UniProt: A0A0D0C6Q4

Database: UniProt
Entry: A0A0D0C6Q4_9AGAR

LinkDB:  A0A0D0C6Q4_9AGAR 
Original site:  A0A0D0C6Q4_9AGAR

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
All databases (23)   

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ID   A0A0D0C6Q4_9AGAR        Unreviewed;       845 AA.
AC   A0A0D0C6Q4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=GYMLUDRAFT_71965 {ECO:0000313|EMBL:KIK63846.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK63846.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK63846.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK63846.1,
RC   ECO:0000313|Proteomes:UP000053593};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-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|RuleBase:RU361161}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; KN834763; KIK63846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0C6Q4; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000053593; 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:SF26; 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|RuleBase:RU361161};
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|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053593}.
FT   DOMAIN          407..572
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   845 AA;  93248 MW;  1B558A0410ADFA38 CRC64;
     MSLSFLDADI SNLVSKLRTE EKIALLGAPN WWNTTPISRL EIPSIRMSDG PNGVRGSSHF
     VSSPAQCLPC ATSLASTFDV QLVYQVGQFL AEEAKLKSSV VLLAPTCNIQ RSPLGGRAFE
     SFSEDPYLSG MMAAAYVNGL QSQGVSAAIK HFVGNDQEHE RTAAESIMSD RAFREVYLYP
     FMLAQQLAHP WAFMTSYGRI NGVHCSENVD LLQGILRDEW NFTGIVMSDW YGTYGVDQPL
     NAGLDLEMPG PPRWRTPTLM NHVLTAQKLL PSTLDERAKN MLSFIQHQAH LNPGVVYGDG
     KERTRDTPEM RRFSRDIAAQ GIVLLQNRDS VLPLRPNRVG KLAVIGPNAK GNVISGGGSA
     ALKASYVITP YTGIQDGAFK DLEISYAVGC YAHKYLPTLE NYLLTPTGER GWLATFYAHT
     ADGKLTPPIA EFVLQDTRVK LNDFLPTGLT ETWTLKMTGK LIVDKTASYE LGLTVAGRAK
     LWINNELTID NWTKQTPGDF FYGQGTIEEK STVDLKAGKP VDMLIEYTNT YPPANKDDEG
     SSTPESQPAL MRGLRLGGCE KIDAEVAMKE AVKLAKESDV VVFIGGLTPE WESEGFDRPS
     LDLPGRQAEV IHNLAEVNRN TVVCIQAGSA TAMPWKDEVA GILQAWYLGN EVGNAIADIL
     YGKVNPCASL PMTFPKRMED IAAYPNIRSE FGKIHYREGI MVGYKHFLKA GVAPLFCFGH
     GLSYTEFELS DCEVNQTGTD VEISLQVYNV GSIAGSKVVQ LYVAYPETGI THPPLQLKAF
     SKVHDVAAGK SATAKMRLDK WAFSYWNERT SKWEVDQGQY VLEIGFSCEC IKWKKNVEVK
     EGMSW
//

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