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Q4JHP5 (XYNC_ASPTE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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 C

Short name=Xylanase C
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C
Gene names
Name:xlnC
OrganismAspergillus terreus
Taxonomic identifier33178 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Induction

Expressed in presence of xylan and repressed by glucose.

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
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 – 326307Probable endo-1,4-beta-xylanase C
PRO_0000393193

Sites

Active site1561Proton donor By similarity
Active site2621Nucleophile By similarity

Amino acid modifications

Disulfide bond280 ↔ 286 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JHP5 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 9DC41D6EC492DE23

FASTA32635,346
        10         20         30         40         50         60 
MVRLTVLAGF LLTSAACSAC VIGERQAASS INNAFKAKGK KYFGTCGDQG TLSDSTNSAI 

        70         80         90        100        110        120 
VKADFGQLTP ENSMKWDATE PNRGQFSFGG ADYLVNYAAS NGKMIRGHTL VWHSQLPGWV 

       130        140        150        160        170        180 
QGITDKNTLT SVLKNHITTV MQRYKGKVYA WDVVNEIFNE DGSLRKSVFY NVLGEDFVRI 

       190        200        210        220        230        240 
AFETARSVDP QAKLYINDYN LDNANYAKTK GMADHVRKWI SQGIPIDGIG SQTHLGSGGS 

       250        260        270        280        290        300 
WTVKDALNTL ASSGVSEVAI TELDIAGASS TDYVNVVNAC LSVSKCVGIT VWGVSDKYSW 

       310        320 
RSNDKPLLFD SNFQPKAAYN AIISAL 

« Hide

References

[1]"Cloning, expression, and characterization of a xylanase 10 from Aspergillus terreus (BCC129) in Pichia pastoris."
Chantasingh D., Pootanakit K., Champreda V., Kanokratana P., Eurwilaichitr L.
Protein Expr. Purif. 46:143-149(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BCC129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ087436 mRNA. Translation: AAY86996.1.

3D structure databases

ProteinModelPortalQ4JHP5.
SMRQ4JHP5. Positions 26-326.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.
mycoCLAPXYN10A_ASPTE.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
ProtoNetSearch...

Entry information

Entry nameXYNC_ASPTE
AccessionPrimary (citable) accession number: Q4JHP5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: August 2, 2005
Last modified: February 19, 2014
This is version 39 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