ID A0A161VFA5_9PEZI Unreviewed; 751 AA.
AC A0A161VFA5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE Flags: Fragment;
GN ORFNames=CI238_00574 {ECO:0000313|EMBL:KZL64265.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL64265.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL64265.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL64265.1,
RC ECO:0000313|Proteomes:UP000076584};
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:KZL64265.1}.
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DR EMBL; LFIW01002706; KZL64265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161VFA5; -.
DR STRING; 1573173.A0A161VFA5; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 2.
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; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF5; BETA-GLUCOSIDASE M-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 2.
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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZL64265.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT DOMAIN 672..740
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL64265.1"
SQ SEQUENCE 751 AA; 80701 MW; A0607E7B4E24019C CRC64;
LLMDVTHAHC ILRSWRKDED LGFHTGCGPC RPYALRRSEN LHQRDPYYGQ SPPVYPSPVG
NGASNDAWAL AYQRAKSLAS HMTVEELANF THGWSGLCTG NTGSVPRLGV EPICLQDGPD
GVRAQEFVSA FPAGIHLGAT WNRNLSYAYG IALGAEFRGK GINVGLGPVG GPLGRIARGG
RNWEGLSNDP YLSSVGVGGV TKGMQDADTI ACPKHWLLNE QEYRRNPDEE EGEAASSNVD
DRTLHELYVF PFMDALNEGA ASVMCSYNRA NNSYGCQNSK LLNGVLKTEL GFEGFVVRGA
QHAGVASANA GLDLVMPNEA FWGSGLVEAV NNGSVTRERV EDMTTRILAA WYYIGQDSDD
YPAFGVYSNL QKHAPVDVQN GHKALIREIG AAGTVLVKNI NGALPLKSPK FLTVFGYDAT
VLCTPWTSTS YGPGFGTQIG DTYNGTLIAG GGSGITTPPY VISPFQAIQE RVVADGGVAS
EGYDRPNLSD GFSDNLVNNV AANCSNTIVV LHSAGTRVVD AWADHPNVTA ILFAGLPGQE
SGHSLTDILY GDVNPSGRLP YTVAHAESDF GALLNSSVDP GPFPQDDFSE GLFIDYRAFD
RDGITPRYEF GFGLSYTTFE YSSLSASPVG TPVAGFLNPD VAIVQGGHPA LWEDVYSVSV
QVQNTGELAG HEVAQLYVGI PGEGTPARQL RGFKRVFIEA GGSATVDFRL TRRDLSVWDI
VAQQWRLAEG EYDVFVGASN RDLRLNEIFT I
//
