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Q0CR35

- EXGA_ASPTN

UniProt

Q0CR35 - EXGA_ASPTN

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Protein

Probable glucan 1,3-beta-glucosidase A

Gene

exgA

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (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.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei209 – 2091Proton donorBy similarity
Active sitei308 – 3081NucleophileBy similarity

GO - Molecular functioni

  1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glucan 1,3-beta-glucosidase A (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase 1
Exo-1,3-beta-glucanase A
Gene namesi
Name:exgA
Synonyms:exg1
ORF Names:ATEG_03849
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000007963: Unassembled WGS sequence

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 416395Probable glucan 1,3-beta-glucosidase APRO_0000393531Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi290 ↔ 415By similarity
Disulfide bondi316 ↔ 341By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi33178.CADATEAP00008924.

Structurei

3D structure databases

ProteinModelPortaliQ0CR35.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
OMAiIINEPNT.
OrthoDBiEOG7JT75H.

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.

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

Q0CR35-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLYNLSKAVL ALSVLAASAD AAGIRLEKRA STFDYETEMV RGVCLGGWLV
60 70 80 90 100
LEPWLSPGLF DAAPDGAVDE WTYTEILGQD EAKARLIGHW DTFITEQDFF
110 120 130 140 150
DIAAAGMNHV RIPIGYWAVE ALPGDPYVDG QLEYLDRAIE WAGAAGLKVI
160 170 180 190 200
VDLHGAPGSQ NGFDNSGRKG AIQWGQGDTL GQTVNAFRKL AERYVPSSDV
210 220 230 240 250
VTAIEAVNEP FIPGGVNEDQ LKEYYQQAYD IVTQMSPDVD LVFSDGFINP
260 270 280 290 300
TPWNGFISDS GNIVMDNHHY EVFDINLLRM SVDDHVRSVC DFGRTQLAPA
310 320 330 340 350
TKPVVVGEWT GAMTDCARYL NGRGVGARYD GAMGGESVGD CGPFIQGSVS
360 370 380 390 400
DLSPDDQKNM RRFIEAQLDA WEMKSGWLFW NWKTEQGAPG WDMKDLLDNG
410
VFPFPLESRK YPGQCG
Length:416
Mass (Da):45,747
Last modified:October 17, 2006 - v1
Checksum:i24F9987F9D3BA259
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476598 Genomic DNA. Translation: EAU35651.1.
RefSeqiXP_001213027.1. XM_001213027.1.

Genome annotation databases

EnsemblFungiiCADATEAT00008924; CADATEAP00008924; CADATEAG00008924.
GeneIDi4318487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476598 Genomic DNA. Translation: EAU35651.1 .
RefSeqi XP_001213027.1. XM_001213027.1.

3D structure databases

ProteinModelPortali Q0CR35.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 33178.CADATEAP00008924.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADATEAT00008924 ; CADATEAP00008924 ; CADATEAG00008924 .
GeneIDi 4318487.

Phylogenomic databases

eggNOGi COG2730.
HOGENOMi HOG000114462.
OMAi IINEPNT.
OrthoDBi EOG7JT75H.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NIH 2624 / FGSC A1156.

Entry informationi

Entry nameiEXGA_ASPTN
AccessioniPrimary (citable) accession number: Q0CR35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: October 17, 2006
Last modified: November 26, 2014
This is version 49 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