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Database: UniProt
Entry: A0A397JM61_9GLOM
LinkDB: A0A397JM61_9GLOM
Original site: A0A397JM61_9GLOM 
ID   A0A397JM61_9GLOM        Unreviewed;       391 AA.
AC   A0A397JM61;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=GH18 domain-containing protein {ECO:0000259|PROSITE:PS51910};
GN   ORFNames=Glove_14g58 {ECO:0000313|EMBL:RHZ89445.1};
OS   Diversispora epigaea.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX   NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ89445.1, ECO:0000313|Proteomes:UP000266861};
RN   [1] {ECO:0000313|EMBL:RHZ89445.1, ECO:0000313|Proteomes:UP000266861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT104 {ECO:0000313|EMBL:RHZ89445.1,
RC   ECO:0000313|Proteomes:UP000266861};
RA   Sun X., Fei Z., Harrison M.;
RT   "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT   epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL   Submitted (AUG-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RHZ89445.1}.
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DR   EMBL; PQFF01000012; RHZ89445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397JM61; -.
DR   STRING; 1348612.A0A397JM61; -.
DR   Proteomes; UP000266861; 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   CDD; cd06548; GH18_chitinase; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000266861}.
FT   DOMAIN          4..376
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   391 AA;  44822 MW;  D6621B81CB5B80EA CRC64;
     MDKPKIVGYF TAWSIYARSF NVSDIDATKL THINYAFYNL DTNGKVFSGD SWADTDKHFE
     GDSWNEEGNN LYGNLKQLAL LKKKYRHLKI LISIGGWSWS TNFGSVTANP VTRKNLVESL
     VKLVKDYYID GIDIDWEYPK TPQEGENYVK LVRELRIALD NYANEIRERI PFLITAAMPC
     GPDNYNKIPL EEFSKYVNYL NLMAYDFSGS WSEIVGHQSN LYDFLGIPLS VDKAVTDYLN
     SRVPHNKIVI GIPMYGRAFE NTEGIGAKFN GIGPGSFEPG IYDYKALPRD ENTKEIYIDK
     LGASFSYNPT TKELITYDSP QVIKEKIKYI KKKKLNGVMF WELSNDLSTN NTRSLLFNAF
     DAFDSLEHLD DSLNHLDYPL SIYDNVKNQF N
//
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