ID A0A2T4BI09_9HYPO Unreviewed; 714 AA.
AC A0A2T4BI09;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
DE AltName: Full=Exo-1,3-beta-glucanase D {ECO:0000256|ARBA:ARBA00041260};
GN ORFNames=BBK36DRAFT_1192480 {ECO:0000313|EMBL:PTB68940.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB68940.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., 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 -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Active on lichenan. {ECO:0000256|ARBA:ARBA00037126}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641}.
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DR EMBL; KZ680209; PTB68940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4BI09; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000241546; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF22; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000313|EMBL:PTB68940.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000241546};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 349..547
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 81749 MW; 11CA87E50D5C47BE CRC64;
MSDTDIPRAH RHRSARGESS RRDRERTRDR ERDRERTRDR DRERDGERDR SRKHESRTRR
GASSADEGRA DRRSRSQSQS LRRERERTAG HEERERERAE RHQRRERERE RRREQERERE
RERERHPGPE RVRPSKQKKS RVVSGAAMEE GRTRGWGFGF GHAREDSYDS LRKEELYSQP
EKKKTKWSKR KKWIVGGICG LILLIIIIVA AVVGSKKKSG GSNDSPSSSA SNSKVPTQYI
GTYLDPSTWA STTDFNTTFT NETVGGLSVM GLYSDWDDSA QANDNVPPLN KPWGNYSKTP
ARGVNLGGWL SIEPFITPSL FNYPLSAGIV DEWTLCAHLG AKAAETIENH YNTFVDESTF
KDIADAGLDH VRIPFSYWAV KTYDGDQYVA HTSWRYLLRG IEWARKYGLR VNLDLHGLPG
SQNGWNHSGR QGQINWLNGT DGDLNAQRSL DIHNSLSQFF SQKRYQNIIT HYGLANEPKM
VYLDHARVIN WTETAFNLVR KNGYKGLVIF GDGFMGLNNW QGLMQGYDGL VLDVHQYVIF
NVNQIDFTHQ KKVEYACAGW TQQAEQSQDP STGYGPTQFA EWSQADTDCA QYVTNVGQGS
RWEGTLSGNA STAVLSPGCP TKNSQCSCAQ ANADPSKWSD EYKKFLSMFA EAQMYSFEKG
LGWWYWTWKT ESSPQWSYQA GMQAGVLPKK AYDRDFNCDV AVPDFSKEGL PEYY
//
