EGLD_ASPCL
ID EGLD_ASPCL Reviewed; 353 AA.
AC A1C4H2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=ACLA_059790;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS026990; EAW15312.1; -; Genomic_DNA.
DR RefSeq; XP_001276738.1; XM_001276737.1.
DR AlphaFoldDB; A1C4H2; -.
DR SMR; A1C4H2; -.
DR EnsemblFungi; EAW15312; EAW15312; ACLA_059790.
DR GeneID; 4708945; -.
DR KEGG; act:ACLA_059790; -.
DR VEuPathDB; FungiDB:ACLA_059790; -.
DR eggNOG; ENOG502RXMI; Eukaryota.
DR HOGENOM; CLU_031730_0_0_1; -.
DR OMA; YIDSPPN; -.
DR OrthoDB; 1307231at2759; -.
DR Proteomes; UP000006701; 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..353
FT /note="Probable endo-beta-1,4-glucanase D"
FT /id="PRO_0000394060"
FT DOMAIN 315..351
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 20..234
FT /note="Catalytic"
FT REGION 235..311
FT /note="Ser/Thr-rich linker"
FT REGION 266..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 323..340
FT /evidence="ECO:0000250"
FT DISULFID 334..350
FT /evidence="ECO:0000250"
SQ SEQUENCE 353 AA; 36822 MW; CA30252C3CAB5C4C CRC64;
MKSTFGLLAL AAAAKMAHAH ATVQAIWING VDQGAGNSAS GYIRSPPNNS PLVDVTSADM
TCNVNGKNPV AKTLPVKAGD KITFEWHHTD RSPSDDIIAS SHRGPIMVYM APTAKGAAGN
GWVKIAEEGY SNGKWAVDNL IANRGKHSIV VPDVPAGDYL FRPEIIALHE GNRLGGAQFY
MECVQVKVTS NGANALPAGV SIPGAYKATD PGVHFDIYNS FSSYPMPGPA VWNGASAAGS
APAPTAAPTQ KPVVTAAPTT LATLVKPTTT TAAAPAETDS CDGDDDDYET ETPAPQASAT
QAPAPQRPAP QTPSGSVKEW YQCGGINYTG AKNCESGLVC KEWNPYYHQC IKA
