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Database: UniProt
Entry: A0A0C2XJ75_HEBCY
LinkDB: A0A0C2XJ75_HEBCY
Original site: A0A0C2XJ75_HEBCY 
ID   A0A0C2XJ75_HEBCY        Unreviewed;       542 AA.
AC   A0A0C2XJ75;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Glycoside hydrolase family 18 protein {ECO:0000313|EMBL:KIM37878.1};
GN   ORFNames=M413DRAFT_13075 {ECO:0000313|EMBL:KIM37878.1};
OS   Hebeloma cylindrosporum h7.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX   NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM37878.1, ECO:0000313|Proteomes:UP000053424};
RN   [1] {ECO:0000313|EMBL:KIM37878.1, ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RA   Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) 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; KN831794; KIM37878.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2XJ75; -.
DR   STRING; 686832.A0A0C2XJ75; -.
DR   HOGENOM; CLU_002833_6_2_1; -.
DR   OrthoDB; 3203764at2759; -.
DR   Proteomes; UP000053424; 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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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; 2.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 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   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF406; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
DR   PROSITE; PS50195; PX; 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:UP000053424}.
FT   DOMAIN          1..113
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          131..542
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          408..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  58186 MW;  C75FA285A0BA4A13 CRC64;
     MSALVTSASH TTSSVPRPHI VYTTHVNVDG KEITVHRRYS EFAALQEALK DPYNLPPKRL
     LVTTFIPSAW ADDTLIAERK AGLAEYLFDV LSTPKYKDRA VVQEFLSGRT AETEQKFDLE
     DSLPSTVTRN KALALASDPL DGKISAQAAM IYGAYYTSWT FVTPSSDNTI NWGGSSNQDL
     LRRLVAGARS SGYGTRVVLS IGGWGGCYYF SQACSTAANR TKFANAIATA VNTYNLDGVD
     FDWEFPNYAG PGQPYSAADS ANLLSLFKLM RISLGPCKII SAAVSHVPWL GSNGQPLKDV
     SAYAAELDYV NIMQVLTPLM LGNLCGTSKQ PQASAQGALA AWTAAKFPAS QLLLGLALYG
     YVSKSSKTVL TGSSMPSQEM VLLHKIEEKD DNGKASIVAF LNGAHANDTI DGEPPKPEPV
     HEAARTAGGP LDEPVKALAT LTGYWGKQIA FKDIVASGAL VKKSDGNYGQ AGGFTMGWDN
     CSNTPYLFNT AQTTVVTYDD TWSLTDKAKF AKSSGMAGCF TWSLDQDDGM TLQNAIRKGL
     GK
//
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