ID B6QDA3_TALMQ Unreviewed; 720 AA.
AC B6QDA3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=PMAA_077840 {ECO:0000313|EMBL:EEA23753.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA23753.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
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 -!- FUNCTION: Might have a role in sequestration of chitin oligosaccharides
CC (breakdown products of fungal cell walls that are released during
CC invasion and act as triggers of host immunity) to dampen host defense.
CC {ECO:0000256|ARBA:ARBA00037375}.
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; DS995901; EEA23753.1; -; Genomic_DNA.
DR RefSeq; XP_002147264.1; XM_002147228.1.
DR AlphaFoldDB; B6QDA3; -.
DR STRING; 441960.B6QDA3; -.
DR VEuPathDB; FungiDB:PMAA_077840; -.
DR HOGENOM; CLU_019903_0_0_1; -.
DR OrthoDB; 2244480at2759; -.
DR PhylomeDB; B6QDA3; -.
DR Proteomes; UP000001294; 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 CDD; cd00118; LysM; 3.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
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 InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR34997; AM15; 1.
DR PANTHER; PTHR34997:SF1; LYSM DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF01476; LysM; 3.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF54106; LysM domain; 3.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 3.
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:UP000001294};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..720
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002848107"
FT DOMAIN 34..402
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 468..514
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 553..599
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 656..702
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 622..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 77703 MW; 06CA00A907F97FA9 CRC64;
MYLLVVFAWI VVCATASKST VRHLIPRNDS KPAPRTVGYF GNWDIYGSTP YYIPNIPARN
LTHLIYSFAN VNSTTGEVYL SDTWADLQYP YPGDDRSAIG NNVYGNIKQL YLWKKQQRNL
KTMLSIGGGT YSSNIVPVLA NDTLRQKFAD SAVALLANLG FDGLDIDYES VSDSVQAEQF
VDLLNKTRTA LDTFAANISA SPFSLSFASP GGSSFYGLLD FSAMDKYLDF WNFMGYAYTG
SWNTYSGHQA SLYNSTTNPL STPVDTHTGI LYYISEGVTR NKINLGCPLY GASFNNTSGP
GTAFDGIGTL GTNGAAGLWN YNSLPVPGFN ATTYNLPDIG ASYSYDPVKK YMISYDSPKI
AAVKAQYVLD MGLGGTMWWE VSQDRTDDSS LIGTTVDTYG GQSTLDQTLN HLNYSTSVYD
NLRAGFPAES VANITAPSTS TTATATPSWT SSVTSSLMEP STVPGCTKYH LVVSGDTCQK
IESEYGITNA EFMQWNPYSG STCANLWLGY YVCVQGPTTS ISSSTPVTTS ATILTTAAPP
SPTEPRTISS CASYHLVVSG DTCYSIENKY GITPHDFSQW NPYIGSDCMN LWLGFYICVQ
GPTSSTSSSA FVTSSAIAAS SSTPRTIPTK TTPTPTTSST APPSPTEPRT ISTCTDYHLV
VSGDTCYSIE QKYGITANQF NEWNPYVGSE CGSLWLAFYV CIGAPSTDSG SSSSRKGYLG
//