UniProt: A0A178B875

Database: UniProt
Entry: A0A178B875_9PLEO

LinkDB:  A0A178B875_9PLEO 
Original site:  A0A178B875_9PLEO

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (19)   

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ID   A0A178B875_9PLEO        Unreviewed;       869 AA.
AC   A0A178B875;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=IQ06DRAFT_266414 {ECO:0000313|EMBL:OAL05954.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL05954.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAL05954.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL05954.1,
RC   ECO:0000313|Proteomes:UP000077206};
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         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}.
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DR   EMBL; KV441706; OAL05954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178B875; -.
DR   STRING; 765868.A0A178B875; -.
DR   InParanoid; A0A178B875; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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:UP000077206}.
FT   DOMAIN          774..847
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          728..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   869 AA;  93468 MW;  CD1E7C24190800D1 CRC64;
     MRSTIILGLS SAAAGAVIDR RDPVPAGYVA PPYYPAPHGG WVSDWSESFQ KASQLVANMT
     LAEKTNLTAG TGIFMGRCVG NTGSAERVGI PQLCLQDGPL GVRNTEQNTA FPPGITVGAT
     WSKDLMYRRA VAIGEEFRGK GINIHLGPSV GALGRKPRGG RNWEGFGSDP VLQAFGGALT
     IEGVQSTGVI ATLKHLIANE QEQYRMYSIV KPGISSNLDD RTMHELYLWP FAEGVRSGVG
     SVMIAYNAVN GSACAQNSYL INGLLKDELG FQGFVMSDWL AQISGVPSAL AGLDMSMPGD
     INAVPLVLGE SLWAYQYTRS ILNGSVPVDR LDDSVTRILA AWYKMGQDKN YPEPNFSANT
     LDAEGPLYPG LLFGPTGVVN EFVNVQGNHA EVAREVARDA ITLLKNQGNF LPLSRNSTLK
     IFGTDAEKNP DGINSCADQG CNKGTLGMGW GSGSARYPYM DSPIDGFKSR SANYQFFNTD
     NFPSNSNPSP NDTAVVFVTA DAGENYITVE NNPGDRTSAG LNLWHNGDKL VKDVAAKYSN
     VVVIVHTVGP ILMEEWNDLP SVKAILFAHL PGQEAGKSLM EVLYGDVSPS GHLPYTVPKS
     ESNYPASVGL TGYQIGQPQD TFTEGLYIDY RHFHKANIKP RYAFGYGLSY TNFSYSDVTI
     SAVTPLTSSP PARPAKGATP NYSTEIPPAS EAVWPANFNR YLRYIYSFLS QNEANDAAKA
     ANSSTKYPYP VGYSNEQKPG PKAGGGEGGN PALFDVAYDI SVKVTNTGSR SGKAVAQLYV
     QFPTSNFDTP ILQLRDFEKT TELAPNATQT LSLRVTRKDL SVWDVVSQDW IIPSLGSDYG
     IWVGDSSDNL HIRCSTTSGS CASGQTSLV
//

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