ID   A0A165I0L0_EXIGL        Unreviewed;       328 AA.
AC   A0A165I0L0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KZV92726.1};
GN   ORFNames=EXIGLDRAFT_674807 {ECO:0000313|EMBL:KZV92726.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV92726.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV92726.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV92726.1,
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; KZV92726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165I0L0; -.
DR   InParanoid; A0A165I0L0; -.
DR   OrthoDB; 2783699at2759; -.
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   CDD; cd00598; GH18_chitinase-like; 1.
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.
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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..328
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007858984"
FT   DOMAIN          129..310
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|Pfam:PF00704"
SQ   SEQUENCE   328 AA;  35526 MW;  EF0ED20EE04B960B CRC64;
     MKSTIFFTLA IAALVNAAPF NRNGTTLRRR DLPARSGPVY SVYADVGTTA ETWPSAENLG
     DWNDFLMSFW VSDGSEPRDV AAVWASMDPT LRQTILDQYH AAGKTLRVAV FGQFDLPLQR
     SPPGDPVEIA SAIVDFVKQF NLDGVDVDYE DTDSFSGAKA GTGEDFVIQL TKSLRELLPS
     GQFLISHAPQ SPYFIPNSSI FTEGAYLKIN EEVGDSIDFY NIQFYNQGIG AYETCEEHFT
     AAPSNFPGTT VNDLIDSGIP QEKIILGKPG LVSNPADATV DDAINGFVDP VTLGQCITSQ
     STKPGGVMAF QFRNANAAWI AEAKGDLP
//