ID A0A2C5WVR3_9PEZI Unreviewed; 567 AA.
AC A0A2C5WVR3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361164};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361164};
GN Name=cbh-1 {ECO:0000313|EMBL:PHH52909.1};
GN ORFNames=CFIMG_005662RA {ECO:0000313|EMBL:PHH52909.1};
OS Ceratocystis fimbriata CBS 114723.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH52909.1, ECO:0000313|Proteomes:UP000222788};
RN [1] {ECO:0000313|EMBL:PHH52909.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH52909.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT "Analysis of microsatellite markers in the genome of the plant pathogen
RT Ceratocystis fimbriata.";
RL Fungal Biol. 117:545-555(2013).
RN [2] {ECO:0000313|EMBL:PHH52909.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH52909.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT the plant pathogen, Ceratocystis fimbriata.";
RL IMA Fungus 4:357-358(2013).
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:PHH52909.1}.
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DR EMBL; APWK03000054; PHH52909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5WVR3; -.
DR STRING; 1035309.A0A2C5WVR3; -.
DR OrthoDB; 3014058at2759; -.
DR Proteomes; UP000222788; 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:UP000222788};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..567
FT /note="Glucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012790246"
FT DOMAIN 531..567
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 450..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 58954 MW; 150177D71CD156C7 CRC64;
MYGQKLSVLA TLVATVRAQQ ACSLTAETHP SMNWQQCTTA GCDTVKGGIT VDANWRWTHE
VSSSTNCYTG NTWSSTCTNG TTCAEKCCVD GADYSGTYGA TTTDDSLSLS FVTKGAYSTN
VGSRMYMMAD ENKYQMFQLL GKEFTFDVDV SNLGCGLNGA LYFVSMDEDG GMSKYPGNKA
GAKYGTGYCD SQCPRDIKFI GGVANSDEWT PSSTDANAGI GGMGSCCSEM DIWEANKMAT
AYTPHPCNTI GQKTCQGDAC GGTYSGQRYG DNCDPDGCDF NSYRMGDTEF FGAGKKIDST
KKVTVVTQFI KGSDGKLADI KRFYVQDGVT FENSESKISG VSGNSINEEF CSAQKKAFGD
KDSFTSSGGL AQMGAALEQG MVLVMSLWDD NYASMLWLDS TYPVDSTAAG SARGECSTSS
GKPSDIRASD ANSKVIFSNI KFGDIGTTFT APSGSTSPST DNSGSSSSAA SSSYPAAATA
PSSAPSSSKV AAAAVTPEAV TPAAPVNQKA STPAGSASTP ASNPASGSAS DAIPRYGKCG
GGDYSGSSNC VQGTTCKVMN PYYSQCI
//
