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Database: UniProt
Entry: G2X292_VERDV
LinkDB: G2X292_VERDV
Original site: G2X292_VERDV 
ID   G2X292_VERDV            Unreviewed;       441 AA.
AC   G2X292;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=VDAG_04416 {ECO:0000313|EMBL:EGY22978.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY22978.1};
RN   [1] {ECO:0000313|EMBL:EGY22978.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY22978.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA   Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL   Submitted (MAR-2008) 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; DS572701; EGY22978.1; -; Genomic_DNA.
DR   RefSeq; XP_009649158.1; XM_009650863.1.
DR   AlphaFoldDB; G2X292; -.
DR   STRING; 498257.G2X292; -.
DR   EnsemblFungi; EGY22978; EGY22978; VDAG_04416.
DR   GeneID; 20705879; -.
DR   KEGG; vda:VDAG_04416; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   HOGENOM; CLU_002833_1_1_1; -.
DR   InParanoid; G2X292; -.
DR   OMA; VKQMYLL; -.
DR   OrthoDB; 3203764at2759; -.
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 6, ISOFORM C; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..441
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003439024"
FT   DOMAIN          82..417
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   441 AA;  48800 MW;  CFB3B19AE77D4EC6 CRC64;
     MLGKDLFTSA LLFAAAASAS PYNKNLDLDG PKSVEIAVQT VTKVVHLQST ARPTSVAPKD
     DDENLPVIDE PVDDLRNITE RAAVAGYRNA VYFTNCVSSD TYADLEKHFP GDSWNEQGTN
     AYGCIKQLYL RKKKFRQLKL LLSIGGWTWS PKFAPVARTE AGRQRFASSA VALMADWGFD
     GLDIDWEYPK NANEALDFVR LLAACRQALD NYAARYAKGY RFQLTIAVPA GPTNYRVLDM
     KKMAPFVDGW HLMAYDYAGS WSGKTGHQSN LYRSKSNPAA TQYDTETAVN YYLSQGINPS
     KVLLGVPLYG RSFARTDGLG KPYSGIGKGS IEAGVYHYKA LPAPGAEERW DAEAVAAWSY
     DKKTRELVTY DNQNSVKRKA DYLVKKRLGG AVFWESAGDR AGDRSLVRTV SKAMGAMDQT
     KNWLSYPASK YANIRKGMPG Q
//
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