ID F6MIV5_BEABA Unreviewed; 348 AA.
AC F6MIV5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN Name=chit-1 {ECO:0000313|EMBL:AEG21075.1};
GN ORFNames=BB8028_0006g05320 {ECO:0000313|EMBL:PQK16211.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:AEG21075.1};
RN [1] {ECO:0000313|EMBL:AEG21075.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B-10 {ECO:0000313|EMBL:AEG21075.1};
RA Prakash A., Senthilraja G., Raguchander T., Samiyappan R.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PQK16211.1, ECO:0000313|Proteomes:UP000237441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 8028 {ECO:0000313|EMBL:PQK16211.1,
RC ECO:0000313|Proteomes:UP000237441};
RA Valero Jimenez C.A., Zwaan B.J., Van Kan J.A., Takken W., Debets A.J.,
RA Schoustra S.E., Koenraadt C.J.;
RT "Comparative genomics of the entomopathogenic fungus Beauveria bassiana.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JF834544; AEG21075.1; -; Genomic_DNA.
DR EMBL; JRHA01000006; PQK16211.1; -; Genomic_DNA.
DR AlphaFoldDB; F6MIV5; -.
DR SMR; F6MIV5; -.
DR EnsemblFungi; BB8028_0006g05320.1; BB8028_0006g05320.1; BB8028_0006g05320.
DR OrthoDB; 54784at2759; -.
DR Proteomes; UP000237441; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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; cd02871; GH18_chitinase_D-like; 1.
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; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 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 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..348
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033696935"
FT DOMAIN 41..348
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 348 AA; 36795 MW; DC054168BEEF4A31 CRC64;
MAPFLQTSLA LLPLLASTMV SASPLAPRAD TCATKGRPAG KVLQGYWENW DGAKNGVHPP
FGWTPIQNPD IRKHGYNVIN AAFPIIQPDG TALWEDGMDT GVKVASPADM CEAKAAGATI
LMSIGGATAA IDLSSSAVAD KFVSTIVPIL KKYNFDGIDI DIESGLTGSG NINTLSTSQT
NLIRIIDGVL AQMPANFGLT MAPETAYVTG GTITYGSIWG SYLPIIKKYL DNGRLWWLNM
QYYNGEMYGC SGDSHKAGTV EGFIAQTDCL NKGLSIQGVT ITIPYDKQVP GLPAQPGAGG
GHMSPSNVAQ VLSHYKGALK GLMTWSLNWD GSKNWTFGDN VKGTLGTA
//
