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Database: UniProt
Entry: A0A0F9XW63_TRIHA
LinkDB: A0A0F9XW63_TRIHA
Original site: A0A0F9XW63_TRIHA 
ID   A0A0F9XW63_TRIHA        Unreviewed;       839 AA.
AC   A0A0F9XW63;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Probable beta-glucosidase H {ECO:0000256|ARBA:ARBA00039581};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE   AltName: Full=Beta-D-glucoside glucohydrolase H {ECO:0000256|ARBA:ARBA00041278};
DE   AltName: Full=Cellobiase H {ECO:0000256|ARBA:ARBA00041602};
DE   AltName: Full=Gentiobiase H {ECO:0000256|ARBA:ARBA00041806};
GN   ORFNames=THAR02_03585 {ECO:0000313|EMBL:KKP04308.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP04308.1, ECO:0000313|Proteomes:UP000034112};
RN   [1] {ECO:0000313|Proteomes:UP000034112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX   PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
CC   -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC       involved in the degradation of cellulosic biomass. Catalyzes the last
CC       step releasing glucose from the inhibitory cellobiose.
CC       {ECO:0000256|ARBA:ARBA00024983}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KKP04308.1}.
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DR   EMBL; JOKZ01000081; KKP04308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9XW63; -.
DR   OMA; DVKHNPA; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000034112; 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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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:SF17; BETA-GLUCOSIDASE H-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; PS51820; PA14; 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:UP000034112}.
FT   DOMAIN          397..558
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   839 AA;  91926 MW;  35F40480D81C7839 CRC64;
     MGEWQQETKL GFDVETVLAQ LSQNQKIALL SGIDFWHTYP IPEHNVPSVR LTDGPNGIRG
     TKFFAGVPAA CLPCGTALAS TWDKQLLRRA GKLLGDECIA KGAHCWLGPT INTPRSPLGG
     RGFESFSEDP HLSGILAASM ILGCESTGVI SAVKHFVGND QEHERRAVDC LITPRALREV
     YLRPFQIVAR DAKPGALMTS YNKVNGKHVA DSSEMLEELL REEWDWDPLI VSDWYGTYTT
     IDAIKAGLDL EMPGVSRYRG KYIESALQAR LLKQSTIDER ARRVLKFAQK AGQLKVSEIE
     RGRDFPEDRA LNRQISSSSI VLLKNEDSFL PLPKTNAKVA LIGSHVRLPA ISGGGSASLL
     PYYTVSLYDA VSEALPGASI THEVGAYAHQ MLPVISSMLS RAVIHFYNDP ITVTDRKLLG
     SENVASTSFQ LMDYNGVPSL NKAMFWGTLL GDFVPTETGT WEFGLSVFGT ANLYIDDELL
     IDNTTHQTRG TAFFGKGTTE KIGSKQMVAG STYKLRLEFG SANTTKMETV GMVNFGGGAV
     HLGACVKIEP RKMIARAVRA AADADYTIIC TGLNGEWESE GFDRPHMDLP PGVDTMISQV
     LDAAPNAVVV NQSGTPVTMK WAHKAKAIVQ AWYGGNETGH GIADVLFGDV NPSGKLSLSW
     PVDVKHNPAY LNYASVGGRV LYGEDVYVGY KFYEKTEREV LFPFGHGLSY ATFALSDPVV
     KTVPETFRPN QPSVAIVRLK NTSKVAGAQV LQLYISAPNS PTQRPAKELQ GFEKVFLEAG
     EEKEVHIPID KYATSFWDEI ENKFKSEEGT YEVLVGVSSQ EILGRGKLVV PETRYWLGL
//
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