTSSPFP GPNAPMYDGC QNSTQPESNA VAGVQKWTSA GFSSAQLVLG VPSYGYLSSS
     SAQGLRQRRR ARPNRLRNGA PADVKLVGED GQIMFRELVK QGALVRIPPT DNTSYSTFAT
     FVGAGGFTRS WDGCSGTPYL HSDSAQQTIS YDDNESLRMK AEFAKGTGMG GVNMFNADGD
     TEQRDLIEAI RQGLSATGII ENIQKDSMTT VVRA
//
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