EGLC_NEOFI
ID EGLC_NEOFI Reviewed; 450 AA.
AC A1DJ47;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=NFIA_000800;
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: 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; DS027697; EAW16736.1; -; Genomic_DNA.
DR RefSeq; XP_001258633.1; XM_001258632.1.
DR AlphaFoldDB; A1DJ47; -.
DR SMR; A1DJ47; -.
DR STRING; 36630.CADNFIAP00000372; -.
DR PRIDE; A1DJ47; -.
DR EnsemblFungi; EAW16736; EAW16736; NFIA_000800.
DR GeneID; 4585162; -.
DR KEGG; nfi:NFIA_000800; -.
DR VEuPathDB; FungiDB:NFIA_000800; -.
DR eggNOG; ENOG502SI3D; Eukaryota.
DR HOGENOM; CLU_028820_1_0_1; -.
DR OMA; TNTWWYI; -.
DR OrthoDB; 966331at2759; -.
DR Proteomes; UP000006702; 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; Reference proteome;
KW 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_0000395151"
FT PROPEP 428..450
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395152"
FT REGION 380..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 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 450 AA; 44878 MW; 1693931602240F26 CRC64;
MQFTQLVALA LALATSEAAH QGFNYGNTKS DGSAKSQSDF QAEFSTAKNL VGTSGFTSAR
LYTMIQGGTA NTPISAIPAA VAEETSLLLG LWASGGNFAN EIAALKTAIA DYGDDLAKLV
VGISVGSEDL YRNSVDGVKA KAGLGTNPDE IVSYINQVRS TIAGTKLSGA PIGHVDTWTA
WVNGSNSAVI DACDWLGFDG YPYFQNTMAN SISDAKALFD ESVAKTEAVA KGKEVWITET
GWPVSGNTEN LAVANLANAK TYWDEVGCPL FGKTNTWWYI LQDANPVTPN PSFGIVGSTL
STTPLFDLSC SASSSAAASS TAVPSASSVA GAKASGFATA AASSGAAGSA KPTFTVGKGP
GGSYNGTGFW NSTSSARPSS TAISGSSSGS ASGSSGSSGS GASGASGQSS SSTGSSSAPS
SSNILSNAAS GLSGSIFGAV VAVCLALAAL
