ID A0A2T3ZGX8_9HYPO Unreviewed; 754 AA.
AC A0A2T3ZGX8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=M441DRAFT_65834 {ECO:0000313|EMBL:PTB44067.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB44067.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB44067.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB44067.1,
RC ECO:0000313|Proteomes:UP000240493};
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 -!- 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; KZ679258; PTB44067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3ZGX8; -.
DR STRING; 1042311.A0A2T3ZGX8; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000240493; 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:PTB44067.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493};
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 232..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 387..606
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 86243 MW; F40A804205E8CD2E CRC64;
MSDTEIPRAH RSRNRSARGE SSRRDRPRKK ESRTRRGASS ADEGRADRRS RSQSLSAGAL
AQLNQDNVRQ QRQAERERRK RDRERGEGHD ERARERLERQ QRRERERRRE REAERDRDRE
REMEWERERQ REREREQRRT RARDRSPSPD PETEPVIIPK KYHKPGRQKK KSRVVSGAVM
EEGRSKGWTF GFGGWGNGNH SRDGSYDSLR KEDLYSQPEK KKKKTWSKRK KWIIGGICAV
ILLIIIIVAA VVGSKHNSGS NSNSSGPSAS NSDVPAKWIN TYLDPTTWAS TEDFNTTFTD
VMVGGLPIMG LDSSWDDSAQ ANDNVPALNK PWGSYSKAPA RGVNLGGWLS IEPFITPSLF
NYPLSAGVVD EWTLCAHLGS QAASTIENHY NTFVTESTFQ DIANAGLDHV RIPFSYWAVK
VYDGDQYIYR TSWRYLLRGI EWARKYGLRV NLDLHGLPGS QNGWNHSGRQ GSIGWLNGTN
GNLNAERSLD IHNSLSQFFA QDRYKNIITH YGLANEPRMT FLKASTVVNW TETAFKMVRK
NGYNGLVIFG DGFMGLNNWQ GLMQGYDGLV LDVHQYVIFN QNQIDFTHQK KVQYACQGWT
QQAEQSQDTR TGYGPTQFAE WSQADTDCAQ YVTNVGQGNR WEGTLNTGNA STAILTPDCP
TKNSQCSCDQ ANADASKWSS EYKQFLTMFA EAQMYSFEKG LGWWYWTWQT ESSPQWSYKA
GMQAGVLPQK AWERNFNCDT DVPDFSKSGL PEYY
//
