Endo-1,4-beta-xylanase precursor - Chaetomium thermophilum

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Unreviewed, UniProtKB/TrEMBL Q8J1V6 (Q8J1V6_9PEZI)

Last modified June 16, 2009. Version 38. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase RuleBase RU004392V0
EC=3.2.1.8

Gene names

Name:

xyn11A EMBL CAD48749.1

Organism

Chaetomium thermophilum EMBL CAD48749.1

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Chaetomiaceae › Chaetomium

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. RuleBase RU004392V0
Pathway	Glycan degradation; xylan degradation. RuleBase RU004392V0
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family. RuleBase RU003433V0

Ontologies

Keywords
Biological process	Xylan degradation RuleBase RU003433V0
Domain	Signal
Molecular function	Glycosidase RuleBase RU003433V0 Hydrolase
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

19

Potential EMBL CAD48749.1

Chain

242

endoxylanase 11A EMBL CAD48749.1

PRO_5000068860

Sequences

Sequence

Length

Mass (Da)

Tools

Q8J1V6-1 [UniParc].

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

261

27,844

        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

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 27-217.
[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 27-222.

Cross-references

Sequence databases

AJ508931 Genomic DNA. Translation: CAD48749.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H1A	X-ray	1.75	A/B	28-217	[»]
1XNK	X-ray	1.55	A/B	28-222	[»]

ModBase

Protein family/group databases

CAZy

GH11. Glycoside Hydrolase Family 11.

Family and domain databases

InterPro

IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]

Gene3D

G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.

Pfam

PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]

PRINTS

PR00911. GLHYDRLASE11.

PROSITE

PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

Q8J1V6_9PEZI

Accession

Primary (citable) accession number: Q8J1V6

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2003
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information