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Database: UniProt
Entry: A0A484FKP9_COLOR
LinkDB: A0A484FKP9_COLOR
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ID   A0A484FKP9_COLOR        Unreviewed;       841 AA.
AC   A0A484FKP9;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   Name=bglI-2 {ECO:0000313|EMBL:TDZ17497.1};
GN   ORFNames=Cob_v009520 {ECO:0000313|EMBL:TDZ17497.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS   414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum orbiculare species complex.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ17497.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT   stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
RN   [2] {ECO:0000313|Proteomes:UP000014480}
RP   GENOME REANNOTATION.
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA   Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA   Shirasu K.;
RT   "Genome sequence resources for four phytopathogenic fungi from the
RT   Colletotrichum orbiculare species complex.";
RL   Mol. Plant Microbe Interact. 32:1088-1090(2019).
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         ECO:0000256|RuleBase:RU361161};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:TDZ17497.1}.
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DR   EMBL; AMCV02000028; TDZ17497.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A484FKP9; -.
DR   STRING; 1213857.A0A484FKP9; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000014480; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; IPR019800; Glyco_hydro_3_AS.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; 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   Pfam; PF07691; PA14; 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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014480}.
FT   DOMAIN          400..553
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   841 AA;  92169 MW;  DE79B29619A8DA6B CRC64;
     MSSSGVPLDV EGLVSQLTLE EKVDLLAGQG SFRTTGLPHR GIPDLVTSDG PHGIRGRRAF
     HRNPSPMLPS ATGMGATFNA PLLRRVGNLL GEEARARGVH VLLAPTICLQ RSPLFGRGFE
     AFAEDPYLSG VLGGAYVNGV QDRGVATSVK HYAAHDQSDN SVEDNVCMTQ RTLREVHLLP
     FQLVLRDADP WTFMTSYNKI NGVHASEDPL LLKTILREEW GFKGLVMSDW FGTYSTSEAI
     NAGLDLEMPG PTQWRGKCLG LAVNSRKVLR TTVDECVRNV LNLVNKVTDT KPEGYFAASN
     TPEQQALIRQ LVAESIVLLK NERGILPIKA AEKKKIGLIG DHVKNPALSG GGSAEVEPYY
     SVTPYNAIVE QVGEDNVSYA LGCHSFRFSP LLKNLKPLHA DGFGWSIEIF AENPDANPHA
     EVLVSATAEK ELIDVPESFH ARLPKMFYAR ARATYTPETT GPFRFGFSTS GKGRVRVDGK
     DVIDLWTSQP PKTGPTPCFN RLSMEEFCDV ELAAGKSVEI EVVQVNEDLA GGVGTALTLA
     GRVGGFRVID EDEAIREAAE LARNVDVPIV VTGLSSDFEY EGADRKHLRL PGRVDDLITA
     VLAANPNTII VTQSGCPIEM PWEPQTPTLV HAWFGGQETG HGLADVLFGT SNPSGRLSQT
     FPKSVKHNPA YLNFSKTDYD IVYGEGVFLG HRYYEVTDRE PLFYFGHGLS YSKFTYTDLV
     VPETFTASAD HEMRISVTVT NEGPYDGAEV VQVYVHDPQS SLQRPVRELK AFAKVYLAVG
     ETRTADLVLD KYSLSFWSQE RSKWQAEAGG FVVIVASSSN PRDEILRASF SLPETFFWQG
     V
//
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