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Database: UniProt
Entry: A0A1Z5TJY4_HORWE
LinkDB: A0A1Z5TJY4_HORWE
Original site: A0A1Z5TJY4_HORWE 
ID   A0A1Z5TJY4_HORWE        Unreviewed;       766 AA.
AC   A0A1Z5TJY4;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=BTJ68_04494 {ECO:0000313|EMBL:OTA36336.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA36336.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA36336.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA36336.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) 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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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:OTA36336.1}.
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DR   EMBL; MUNK01000033; OTA36336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5TJY4; -.
DR   STRING; 1157616.A0A1Z5TJY4; -.
DR   VEuPathDB; FungiDB:BTJ68_04494; -.
DR   InParanoid; A0A1Z5TJY4; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000194280; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..766
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012487247"
FT   DOMAIN          685..751
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   766 AA;  83598 MW;  389CDD8F62A49CE6 CRC64;
     MAKLLSVLGA LLPLLHQADA VGYTNVSEVP YYGLSPPVYP TPEGNGGNSS SWQAAYARAY
     SLISQMTLEE KVNVTHGHGG QCVGNSGAVP RLGLPQLCFA DAPDGIRGQE FVSSFPAQIM
     VGASFDRDLM YRYGKALGEE YRGKGINAAL LPVAGPLGRV ARGGRNWEGF GADPYLSGAG
     MENVVLGLQD QGVIGTAKHF LLNEEEFRRN PGELGEAMSS NVDDRTIHEL YAFPFMDALH
     AGVASIMCSY QRANNSYACQ NSKLMNGILK SELGFQGYVV SDWGGQHAGV ASANAGLDLV
     MPDAGYWGGN LTQAVNNGSV TDTRLDDMVA RILASYYYLN QDQGYPEPGV YPYNVEHEII
     DVRGDHASLI REIGAAGTVL VKNVNNTLPL KNPRYLDIFG YDAKLPASPW TNPSRFGGGY
     EVNFGWNTLN GTLITGGGSG SSTPPYVISP FQALQDRVLK DRGTVRWDFD AENPIVFANA
     EACIVFINAY ASESFDRTTL QDDFSDRLVQ NVAANCSNTI VVMHDAGIRV VDSWIDHPNI
     TAVLYAMLPG QESGNAIADV LYGDVSPSGR LPFTVAKKES DYGLLLNSTI SFEPFPQSNF
     TEGLYIDYRY FDKHNITPRY EFGYGLSYSS FDYSDISVEC HDDTAPEYVP STTNTTTQGG
     DSALWEALYT VKASITNSGE VAAHEVPQLY LGVPNAPGRQ LRGFERVFVK PGETQEVEFK
     VTRRDLSIWD VLKQDWQLQK GRYSVDVGRA VEILDSRIRF TGSKVR
//
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