ID A0A137Q669_9AGAR Unreviewed; 512 AA.
AC A0A137Q669;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361164};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361164};
GN ORFNames=AN958_02182 {ECO:0000313|EMBL:KXN82743.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN82743.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN82743.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN82743.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91; Evidence={ECO:0000256|ARBA:ARBA00001641};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000256|ARBA:ARBA00006044, ECO:0000256|RuleBase:RU361164}.
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DR EMBL; KQ962922; KXN82743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137Q669; -.
DR STRING; 1714833.A0A137Q669; -.
DR OrthoDB; 3014058at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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 CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001722; Glyco_hydro_7.
DR InterPro; IPR037019; Glyco_hydro_7_sf.
DR PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR PANTHER; PTHR33753:SF2; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361164};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361164};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|RuleBase:RU361164};
KW Hydrolase {ECO:0000256|RuleBase:RU361164};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361164};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..512
FT /note="Glucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007295041"
FT DOMAIN 476..512
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 453..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 53928 MW; A6BE5F2F11B985D0 CRC64;
MFPKATLLAL SFAAAVLGQQ VGTNTAETHP SLSWQKCTKS GGCTTVSSGK ITLDANWRWL
HTTTGYTNCY TGNTWDATLC PDGATCAANC ALDGADYPGT YGITSSGNAL TLKFVTQSQQ
KNVGSRVYLM ADDSTYQMFK PLNQEFTFDV DVSNLPCGLN GALYFSEMAA DGGMSQYPTN
KAGAKYGTGY CDSQCPRDIK FINGEANVAG WAGSSNDPNA GTGNWGSCCN EMDIWEANSI
SAAYTPHPCT TSGLSRCSGA ACGANDRYGT VCDPDGCDFN SFRMGDQTFY GPGKTVDTSR
KFTVVTQFIT NDGTANGNLS EIRRLYVQDG KVIQNSKVNV PGMDAHDSIT EAYCDAAKSA
FGDTPQFQNK GGLTGMGASM KRGMVLVLSV WDDHAVNMLW LDSDYPTDAD ASKPGIARGT
CATTSGTPND VESNSPNASV VYSNIRFGDI DSTYTGGGGS TTTPTTTTPT TSAPGATQTK
WGQCGGTGWT GPTVCAAGTT CQKLNDYYSQ CL
//
