ID B8MJ29_TALSN Unreviewed; 375 AA.
AC B8MJ29;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 22-FEB-2023, entry version 52.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=TSTA_051270 {ECO:0000313|EMBL:EED15691.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED15691.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962657; EED15691.1; -; Genomic_DNA.
DR RefSeq; XP_002485644.1; XM_002485599.1.
DR AlphaFoldDB; B8MJ29; -.
DR STRING; 441959.B8MJ29; -.
DR GeneID; 8106329; -.
DR VEuPathDB; FungiDB:TSTA_051270; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_031465_1_0_1; -.
DR InParanoid; B8MJ29; -.
DR OMA; WEIDAFP; -.
DR OrthoDB; 1449869at2759; -.
DR PhylomeDB; B8MJ29; -.
DR Proteomes; UP000001745; 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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
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:SF337; CHITINASE; 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:UP000001745};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..375
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002877629"
FT DOMAIN 17..374
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 375 AA; 40060 MW; 60E69FB81009DA83 CRC64;
MKYLALTGFL AAHAAALRNV MYVDQWHISS LPSSDLVSSV THAIMAFAPS ENFNSGSTFT
PFESIDTFRA RFPSTTKIMV AIGGWGDNAG FSTAAVSETS RSTYAKNVAA MLESTGLDGV
DLDWEYPGGN GADYKTVPNS QRAAEVNTLP LLVRAIRDAI GDDKILSIAT PGLKRDMIGY
TAENGPTVFG AVDMVNIMSY DLMNRRDNVT KHHTSIKDSL ETVNNYLDIG MNATKGNLGI
AFYAKYFTTD PSSDCATNPV GCATVELEDA NGQDTGKSGA VTFETSPEVS SSSITSSWSK
AKANGITDED AGGQYYWDSD AQLFWTWDTP DLITQKFADI IAATGLGGVM AWSLGEDSLD
WSELKAINSG VAAAP
//