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Database: UniProt
Entry: A0A194VJ31_9PEZI
LinkDB: A0A194VJ31_9PEZI
Original site: A0A194VJ31_9PEZI 
ID   A0A194VJ31_9PEZI        Unreviewed;       359 AA.
AC   A0A194VJ31;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Xylosidase/arabinosidase {ECO:0000313|EMBL:KUI64151.1};
GN   ORFNames=VM1G_10927 {ECO:0000313|EMBL:KUI64151.1};
OS   Valsa mali.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI64151.1};
RN   [1] {ECO:0000313|EMBL:KUI64151.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-8 {ECO:0000313|EMBL:KUI64151.1};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) 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; KN796121; KUI64151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194VJ31; -.
DR   OrthoDB; 5470935at2759; -.
DR   Proteomes; UP000078559; 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:UniProtKB-KW.
DR   CDD; cd18619; GH43_CoXyl43_like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}.
FT   SITE            146
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   359 AA;  39974 MW;  CCEF6E8FB6C27E03 CRC64;
     MPPLITHLYT ADPSAHVFNG KIYIYPSHDE DTGAESNDNG DQYDMADYHV FSIDCSPDPN
     IARPATSPAP TVTDHGVVLR LADVPWASKQ LWAPDAAHNP RDGRYYLFFP ARDKDGIFRI
     GVAAGDKPEG PFTPEENYIP GTYSIDPAVL VDDDDDDEEE EEEEKKQAYL YFGGIWGGQL
     QCYQKGNDVF DPSWTGPKEP SGAGVHALGP RVARLSGDMR SLASEVREIE ILDPETGARI
     AADDHERRFF EAAWCHKRRG KYYFSYSTGD THFLCYAVGD GPMGPFTYGG RLLEPVLGWT
     THHSVVEFPV GSDRWWLFYH DCELSGGVSH LRSVKVRELW YDGDRIVGGK PTSSSSQGD
//
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