Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8RMN7 (Q8RMN7_BACPU) Unreviewed, UniProtKB/TrEMBL

Last modified March 8, 2011. Version 41. 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·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismBacillus pumilus (Bacillus mesentericus) EMBL AAM08361.1
Taxonomic identifier1408 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 AAM08361.1
   Molecular functionGlycosidase RuleBase RU003433
Hydrolase
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...

Sequences

Sequence LengthMass (Da)Tools
Q8RMN7 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E879FDB1F9086285

FASTA22825,486
        10         20         30         40         50         60 
MNLRKLRLLF VMCIGLTLIL TAVPAHARTI TNNEMGNHSG YDYELWEDYG NTSMTLNNGG 

        70         80         90        100        110        120 
ALSAGWNNIG NALFRKGRKF DSTRTHHQLG NISINYNASF NPGGNSYLCV YGWTQSPLAE 

       130        140        150        160        170        180 
YYIVDSWGTY RPTGAYKGSF YADGGTYDIY ETTRVNQPSI IGIATFKQYW SVRQTKRTSG 

       190        200        210        220 
TVSVSAHFRK WESLGMPMGK MYETAFTVEG YQSSGSANVM TNQLFIGN

« Hide

References

[1]Sun J., Li W., Zhao H., Xu Z., Gu S., Xiao J.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF490981 Genomic DNA. Translation: AAM08361.1.

3D structure databases

HSSPHSSP built from PDB template 1F5J based on UniProtKB P77853.
ProteinModelPortalQ8RMN7.
SMRQ8RMN7. Positions 27-227.
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.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ8RMN7_BACPU
AccessionPrimary (citable) accession number: Q8RMN7
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2002
Last modified: March 8, 2011
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info