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Database: UniProt
Entry: W2PWM1_PHYPN
LinkDB: W2PWM1_PHYPN
Original site: W2PWM1_PHYPN 
ID   W2PWM1_PHYPN            Unreviewed;       811 AA.
AC   W2PWM1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=PPTG_14483 {ECO:0000313|EMBL:ETN04664.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN04664.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN04664.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN04664.1,
RC   ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
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DR   EMBL; KI669603; ETN04664.1; -; Genomic_DNA.
DR   RefSeq; XP_008910058.1; XM_008911810.1.
DR   AlphaFoldDB; W2PWM1; -.
DR   STRING; 761204.W2PWM1; -.
DR   EnsemblProtists; ETN04664; ETN04664; PPTG_14483.
DR   GeneID; 20183768; -.
DR   VEuPathDB; FungiDB:PPTG_14483; -.
DR   OMA; MSAYHSY; -.
DR   OrthoDB; 67286at2759; -.
DR   Proteomes; UP000018817; 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   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018817};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..811
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004823226"
FT   DOMAIN          668..742
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          792..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  88923 MW;  0DB5E8618CC7B097 CRC64;
     MWTSWITAAS LAATATLAVA NDDAYETKAQ AIVDGFSTAQ VIGQMTQVDI STVMNKDNTL
     NEDYVRAYAQ QYVGSYLNTI WDEPLGEKYG WNATEWRAVV SRIQEITMEE NGGHPIIYGL
     DSVHGANYVT GAVIFGQQIN SGASFNPDLV HKAGQITARD TQAAGIPWVF GPILEISQNP
     LWSRTYETFS EDPYLVTVLG EALVRGLQSY NQTGACMKHF IGYSKTPTGH DRDNVIMDDF
     DLLNYFLPPF KAAIEAGALS TMENYISING EPVIANPRIL NDLLRSDLGF DGLLVSDWAE
     INNLKDWHRV AETYEDAVRL SLTHTSLDMS MVPNDTSFIN YTENMLVGYP QYETRLRESA
     KRIVKMKLKL GLYENPVPGE EFEFLVGNDE DKAVALDLAR ESIVLLKNNE SVLPLAKDAS
     VFLTGHSADN VGYQCGGWSI AWQGYSGNEM FLNGISVRQG FEDLVGNNSF TYFNGLYENG
     TYSEADLAKA VELAGQHEYT IAVIGEKQYT EKPGDIDDLA LPPGQIEYVE ALAATGTKVI
     IVLFEGRPRL LGSLPDTASA IIDGLLPCEL GGKAMAEIIY GDVNPSGRLP ISYPKDPANV
     AIPYYHRVNT QCAYDHCWMQ WDFGAGLSYT EFNYSAVSLD STTITNADAF TVTATVTVTN
     VGTRAGKETV MLFLTQPYRT ISVPEVKMLK KFKKIELQPG ESQDVSFTLT ADDWSVYDPQ
     IGNGFKKVTE DSNYVVAIKP DTWCNVYKNI TNPLCAVFKI DTGRDNFGLP PPVANVTGTD
     APVLQGTVAI PGTTEPPADE AGAGTVEAGN Y
//
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