ID A0A135TIM5_9PEZI Unreviewed; 881 AA.
AC A0A135TIM5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=CNYM01_02563 {ECO:0000313|EMBL:KXH47975.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH47975.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH47975.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH47975.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) 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 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:KXH47975.1}.
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DR EMBL; JEMN01001104; KXH47975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TIM5; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000070054; 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:SF27; BETA-GLUCOSIDASE; 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; 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}.
FT DOMAIN 444..604
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 881 AA; 97060 MW; F092D333D989931F CRC64;
MSAVTDSQAE RDVEAPISPP ETETSNSTPN TVFSPPYSPP QKIQQLLRDT RAAARKKLDQ
LTLEEKVSLL TAADFWRTKA IPSKSIPSVK TSDGPNGARG GIFVGGTKAA LFPCGVSLAA
TWNKDLLYEV GQHLADEAKA RSANILLAPT VCMHRHPLGG RNFESFSEDP LLTGKLAAQY
VRGLQDKGVA ATIKHFVGNE QETHRLTIDS LIQERPLREI YLRPFEIAVR EANPWALMSS
YNLVNGVHAD MHNLVLRDIL RGEWGYDGTV VSDWGGTNST AESIIAGCDV EFPYSPNWRF
EKVIEAMKEG KVTLEDINRA AENVLTLVER LKGDDMSAEL PEREDNREST RSLIRTAGAE
GLTLLKNDGA VLPLNRKTTK VAVIGPNANR AIAGGGGSAS LNPYYRTLPL DSIRATSEQE
ITFAQGCHIY KWLPVASPYC TEKSGKPGVN IDWYSGDKFK GEVVVVQRRV NTDLFLWDSA
PLAEIGPEWS AVATTYLTPK STGKHTVSFM SVGPGKLYVN GKLALDLWDW TEEGEAMFDG
SVDYLVDVDM EASKPVELKV EMTNELRPVA KQKQFGITHK YGGCRIGFKE EDQVDFLQEA
VDAAKAADVA VVIVGLDAEW ESEGYDRQTM DLPSDGSQDR LIEAVVKANP RTVVINQSGT
PVTMPWVDQV PAIIQGWYQG QEAGNALADV LFGIKSPSGK LPSTFPKRIQ DTPAFNNWPG
ENLKVNYGEG LYIGYRHYER ARIEPLFPFG HGLSYTIFEY GRPSISTKTL TSRGTIEVIF
AISNVGSVPG SEAVQIYVRD DKSRLPRPEK ELVAFEKVFL EAGETKHLTI HLDKYAVGYY
DTSVPGWVAE EGTFKILIGA SSADIKHSVQ FEVKESFNWV F
//
