ID   EGLC_ASPCL              Reviewed;         453 AA.
AC   A1CD22;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   04-NOV-2026, entry version 83.
DE   RecName: Full=Probable glucan endo-1,3-beta-glucosidase eglC;
DE            EC=3.2.1.39;
DE   AltName: Full=Endo-1,3-beta-glucanase eglC;
DE   AltName: Full=Laminarinase eglC;
DE   Flags: Precursor;
GN   Name=eglC; ORFNames=ACLA_064000;
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 / QM 1276
RC   / 107;
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: Glucanases play a role in cell expansion during growth, in
CC       cell-cell fusion during mating, and in spore release during
CC       sporulation. This enzyme may be involved in beta-glucan degradation and
CC       also function biosynthetically as a transglycosylase (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
CC       Note=Covalently-linked GPI-modified cell wall protein. {ECO:0000250}.
CC   -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC       reticulum and serves to target the protein to the cell surface. There,
CC       the glucosamine-inositol phospholipid moiety is cleaved off and the
CC       GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC       glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; DS027050; EAW12429.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1CD22; -.
DR   SMR; A1CD22; -.
DR   STRING; 344612.A1CD22; -.
DR   GlyCosmos; A1CD22; 4 sites, No reported glycans.
DR   EnsemblFungi; EAW12429; EAW12429; ACLA_064000.
DR   KEGG; act:ACLA_064000; -.
DR   VEuPathDB; FungiDB:ACLA_064000; -.
DR   eggNOG; ENOG502SI3D; Eukaryota.
DR   HOGENOM; CLU_028820_1_1_1; -.
DR   OMA; AAHQTHW; -.
DR   OrthoDB; 77201at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR   GO; GO:0009277; C:fungal-type cell wall; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:TreeGrafter.
DR   FunFam; 3.20.20.80:FF:000233; Probable glucan endo-1,3-beta-glucosidase eglC; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR050732; Beta-glucan_modifiers.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR16631:SF13; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE EGLC-RELATED; 1.
DR   Pfam; PF29664; BtgE-BtgC_glyc-hydro; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell membrane; Cell wall;
KW   Cell wall biogenesis/degradation; Glycoprotein; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..430
FT                   /note="Probable glucan endo-1,3-beta-glucosidase eglC"
FT                   /id="PRO_0000395138"
FT   PROPEP          431..453
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395139"
FT   REGION          370..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..402
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..423
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        239
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   LIPID           430
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   453 AA;  45031 MW;  0A1ACC08C6AA896A CRC64;
     MQTRQLLALA LAVAATEAAH QGFNYGNTKS DGSAKSQSDF AAEFSTAKNL VGTSGFTSAR
     LYTMIQGGTS ATPISAIPAA IAEDTSLLLG IWASGGNVAN EIAALKAAIA QYGADFGKHV
     VGISVGSEDL YRNSVDGVKS KAGLGANPDD LVSYIHQVRE AIAGTSLSGA PIGHVDTWTA
     WVNGSNSAVI DACDWLGFDG YPYFQNTMPN SISDAKALFD ESVAKTQAVA KGKEVWITET
     GWPVSGKTEN LAVANTANAK AYWDQVGCPL FGNTNTWWYI LQDADPVTPN PSFGIVGSTL
     STTPLFDLSC SAVSSSSAVP SATAAATAAS GAGASGSQTS GFATAAAGSS SAAKPTFSVG
     KGPNGSYNGT YPGSWNSTRP GANGGSSGSS GSSGSSGSSG SSGSSGSGAS GHSSSTGSSS
     FPSSTNLLSN SASGLSGSLF GAVAAVFVAL AAL
//