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EXGD_ASPFN
ID   EXGD_ASPFN              Reviewed;         831 AA.
AC   B8NNK9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=AFLA_129100;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963481; EED48687.1; -; Genomic_DNA.
DR   RefSeq; XP_002382103.1; XM_002382062.1.
DR   AlphaFoldDB; B8NNK9; -.
DR   SMR; B8NNK9; -.
DR   STRING; 5059.CADAFLAP00009968; -.
DR   EnsemblFungi; EED48687; EED48687; AFLA_129100.
DR   VEuPathDB; FungiDB:AFLA_129100; -.
DR   eggNOG; ENOG502QRG8; Eukaryota.
DR   HOGENOM; CLU_004624_4_0_1; -.
DR   OMA; THQYTIF; -.
DR   Proteomes; UP000001875; 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   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..831
FT                   /note="Probable glucan 1,3-beta-glucosidase D"
FT                   /id="PRO_0000395163"
FT   TOPO_DOM        1..297
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..831
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        597
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        702
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        442
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        558
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        610
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        636
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        669
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        689
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   831 AA;  95079 MW;  9898B3C61F07541B CRC64;
     MPSHSRSRDR YRGERDPSRR YREVYDDDDD DDFDYHPRER RRYRRDDYQH DIRSHESPNY
     NDDLNEYDAA AEDPAVPLRS HDVEGRRRER SRAGESPIAS PSRRDRNRGG EEYRRHGTYG
     DGGSPTRAMR DRRHRSRDGQ RARPRDMDRE ARRQRRRERA RGAAAMKHKS SDSTNSGSHL
     LSADALAKLR SHYDEEDQRE RSQEQEQPRL ESKRQRKRPI VGDEPQALAP FPDETPRGQS
     KGRIVSGAYL EEGHPEMEVR HRGGGGPAME ARWRKEGNWD GTMEGSDAQP PFWKRKKWWI
     VIGVLVVVLA IVIPVAVVMS KKHGHDDDKS GSSSSVDNSD SPYISSLDGL SHDSIPESAQ
     GSILDPWTWY DTRDFNLTFT NETVGGLPIM GLNSTWDDST RPNDNVPPLN ESFPYGSQPI
     RGVNLGGWLS IEPFIVPSLF ENYSSKDRII DEYTLCKKLG SSAASTIEKH YADFISEQDF
     IDMRDAGLDH VRIQFSYWAV TTYDDDPYVA KISWRYLLRA IEYCRKYGLR VNLDPHGIPG
     SQNGWNHSGR EGVIGWLNGT DGQLNRQRSL DFHNQISQFF AQPRYKNVVT IYGLVNEPLM
     LSLPVEDVLN WTTDATKLVQ KNGISAYVTV HDGFLNLSKW KQMLKDRPDR MFLDTHQYTI
     FNTGQIVLNH TDRVKLICND WYNMIKEINT TSAGWGPTIC GEWSQADTDC AQYLNNVGRG
     TRWEGTFAIG DSTVYCPTAD TGPTCSCASA NAPPADYSDG YKKFLQTYAE AQMSAFGTAQ
     GWFYWTWHTE SAAQWSYKTA WKNGYMPKKA YAPDFKCGDD IPSFGDLPEY Y
 
 
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