EXGD_ASPTN
ID EXGD_ASPTN Reviewed; 838 AA.
AC Q0CHZ8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=ATEG_06686;
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: 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; CH476602; EAU33230.1; -; Genomic_DNA.
DR RefSeq; XP_001215864.1; XM_001215864.1.
DR AlphaFoldDB; Q0CHZ8; -.
DR SMR; Q0CHZ8; -.
DR STRING; 341663.Q0CHZ8; -.
DR EnsemblFungi; EAU33230; EAU33230; ATEG_06686.
DR GeneID; 4322028; -.
DR VEuPathDB; FungiDB:ATEG_06686; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_4_0_1; -.
DR OMA; THQYTIF; -.
DR OrthoDB; 896412at2759; -.
DR Proteomes; UP000007963; 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..838
FT /note="Probable glucan 1,3-beta-glucosidase D"
FT /id="PRO_0000395167"
FT TOPO_DOM 1..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..838
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 604
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 709
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 838 AA; 96217 MW; B2070EDC943C81AB CRC64;
MPSHSRSRDR YRGRDESEPE RDRRHYSRRR YRETDYEDDE LDDDDYDRRR RYRRDDVYRR
SRGQSRGYES HEYHEDDANE YDLAGEDPAV PLRRSRGDER ERSAGAYDDY DSPRRRDRHR
DGDRRRRHRA YEAEGSPPRG APDHRRHRSR DDRRERAYES EREARRHRRR ERGREAAAAK
HQSSDSTNSG SHLLSADALA KLRSEYDKED RSRAKADAKA EKKQRRKRPV VADQPRRLDP
FPEETPRGQS KGRIVSGAYL EEGRSPEMKV RHRGGGGGGG AGSKWRDEGA SDSDMDGAEG
GTPFWKKKKT WIAVGVVVVL LAIIIPVAVV VSKKNNEKKS DSTTDDTTPR NSNLDGISRD
SIPDYAKGTV LDPWTWYDTM GFNVTFTNET VGGLSIMGLN STWDDSTRPN DNVPPLNEPF
PYGSQPIRGV NLGGWLSIEP FIVPSLFESY SSVDGVVDEW TLCQKLGDSA ASRIERHYAT
FITEQDFADI RDAGLDHVRI QFSYWAVTTY DGDQYVPKIS WRYLLRAIEY CRKYGLRVKL
DPHGIPGSQN GWNHSGRQGP IGWLNGTDGQ LNRKRSLEMH DQLSQFFAQD RYKNIVTIYG
LVNEPMMLSL PVEDVLDWST EATKLIQKNG ITAYVTVHDG FLNLSKWKQM LKTRPDRMFL
DTHQYTIFNT AQIVMKHTEK IKLVCNDWHS MIQQINTTSA GWGPTICGEW SQADTDCTKY
LNNVGRGTRW EGTFSLTDST AYCPTAKSGP SCSCSSANAD PSQYSDQYKK FLKTYAEAQM
SAFETAQGWF YWTWHTESAP QWSYKTAWKN GFMPQKAYAP DFKCGDDVPD FGDLPENY
