ID A0A066XFB4_COLSU Unreviewed; 833 AA.
AC A0A066XFB4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=CSUB01_03266 {ECO:0000313|EMBL:KDN66339.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN66339.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN66339.1}.
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DR EMBL; JMSE01000945; KDN66339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XFB4; -.
DR STRING; 1173701.A0A066XFB4; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OMA; GNETGNC; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000027238; 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: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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT DOMAIN 395..554
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 833 AA; 91254 MW; 8D95ADF6EAD0AD74 CRC64;
MADFDVEELL KKLTVSEKVD LLAGIDFWHT KALPNRNIPS IRLSDGPNGV RGTKFFNGIK
AACFPCGTAL GATFNTELLE EAGRKMGEEA KLKGAHCILG PTINMQRSPL GGRGFESIGE
DPVLAGLGSA AIVRGIESTG IQATPKHFVC NDQEHRRNAV HSIVTERALR EIYALPFQLT
FRDSAPGALM TAYNGVNGTF CSENPDLLDK LVRKEWGWNG MIMSDWYGTY STTEAANAGL
DLEMPGPPRF RGEPLKFNVS TDKVRQHVLD ERARAMLRFI KKAVATGIPE GAPERTGDTP
ETAELLRRIG GESIVLLKNE ENVLPLKKDK KTVVIGPNAK IATYHGGGSA SLAAYYAVTP
FDGISKKLES PPQYTEGAYS HKLLPLLGNV CKSADGKHGM TMRAYNEPPT DHNREPVDEL
VLTKTELLLV DYYNPKLKSK LWYADFQGSF VAEEDCTYEL GLIVCGTANL FVNDKLVIDN
STKQRQGDAF FGAATLEEKG RVELKKGETY TFKVEFASAP SSKLQGDNVV FGGGALRIGG
CKVIDDKAEI TKAAALAKDA DQVIICSGLN ADWETEGNDR ADMDLPGYLN KLISAVVQAN
PNTVVVNQSG TPVRMPWAKD VKALVQAWYG GNETGNAIAD VLFGDVNPSA KLSLSFPERV
QDNPAYLNYR AEASRTLYGE DIYIGYRYYE YIDRPVLFPF GHGLSYTSFD FSGLKVREKD
GKIAVDVTVK NTGKVQGAEV VQVYIAPKQK AKVNRPLKEL KGFAKVSLAP GESKIATVDI
ETKYAASYFD EERHQWCAEE GEYEIIVSDS SVLTDKAIKS SFKVGETFWW SGL
//
