ID A0A0L6WPG0_9AGAR Unreviewed; 533 AA.
AC A0A0L6WPG0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=J132_05524 {ECO:0000313|EMBL:KNZ77417.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ77417.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) 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; KQ412519; KNZ77417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6WPG0; -.
DR STRING; 1306850.A0A0L6WPG0; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000053712; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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; cd12215; ChiC_BD; 1.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding 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 Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
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:UP000053712};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..533
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005568972"
FT DOMAIN 48..364
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 363..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 56027 MW; 9487ACDBA96890DF CRC64;
MAFLQRFRVF LTKCIILAPA LLQTHAFDNS RSDNCKFLVA LRKYFQFTEI CSYWGQNSYG
ATHTSDTVNW QQGLAHYCQD DTINAFPIAF LNVFFSTGGL PEINLANTCN PTDSGVFSGT
NLANCQFLAA DIQACQTKGK IVTLSLGGAT GAASFSSDAQ AQDFADTIWN LFLGGSSSTR
PFGAAVLDGV DLDIEGGGTT YYASFISRIR SHASGANKQY YVTAAPQCVY PDAYLGTVLN
AAAFDAVYVQ YFQFRLTNNS HATLSYNNFC GLQNYNNANA WDFGLWDNWA KTVAVNKNVK
VYIGAPASST AAGSGYVDAA TLGSIAKATR ATYSSFGGIM LWDASQAYAN GRFDSAVKSA
MGAGTGSNPS TTTQATTTLS TTKSTTTTKS TTATSISPSA TTTVGTGNCA SVAAWASNVA
YVGGQQVTYN GHLWTAQWWT YGDTPGGSAG VWTDNGACNL KLVATSAISA SASAGHHTTA
THSVAFVKAV SSASIISSKA SVGARTTLSQ STTSHSAASA SSLGVHSSRF FRF
//
