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Protein

Endo-1,4-beta-xylanase 5

Gene

XYL5

Organism
Magnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.

Catalytic activityi

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

Pathwayi: xylan degradation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei166Proton donorBy similarity1
Active sitei273NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayi
UPA00114

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase 5 (EC:3.2.1.8)
Short name:
Xylanase 5
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 5
Gene namesi
Name:XYL5
OrganismiMagnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea)
Taxonomic identifieri148305 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000042962723 – 380Endo-1,4-beta-xylanase 5Add BLAST358
PropeptideiPRO_0000429628381 – 405Removed in mature formSequence analysisAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi27N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi69N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi171N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi302 ↔ 308By similarity
Lipidationi380GPI-anchor amidated glycineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Structurei

3D structure databases

ProteinModelPortaliQ8J1Y4
SMRiQ8J1Y4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 352GH10PROSITE-ProRule annotationAdd BLAST321

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi354 – 362Poly-Ala9

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3693 LUCA
OMAiEWRDSVF

Family and domain databases

InterProiView protein in InterPro
IPR001000 GH10
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00331 Glyco_hydro_10, 1 hit
PRINTSiPR00134 GLHYDRLASE10
SMARTiView protein in SMART
SM00633 Glyco_10, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS51760 GH10_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8J1Y4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTRLATLITL AGLLAVSPGA YAQRNRNDTG GSTGAEGLNS LAVKAGLLYF
60 70 80 90 100
GTASDTRNFA DEPYMSVVNN TNEFGMIVPE NSMKWEATEK EPGRFSFANA
110 120 130 140 150
DRVRALTKAN GQMLRCHALT WHSQLPNFVK TTAWTRDTLT AAIESHISNE
160 170 180 190 200
VGHFAGDCYA WDVVNEAVNE NGSFRDSPFH RTLGTDFLAI SFRAAAAADP
210 220 230 240 250
NAKLYYNDFN IETPGPKANA AMGIVRLLKE QGVRIDGVGF QGHLTVGSTP
260 270 280 290 300
SRAQLASQLQ RFADLGVEVT YTELDIRHKS LPVSSRAAQD QARDYVSVIG
310 320 330 340 350
SCLDVTACVG VMVWQPTDKY SWIPETFPGT GDACLFDANM NPKPAYTSVS
360 370 380 390 400
SLLAAAAATA PASVVPPASV TTSKTPIQAG AGRETVSIAG LTLALSSLAF

GMFML
Length:405
Mass (Da):43,247
Last modified:March 1, 2003 - v1
Checksum:i3B41DEFAB55501EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY144348 Genomic DNA Translation: AAN60060.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY144348 Genomic DNA Translation: AAN60060.1

3D structure databases

ProteinModelPortaliQ8J1Y4
SMRiQ8J1Y4
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG3693 LUCA
OMAiEWRDSVF

Enzyme and pathway databases

UniPathwayi
UPA00114

Family and domain databases

InterProiView protein in InterPro
IPR001000 GH10
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00331 Glyco_hydro_10, 1 hit
PRINTSiPR00134 GLHYDRLASE10
SMARTiView protein in SMART
SM00633 Glyco_10, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS51760 GH10_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiXYN5_MAGGR
AccessioniPrimary (citable) accession number: Q8J1Y4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: March 1, 2003
Last modified: November 7, 2018
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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Main funding by: National Institutes of Health

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