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A2QN74

- BTGC_ASPNC

UniProt

A2QN74 - BTGC_ASPNC

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Protein

Putative glucan endo-1,3-beta-glucosidase btgC

Gene

btgC

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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. Active on laminarin and lichenan 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 sitei586 – 5861NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative glucan endo-1,3-beta-glucosidase btgC (EC:3.2.1.39)
Alternative name(s):
Endo-1,3-beta-glucanase btgC
Laminarinase btgC
Gene namesi
Name:btgC
ORF Names:An07g04650
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 4L

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 684684Putative glucan endo-1,3-beta-glucosidase btgCPRO_0000395125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi455 – 4551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi474 – 4741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 302302CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini324 – 684361ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei303 – 32321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi245 – 358114Gly-richAdd
BLAST
Compositional biasi337 – 34610Poly-Ser

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5309.
HOGENOMiHOG000173877.
OrthoDBiEOG7P8PHC.

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.

A2QN74-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MAGVNRSFSY SRGDDALLRD DEREISPLRS AEDGLYSTSY GDVSPLSAGV
60 70 80 90 100
QAQNRPFDRG LVSVPEGQTL ERHMTSTPGM DNLGPASVGG GISGIALGVA
110 120 130 140 150
NSHNRQSGVD AFRETDVPVR NLPAERDFNT TGSDNPYIPA PPDGDIYPSS
160 170 180 190 200
EAVRYRDSYS SHTGLGAGAP FAEHSTPGTT PSQRSFFDSP YQGVDAGPYQ
210 220 230 240 250
RHSAYSSHDY PLVINPDDIA DDGDDGFPVH PKGAADYRSN ANVPGTGVAG
260 270 280 290 300
AAAAGGFLGK FRALFKREEP SPFYDSDIGG GLGGAEKAQG GRHIIGGGSR
310 320 330 340 350
KRGWIVGLIL AAVIVAAIVG GAVGGILGHQ EHDGDTSSSS SSSSSSGTGS
360 370 380 390 400
GGSDKGDGLL DKDSDEIKAL MNNKNLHKVF PGVDYTPWGV QYPLCLQYPP
410 420 430 440 450
SQNNVTRDLA VLTQLTNTIR LYGTDCNQTE MVLEAIDRLQ LTNMKLWLGV
460 470 480 490 500
WIDTNTTTTD RQISQLYKIV ENANDTSIFK GAIVGNEALY RAGSDVASAE
510 520 530 540 550
TNLIGYINDV KDHFKDKNID LPVGTSDLGD NWNAQLVSAA DFVMSNIHPF
560 570 580 590 600
FGGVEIDDAA SWTWTFWQTH DTPLTAGTNK QQIISEVGWP TGGGNDCGSD
610 620 630 640 650
NKCQNDKQGA VAGIDELNQF LSEWVCQALD NGTEYFWFEA FDEPWKVQYN
660 670 680
TPGQEWEDKW GLMDSARNLK PGVKIPDCGG KTIT
Length:684
Mass (Da):73,248
Last modified:June 15, 2010 - v2
Checksum:i5CB65C56222424D0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270130 Genomic DNA. Translation: CAK39383.1.
RefSeqiXP_001391547.2. XM_001391510.2.

Genome annotation databases

GeneIDi4981731.
KEGGiang:ANI_1_1742064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270130 Genomic DNA. Translation: CAK39383.1 .
RefSeqi XP_001391547.2. XM_001391510.2.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 4981731.
KEGGi ang:ANI_1_1742064.

Phylogenomic databases

eggNOGi COG5309.
HOGENOMi HOG000173877.
OrthoDBi EOG7P8PHC.

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 the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiBTGC_ASPNC
AccessioniPrimary (citable) accession number: A2QN74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: October 29, 2014
This is version 41 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Lacks the conserved Glu residue in position 619 essential for glucanase activity. Its enzyme activity is therefore unsure.Curated

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