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Database: UniProt
Entry: W2YVN9_PHYPR
LinkDB: W2YVN9_PHYPR
Original site: W2YVN9_PHYPR 
ID   W2YVN9_PHYPR            Unreviewed;       786 AA.
AC   W2YVN9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=F442_14257 {ECO:0000313|EMBL:ETP38014.1};
OS   Phytophthora parasitica P10297.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP38014.1, ECO:0000313|Proteomes:UP000018948};
RN   [1] {ECO:0000313|EMBL:ETP38014.1, ECO:0000313|Proteomes:UP000018948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P10297 {ECO:0000313|EMBL:ETP38014.1,
RC   ECO:0000313|Proteomes:UP000018948};
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., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P10297.";
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};
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:ETP38014.1}.
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DR   EMBL; ANIY01002966; ETP38014.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2YVN9; -.
DR   EnsemblProtists; ETP38014; ETP38014; F442_14257.
DR   Proteomes; UP000018948; 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:UP000018948};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..786
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004831173"
FT   DOMAIN          677..751
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   786 AA;  85557 MW;  F200C2AEBBC14112 CRC64;
     MLTSWAVALG CIAAFTTVPV AARNLADDVY DSQAQAIVDG FSIAEVLGQM TQITITQVLN
     SDYSLNEDSV RTYAKLYVGS YLNTPWGSEI DGKWGWNATE WRAIVTRIQA ITMEENGGHP
     MVYGLDSVHG ANYVAGSVLF GQEINSGASF NPDLVYEVGR ITGRDTEAAG IPWVFGPILD
     LAQNPLWART YETFGEDPYL CSVMGDAIIR GLQSNNQTAA CMKHFVGYSK TPTGHDRDGV
     TMADFDLLNY FVQPYQAGIS AGALSTMENY ISINGIPVVA NTKILEDLVR NDLNYDGVVV
     TDWAEINNLK DWHRVVDTYE EAVRLSLTRT ALDMSMVPYD TEFITHATTM LSSFPEYESR
     LRESAKRVIK MKLKLGLYET PVPGASNEFL VGNDDDKAVA LDLARESIVL LKNNDNILPL
     SNGSSVFLTG HSADNVGYQC GGWSIAWQGY SGNDMYPNGI SVRQGLENVV GNNSFTYFNG
     LNADGTYSDA DLATAVNLAS QHEYTIAVIG EDTYAEKPGD IDDLDLPAGQ IAYVEALAAT
     GTKVILVLFE GRPRLLGSLP DMASAVIHGL LACELGGQAL TEIVYGQVNP SGRLPLTYPK
     DSGNVMIPYN HRVTTKCVDD TGSYVDCEMQ WDFGTGLSYT TFTYSALTLS KTTVSGPDDA
     LTASVFVTNS GSVAGKETVM LFVVQPYRLI SVPEVKMLRK FKKISLEPGI TEEVTFTLTA
     DDWSVYDPQI GSGFNQVAED GTFVVAIKPE TDCDVYNTIT NELCAQFTLD TGSVNFGING
     TTSRRR
//
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