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Database: UniProt
Entry: A0A2H3TPS0_FUSOX
LinkDB: A0A2H3TPS0_FUSOX
Original site: A0A2H3TPS0_FUSOX 
ID   A0A2H3TPS0_FUSOX        Unreviewed;       338 AA.
AC   A0A2H3TPS0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Related to endo-arabinase {ECO:0000313|EMBL:SCO83839.1};
GN   ORFNames=FRV6_07966 {ECO:0000313|EMBL:SCO83839.1};
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:SCO83839.1, ECO:0000313|Proteomes:UP000219369};
RN   [1] {ECO:0000313|Proteomes:UP000219369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA   Guldener U.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; FMJY01000004; SCO83839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3TPS0; -.
DR   VEuPathDB; FungiDB:FOC1_g10005539; -.
DR   VEuPathDB; FungiDB:FOC4_g10011122; -.
DR   VEuPathDB; FungiDB:FOIG_02861; -.
DR   VEuPathDB; FungiDB:FOMG_05533; -.
DR   VEuPathDB; FungiDB:FOXG_01604; -.
DR   VEuPathDB; FungiDB:FOZG_05694; -.
DR   VEuPathDB; FungiDB:HZS61_009525; -.
DR   OrthoDB; 1435052at2759; -.
DR   Proteomes; UP000219369; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd08999; GH43_ABN-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR   PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..338
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013783242"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        245
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            181
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   338 AA;  37133 MW;  2FF845A8114842EC CRC64;
     MPVSSSLWGR IIFFILSVFL FDTASALPAN ISSPVLRPFV LPPPKQHLSR RHKGRDKSFS
     PRLDVNFPDP CLVQDQDDHW VSFATSGGGY HIQVAVADDL FGEWTHLQQD ALPGDGWTSG
     RNYWAPDVRK LEDDSYIMYF SGELPEGGHC IGVARSHNST GPYTMDPKPF ACPRDEGGAI
     DPAGFFDEST NKRYVVYKVD GNALNNGSGT PIRLQEVSTK DGSTPIGKPV DILDRIASED
     GPLVEAPSLV RTEQGKYLLF FSSHMYTGDA YDVKWAMSDR VEGPYTRGSS PFLKTPALGL
     KGPGGGTSSE NGQFMVFHAW CGKGKRCMYA IGYGLDYE
//
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