ID B8MHA5_TALSN Unreviewed; 392 AA.
AC B8MHA5;
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_021410 {ECO:0000313|EMBL:EED17084.1};
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:EED17084.1, 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; EQ962656; EED17084.1; -; Genomic_DNA.
DR RefSeq; XP_002484318.1; XM_002484273.1.
DR AlphaFoldDB; B8MHA5; -.
DR STRING; 441959.B8MHA5; -.
DR GeneID; 8109398; -.
DR VEuPathDB; FungiDB:TSTA_021410; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_1_2_1; -.
DR InParanoid; B8MHA5; -.
DR OMA; NPMTYDF; -.
DR OrthoDB; 3203764at2759; -.
DR PhylomeDB; B8MHA5; -.
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; 3.10.50.10; -; 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:SF228; CHITINASE; 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 48..392
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 392 AA; 42971 MW; E6DA923BE6790922 CRC64;
MYSFMTPSIS APNNAWTVPA LNDPSSTTPS SALASSSSSS AAFDIPIYAN AAYYPNWRIY
KKQPPSSLRL GFVSHVFYAF AWVKEDGQVY LSDEWADSQM PVDGTEGCLR AFTQLKQQYP
QLKVILSIGG SGKGSENFAK VAKSQTAVAN FAYSARALVD QFGLDGIDVD WEHPSDLQQG
ESFVYLLSQL RIALPSPRYI VTCALPAGEW ALKYINLTVA QKYVDLFMIM CYDFSGPWLD
RTGHQSQLYT PPNPCNEAAA ISCHSAVTYI LSQRVQSNKI LTGIPVYGRS FVGADNVNQP
YTGTDGDDGV FDYSDLPRPG AKEVYDESAG AAYCVGGTDG GFVSYDTPQT VEQKAKFVTR
SRLGGLFYWH ITADKRGANS LLETGYNTLH DF
//
