ID   EGLD_NEOFI              Reviewed;         348 AA.
AC   A1DBS6;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=NFIA_099510;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027694; EAW20316.1; -; Genomic_DNA.
DR   RefSeq; XP_001262213.1; XM_001262212.1.
DR   AlphaFoldDB; A1DBS6; -.
DR   SMR; A1DBS6; -.
DR   EnsemblFungi; EAW20316; EAW20316; NFIA_099510.
DR   GeneID; 4588579; -.
DR   KEGG; nfi:NFIA_099510; -.
DR   VEuPathDB; FungiDB:NFIA_099510; -.
DR   eggNOG; ENOG502RXMI; Eukaryota.
DR   HOGENOM; CLU_031730_0_0_1; -.
DR   OMA; YIDSPPN; -.
DR   OrthoDB; 1307231at2759; -.
DR   Proteomes; UP000006702; 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;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..348
FT                   /note="Probable endo-beta-1,4-glucanase D"
FT                   /id="PRO_0000394068"
FT   DOMAIN          310..346
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          20..234
FT                   /note="Catalytic"
FT   REGION          233..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..311
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        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        318..335
FT                   /evidence="ECO:0000250"
FT   DISULFID        329..345
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   348 AA;  35569 MW;  3126BF3D4DC88161 CRC64;
     MKSTFGLLAL AAAAKLVSAH ATVHAVWIND VDQGAGNSAD GYIRTPPNNS PITDVTSADM
     TCNVNGKNSV AKTLSVKAGD KVTFEWHHDS RSASDDIIAS SHMGPVMVYM APTEKGTAGN
     GWVKIAEEGY SNGKWAVANL IANKGKHSIT VPDVPAGEYL LRPEIIALHE GNRQGGAQFY
     MECVQVKVTS AGTKTLPAGV SIPGAYKATD PGVLFDMYNS FTSYPIPGPA VWDGSSSGSS
     GSSDSSPATT APEASVTSAP TKQGSADTSA SPTTFVTATK PTTTAAPAAP PASTGSNSGS
     GSSGSGSASG SVKIYQQCGG KNYSGATSCE AGLTCKEWNP YYHQCLKA