ID   EGLC_ASPFC              Reviewed;         450 AA.
AC   B0XXF8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
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=AFUB_048180;
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: 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; DS499596; EDP53632.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XXF8; -.
DR   SMR; B0XXF8; -.
DR   PRIDE; B0XXF8; -.
DR   EnsemblFungi; EDP53632; EDP53632; AFUB_048180.
DR   VEuPathDB; FungiDB:AFUB_048180; -.
DR   HOGENOM; CLU_028820_0_2_1; -.
DR   PhylomeDB; B0XXF8; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; SSF51445; 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; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..427
FT                   /note="Probable glucan endo-1,3-beta-glucosidase eglC"
FT                   /id="PRO_0000395140"
FT   PROPEP          428..450
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395141"
FT   REGION          377..420
FT                   /note="Disordered"
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           427
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        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   450 AA;  44943 MW;  F687F0613C6FA2B5 CRC64;
     MQFTHLVALA LALATSEAAH QGFNYGNTKS DGSAKSQADF QAEFSTAKNL VGTSGFTSAR
     LYTMIQGGTA NTPISAIPAA ITEQTSLLLG LWASGGNFAN EIAALKAAIA QYGDDLAKLV
     VGISVGSEDL YRNSVDGVKA NAGIGTNPDE IVSYINEVRS TIAGTKLSGA PIGHVDTWTA
     WVNGSNSAVI DACDWLGFDG YPYFQNTMAN SISDAKALFD ESVAKTQAVA KGKEVWITET
     GWPVSGKTEN LAVANLANAK TYWDEVGCPL FGKTNTWWYI LQDADPVTPN PSFGIVGSTL
     STTPLFDLSC SASSSSSAAA SSTAGPSASS VIGGKASGFT TAAANSAKPT FTVGKGPGGS
     YNGTGFWNST SSARPSSSAI SGSSSGSAAG SSGSSGSSGS GASGASGQSS SSTGSSSAPS
     TSNILSNAAS GLSGSICGAV VAVCLALAAL