ID A0A165I009_EXIGL Unreviewed; 340 AA.
AC A0A165I009;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE SubName: Full=Glycoside hydrolase family 18 protein {ECO:0000313|EMBL:KZV92702.1};
GN ORFNames=EXIGLDRAFT_674772 {ECO:0000313|EMBL:KZV92702.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV92702.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV92702.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV92702.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV426003; KZV92702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165I009; -.
DR STRING; 1314781.A0A165I009; -.
DR InParanoid; A0A165I009; -.
DR OrthoDB; 1537817at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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 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:UP000077266}.
FT DOMAIN 5..286
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 340 AA; 36983 MW; E646FF399C8B89FB CRC64;
MSDGHRVAVY YQTQYDWGHN ATYVSPLPLI GLITHLYLAA YHINFKSVGD SITLNDNKPY
APYYDQMWSD ISQLKAAGIK IVGMLGGAAA GTYSSLTPQY WDTYYPDLYQ TIKDYDLDGM
DLDVEQSTDI GVAIRLITQL KADFGPDFIV TLAPVASALR GGGNLSGFNY VQLESQVGAN
ISWYNAQFYS GFGTIFPDSQ YVSITEYQGG IFPPEKLVAS VLTNSNLGSG YVSVDNVVKS
LKDLVTLYGD QFGGVAGWEY FASNPSPHPG EPWQWSQIMK DAIAGLSRKF SSASASVAAA
ARKSIMDRAA ANKAAALAAG VTFPDINSQE FAEAHRRKES
//
