ID A0AAE1IAG0_9HYPO Unreviewed; 560 AA.
AC A0AAE1IAG0;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=Triagg1_8412 {ECO:0000313|EMBL:KAK4065860.1};
OS Trichoderma aggressivum f. europaeum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=173218 {ECO:0000313|EMBL:KAK4065860.1, ECO:0000313|Proteomes:UP001273209};
RN [1] {ECO:0000313|EMBL:KAK4065860.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 100526 {ECO:0000313|EMBL:KAK4065860.1};
RA Beijen E., Ohm R.A.;
RT "The genome sequences of three competitors of mushroom-forming fungi.";
RL Submitted (NOV-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC {ECO:0000256|RuleBase:RU361186}.
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:KAK4065860.1}.
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DR EMBL; JAWRVG010000041; KAK4065860.1; -; Genomic_DNA.
DR RefSeq; XP_062752605.1; XM_062903256.1.
DR AlphaFoldDB; A0AAE1IAG0; -.
DR GeneID; 87923161; -.
DR Proteomes; UP001273209; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR FunFam; 3.20.20.40:FF:000001; Glucanase; 1.
DR Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR000254; CBD.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; -; 1.
DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361186};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361186};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361186};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361186};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361186};
KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283};
KW Reference proteome {ECO:0000313|Proteomes:UP001273209};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 19..560
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5041780921"
FT DOMAIN 26..62
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 64..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..91
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1,
FT ECO:0000256|PROSITE-ProRule:PRU10057"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ SEQUENCE 560 AA; 59234 MW; 9CA6B9D5E7F343EF CRC64;
MVVGILATLA ALATLAAGVP LEERQSCSSV WGQCGGQNWA GPFCCASGST CVFSNDYYSQ
CIPGAASSSS STRASSTTSR ASATSTRSSS STPPPASSTA PPPPVGSGTA TYQGNPFSGV
TPWANSFYAS EVSTLAIPSL TGAMATAAAA VAKVPSFMWL DTLDKTSLMS STLSDIRAAN
KAGGNYAGQF VVYDLPDRDC AAAASNGEYS IADGGVAKYK NYIDTIRGIV TTFSDIRILL
VVEPDSLANL VTNLATPKCS NAQAAYLECI NYAITQLNLP NVAMYLDAGH AGWLGWPANQ
DPAAQLFANV YKNASSPRAV RGLATNVANY NAWNISTAPS YTQGNAVYNE KLYIHAIGPL
LANHGWSNAF FITDQGRSGK QPTGQLEWGN WCNAVGTGFG IRPSTNTGDS LLDSFVWIKP
GGECDGTSNS SAPRFDYHCA SADALQPAPQ AGSWFQAYFV QLLTNANPSF LLSECGERFL
LKVEPNWRGV VSHQVEESVT HLMRILRAHF QCDFAGMDLP KNIIDSISNG LMVLFANTVV
MDDPLAKNDE DSFTKVEASD
//
