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Q84F19 (Q84F19_9BACI) Unreviewed, UniProtKB/TrEMBL

Last modified March 8, 2011. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

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

EC=3.2.1.8 RuleBase RU004392
Gene names
Name:xynA EMBL CAD60654.1
OrganismBacillus sp. BP-7 EMBL CAD60654.1
Taxonomic identifier126733 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 CAD60654.1
   DomainSignal EMBL CAD60654.1
   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential EMBL CAD60654.1
Chain29 – 213185endo-1,4-beta-xylanase A EMBL CAD60654.1
PRO_5000070402

Sequences

Sequence LengthMass (Da)Tools
Q84F19 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: F1E194D24A329516

FASTA21323,475
        10         20         30         40         50         60 
MFKFTKKFLV GLTAALMSIS LFSANASAAN TDYWQNWTDG GGTVNAVNGS GGNYSVNWSN 

        70         80         90        100        110        120 
TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NAYLTLYGWT RSPLIEYYVV DSWGTYRPTG 

       130        140        150        160        170        180 
TYKGTVYSDG GTYDVYTTTR YDAPSIDGDK TTFTQYWSVR QSKRPTGSNA TITFSNHVNA 

       190        200        210 
WKRYGMNLGS NWSYQVLATE GYQSSGSSNV TVW 

« Hide

References

[1]"Cloning and characterization of xylanase A from the strain Bacillus sp. BP-7: comparison with alkaline pI-low molecular weight xylanases of family 11."
Gallardo O., Diaz P., Pastor F.I.
Curr. Microbiol. 48:276-279(2004) [PubMed: 15057452] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ536759 Genomic DNA. Translation: CAD60654.1.

3D structure databases

HSSPHSSP built from PDB template 1XNB based on UniProtKB P09850.
ProteinModelPortalQ84F19.
SMRQ84F19. Positions 27-213.
ModBaseSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.8. 1000.

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 nameQ84F19_9BACI
AccessionPrimary (citable) accession number: Q84F19
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: March 8, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)