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Protein

Probable glucan 1,3-beta-glucosidase D

Gene

exgD

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan (By similarity).By similarity

Catalytic activityi

Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei599 – 5991Proton donorBy similarity
Active sitei704 – 7041NucleophileBy similarity

GO - Molecular functioni

  1. glucan endo-1,6-beta-glucosidase activity Source: EnsemblFungi
  2. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. fungal-type cell wall beta-glucan biosynthetic process Source: EnsemblFungi
  3. polysaccharide catabolic process Source: UniProtKB-KW
  4. regulation of cell shape Source: EnsemblFungi
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glucan 1,3-beta-glucosidase D (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase D
Gene namesi
Name:exgD
ORF Names:AFUA_6G09250
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530 Componenti: Chromosome 6

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 305305CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei306 – 32621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini327 – 833507ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: EnsemblFungi
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 833833Probable glucan 1,3-beta-glucosidase DPRO_0000395164Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi383 – 3831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi560 – 5601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi638 – 6381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi671 – 6711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi691 – 6911N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00002365.

Structurei

3D structure databases

ProteinModelPortaliQ4WMP0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 176171Arg-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ4WMP0.
KOiK01210.
OMAiNIITHYG.
OrthoDBiEOG7ZPNTV.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q4WMP0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTHSRSRDR YGGRDSDREA RYDYDYARRR YATDDDDDYD DDELEHDLTE
60 70 80 90 100
RRYRRDGYRP PRESRARGYY ERDAEGAADE ELLGNERDPG PRASRSYGDD
110 120 130 140 150
YDARRREHSR AREAPRRSER HRDRDREGRS RRRAYEDDGR HRTRDGRRDR
160 170 180 190 200
GRESDGEARR SRRREAGRET AARKHRSSDS TNSASHLLSA DALAKLGAQY
210 220 230 240 250
EKEERRKREI AKDAAKAERK RQKKLAVVGE ETRALRDPPG ESHRDRTKAR
260 270 280 290 300
VASGAYLEEG RSPEMRVRHR GGGGPAMEAR WRKEGSWGGT MDDSGGGRPF
310 320 330 340 350
WKRKRWIGLG ALIIILVIVI PVAVVVSKKH DNKSDPADSQ GTSPGKSNLD
360 370 380 390 400
GLSHDSIPAY AQGTYLDPWT WYDTTDFNVT FTNETVGGLS IMGLNSTWDD
410 420 430 440 450
SARPNDNVPP LNEPFPYGSQ PIRGVNLGGW LSIEPFIVPS LFDSYSSVSG
460 470 480 490 500
IIDEWTLSKR LGSSAASTLE KHYATFITEQ DFADIRDAGL DHVRIQYSYW
510 520 530 540 550
AVATYDDDPY VAKISWRYLL RAIEYCRKYG LRVNLDPHGI PGSQNGWNHS
560 570 580 590 600
GREGVIGWLN GTDGELNRNR SLAVHDSVSK FFAQDRYKNI VTIYGLVNEP
610 620 630 640 650
LMLSLSIEDV LDWTTEATKL VQKNGITAYV ALHDGFLNLS KWKSMLKNRP
660 670 680 690 700
DKMLLDTHQY TIFNTGQIGL NHTAKVNLIC NDWYNMIKEI NSTSTGWGPT
710 720 730 740 750
ICGEWSQADT DCAKYLNNVG RGTRWEGTFS LTDSTQYCPT ADTGPPCSCA
760 770 780 790 800
NANADVSKYS ADYKKFLQTY AEAQMSAFET GQGWFYWTWR TESAAQWSYR
810 820 830
TAWKNGFMPA KAYAPSFRCG DAVPDFGDLP EYY
Length:833
Mass (Da):94,775
Last modified:July 5, 2005 - v1
Checksum:i6A08231B6A8A1855
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL88774.1.
RefSeqiXP_750812.1. XM_745719.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00002365; CADAFUAP00002365; CADAFUAG00002365.
GeneIDi3508103.
KEGGiafm:AFUA_6G09250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL88774.1.
RefSeqiXP_750812.1. XM_745719.1.

3D structure databases

ProteinModelPortaliQ4WMP0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5085.CADAFUAP00002365.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00002365; CADAFUAP00002365; CADAFUAG00002365.
GeneIDi3508103.
KEGGiafm:AFUA_6G09250.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ4WMP0.
KOiK01210.
OMAiNIITHYG.
OrthoDBiEOG7ZPNTV.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiEXGD_ASPFU
AccessioniPrimary (citable) accession number: Q4WMP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: April 1, 2015
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.