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Database: UniProt
Entry: G4YPF4_PHYSP
LinkDB: G4YPF4_PHYSP
Original site: G4YPF4_PHYSP 
ID   G4YPF4_PHYSP            Unreviewed;      1152 AA.
AC   G4YPF4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=PHYSODRAFT_554256 {ECO:0000313|EMBL:EGZ27934.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ27934.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ27934.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ27934.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; JH159151; EGZ27934.1; -; Genomic_DNA.
DR   RefSeq; XP_009515209.1; XM_009516914.1.
DR   AlphaFoldDB; G4YPF4; -.
DR   STRING; 1094619.G4YPF4; -.
DR   EnsemblProtists; EGZ27934; EGZ27934; PHYSODRAFT_554256.
DR   GeneID; 20662983; -.
DR   KEGG; psoj:PHYSODRAFT_554256; -.
DR   InParanoid; G4YPF4; -.
DR   OMA; NFPGLCV; -.
DR   Proteomes; UP000002640; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT   DOMAIN          1043..1117
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   COILED          93..120
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1152 AA;  127764 MW;  E652DE39044D2648 CRC64;
     MALFQQEDEE EEGVFEAALS FVDEFEFNTG DAISSLNQLP TQRRQETSVS LSNEVAIGGA
     VGPLSREEKR RRQAEKKRLL RKAGIYSDPN RARNEQTREI AFLREQMDKL QLNLKVLQAR
     KHQNGAKALV PVNTKTHRPS LWQEQAMRQR RRREQAECDN VRLKLAVERQ RKVADSLGVL
     IRKRTRQLNN ECASLINQCC VDHPAIAVLD FCGDVEDFRG LFHLLDEAYR DVDSIFMANG
     LATMSIPIGD VHMREGVDGK YLEFFTYKDL PFGLQDTAQA SWDYFKGAEK HMAYGNLYEK
     AAKSLDEPYT VIEEFTKEVY SNTSRADVKM RQVVRRYVEA DRDVVIRVSH AAPIEVKNKV
     LRGLTHNVRG FAITKRSPAS TPSQELTQLQ LCTQIALELN DGVTYDPKNV RALTNFLIAH
     GLKNTVVNCE YIENALADHA LRRRIADDVY DSQAQAIVDG FSVAQVLGQM TQINIGQVLN
     SDYSLNEDSI DGKWGWNATE WRAIVTRIQE ITMEENGGHP MVYGIDSVHG AIYVSGAVIF
     GQEINSGASF NPDLVYQVGA ITGRDTEAAG IPWIFGPILD LAQNPLWART YETFGEDPYL
     CSVLGDAIIR GLQSNNQTAA CMKHFVGYSK TPTGHDRDGV TMADFDLLNN FVKPYQAGIA
     AGALSTMENY ISINGIPVVA NTKILEDLVR NDLDYDGVVV TDWAEINNLK DWHRVVDTYD
     EAVRLSLTRT ALDMSMVPYD TEFITYATEM LSNYPEYESR LRESAKRVIK MKIKLGLYET
     PVPGADYEYL VGNDDDKAVA LELARESIVL LKNDNNILPL ANGSSVFLTG HSADNIGYQC
     GGWSVAWQGY SGNDMFPNGV SVRQGLENVV GNNSFTYFNG LSVNGNYTSE DLATAVALAS
     QHEYTIAVIG EDTYAEKPGD IDDLALPAGQ IAYVEALAAT GTKVILVLFE GRPRLLDTLP
     DTASAVVHGL LACELGGQAM AEILYGQVNP SGRLPLTYPK DSANVMIPYN HRVTTKCTTV
     SGPDDSLTAS VFVTNSGSVA GKETVMLFVI QPYRLISVPE VKMLRKFKKI DLEPGITQEV
     TFTLTADDWS VYDPQIGSGF NQVAEDGTFV VAIKPETDCD VYNTITNDLC AQFTLNTGSV
     NFGINGTTSR RR
//
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