ID A0A166I3V3_9AGAM Unreviewed; 370 AA.
AC A0A166I3V3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SISSUDRAFT_1057768 {ECO:0000313|EMBL:KZT43365.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT43365.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT43365.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT43365.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV428008; KZT43365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166I3V3; -.
DR STRING; 1314776.A0A166I3V3; -.
DR Proteomes; UP000076798; 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:SF9; ENDOGLUCANASE II; 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:UP000076798};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368122};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368122}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..370
FT /note="Endo-beta-1,4-glucanase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007875009"
FT DOMAIN 334..370
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 233..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 37685 MW; 99CCAC893D9733FD CRC64;
MLFYSAVIAA SIASVAAHAT FQELWINGVD QGGYCVRAPQ SNSPVTSVTS NDIACNVNAN
PSPGTCAINA GDTLTVEMHQ QPGDRSCADE AIGGAHYGPI NIYLAKVADA SSAVGSSAAW
FKISEMGLPS SDPDYWATEV LNDNCGHYTF KVPSDIAPGQ YLLRAEVIAL HVASSVGGAQ
FYMSCYQITI GGSGSAAPPT VSIPGTYNAN DPGILINIYT QLNTYQIPGP SPYGTTSPTV
ATTPWPTTAT WNTAGQPSTD PTTPPAGSGS KTTTSSSTSS TSTSKSTTTT TTSSTTTTTS
STSKSTSTTT SSSTKTTSTT SSTTKTTTST ASGATQTKYG QCGGIGWSGP TTCASGSTCT
VGNAYYSQCL
//