ID A0A194UZS5_9PEZI Unreviewed; 780 AA.
AC A0A194UZS5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Xylan 1,3-beta-xylosidase {ECO:0000313|EMBL:KUI57111.1};
GN ORFNames=VP1G_04424 {ECO:0000313|EMBL:KUI57111.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI57111.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN714696; KUI57111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194UZS5; -.
DR STRING; 694573.A0A194UZS5; -.
DR OrthoDB; 1891044at2759; -.
DR Proteomes; UP000078576; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000078576}.
FT DOMAIN 387..485
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
SQ SEQUENCE 780 AA; 87907 MW; 3B7EE26B573CE0A5 CRC64;
MSASPDTPSD PLTFQNPVIR GFNPDPTVCV VPASGDTPAT YFLSTSTFEY FPGCAIYTST
DLLNWRLIGH ALNRRSQIEL RTVEPGAGSW ASTLRYRVAE KRWYLANCLF QRYRPASDER
IFPRGFYVYT DDIWDDNAWS DPVYFDDPGF DQDLFWDDDG KVYLSTTRRI SNRPPNSKLK
DFAIHISEID LPTGRTLTPP AVIRQSPHGL AEGSHILKRD GWYYLFTAEG GTEAGHQEWV
FRSSEGVYGP WEEQGKPLWY NGPDEEVQRT GHADVFEDRQ GRWWAVLLGV RPMRDGKGGW
LEPQLGRETF LVKIDWVDDW PIFNEGKNIS LSTRGRDPRP QVSPALGEGS SVWKADLDRQ
EIELGWYQKR ESRKFTEGHS MLTIMSFADT PIKRSYSVTE RPGYLRLWGN CYDLSSPEAP
AMLLRKQSAY FQTFEVTMEF DPRRVGYEAG IVLWWNQFSY ATIGVASVAL PNGEEAQTVL
ARNATGQVGM IKQLPEFVVV QYIRVMEPRH KFLINIMNTD RLPEFSLKDK VIIVSGAGRG
LGLVQSEALL EAGAKVYTID RLEEPDPGFQ RLQERAQELG TSLSYNRLDV RDNISLNATM
AKIADENGRL DGLLACAGIQ QETSALEYTM EDADKMFGVN ITGTFMTAQA VARQMKRLDK
RGSMVFIGSM SGTVANKGLI CPAYNASKAG VIQLARNLAM EWGPYGIRVN TISPGYIVTA
MTAPLFKQFP DRKENWPKEN MLGRLSYPEE YRGAAVFLLS EASSFMTGAD LRMDGGHAAW
//
