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Database: UniProt
Entry: A0A0G4L1X8_9PEZI
LinkDB: A0A0G4L1X8_9PEZI
Original site: A0A0G4L1X8_9PEZI 
ID   A0A0G4L1X8_9PEZI        Unreviewed;       266 AA.
AC   A0A0G4L1X8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=BN1708_011633 {ECO:0000313|EMBL:CRK16002.1}, BN1723_010383
GN   {ECO:0000313|EMBL:CRK14551.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK16002.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|Proteomes:UP000044602, ECO:0000313|Proteomes:UP000045706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK16002.1}, and VL2
RC   {ECO:0000313|EMBL:CRK14551.1};
RA   Fogelqvist Johan;
RL   Submitted (MAY-2015) 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}.
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DR   EMBL; CVQI01005113; CRK14551.1; -; Genomic_DNA.
DR   EMBL; CVQH01007113; CRK16002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4L1X8; -.
DR   STRING; 100787.A0A0G4L1X8; -.
DR   OrthoDB; 3203764at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   Proteomes; UP000045706; Unassembled WGS sequence.
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   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; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF384; CHITINASE; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000044602};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..266
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007404722"
FT   DOMAIN          20..266
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   266 AA;  29335 MW;  8BAB36B1F86F3861 CRC64;
     MKASSTLTVL CAMAGLTSCY QNAVYFPNCA IYGRDYHPQN LPASRLSHVL YAFLDVRPSG
     EVHSIDTYAD LEKHYPGDSW IESGKSAYGC VNQLFLLKKS NRYLKTMLSI GGWTLSANFP
     VVASTHAGRL AFAQSSVALM KDWGFDGIDV DWEYPADEEE AENFTLLLAA VRQELDAYAS
     QYAPGHHFLL TIASPAGPTH YEKLDLKTIS GIIDTFYLMG YDYSGSWNSY AAHQANLYPN
     SINKTTTPFS TEDAVTAYLK EGVPAS
//
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