ID A0A0U1M818_TALIS Unreviewed; 419 AA.
AC A0A0U1M818;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN Name=CHT3 {ECO:0000313|EMBL:CRG91784.1};
GN ORFNames=PISL3812_08836 {ECO:0000313|EMBL:CRG91784.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG91784.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG91784.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG91784.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-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; CVMT01000010; CRG91784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1M818; -.
DR STRING; 28573.A0A0U1M818; -.
DR OMA; WTSFIAT; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose 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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS51164; CBM1_2; 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:UP000054383};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..419
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006711638"
FT DOMAIN 31..341
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 378..414
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 419 AA; 43611 MW; A7AA1BCB23D405A0 CRC64;
MLSSLSLSLG FLASQTLSSP VSLPRRSSSG GQTVVYWGQN GGGTEENNDL SAYCTGSQGI
DILVLSFLYQ YGNGVTVPGG SFGQSCTILA TSGESQNCES VASSITTCQE AGIKVLLSLG
GGNGGYTVTS QSEAEAIGQY LWDAYGNSAS STVTRPFGDV IVNGFDFDIE NNSNGNNQYY
KYMISTLRSN FATDTANTYY ISGAPQCPLP EPNMGEIIGN STFDYIWPQF YNNNNYTYPC
ALGINGDAAF NFDDWETFIA GTPSSGAQLF IGVPAAPLAA NGGTAGEVYY ATPSQLATIV
SSVDSYSQFG GIMMWSAGFS DSNVNDDCTY AQEADSILLT GSPCGSAGFT LAPSLTPVAP
TPAFSTSTGT TAPTGTGTPV PEYGQCGGEG YTGSTACQSP YVCVKQSDYW SSCQAAEVL
//
