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Q2UUZ1

- EGLC_ASPOR

UniProt

Q2UUZ1 - EGLC_ASPOR

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Protein

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

Gene
eglC, AO090009000117
Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 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.

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 – 1281Nucleophile By similarity
Active sitei239 – 2391Proton donor By similarity

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. 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:AO090009000117
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 1

Subcellular locationi

Cell membrane; 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-SubCell
  3. extracellular region Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell wall, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 440422Probable glucan endo-1,3-beta-glucosidase eglCPRO_0000395145Add
BLAST
Propeptidei441 – 46323Removed in mature form Reviewed predictionPRO_0000395146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841N-linked (GlcNAc...) Reviewed prediction
Glycosylationi183 – 1831N-linked (GlcNAc...) Reviewed prediction
Glycosylationi312 – 3121N-linked (GlcNAc...) Reviewed prediction
Lipidationi440 – 4401GPI-anchor amidated glycine Reviewed prediction

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.

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Structurei

3D structure databases

ProteinModelPortaliQ2UUZ1.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi309 – 448140Ser-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5309.
HOGENOMiHOG000179527.
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.

Q2UUZ1-1 [UniParc]FASTAAdd to Basket

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MQLTHLLAFA LSLATSEAAY KGFNYGATKS DGSVKSQSDF ESEFSTAKNL    50
VGTSGFTSAR LYTMIQGGTT NSPISAIPAA IAENTSLLLG LWASGGGMDN 100
ELAALKSAIS QYGDSFAKLV VGISVGSEDL YRASSEGEKV NAGIGIGPDD 150
LVSFIKEVRS IISGTALSSV PIGHVDTWTA WTNGSNSAVI DAVDWLGFDG 200
YPYFQSSMSN SISDAKSLFD DSVAKTKAVA KGKEVWITET GWPVSGSTQN 250
LGVASLANAK TYWDEVGCPL FDETNTWWYI LQDANPTTPN PSFGVVGSTL 300
STTPLFDLSC SNSTRPSASA SSSAAGSATP VGSAVPSGSA AVNPSSSGIV 350
SSAVPSTTPG FTVGKGFRPS NSSAAAYYSS ASASGSAYPK FTKTASGSSA 400
TSTTAGSSSD SSSTNSGKSS SESSSTNSGA SASSSILATG GASSVSGSVF 450
GALVAVFAFV ATL 463
Length:463
Mass (Da):46,656
Last modified:January 24, 2006 - v1
Checksum:i0D6C9932A360FDA8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP007150 Genomic DNA. Translation: BAE54624.1.
RefSeqiXP_001816626.1. XM_001816574.2.

Genome annotation databases

EnsemblFungiiCADAORAT00003607; CADAORAP00003547; CADAORAG00003607.
GeneIDi5988556.
KEGGiaor:AOR_1_198184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP007150 Genomic DNA. Translation: BAE54624.1 .
RefSeqi XP_001816626.1. XM_001816574.2.

3D structure databases

ProteinModelPortali Q2UUZ1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00003607 ; CADAORAP00003547 ; CADAORAG00003607 .
GeneIDi 5988556.
KEGGi aor:AOR_1_198184.

Phylogenomic databases

eggNOGi COG5309.
HOGENOMi HOG000179527.
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. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiEGLC_ASPOR
AccessioniPrimary (citable) accession number: Q2UUZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 47 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

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

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