UniProt: A0A084QV99

Database: UniProt
Entry: A0A084QV99_STAC4

LinkDB:  A0A084QV99_STAC4 
Original site:  A0A084QV99_STAC4

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

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ID   A0A084QV99_STAC4        Unreviewed;       822 AA.
AC   A0A084QV99;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   28-JUN-2023, entry version 33.
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=S40285_04107 {ECO:0000313|EMBL:KFA67884.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA67884.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA67884.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA67884.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(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}.
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DR   EMBL; KL660079; KFA67884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QV99; -.
DR   STRING; 1283841.A0A084QV99; -.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   InParanoid; A0A084QV99; -.
DR   OMA; NFPGLCV; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000028524; 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; 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:SF5; BETA-GLUCOSIDASE M-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   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:UP000028524}.
FT   DOMAIN          743..809
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   822 AA;  88823 MW;  3E62339357B2DB22 CRC64;
     MVNSMDESRP MASNVDMPRK PSSEARPRRG LALLIVVPLI LLSGLAGLAA LDSGSSGSGD
     DGANAERQEV IQDDTHFYGD SPPVYPSPDM TGRGSWAIAF DKARHMVSLT AGIAPDSGCV
     GRVPEVRSVG FPGLCLGDAG QGLRGTDFVS SFPSGIHTGA SWNRNLTYWR GAAMGHEFRT
     KGVHVLLGPV VGPALRVVSS GRNWEGFSAD PYLAGALAYE TVVGVQVQGH FIANEQETHR
     NPHRGVEATS SNIDDRTMHE FYLWPFQDAV RAGTGNIMCS YQRINNSYGC ANSKTMNGLL
     KTELGFQGFV ISDWSAQHAG VATALSGMDM AMPTAGNFWG DRLVEAVNNG SVPESRVTDM
     AMRIVSSWYQ MKQDSGFPDL GAGMPSSVTR PHRVVDARDP EASPTIFQGA VEGHVLVKNT
     KNTLPLRSPR MLTVVGYSAK SPDFYSPGGG DLGEYSWRFG TEATDPREMQ AGFAGELDAD
     YSSIALDGTL IHGGGSGATT PAIFLSPFEA LKMKAFQNGT ALFHDFTSAE PVVDPVSDAC
     IVFGNAWASE GYDRPALRDD YTDNMIIKVA DQCNKTIVVL HNAGARLVDQ FVDHPNVTAI
     IFAHLPGQDS GSALVSLLYG ESNFSGKLPY TVARNESDYG NMLGPDRAEG EFVNFPQSDF
     TEGVYVDYRR FDQQDIAPRY EFGFGLSYTT FEFSNLTVQT RRNASLAEWP TGAVVQGGQQ
     DLWDHVATVT AEIRNTGDVP GAEVAQLYLG IPNSPARQLR GFEKPVLDVN ATAAVSFTLT
     RRDLSVWDAV AQRWRLQSGR YGVFIGSSSR RIHLNGTLQV RA
//

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