ID A0A0K6GBN2_9AGAM Unreviewed; 411 AA.
AC A0A0K6GBN2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Endo-beta-1,4-glucanase D {ECO:0000256|RuleBase:RU368122};
DE Short=Endoglucanase D {ECO:0000256|RuleBase:RU368122};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU368122};
DE AltName: Full=Carboxymethylcellulase D {ECO:0000256|RuleBase:RU368122};
DE AltName: Full=Cellulase D {ECO:0000256|RuleBase:RU368122};
GN ORFNames=RSOLAG22IIIB_06070 {ECO:0000313|EMBL:CUA75789.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA75789.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA75789.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA75789.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC glycosidic bonds. Involved in the degradation of complex natural
CC cellulosic substrates. {ECO:0000256|RuleBase:RU368122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|RuleBase:RU368122};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU368122}.
CC -!- DOMAIN: Has a modular structure: an endo-beta-1,4-glucanase catalytic
CC module at the N-terminus, a linker rich in serines and threonines, and
CC a C-terminal carbohydrate-binding module (CBM). The genes for catalytic
CC modules and CBMs seem to have evolved separately and have been linked
CC by gene fusion. {ECO:0000256|RuleBase:RU368122}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family.
CC {ECO:0000256|ARBA:ARBA00009585}.
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DR EMBL; CYGV01001611; CUA75789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K6GBN2; -.
DR Proteomes; UP000044841; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030248; F:cellulose binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd21175; LPMO_AA9; 1.
DR Gene3D; 2.70.50.70; -; 1.
DR InterPro; IPR005103; AA9.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR PANTHER; PTHR33353:SF6; ENDOGLUCANASE IV; 1.
DR PANTHER; PTHR33353; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12560)-RELATED; 1.
DR Pfam; PF03443; AA9; 1.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU368122};
KW Cellulose degradation {ECO:0000256|RuleBase:RU368122};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU368122};
KW Glycosidase {ECO:0000256|RuleBase:RU368122};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368122};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU368122};
KW Reference proteome {ECO:0000313|Proteomes:UP000044841};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368122};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368122}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..411
FT /note="Endo-beta-1,4-glucanase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005503254"
FT DOMAIN 373..409
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 239..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 41692 MW; 56FE6AE314ED3EDC CRC64;
MLAEVAFAFL SVASSVLAHG NLQEIVVENP PATYIPWLPF QDPYKPTAPE RVGRKIPDSG
PVEDVTSIDI QCNKGAVPAA LIATAAAGSK VALNWTEWPT SHIGPVITYL AQAPSDITQW
SPGTDKVWFK IDEAGLDNGK WAATDVLLSQ NGLWTVTIPQ NLKPGQYLMR HEIIALHAAQ
NYPGAQFYPS CIQFEITGSG SALPNDSDLV AFPGAYSGTD PGVKYNPYAG ATTYPIPGPP
VWDGTGSGTG SGGSGAPSSS AAAPSSSAEV SSTAEESSTA EASSTAAASS TLVASNTIVA
PSSSVAVTET AGAPVETGAP TESEAPTETE TGAPISTPVA TSTAAVSSAA PASSSVAAPS
SVVTAPSTPT SGSGAALYAQ CGGMNFNGPK GCVAPYTCKD WNPYYSQCVQ A
//
