EXGD_NEOFI
ID EXGD_NEOFI Reviewed; 834 AA.
AC A1DMX4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Probable glucan 1,3-beta-glucosidase D;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase D;
GN Name=exgD; ORFNames=NFIA_054930;
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: Glucosidase involved in the degradation of cellulosic
CC biomass. Active on lichenan (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; DS027698; EAW16145.1; -; Genomic_DNA.
DR RefSeq; XP_001258042.1; XM_001258041.1.
DR AlphaFoldDB; A1DMX4; -.
DR SMR; A1DMX4; -.
DR STRING; 36630.CADNFIAP00005040; -.
DR EnsemblFungi; EAW16145; EAW16145; NFIA_054930.
DR GeneID; 4584557; -.
DR KEGG; nfi:NFIA_054930; -.
DR VEuPathDB; FungiDB:NFIA_054930; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_4_0_1; -.
DR OMA; THQYTIF; -.
DR OrthoDB; 896412at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004338; F:glucan exo-1,3-beta-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; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell membrane; Cell wall biogenesis/degradation;
KW Glycoprotein; Glycosidase; Hydrolase; Membrane; Polysaccharide degradation;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..834
FT /note="Probable glucan 1,3-beta-glucosidase D"
FT /id="PRO_0000395169"
FT TOPO_DOM 1..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..834
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 600
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 705
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
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 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 834 AA; 94751 MW; 3C79949E1E4CB32F CRC64;
MPSHSRSRDR YGGRDSDREA RYDYDYARRR YATDDNDDDY DDDELEHGLN ERRYRRDGYL
PPRESRTRGY YERDAEGAAD EELLGDERNP GPRASRSYGH DYDARRGERS RAREAPRRSE
RHRDRDREGQ SRRRAYEDDG RHRTRDGRRE RGRESDAEAR RSRRREAGRE TAARKHQSSD
STNSASHLLS ADALARLGAQ YEKEERRKRE NAKDAAKAER KRQKKRAVVG EESRALRDPP
GESHRDRTKA RVASGAYLEE GRSPEMQVRH RGGGGPAMEA RWRKEGSWGG TMDDAGGGRP
FWKRKKWIGL GALILILVIV IPVAVVVSKK HDNKSDPADP QGTSPGKSNL DGLSHDSIPA
YAQGTYLDPW TWYDTTDFNV TFTNETVGGL SIMGLNSTWD DSARPNDNVP PLNEPFPYGS
QPIRGVNLGG WLSIEPFIVP SLFDSYSSVA GIIDEWTLSK RLGSSAARTL EKHYATFITE
QDFADIRDAG LDHVRIQYSY WAVATYDDDP YVAKISWRYL LRAIEYCRKY GLRVKLDPHG
IPGSQNGWNH SGREGVIGWL NGTDGELNRN RSLAVHDSVS KFFAQDRYKN IVTIYGLVNE
PLMLSLSVED VLDWTTEATK LVQKNGITAY VALHDGFLNL SKWKSMLKNR PDKMLLDTHQ
YTIFNTGQIG LNHTAKVNLI CNDWYNMIKE INSTSTGWGP TICGEWSQAD TDCAKYLNNV
GRGTRWEGTF SLTDSTQYCP TADTGPPCSC ANANADVSEY SADYKKFLQT YAEAQMSAFE
TGQGWFYWTW RTESAAQWSY RTAWKNGFMP AKAYAPSFKC GDAVPDFGNL PEYY
