ID   EGLD_ASPFC              Reviewed;         349 AA.
AC   B0Y9G4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Probable endo-beta-1,4-glucanase D;
DE            Short=Endoglucanase D;
DE            EC=3.2.1.4;
DE   AltName: Full=Carboxymethylcellulase D;
DE   AltName: Full=Cellulase D;
DE   Flags: Precursor;
GN   Name=eglD; ORFNames=AFUB_080950;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC       glycosidic bonds, like in carboxymethylcellulose (CMC),
CC       hydroxyethylcellulose (HEC) and beta-glucan. Involved in the
CC       degradation of complex natural cellulosic substrates (By similarity).
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family. {ECO:0000305}.
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DR   EMBL; DS499600; EDP48657.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y9G4; -.
DR   SMR; B0Y9G4; -.
DR   EnsemblFungi; EDP48657; EDP48657; AFUB_080950.
DR   VEuPathDB; FungiDB:AFUB_080950; -.
DR   HOGENOM; CLU_031730_0_0_1; -.
DR   PhylomeDB; B0Y9G4; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005103; AA9.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   Pfam; PF03443; AA9; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..349
FT                   /note="Probable endo-beta-1,4-glucanase D"
FT                   /id="PRO_0000394061"
FT   DOMAIN          311..347
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          20..235
FT                   /note="Catalytic"
FT   REGION          233..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..307
FT                   /note="Ser/Thr-rich linker"
FT   ACT_SITE        164
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        210
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        319..336
FT                   /evidence="ECO:0000250"
FT   DISULFID        330..346
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   349 AA;  35763 MW;  19610E8678EA60AE CRC64;
     MKSTFGLLAL AAAAKLVSAH ATVHAVWIND VDQGAGNSAD GYIRSPPNNS PITDVTSTDM
     TCNVNGKNPV AKTLSVKAGD KVTFEWHHDT RSDSDDIIAS SHMGPVMVYM APTEKGTAGN
     GWVKIAEEGY SNGKWAVANL IANRGKHSIT VPDVPAGEYL LRPEIIALHE GNRQGGAQFY
     MECVQVKVTS AGTKTLPAGV SIPGAYKATD PGVLFDMYNS FTSYPIPGPA VWDGSSSGSS
     GSSGSSPATT TAPAVSVTAV PTKEAPVDTS ATPTTFVTAT KPATTAAPAA PSASSGSNSG
     SDSCNSGSAS GSVKIYGQCG GQNYSGPTSC EAGLICKEWN PYYHQCVSA