ID M5C0X6_THACB Unreviewed; 508 AA.
AC M5C0X6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361164};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361164};
GN Name=cbhB {ECO:0000313|EMBL:CCO32610.1};
GN ORFNames=BN14_06673 {ECO:0000313|EMBL:CCO32610.1}, RSOLAG1IB_10160
GN {ECO:0000313|EMBL:CEL62047.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO32610.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO32610.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Isolate 7/3/14 {ECO:0000313|EMBL:CCO32610.1};
RA Jelonek L.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCO32610.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065},
RC and Isolate 7/3/14 {ECO:0000313|EMBL:CCO32610.1};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
RN [3] {ECO:0000313|EMBL:CEL62047.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL62047.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) 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; CAOJ01010121; CCO32610.1; -; Genomic_DNA.
DR EMBL; LN679159; CEL62047.1; -; Genomic_DNA.
DR AlphaFoldDB; M5C0X6; -.
DR STRING; 1108050.M5C0X6; -.
DR HOGENOM; CLU_020817_3_2_1; -.
DR Proteomes; UP000012065; Unassembled WGS sequence.
DR Proteomes; UP000059188; 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:UP000059188};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..508
FT /note="Glucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010503043"
FT DOMAIN 472..508
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 448..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 53846 MW; E9CD51951B9DDD74 CRC64;
MYSAVVLLSL YLAAVKAQQV GTNKAEVHPP LPWQKCTKSG GCVSQSNGKV VLDANWRWVH
TTTGYTNCYT GQKWDASICP DGATCAKNCA VDGADYSGTY GITTSGNALT LKFVTKGDGT
NVGSRVYLMA SDDTKYELFK LKNQEFTFDV DVSNLPCGLN GALYFSEMDA DGGLSKYPNN
KAGAKYGTGY CDAQCPKDIK FINGEANVAG WNGAPNDPNS GTGNYGTCCT EMDIWEANSM
ATAYTPHPCD VSGQTRCSGT QCSSYCDQPG CDFNSYRMGD KSYYGKGLTV DTNKKMTVVT
QFITSDGTAN GALTEIRRIY VQDGKVIQNS KTKVPGLDAY DSITDKFCSA QKTAFNDQNV
FGNKGGLATM DKSFTKGHVL VLSIWDDHAA NMLWLDSDYP VGANTNTPGV ARGACATTSG
VPSDVETNSP NASVTFSNIK FGDIGSTFGS SSGTPTTPTT SAPATTTTAS SGTVPHWGQC
GGIGYTGPTV CQSPYTCTKN GDYYSQCL
//
