ID A0A2V5ICT6_9EURO Unreviewed; 611 AA.
AC A0A2V5ICT6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361164};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361164};
GN ORFNames=BP00DRAFT_443637 {ECO:0000313|EMBL:PYI34595.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI34595.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI34595.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI34595.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
CC {ECO:0000256|ARBA:ARBA00002392}.
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; KZ825475; PYI34595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5ICT6; -.
DR Proteomes; UP000248817; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; 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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361164};
KW Hydrolase {ECO:0000256|RuleBase:RU361164, ECO:0000313|EMBL:PYI34595.1};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361164};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..611
FT /note="Glucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016027046"
FT DOMAIN 505..540
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 464..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 64723 MW; 1D3C661A4DB34203 CRC64;
MVDSFSIYKT ALLLSMLATS NAQQVGTYTA ETHPSLTWQT CSGSGSCTTT SGSVVIDANW
RWVHEVGGYT NCYSGNTWDS SICSTDTTCA SECALEGATY ESTYGVTTSG SSLRLNFVTT
SSQKNIGSRL YLLADDSTYE TFKLLNREFT FDVDVSNLPC GLNGALYFVS MDADGGVSRF
PTNKAGAKYG TGYCDSQCPR DLKFIDGQAN IEGWEPSSTD VNAGTGNHGS CCPEMDIWEA
NSISSAFTAH PCDSVQQTMC TGDSCGGTYS DTADRYSGTC DPDGCDFNPY RLGNTNFYGP
GKTVDTSKPF TVVTQFITND GTDTGTLTEI RRLYVQNGVV IGNGPSTYTA ASGNSITESF
CEAEKTLFGD TNVFDTHGGL SAMGDALGDG MVLVLSLWDD HAADMLWLDS DYPTTSSATS
PGVARGTCPT TTGNATYVEA NYPNSYVTYS NIKFGALNST YSGTTSGGSS SSSTTLTTKA
STSTTSSKTT TTTSKTSTTS SSSTNVAQLY GQCGGQGWTG PTTCASGTCT KQNDYYSQCF
PLISAGISGK RHSIWSNIPV AKSSSLNFRK DFTQAPRSHP IIPQGHLTTH HATDVSAVIK
TMLIPNAKRV H
//
