ID A0A2T4APW4_TRIHA Unreviewed; 882 AA.
AC A0A2T4APW4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=M431DRAFT_504078 {ECO:0000313|EMBL:PTB59113.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB59113.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB59113.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB59113.1,
RC ECO:0000313|Proteomes:UP000241690};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; KZ679676; PTB59113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4APW4; -.
DR STRING; 983964.A0A2T4APW4; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000241690; 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:SF12; BETA-GLUCOSIDASE A-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, ECO:0000313|EMBL:PTB59113.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..882
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015604436"
FT DOMAIN 803..872
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 757..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 94978 MW; 062AFC25EBBD94FB CRC64;
MKTSFLLAAS TATILDFAAA NALPNPQPYP PPHSNEAYSP PFYPSPWMDP NAPGWEQAYA
QAKEFVSGLT LLEKVNLTTG VGWMGEKCVG NVGTVPRLGL RSLCMQDGPL GLRFNRYNSA
FATGLTAAAS WSRHLWVDRG TALGSEAKNK GVDVLLGPVA GPLGRNPNGG RNVEGFGNDP
YLAGVALADT VTGIQNAGTV ACAKHFLLNE QEHFRQVGEA NGYGYPIKEA LSSNVDDKTI
HEVYGWPFQD AVKAGVGSIM CSYNQVNNSY ACQNSKLLNG LLKEEYGFQG FVMSDWQAQH
AGVSTAAAGL DMTMPGDTLF NTGASYFGSN LTLAVLNGTV PEWRIDDMVM RIMASFFKVG
KSINNLVDTN FDSWTDGEFG YVQAAVNENW EKVNYGVDVR ADHANHIREA GAKGTVILKN
NGILPLNKPK FLTVIGEDAG SNPAGPNGCG DRGCDDGTLA MEWGSGTTNF PYLVTPDTAI
QNQALQDGSR YESILNNYAT SAIQSLVSQP EAIAIVFANS DSGEGYLHPD GNEGDRKNIT
LWKNGDDLIK TVAANNAKTI VVVHSTGPVI LKDYAVHPNI SAIVWAGTPG QESGNSLVDI
LYGKQSPGRT PFTWGPSLES YGVQVMTTPN NGNNAPQDDF TEGAFIDYRY FDKVAPGKPR
SSDKAPTYEF GFGLSWSTFK FSNLQIQKNN AGPLNPTTGK TIAAPALGTF SKNLKDYGFP
KNIRRIKEFI YPYLSSTSSG QAASGDSHYG QTAKQFLPAG ATDGSPQPRS PSSGEPGGNR
QLYDVIYTIT ATITNTGKVM DDAVPQLYLS HGGPNEPVRV LRGFDRIERI APGQSVTFKA
DLTRRDISNW DTKTQQWVVT KFPKTVYVGS SSRDLPLSAR LP
//
