ID K3VX30_FUSPC Unreviewed; 440 AA.
AC K3VX30;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 28-JAN-2026, entry version 46.
DE RecName: Full=glucan endo-1,3-beta-D-glucosidase {ECO:0000256|ARBA:ARBA00012780};
DE EC=3.2.1.39 {ECO:0000256|ARBA:ARBA00012780};
GN ORFNames=FPSE_11652 {ECO:0000313|EMBL:EKJ68185.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ68185.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ68185.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ68185.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC beta-D-glucans.; EC=3.2.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00000382};
CC -!- SIMILARITY: Belongs to the PGA52 family.
CC {ECO:0000256|ARBA:ARBA00006055}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKJ68185.1}.
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DR EMBL; AFNW01000610; EKJ68185.1; -; Genomic_DNA.
DR RefSeq; XP_009263044.1; XM_009264769.1.
DR AlphaFoldDB; K3VX30; -.
DR GeneID; 20370269; -.
DR KEGG; fpu:FPSE_11652; -.
DR eggNOG; ENOG502QSI7; Eukaryota.
DR HOGENOM; CLU_030276_0_0_1; -.
DR OrthoDB; 118256at2759; -.
DR Proteomes; UP000007978; Chromosome 1.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:TreeGrafter.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR018805; YJL171C/Tos1_C.
DR InterPro; IPR018807; YJL171C/Tos1_N.
DR PANTHER; PTHR31737; PROTEIN TOS1; 1.
DR PANTHER; PTHR31737:SF2; PROTEIN TOS1; 1.
DR Pfam; PF10287; YJL171C_Tos1_C; 1.
DR Pfam; PF10290; YJL171C_Tos1_N; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007978};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..440
FT /note="glucan endo-1,3-beta-D-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003870384"
FT DOMAIN 40..99
FT /note="Cell wall protein YJL171C/Tos1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10290"
FT DOMAIN 202..422
FT /note="Cell wall protein YJL171C/Tos1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10287"
FT REGION 103..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..130
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 48034 MW; 232439979EECECAB CRC64;
MKLSNVSLLA YTGLASALTQ QCTGKAVNEG GNWFCGAIEE IIYQGFSSKG SYQAVSKMGG
DGSCQRESVS YDGALGPLSE DLSVHIRGPF KLKEFAVYNL GSSKNKRDTE SAPSPHLHGH
RHLHEQRKKK RAEWVTATID GKVVSWKNNW FGPSATKAPS AVAGAPTNKA NEPVPKLKET
EKKTPKKDDI SKTKPYGGSS RGNWERTSYY NAQQRVADNV MFLGNYGGEG SGVFDNTWGN
SLSYLNAKGT GGSSSPKVLK HIYIPSNKEF SIWSAEKCDE SCGYSRAKDV AYKGFSGSNK
IFLFQFKMPF DGNTGFNGDM PALWALNGRI PRTGQYSECS CWKTGCGEVD IYEVLASGDD
KCKSTFHMNN GAGSSDYFKR PADKYIKAAV VFCERTSSVA IKQLPDSFDF GSSLSDETVQ
SWVKEMTSHK KGSSIFQIAA
//
