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Database: UniProt
Entry: B3VQV5_9HYPO
LinkDB: B3VQV5_9HYPO
Original site: B3VQV5_9HYPO 
ID   B3VQV5_9HYPO            Unreviewed;       424 AA.
AC   B3VQV5;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   Name=chit1 {ECO:0000313|EMBL:ACF10394.1};
OS   Metarhizium rileyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1649241 {ECO:0000313|EMBL:ACF10394.1};
RN   [1] {ECO:0000313|EMBL:ACF10394.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CQ031021 {ECO:0000313|EMBL:ACF10394.1};
RA   Wang J.-F., Wan Y.-J.;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACF10394.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CQ031021 {ECO:0000313|EMBL:ACF10394.1};
RX   PubMed=20560352;
RA   Wang J., Liu G., Zhai Y., Wan Y.;
RT   "Cloning and expression of the chitinase gene Chit1 from entomopathogenic
RT   fungus Nomuraea rileyi CQ.";
RL   Wei Sheng Wu Xue Bao 50:493-499(2010).
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}.
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DR   EMBL; EU795711; ACF10394.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3VQV5; -.
DR   SMR; B3VQV5; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:SF317; CHITINASE 11; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..424
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002798774"
FT   DOMAIN          39..402
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   424 AA;  45966 MW;  9F58CFB304702D42 CRC64;
     MSSLLVRSLA VVATWQAALG LATPMSASNA AIEKRASGYA NSVYFTNWGI YGRNYQPADL
     PASQISHVLY SFMNLRADGT IYSGDTYADT DKHYPNDSWN DVGNNVYGCV KQFFLLKKAN
     RKMKVMLSIG GWTWSTNFPA AASTAAARAT FAKSAVTFMK DWGFDGIDID WEYPADDTQA
     TNMVLLLQAV RAELDAYAAN FAPGYHFLLS IAAPAGPDNY KKLHFTELGT VLDHVNLMAY
     DYAGSWGNYS GHDANVYSDS SNLNATPFNT DDAVNAYVKG GVPASKIVLG MPVYGRSFQQ
     TDGIGKPYSG VGSGSWENGV WDYKALPKPG ATVVYDSVAK GYYSYDASTK ELISFDTPAM
     VKEKVTYLQG KGLGGSMFWE ASADRKGSDS LIGTSISALG GLDDTTNLLD YPDSKYDNIK
     KQMA
//
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