ID   EGLD_ASPFN              Reviewed;         367 AA.
AC   B8MXJ7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=AFLA_077840;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963472; EED57089.1; -; Genomic_DNA.
DR   RefSeq; XP_002372701.1; XM_002372660.1.
DR   AlphaFoldDB; B8MXJ7; -.
DR   SMR; B8MXJ7; -.
DR   EnsemblFungi; EED57089; EED57089; AFLA_077840.
DR   VEuPathDB; FungiDB:AFLA_077840; -.
DR   eggNOG; ENOG502RXMI; Eukaryota.
DR   HOGENOM; CLU_031730_0_0_1; -.
DR   OMA; YIDSPPN; -.
DR   Proteomes; UP000001875; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..367
FT                   /note="Probable endo-beta-1,4-glucanase D"
FT                   /id="PRO_0000394062"
FT   DOMAIN          329..365
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          21..235
FT                   /note="Catalytic"
FT   REGION          37..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..325
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        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        337..354
FT                   /evidence="ECO:0000250"
FT   DISULFID        348..364
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   367 AA;  38033 MW;  0C038474B7C681F3 CRC64;
     MKSSTFGMLA LAAAAKLVSA HATVHAVWIN DVDQGEGNSE SGYIRSPPSN SPITDVTSKD
     MTCNVNNKAT AKTLEVKAGD KITFEWHHDS RSDSDDIIAS SHKGPIMVYM APTEKGTAGN
     GWVKIAEDGY TDGTWAVDTL IKNRGKHSVT VPDVAAGEYL FRPEIIALHE GNRQGGAQFY
     MECVQVKVTS SGSKTLPEGV SIPGAYTATD KGILFDIYNS FDSYPFPGPA VWDGASGSSS
     SPSASASASA PAATSAAPAP SSFTTIAKQP ATSSTEAPST ENTSTTSTIV STTAAASATA
     PATPSSTSAI ASSAASTNSV PQPSSNAGGA VKEWYQCGGL NYKGSTQCEE GLTCKKWNPY
     YYQCISA