EXGD_ASPCL
ID EXGD_ASPCL Reviewed; 830 AA.
AC A1CTI3;
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=ACLA_083150;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW06620.1; -; Genomic_DNA.
DR RefSeq; XP_001268046.1; XM_001268045.1.
DR AlphaFoldDB; A1CTI3; -.
DR SMR; A1CTI3; -.
DR STRING; 5057.CADACLAP00007666; -.
DR EnsemblFungi; EAW06620; EAW06620; ACLA_083150.
DR GeneID; 4700413; -.
DR KEGG; act:ACLA_083150; -.
DR VEuPathDB; FungiDB:ACLA_083150; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_4_2_1; -.
DR OMA; THQYTIF; -.
DR OrthoDB; 896412at2759; -.
DR Proteomes; UP000006701; 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..830
FT /note="Probable glucan 1,3-beta-glucosidase D"
FT /id="PRO_0000395161"
FT TOPO_DOM 1..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..830
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..247
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 701
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 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 830 AA; 94264 MW; 6B3691C5BBE14B90 CRC64;
MPSQSRSRDR YRGRDTEYTR RRYPDEHDYS HDDHDYDYDD DDDDNDDLEQ DVTERRYRRD
GYRRPRGESR ARAYYERDAA AAAAHDEELL AEERERRRAG ASGSPRKSGQ HRERDRDRER
DREAQSRRRT YEDDGRHRTR DGRRERRREG GGEGGRRERR RGESRRGEAA RKHQSSDSTN
SASHLLSADA LARLGSQYEK EDRRERAHAK DAAKAERKRR KKRAVVGEQE RGLRAEKPRD
RSRARVASGA YMEEGRGPEM EFRRRGGGGP PMDARWPKGG GWGGSVDGGD AGRPFWKQKK
WLIGIGVVIL ILVIVIPVAV VVSKKHNDKP NATTTQPDGT TPSNSNLDGL SPDSIPGYAK
GTFLDPWTWY DTNDFNVTFT NETVGGLSLM GLNSTWDDSA RPNDNVPPLN KPFPYGKQPI
RGVNLGGWLS LEPFITPSFF QSYSALSGVI DEYTLTQKLG STAGARLEKH YATFITEQDF
ADIRDAGLDH VRIQYSYWAV TTYDGDPYVA KTSWRYLLRA IEYCRKYGLR VKLDPHGIPG
SQNGWNHSGR QGAIGWLNGT DGELNRKRSL EVHDQVSKFF AQDRYKNVVT IYGLVNEPLM
LSLSVEDVLN WTVEATKLVQ KNGITAYIAL HDGFLNLSKW KSILKTRPDN MLLDTHQYTI
FNTGQIVLNH TARVNLICND WSAMIKEVNS TSGFGPTICG EWSQADTDCA QYLNNVGRGT
RWEGTFSLTD STQYCPTADS GPRCSCANAN ADPSAYSADY KKFLQTYAEA QMSAFETGQG
WFYWTWRTES AAQWSYRTAW KGGFMPQKAY SPSFKCGDTV PDFGSLPEYY
