ID A0A177CYT8_9PLEO Unreviewed; 872 AA.
AC A0A177CYT8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=CC84DRAFT_1192339 {ECO:0000313|EMBL:OAG12000.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG12000.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG12000.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG12000.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441548; OAG12000.1; -; Genomic_DNA.
DR RefSeq; XP_018042365.1; XM_018181244.1.
DR AlphaFoldDB; A0A177CYT8; -.
DR STRING; 1460663.A0A177CYT8; -.
DR GeneID; 28764730; -.
DR InParanoid; A0A177CYT8; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000077069; 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; 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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF12; BETA-GLUCOSIDASE A-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 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.
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:UP000077069};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..872
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008058809"
FT DOMAIN 793..861
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 872 AA; 93840 MW; 960666A805373A96 CRC64;
MTPGLAHFFL SLFPFLRVTD YSTTPVGPNS TTPGDLNNAY SPPYYPSPWV DSSAEGWQDA
VTRARAFVSQ LTLLEKVNLT TGVGWEGEAC VGNTGAIPRL GFPGFCAQDS PLGVRFADYV
SAFPAGGTIA ASWDRGEFYR RGYQMGVEHR GKGVDVQLGP VVGPLGRNPK GGRNWEGFSP
DPVLSGIAVA ETVKGIQDAG VIACTKHYIL NEQEHFRSPG QFEDFGFVDA ISSNVDDKTL
HELYLWPFAD AVRAGTGSIM CSYNKANNSQ VCQNSYLQNY ILKGELGFQG FIMSDWDAQH
SGVASTLAGL DMTMPGDSDF DSGFSFWGAN LTLSIINGTV PEWRLDDAAT RIMAAYYLVG
RDKHAVPVNF NSWSRDTYGY QHAFAETGYG LINQHVDVRA DHYKAIRVAS AKSTVLLKNL
NGALPLKGNE KNTAIFGQDA GDSQYGPNGC ADRGCDNGTL AMGWGSGTAD FPYLVTPLDA
IKNELAGNGG IVQSVTDNYA WAQIMSLAKQ ASTAIVFVNA DSGEGYITVD GNAGDRNNLT
IWQGGETLVQ NVSAYCNNTI VVIHSVGPVL IDSFSNSENV TAILWAGLPG QESGNAIADV
LYGRVNPGGK LPFTFGTNAS EYGPDLIYAP TNGNESPQDN FEEGVFIDYR AFDQKNITPV
YEFGFGLSYT TFSYSNLTVT KVAAQAYTPN SGLTEPAPVL GNSSTDPSQY QWPSNLTYVN
KYIYPYLNST DLKEASFDPE YGLNYTYPEG ATDGSAQPKI AAGGGPGGNP QLWDVLFTVT
ATITNNGTVA GDEVPQLYIS LGGPTDPVVA LRNFERLSIA PGKTATFYAD VTRRDVSNWD
TASQNWVVTN YTKTVHVGSS SRKLPLSAKL SF
//
