ID B8M5N7_TALSN Unreviewed; 397 AA.
AC B8M5N7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 03-MAY-2023, entry version 61.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=TSTA_031900 {ECO:0000313|EMBL:EED19931.1};
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:EED19931.1, 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. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
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DR EMBL; EQ962654; EED19931.1; -; Genomic_DNA.
DR RefSeq; XP_002480365.1; XM_002480320.1.
DR AlphaFoldDB; B8M5N7; -.
DR STRING; 441959.B8M5N7; -.
DR GeneID; 8099803; -.
DR VEuPathDB; FungiDB:TSTA_031900; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_1_0_1; -.
DR InParanoid; B8M5N7; -.
DR OMA; SYPESKY; -.
DR OrthoDB; 3203764at2759; -.
DR PhylomeDB; B8M5N7; -.
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 CDD; cd06548; GH18_chitinase; 1.
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:SF365; ENDOCHITINASE B; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion 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 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}.
FT DOMAIN 4..362
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 397 AA; 43535 MW; 4CA3CB2871F35AA5 CRC64;
MSGLRSVVYF VNWAIYGRNH NPQDLPADKL THVLYSFANV RPESGEVYLT DSWADTEKHY
PTDSWNDQGT NAYGCIKQLY LLKKQNRRLK VLISIGGWTY SANFAQPAST ETGRETFAKT
ATQLVLDLGL DGIDIDWEYP QDDTQAQNFV ALLQKCRETL DQAAGPNRKF LLTIACPAGA
SNYQKLRLRE MTPYLDFYNL MGYDYAGSWD QVAGHQANLF PSNQYASATP FSTVGALDYY
IKAAGVPPSK MVLGMPLYGR AFQNTQGPGT SYNGVGEGSW EQGVWDYKAL PRPGGTDYVD
PEVGASWCYD GSTMVSYDNV QVAEIKANFI RNNGLGGGMW WESSGDKGGS AASKADGSLI
GTFVETVGGV GALDQSPNNL DFPESKFDNI RTGMQGA
//
