Unreviewed, UniProtKB/TrEMBL Q84F19 (Q84F19_9BACI)

Names and origin

Protein names

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

Gene names

Name:

xynA EMBL CAD60654.1

Organism

Bacillus sp. BP-7 EMBL CAD60654.1

Taxonomic identifier

126733 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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	1 – 28	28	Potential EMBL CAD60654.1
	Chain	29 – 213	185	endo-1,4-beta-xylanase A EMBL CAD60654.1		PRO_5000070402

Sequences

	Sequence		Length	Mass (Da)
	Q84F19-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: F1E194D24A329516	FASTA	213	23,475
	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

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
EMBLGenBankDDBJ	AJ536759 Genomic DNA. Translation: CAD60654.1.
3D structure databases
HSSP	HSSP built from PDB template 1XNB based on UniProtKB P09850.
SMR	Q84F19. Positions 27-213.
ModBase	Search...
Protein family/group databases
CAZy	GH11. Glycoside Hydrolase Family 11.
Enzyme and pathway databases
BRENDA	3.2.1.8. 1000.
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. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q84F19_9BACI

Accession

Primary (citable) accession number: Q84F19

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2003
Last sequence update:	June 1, 2003
Last modified:	May 5, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)