ID A0A166V4G5_9PEZI Unreviewed; 877 AA.
AC A0A166V4G5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Probable beta-glucosidase I {ECO:0000256|ARBA:ARBA00039569};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase I {ECO:0000256|ARBA:ARBA00041279};
DE AltName: Full=Cellobiase I {ECO:0000256|ARBA:ARBA00041603};
DE AltName: Full=Gentiobiase I {ECO:0000256|ARBA:ARBA00041809};
GN ORFNames=CT0861_01805 {ECO:0000313|EMBL:KZL74152.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL74152.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL74152.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL74152.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:KZL74152.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFIV01000035; KZL74152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166V4G5; -.
DR STRING; 708197.A0A166V4G5; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000076552; 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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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 SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT DOMAIN 433..593
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 311..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 95767 MW; EC1223286B166179 CRC64;
MATKASPPRG IGANDKEAKL LSLLTLEEKC VLLSGKNMWE TQEIPHLGIG SLKTTDGPAG
VRGSRWTDGT HTTHIPCGIS LAATFNPQTV ERVSAILGAE TKGKSAHVLL APTMNLSRSP
FGGRNFENFG EDPFLTGTMA TSYIQGVQSQ GVGACMKHYV ANDQETRRFN MDERIDQRTM
REMYLKPFHM ALDARPWTAM TAYPKVNGKH VDTSQVLVRD ILRREWGFEE LVMSDWGGLN
DTVESILATT DLEMPGPPLR YGEKLARAVR EGNVSETDHI DPSVLRLLRL LGKANLLQDV
PLAATPVNHA SRIGTNGTSG CSEEEGEIDD PQTRRTVREA AAEGIVLLRN QGILPLHPEG
LQKIAIIGPN AKQPTTGGTG SAIVNPYYIT TPLESISAAV RARNPSITIT HERAIFTHLQ
PPLVGDCLTN PDNGAPGFRV DFFRDATLSG DIVSTTYWKN SLVYFMSDGD VPECLQGTKY
GYRASALLRP SVTGLYDWSL SNTGKAKLYL DDQLLIDNSD WTEISGNFMN CGSVEKFAAL
ELEAGKTYRV TVNNVVVPPP TPAHDNTLFH KISGVRVGML YRHDETAMWN RAIDCATDAD
VVVLVVGHNN DTEREGSDRA SLSLPGRTDE LVSAVCSVNK RVVVVSQSAC AISMPWAEEP
SAIVHAWYQG QECGNAIADV LFGDVCPSGK LPITFPQKID DHGSSSWFPG NPETDQAEYG
EGVLIGYRWL DAHGIEPLWP FGHGLSYTSF EISNISCQVL DRQEQLGWIV HAEVYNGGPC
SGHEVVQAYV SPSAEISLLG RAAAPKSLVG FQKVFVPRGE RRRVEISVPR ESVAWFDVDS
HRSASPGGRW RVDPGSYQCY LGRSSRDIQA TIGLIVE
//
