ID A0A428UQS3_9HYPO Unreviewed; 506 AA.
AC A0A428UQS3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361164};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361164};
GN ORFNames=CEP52_000039 {ECO:0000313|EMBL:RSM16628.1};
OS Fusarium oligoseptatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM16628.1, ECO:0000313|Proteomes:UP000287144};
RN [1] {ECO:0000313|EMBL:RSM16628.1, ECO:0000313|Proteomes:UP000287144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM16628.1,
RC ECO:0000313|Proteomes:UP000287144};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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}.
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:RSM16628.1}.
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DR EMBL; NKCK01000001; RSM16628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428UQS3; -.
DR STRING; 1325735.A0A428UQS3; -.
DR Proteomes; UP000287144; 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:UP000287144};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..506
FT /note="Glucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018997847"
FT DOMAIN 470..506
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 406..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 54599 MW; 7DAFACE3740CF5E5 CRC64;
MYRVLATASA LLATARAQQA CTLNTENKPA LTWAKCTSSG CSNVQGSVVV DANWRWTHST
SSSTNCYTGN EWDKTLCPDG KTCADKCCLD GADYSGTYGV TSSGNQLNLK FVTVGPYSTN
VGSRLYLMQD ENNYQMFDLL GNEFTFDVDV NNIGCGLNGA LYFVSMDKDG GKSRYSTNKA
GAKYGTGYCD AQCPRDVKFI NGVANSDEWE PSDSDKNAGV GKYGTCCPEM DIWEANKIST
AYTPHPCKSL TQESCEGDAC GGTYSTTRYA GTCDPDGCDF NPYRQGNKTF YGPGSNFNID
TTKKVTVVTQ FIKGSDGKLS EIKRLYVQNN KVIGNPESEI VGNTGSTITD SFCKAQKVAF
GDPDDFNKKG GWSGMSDALA KPMVLVMSLW HDHYANMLWL DSTYPEGSTT PGSARGSCPQ
DSGDPDTLEK EVPNSSVSFS NIKFGPIGST YSGDGSTDPE EPEEPEEPVG TVPQYGQCGG
INYSGPTACV SPYKCNKIND YYSQCY
//
