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Protein

Endo-1,4-beta-xylanase

Gene

xynS

Organism
Bacillus sp. YA-14
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.UniRule annotation

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationUniRule annotationImported

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
Gene namesi
Name:xynSImported
OrganismiBacillus sp. YA-14Imported
Taxonomic identifieri72411 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 213185Endo-1,4-beta-xylanaseSequence analysisPRO_5004252567Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ59256.
SMRiQ59256. Positions 27-213.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 213194GH11 (glycosyl hydrolase family 11)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 11 (cellulase G) family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59256-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS
60 70 80 90 100
GGNYSVNWSN TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT
110 120 130 140 150
RSPLIEYYVV DSWGTYRPTG TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR
160 170 180 190 200
TTFTQYWSVR QTKRPTGSNA TITFSNHVNA WKSHGMNLGS NWAYQVLATE
210
GYQSSGSSNV TVW
Length:213
Mass (Da):23,341
Last modified:November 1, 1996 - v1
Checksum:i2110D35768CC0034
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59058 Genomic DNA. Translation: CAA41783.1.
PIRiS48126.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59058 Genomic DNA. Translation: CAA41783.1.
PIRiS48126.

3D structure databases

ProteinModelPortaliQ59256.
SMRiQ59256. Positions 27-213.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Hyun Ju Y.
    Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: YA-14Imported.
  2. "Nucleotide sequence and analysis of a xylanase gene (xynS) from alkali-tolerant Bacillus sp. YA-14 and comparison with other xylanases."
    Yu J.H., Park Y.S., Yum D.Y., Kim J.M., Kong I.S., Bai D.H.
    J. Microbiol. Biotechnol. 3:139-145(1993)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: YA-14Imported.

Entry informationi

Entry nameiQ59256_9BACI
AccessioniPrimary (citable) accession number: Q59256
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.