ID A0A135S840_9PEZI Unreviewed; 817 AA.
AC A0A135S840;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=CNYM01_13305 {ECO:0000313|EMBL:KXH32084.1};
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:KXH32084.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH32084.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH32084.1,
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 -!- 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:KXH32084.1}.
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DR EMBL; JEMN01001596; KXH32084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135S840; -.
DR Proteomes; UP000070054; 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 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; 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, ECO:0000313|EMBL:KXH32084.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}.
FT DOMAIN 353..516
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 817 AA; 90321 MW; 292EFC792FA5938B CRC64;
MAPRKKIPDI LASLSLEEKL SLLAGASQWR TTAIDRLGVP ELKVSDGPSG ARGEIFGENV
PAAFLPCGAS LGATWDIDLL REIGELLAEE CKSKFASVSL APTMCIHRHP LGGRNFDSFS
EDPFLSGKLA AAHIRGMQSH GVGATPKHFV TNDQETKRFK VNVHVSPRAL REVYLLPFQM
AVREADPWCM MTAYNKVNGS YSDAFEELLT GIARNEWKWD GLFMSDWGGT TSTVESINNG
LDLEMPGPPS WRSWEALKGP LEEGRINLQR VDESARRVLE LLAKTRRFED AVDGPEYCRD
DPATKELLLR AAYSGITLLK NEHCALPLSP LREKLSKLAV IGPNARRIIA GGGGSSYIKA
PYWTSVLGSV EQEFGQYGTK VLFHEGAKVN RDDLYFMSFG DVPTAVGRPV DFSFRVRACL
KPLTSGIHQL LLASIGPAKL FIDTKEILQQ SGAFEEKSTL FFTYGSGEVQ AAMYMEAGHE
YQVQIDCLSH DRQLDPLLAS LMEPMEDKFQ GFRFGYDECD ATDLPTEAGN LAEECEAAIV
VVGRDKEWET EGQDIPMFEL PGDQVRLIHQ VAAKCERTIV IVQAGSPVRM EPWVDEVQAV
LYTWYQGQEL GNAAAQVISG KINPSGRLPV TFPRDIKDCP AYSSFPGEQN ETYYSEGLFV
GYRWWDLTGV TPQYPIGFGL SYNSFSMHAG AISSNVLTRD CPLVANVLVK NTGGFDVSGT
ETVILWSRKA STRRLVMPEK QICGFAKSSH LKSGEEQLLQ VEIDAYSLGV FDPIQKGWVI
DAGSEFDILV GKDALSSKIA WQIEVPQEIK WIHTLSE
//
