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B0Y429

- BTGC_ASPFC

UniProt

B0Y429 - BTGC_ASPFC

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Protein

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

Gene

btgC

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
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 sitei590 – 5901NucleophileBy similarity
Active sitei658 – 6581Proton donorBy 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

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 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:AFUB_056310
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699: Unassembled WGS sequence

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 307307CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei308 – 32821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini329 – 688360ExtracellularSequence AnalysisAdd
BLAST

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 – 688688Probable glucan endo-1,3-beta-glucosidase btgCPRO_0000395122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi431 – 4311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi609 – 6091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi635 – 6351N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliB0Y429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi254 – 33683Gly-richAdd
BLAST
Compositional biasi341 – 35010Poly-Ser

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

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.

B0Y429-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGPNRTYSF GEGDDGLAHP SSRTHAMHSQ YDDVSPISDG ARMNPMNGQG
60 70 80 90 100
MDHGLASVLE DGRQGWGRSP EPSPSLLTGS SATPGMDNLG PGAVGGGISG
110 120 130 140 150
IALSVANSHD RLSGVEALMG TDGQEANIPA ERGLSTTGSD NPYVPEPPEY
160 170 180 190 200
RYSYGSNIAL GAAAAPAGQL TPGQSVSHLS STNPSQRNLY DIPYQDVGGL
210 220 230 240 250
NAGPYQRHSA YSSNDLPVDI NPDEIVDDGD DGFVPAPNSG SGARKSQAIP
260 270 280 290 300
AAAGGAAAGG VLGNLGGLFG GKSAADTSYG PVPGAGLEAG EKGRWVKPKP
310 320 330 340 350
GGGNKKRGWI VGAILAFIII GAIVGGAVGG TIGHRGNEEP SSASSASSSS
360 370 380 390 400
TQTATEDTSV NGDLDKNSAE IKALMNNKNL HKVFPGIDYT PWGVQYPLCL
410 420 430 440 450
KYPPSQNNVT RDMAVLTQLT NNVRLYGTDC NQTEMVLHAI DKLEIKDMKI
460 470 480 490 500
WLGVWIDSNE TTSRRQIDQL YKIIDDAKDI SIFNGAIVGN EALYRAGSDK
510 520 530 540 550
TSAQTTLINY MQEVKDHFKK KNIDLPVATS DLGDNWDATL VQAADVVMAN
560 570 580 590 600
VHPFFGGIPV DQAAAWTWRF WQDHNVALTK GTNKKQIISE VGWPSGGGND
610 620 630 640 650
CGQGANCPND TAGAVAGVDE LNKFMEDWVC QALDNGTDYF WFEAFDEPWK
660 670 680
IVYNTGKENW EDKWGLMDSA RNLKPGLKIP DCGGKTAT
Length:688
Mass (Da):72,692
Last modified:April 8, 2008 - v1
Checksum:iD7B4BE06E954BF51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499597 Genomic DNA. Translation: EDP51620.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00005610; CADAFUBP00005513; CADAFUBG00005610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499597 Genomic DNA. Translation: EDP51620.1 .

3D structure databases

ProteinModelPortali B0Y429.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUBT00005610 ; CADAFUBP00005513 ; CADAFUBG00005610 .

Phylogenomic databases

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CEA10 / CBS 144.89 / FGSC A1163.

Entry informationi

Entry nameiBTGC_ASPFC
AccessioniPrimary (citable) accession number: B0Y429
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 8, 2008
Last modified: October 29, 2014
This is version 33 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