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Q8J1V6 (Q8J1V6_9PEZI) Unreviewed, UniProtKB/TrEMBL

Last modified March 8, 2011. Version 48. Feed History...

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

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase RuleBase RU004392

EC=3.2.1.8 RuleBase RU004392
Gene names
Name:xyn11A EMBL CAD48749.1
OrganismChaetomium thermophilum EMBL CAD48749.1
Taxonomic identifier209285 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeChaetomium

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. RuleBase RU004392

Pathway

Glycan degradation; xylan degradation. RuleBase RU004392

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family. RuleBase RU003433

Ontologies

Keywords
   Biological processXylan degradation RuleBase RU003433 EMBL CAD48749.1
   DomainSignal EMBL CAD48749.1
   Molecular functionGlycosidase RuleBase RU003433
Hydrolase
   Technical term3D-structure PDB 1H1A PDB 1XNK
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential EMBL CAD48749.1
Chain20 – 261242endoxylanase 11A EMBL CAD48749.1
PRO_5000068860

Sequences

Sequence LengthMass (Da)Tools
Q8J1V6 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 420D6256334D7707

FASTA26127,844
        10         20         30         40         50         60 
MVNFSTLFLA ASTAALAAAA PSIEKRQTLT SSATGTHNGY YYSFWTDGQG NIRFNLESGG 

        70         80         90        100        110        120 
QYSVTWSGNG NWVGGKGWNP GTDNRVINYT ADYRPNGNSY LAVYGWTRNP LIEYYVVESF 

       130        140        150        160        170        180 
GTYDPSTGAT RMGSVTTDGG TYNIYRTQRV NAPSIEGTKT FYQYWSVRTS KRTGGTVTMA 

       190        200        210        220        230        240 
NHFNAWRQAG LQLGSHDYQI VATEGYYSSG SATVNVGGST TGGNNGGNNG GNNGGNNGGN 

       250        260 
TGSNVSISRP RKMGSLASTR S 

« Hide

References

[1]"Production in Trichoderma reesei of three xylanases from Chaetomium thermophilum: a recombinant thermoxylanase for biobleaching of kraft pulp."
Mantyla A., Paloheimo M., Hakola S., Lindberg E., Leskinen S., Kallio J., Vehmaanpera J., Lantto R., Suominen P.
Appl. Microbiol. Biotechnol. 76:377-386(2007) [PubMed: 17549471] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability."
Hakulinen N., Turunen O., Janis J., Leisola M., Rouvinen J.
Eur. J. Biochem. 270:1399-1412(2003) [PubMed: 12653995] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 28-217.
[3]"Determination of thioxylo-oligosaccharide binding to family 11 xylanases using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry and X-ray crystallography."
Janis J., Hakanpaa J., Hakulinen N., Ibatullin F.M., Hoxha A., Derrick P.J., Rouvinen J., Vainiotalo P.
FEBS J. 272:2317-2333(2005) [PubMed: 15853815] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 28-222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ508931 Genomic DNA. Translation: CAD48749.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H1AX-ray1.75A/B28-217[»]
1XNKX-ray1.55A/B28-222[»]
ProteinModelPortalQ8J1V6.
SMRQ8J1V6. Positions 27-217.
ModBaseSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
Gene3DG3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ8J1V6_9PEZI
AccessionPrimary (citable) accession number: Q8J1V6
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: March 8, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)