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B8NER4 (XYNF1_ASPFN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable endo-1,4-beta-xylanase F1

Short name=Xylanase F1
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase F1
Gene names
Name:xynF1
Synonyms:xlnF1
ORF Names:AFLA_063510
OrganismAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) [Complete proteome]
Taxonomic identifier332952 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose By similarity.

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 332313Probable endo-1,4-beta-xylanase F1
PRO_0000393186

Sites

Active site1551Proton donor By similarity
Active site2681Nucleophile By similarity

Amino acid modifications

Disulfide bond286 ↔ 292 By similarity

Sequences

Sequence LengthMass (Da)Tools
B8NER4 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: A374339B5129FDA4

FASTA33235,777
        10         20         30         40         50         60 
MVQFSSIVQC TLLATAASAY VTSRQAAESL HDAFTAAGKK YFGNIAEQAL LENPQNEPII 

        70         80         90        100        110        120 
AADFGALTCE NSMKWDATEP TQGGYNFDGA DYVVNYAVEK GKLLRGHTLL WHSQLPSWVS 

       130        140        150        160        170        180 
QISDPATLTG VIQDHVTTLV SRWKGQIYAW DVVNEIFAED GSLRESVFSN VLGEDFVRIA 

       190        200        210        220        230        240 
FEAARAADPD CKLYINDYNL DDASYSKTQG FVSKVGEWIA AGVPIDGIGM WLACLFKHAY 

       250        260        270        280        290        300 
AGGFPTSGAQ AALEALASTG ASEVAVTELD IGGATSDDWV NVVNACLNVE KCIGITVWGV 

       310        320        330 
SDKDSWRADE SPLLFDVNYQ PKDAYGAIIA AL 

« Hide

References

[1]"Genome sequence of Aspergillus flavus strain NRRL 3357."
Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., Bhatnagar D., Cleveland T.E.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EQ963477 Genomic DNA. Translation: EED52088.1.
RefSeqXP_002379095.1. XM_002379054.1.

3D structure databases

ProteinModelPortalB8NER4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5059.CADAFLAP00006960.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFLAT00006960; CADAFLAP00006960; CADAFLAG00006960.
GeneID7918606.
KEGGafv:AFLA_063510.

Phylogenomic databases

eggNOGCOG3693.
HOGENOMHOG000019847.
KOK01181.
OMACKLYIND.
OrthoDBEOG7GJ6PM.

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNF1_ASPFN
AccessionPrimary (citable) accession number: B8NER4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 3, 2009
Last modified: March 19, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries