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
//