ID A0A1Y2BF35_9TREE Unreviewed; 388 AA.
AC A0A1Y2BF35;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycoside hydrolase superfamily {ECO:0000313|EMBL:ORY33431.1};
GN ORFNames=BCR39DRAFT_491763 {ECO:0000313|EMBL:ORY33431.1};
OS Naematelia encephala.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Naemateliaceae; Naematelia.
OX NCBI_TaxID=71784 {ECO:0000313|EMBL:ORY33431.1, ECO:0000313|Proteomes:UP000193986};
RN [1] {ECO:0000313|EMBL:ORY33431.1, ECO:0000313|Proteomes:UP000193986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-887.2 {ECO:0000313|EMBL:ORY33431.1,
RC ECO:0000313|Proteomes:UP000193986};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY33431.1}.
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DR EMBL; MCFC01000006; ORY33431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2BF35; -.
DR STRING; 71784.A0A1Y2BF35; -.
DR InParanoid; A0A1Y2BF35; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000193986; 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:UP000193986}.
FT DOMAIN 1..388
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 251..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 41449 MW; 9DC6DB948BC07BB5 CRC64;
MAGYYPDWSG DYLSPENVDW SKFDVMDFAF ALPTSDGNLE FTQDDSSDLL KRLVSTGHAA
GKRVKLSIGG WTGSAYFSTI CGSKSLRKTF VSNILTAYNS YNLDGIDIDW EYPGTGGASG
NAVSSSDSAH FLTFLKDLRA ALPSGAIITT ATQVWPFADS NGNPMADVSG FAAVIDWILI
MNYDIWGSSS TPGPNAPLSD ACGNSTQPLA NAYAAVSSWT SAGMPANQIT LGVPAYGYLQ
KSSADHLIQR RGLHPASRHS TSPSSNKTDT RRRRSDITLY NTDGGTTDGQ VMFEDLIQQG
VLVSDSSTGS YIGAGGFVRE WDSCSSTPWL KSKHSDQIVT YDDPQSMSLK GQFAAQAGLR
GCNVFSVDGD YINGAWPLTD AVRSGLGL
//
