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Q4WG16

- EGLC_ASPFU

UniProt

Q4WG16 - EGLC_ASPFU

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Protein

Probable glucan endo-1,3-beta-glucosidase eglC

Gene

eglC

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity).By similarity

Catalytic activityi

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei128 – 1281NucleophileBy similarity
Active sitei239 – 2391Proton donorBy similarity

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC
  2. hydrolase activity, acting on glycosyl bonds Source: ASPGD
  3. transferase activity, transferring glycosyl groups Source: ASPGD

GO - Biological processi

  1. carbohydrate metabolic process Source: ASPGD
  2. cell wall organization Source: UniProtKB-KW
  3. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glucan endo-1,3-beta-glucosidase eglC (EC:3.2.1.39)
Alternative name(s):
Endo-1,3-beta-glucanase eglC
Laminarinase eglC
Gene namesi
Name:eglC
ORF Names:AFUA_3G00270
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 3

Subcellular locationi

Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity. Secretedcell wall By similarity
Note: Covalently-linked GPI-modified cell wall protein.By similarity

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell wall Source: UniProtKB-KW
  3. extracellular region Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell wall, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 423405Probable glucan endo-1,3-beta-glucosidase eglCPRO_0000395142Add
BLAST
Propeptidei424 – 44623Removed in mature formSequence AnalysisPRO_0000395143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
Lipidationi423 – 4231GPI-anchor amidated asparagineSequence Analysis

Post-translational modificationi

The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).By similarity

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiQ4WG16.

Structurei

3D structure databases

ProteinModelPortaliQ4WG16.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi309 – 431123Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5309.
HOGENOMiHOG000179527.
InParanoidiQ4WG16.
KOiK01238.
OMAiTNTWWYI.
OrthoDBiEOG7TBCCK.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4WG16 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQFTHLVALA LALATSEAAH QGFNYGNTKS DGSAKSQADF QAEFSTAKNL
60 70 80 90 100
VGTSGFTSAR LYTMIQGGTA NTPISAIPAA ITEQTSLLLG LWASGGNFAN
110 120 130 140 150
EIAALKAAIA QYGDDLAKLV VGISVGSEDL YRNSVDGVKA NAGIGTNPDE
160 170 180 190 200
IVSYINEVRS TIAGTKLSGA PIGHVDTWTA WVNGSNSAVI DACDWLGFDG
210 220 230 240 250
YPYFQNTMAN SISDAKALFD ESVAKTQAVA KGKEVWITET GWPVSGKTEN
260 270 280 290 300
LAVANLANAK TYWDEVGCPL FGKTNTWWYI LQDADPVTPN PSFGIVGSTL
310 320 330 340 350
STTPLFDLSC SASSSSSAAA AASSTAGPSA SSVIGGKASG FTTAAANSAK
360 370 380 390 400
PTFTVGKGPG GSYNGTGFWN STSSARPSSS AISGSSSGSA AGSSGAGASG
410 420 430 440
ASGQSSSSTG SSSAPSTSNI LSNAASGLSG SIFGAVVAVC LALAAL
Length:446
Mass (Da):44,651
Last modified:July 5, 2005 - v1
Checksum:iBC92A444453E63B3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000010 Genomic DNA. Translation: EAL86311.1.
RefSeqiXP_748349.1. XM_743256.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00000272; CADAFUAP00000272; CADAFUAG00000272.
GeneIDi3506119.
KEGGiafm:AFUA_3G00270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000010 Genomic DNA. Translation: EAL86311.1 .
RefSeqi XP_748349.1. XM_743256.1.

3D structure databases

ProteinModelPortali Q4WG16.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q4WG16.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00000272 ; CADAFUAP00000272 ; CADAFUAG00000272 .
GeneIDi 3506119.
KEGGi afm:AFUA_3G00270.

Phylogenomic databases

eggNOGi COG5309.
HOGENOMi HOG000179527.
InParanoidi Q4WG16.
KOi K01238.
OMAi TNTWWYI.
OrthoDBi EOG7TBCCK.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiEGLC_ASPFU
AccessioniPrimary (citable) accession number: Q4WG16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: October 29, 2014
This is version 57 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