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Database: UniProt
Entry: V9DKT9_9EURO
LinkDB: V9DKT9_9EURO
Original site: V9DKT9_9EURO 
ID   V9DKT9_9EURO            Unreviewed;       836 AA.
AC   V9DKT9;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=G647_09660 {ECO:0000313|EMBL:ETI27470.1};
OS   Cladophialophora carrionii CBS 160.54.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI27470.1, ECO:0000313|Proteomes:UP000030678};
RN   [1] {ECO:0000313|EMBL:ETI27470.1, ECO:0000313|Proteomes:UP000030678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI27470.1,
RC   ECO:0000313|Proteomes:UP000030678};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL   Submitted (MAR-2013) 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; KB822698; ETI27470.1; -; Genomic_DNA.
DR   RefSeq; XP_008723876.1; XM_008725654.1.
DR   AlphaFoldDB; V9DKT9; -.
DR   GeneID; 19988153; -.
DR   VEuPathDB; FungiDB:G647_09660; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000030678; 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}.
FT   DOMAIN          400..560
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   836 AA;  90813 MW;  FDF34AAEE153C9F7 CRC64;
     MGSLPVQTSF DVEDVLSQLT IAEKVALLSG IDFWHTAPVH RLGVPSIRLS DGPNGVRGTR
     FFNGVPAACL PCGTGLAATW DTELVKKGGA LQGTEAIAKG ASVILGPTTN MQRSPLGGRG
     FESFSEDPYL AGAMSASTIN GIQSTGVSAT VKHFVCNDQE DQRQAVDSIL TERALREIYL
     MPFQIAQRDS RPDCYMTAYN KVNGTHASEN PRLLKDVLRG EWGFDGLTMS DWFGTYSTTE
     AIKAGLDLEM PGPSYIRAHL INQALGCGKL LVPDVDDRVR EVLKLVKKTQ ALGIPENAPE
     TTIDSSETSA FLRTLSANGL VLLKNNDNLL PLDKKKTTAV IGPNAAYASY CGGGSASLLP
     YYAISPLDGI REQVPEAKYA LGAPAWKALP LMTRLTKTKS GDNGLTMTVF LDPPSVTSRK
     AVDEVFVNKS DILLVDYKHP LIKSSLYWLE LNGTFTPEQT TDYDFSMCCA GTGKIFVNGE
     VVVDNETHQR PGNSFFGAGT AEEIGRLKLE EGKTYDIKVT FGTLPTMTFS SPGTTGFGAG
     GLRVGLERKA EIATEIERAV QLAKEVDQVV LCAGLNGEWE SEGYDREHMD LPPGSDELIK
     AVLAANPNTA IVIQSGTPVT MPWLEDAPAV VQAWYGGNET GNAIADVVFG NTNPSGKLPL
     SFPVRNEDNP AFLNYKSERN RAIYGEDVYI GYRFYEKTNR EVAFPFGHGL SYTQFDTTDL
     SVADDDVDIL VSATVSNTGK VDGAQVVQVY FSQHKPSINR PKKELKGFAK VFVKAGQSEK
     VEITISKKYA TSFWDEARDA WVMEKDTFDV LVGDSSANTP LKAQVKVLRS EWWRGL
//
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