ID Q8TGC1_FUSOX Unreviewed; 335 AA.
AC Q8TGC1;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Tomatinase {ECO:0000313|EMBL:BAB88660.1};
GN Name=Fotomlr2 {ECO:0000313|EMBL:BAB88660.1};
GN Synonyms=FoTomlck {ECO:0000313|EMBL:BAC02742.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:BAB88660.1};
RN [1] {ECO:0000313|EMBL:BAC02742.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CK3-1 {ECO:0000313|EMBL:BAC02742.1};
RA Ito S., Takahara H., Kawaguchi T., Tanaka S., Kameya-Iwaki M.;
RT "Post-transcriptional Silencing of the Tomatinase Gene in Fusarium
RT oxysporum f. sp lycopersici.";
RL J. Phytopathol. 150:474-480(2002).
RN [2] {ECO:0000313|EMBL:BAB88660.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF103038 race2 {ECO:0000313|EMBL:BAB88660.1};
RA Ito S., Kawaguchi T., Nagata A., Tamura H., Matsushita H., Takahara H.,
RA Tanaka S., Ikeda T.;
RT "Distribution of the FoToml gene encoding tomatinase in formae speciales of
RT Fusarium oxysporum and identification of a novel tomatinase from F.
RT oxysporum f. sp. radicis-lycopersici, the causal agent of Fusarium crown
RT and root rot of tomato.";
RL J. Gen. Plant Pathol. 70:195-201(2004).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|ARBA:ARBA00007495}.
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DR EMBL; AB083007; BAB88660.1; -; Genomic_DNA.
DR EMBL; AB087678; BAC02742.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TGC1; -.
DR SMR; Q8TGC1; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR VEuPathDB; FungiDB:FOC1_g10006435; -.
DR VEuPathDB; FungiDB:FOC4_g10005947; -.
DR VEuPathDB; FungiDB:FOIG_10607; -.
DR VEuPathDB; FungiDB:FOMG_14945; -.
DR VEuPathDB; FungiDB:FOXG_17428; -.
DR VEuPathDB; FungiDB:FOZG_18223; -.
DR VEuPathDB; FungiDB:HZS61_004674; -.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..335
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007714599"
FT DOMAIN 42..327
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 335 AA; 37120 MW; 2D40CF326242780A CRC64;
MKATIIIGAL VAVAQAVKIP CTGTTSLREE AAKKNLLFGS GAINPSYLDD AQFRAVLSEQ
FNSLSPENEL KWNFFHQSPD HYDWHKLDRL VKFAEANNMA VKGHGLISGC CNPDYVLNIT
GPAALRAAIT THFEAVMHRY RGKMDRWDVV SEALKTNGSG LASNIFYDTL GPGYVEEAFR
IARAADPDAK LFLNENLVEV LPKKRQELYE MVAQLVAKGV PIDGIALRMH IALQPLVPGV
IREMVNSYKA LGLEVTIAEM DVHTYNATQQ TEIYGDIIKE ALNSGITDIS FWGFTDKHAY
TWLPGAKPLM FNETYYPKGA FYATHSALAN FVRAS
//
