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Database: UniProt
Entry: B8MJ29_TALSN
LinkDB: B8MJ29_TALSN
Original site: B8MJ29_TALSN 
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
//
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