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Database: UniProt
Entry: K3W690_GLOUD
LinkDB: K3W690_GLOUD
Original site: K3W690_GLOUD 
ID   K3W690_GLOUD            Unreviewed;       489 AA.
AC   K3W690;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   10-JUN-2026, entry version 51.
DE   RecName: Full=glucan endo-1,3-beta-D-glucosidase {ECO:0000256|ARBA:ARBA00012780};
DE            EC=3.2.1.39 {ECO:0000256|ARBA:ARBA00012780};
OS   Globisporangium ultimum (strain ATCC 200006 / CBS 805.95 / DAOM BR144)
OS   (Pythium ultimum).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporomycetes; Pythiales;
OC   Pythiaceae; Globisporangium.
OX   NCBI_TaxID=431595 {ECO:0000313|EnsemblProtists:PYU1_T000481, ECO:0000313|Proteomes:UP000019132};
RN   [1] {ECO:0000313|Proteomes:UP000019132}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RX   PubMed=20626842; DOI=10.1186/gb-2010-11-7-r73;
RA   Levesque C.A., Brouwer H., Cano L., Hamilton J.P., Holt C., Huitema E.,
RA   Raffaele S., Robideau G.P., Thines M., Win J., Zerillo M.M., Beakes G.W.,
RA   Boore J.L., Busam D., Dumas B., Ferriera S., Fuerstenberg S.I.,
RA   Gachon C.M., Gaulin E., Govers F., Grenville-Briggs L., Horner N.,
RA   Hostetler J., Jiang R.H., Johnson J., Krajaejun T., Lin H., Meijer H.J.,
RA   Moore B., Morris P., Phuntmart V., Puiu D., Shetty J., Stajich J.E.,
RA   Tripathy S., Wawra S., van West P., Whitty B.R., Coutinho P.M.,
RA   Henrissat B., Martin F., Thomas P.D., Tyler B.M., De Vries R.P., Kamoun S.,
RA   Yandell M., Tisserat N., Buell C.R.;
RT   "Genome sequence of the necrotrophic plant pathogen Pythium ultimum reveals
RT   original pathogenicity mechanisms and effector repertoire.";
RL   Genome Biol. 11:R73-R73(2010).
RN   [2] {ECO:0000313|EnsemblProtists:PYU1_T000481}
RP   IDENTIFICATION.
RC   STRAIN=DAOM BR144 {ECO:0000313|EnsemblProtists:PYU1_T000481};
RG   EnsemblProtists;
RL   Submitted (FEB-2015) to UniProtKB.
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}.
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DR   EMBL; GL376636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K3W690; -.
DR   STRING; 431595.K3W690; -.
DR   EnsemblProtists; PYU1_T000481; PYU1_T000481; PYU1_G000481.
DR   VEuPathDB; FungiDB:PYU1_G000481; -.
DR   eggNOG; ENOG502SZS8; Eukaryota.
DR   HOGENOM; CLU_030276_3_0_1; -.
DR   InParanoid; K3W690; -.
DR   OMA; FINDCAY; -.
DR   Proteomes; UP000019132; Unassembled WGS sequence.
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   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR   InterPro; IPR001938; Thaumatin.
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.
DR   SMART; SM00205; THN; 1.
DR   SUPFAM; SSF49870; Osmotin, thaumatin-like protein; 1.
DR   PROSITE; PS51367; THAUMATIN_2; 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:UP000019132};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          193..240
FT                   /note="Cell wall protein YJL171C/Tos1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10290"
FT   DOMAIN          248..486
FT                   /note="Cell wall protein YJL171C/Tos1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10287"
FT   REGION          281..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  52343 MW;  E619E9CCBCBC2B9D CRC64;
     MNLNVITPGS TLLQNVARPA LMWRHGYSDQ ATLAEFSIPG DGKAWYDISI ISPGSGTCKS
     FDECRRLTGK TGFNVGLAIV PRTITSGYNC RALYCLADRC DGAYQYPTDD WKTHDCPDTT
     DFDVVFCPTG SATKALTITT TATATTASTT STTTASTSTS ANAGLSIKIP SVSSNAYVRA
     KYAYKGLQAG NVLGYYDMVT NLKTCGRQRV FLKNRIGPLS EEVSMVFRGP MEIYNIAVYM
     GSAANGGPWT RVSWYNRGGA ASNLIFMNNL NIDYSGSGTR GPQGFASADG KSSVSSPQPF
     SGTLAEASNP SQVGGGPGIT TGVEVNIMTG SPCSTKVYDC PGVHGNKWSY HGWGGGKKIF
     VTRVKMPWGK RPNQPAIWML NAQVLWSGQY ACNCRGMGAK GGCGELDIAE VIETNANRDK
     VSTHYYFYDG TVASAPKGDN YATRPVDLPT VYITVLDSSN SVIKILETST FGFAADVLSN
     DQVLTWLNT
//
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