Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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.By similarity

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 sitei155Proton donorBy similarity1
Active sitei252NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable endo-1,4-beta-xylanase C (EC:3.2.1.8)
Short name:
Xylanase C
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C
Gene namesi
Name:xlnC
ORF Names:AFUB_066600
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001699 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000039318920 – 316Probable endo-1,4-beta-xylanase CAdd BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi270 ↔ 276By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Expressed in presence of xylan and repressed by glucose.

Structurei

3D structure databases

ProteinModelPortaliB0Y6E0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 315GH10PROSITE-ProRule annotationAdd BLAST272

Sequence similaritiesi

Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000019847.
OrthoDBiEOG092C45ID.
PhylomeDBiB0Y6E0.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS51760. GH10_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

B0Y6E0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVLSKLVSS ILFVSLVSAG VIEERQAASI NQAFTSHGKK YFGTASDQAL
60 70 80 90 100
LQKSQNEAIV RKDFGQLTPE NSMKWDATEP SQGRFNFAGA DFLVNYAKQN
110 120 130 140 150
GKKVRGHTLV WHSQLPSWVS AISDKNTLTS VLKNHITTVM TRYKGQIYAW
160 170 180 190 200
DVVNEIFNED GSLRDSVFSR VLGEDFVRIA FETARSVDPS AKLYINDYNL
210 220 230 240 250
DSASYGKTQG MVRYVKKWLA AGIPIDGIGT QTHLGALTAL ASSGVSEVAI
260 270 280 290 300
TELDIAGASS QDYVNVVKAC LDVPKCVGIT VWGVSDRDSW RSGSSPLLFD
310
SNYQPKAAYN AIIAAL
Length:316
Mass (Da):34,476
Last modified:March 23, 2010 - v2
Checksum:i4FDDF1F05E93AF30
GO

Sequence cautioni

The sequence EDP50325 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499598 Genomic DNA. Translation: EDP50325.1. Sequence problems.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499598 Genomic DNA. Translation: EDP50325.1. Sequence problems.

3D structure databases

ProteinModelPortaliB0Y6E0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000019847.
OrthoDBiEOG092C45ID.
PhylomeDBiB0Y6E0.

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNC_ASPFC
AccessioniPrimary (citable) accession number: B0Y6E0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: September 7, 2016
This is version 41 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.