ID   EGLC_ASPTN              Reviewed;         486 AA.
AC   Q0C7P6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=ATEG_10288;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476610; EAU29285.1; -; Genomic_DNA.
DR   RefSeq; XP_001218636.1; XM_001218635.1.
DR   AlphaFoldDB; Q0C7P6; -.
DR   SMR; Q0C7P6; -.
DR   STRING; 341663.Q0C7P6; -.
DR   GlyCosmos; Q0C7P6; 6 sites, No reported glycans.
DR   EnsemblFungi; EAU29285; EAU29285; ATEG_10288.
DR   GeneID; 4354731; -.
DR   VEuPathDB; FungiDB:ATEG_10288; -.
DR   eggNOG; ENOG502SI3D; Eukaryota.
DR   HOGENOM; CLU_028820_1_1_1; -.
DR   OMA; WDDVGCP; -.
DR   OrthoDB; 1110018at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR16631:SF13; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE EGLC-RELATED; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 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..463
FT                   /note="Probable glucan endo-1,3-beta-glucosidase eglC"
FT                   /id="PRO_0000395147"
FT   PROPEP          464..486
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395148"
FT   REGION          330..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..458
FT                   /note="Polar residues"
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           463
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   486 AA;  48753 MW;  F168A8CD88AF0DD4 CRC64;
     MQLTQLLALA LSLATSEAAY KGFNYGDKKP DGSSKYQADF ASEFETAQNL VGAPGFTSAR
     LYTMIQAGTA NDPISAIPAA IAQNTSLLLG LWASGNNMNN ELTALKAAIS QYGEDLSKLV
     VGISVGSEDL YRNSVLGQKV NAGVGVDPHV LASYIEEVRS TISGTPLSGA PLGHVDTWND
     WVNGSNAAVI DAVDWVGFDG YPYFQNTMAN SIDDAKALFN EAVAKTKSAA GNKEVWITET
     GWPVSGKTEN LAVASIPNAK RFWDEVGCPL FDNTNTWWYT LQDAFGASVP NPSFGIVGST
     LTTQPLFDLS CSKSNTTSSS AIASPTSTAA AAGGVAGGST GSASGSSTGT GSSSGSGSNS
     NTGAASGAVG AADRETSGTS GSANTNGTSG SGSGSNSTSG HGSNVTVPTR PTSVSNVSPS
     KSSSALFTGA ATSMGASPSS VGNVGPSKSS GAASPSSTTM FTGAATSVSA PVVHVVLLAL
     MMVIAA
//