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Q0H904 (XYNC_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase C

Short name=Xylanase C
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C
Gene names
Name:xlnC
Synonyms:xynf10a
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted By similarity.

Induction

Expressed in presence of xylan and repressed by glucose.

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Sequence caution

The sequence EAL89839.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 325306Endo-1,4-beta-xylanase C
PRO_0000393188

Sites

Active site1551Proton donor By similarity
Active site2611Nucleophile By similarity

Amino acid modifications

Disulfide bond279 ↔ 285 By similarity

Experimental info

Sequence conflict141V → A in ABA40421. Ref.1
Sequence conflict401K → R in ABA40421. Ref.1
Sequence conflict2141Y → C in ABA40421. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q0H904 [UniParc].

Last modified March 23, 2010. Version 2.
Checksum: BB2D1688371B3F92

FASTA32535,221
        10         20         30         40         50         60 
MVVLSKLVSS ILFVSLVSAG VIEERQAASI NQAFTSHGKK YFGTASDQAL LQKSQNEAIV 

        70         80         90        100        110        120 
RKDFGQLTPE NSMKWDATEP SQGRFNFAGA DFLVNYAKQN GKKVRGHTLV WHSQLPSWVS 

       130        140        150        160        170        180 
AISDKNTLTS VLKNHITTVM TRYKGQIYAW DVVNEIFNED GSLRDSVFSR VLGEDFVRIA 

       190        200        210        220        230        240 
FETARSVDPS AKLYINDYNL DSASYGKTQG MVRYVKKWLA AGIPIDGIGT QTHLGAGASS 

       250        260        270        280        290        300 
SVKGALTALA SSGVSEVAIT ELDIAGASSQ DYVNVVKACL DVPKCVGITV WGVSDRDSWR 

       310        320 
SGSSPLLFDS NYQPKAAYNA IIAAL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of recombinant xylan degrading enzymes from Aspergillus fumigatus isolate SL1."
Dabrowski S., Ahring B.K.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SL1.
[2]"Cloning and characterization of xynf10a gene from Aspergillus fumigatus MKU1."
Thiagarajan S., Jeya M., Gunasekaran P.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MKU1.
[3]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ156555 mRNA. Translation: ABA40421.1.
EF375874 Genomic DNA. Translation: ABN48479.1.
AAHF01000005 Genomic DNA. Translation: EAL89839.1. Sequence problems.
RefSeqXP_751877.1. XM_746784.1.

3D structure databases

ProteinModelPortalQ0H904.
SMRQ0H904. Positions 27-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00008146.

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00008146; CADAFUAP00008146; CADAFUAG00008146.
GeneID3509139.
KEGGafm:AFUA_4G09480.

Phylogenomic databases

HOGENOMHOG000019847.
KOK01181.
OrthoDBEOG7GJ6PM.

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXYNC_ASPFU
AccessionPrimary (citable) accession number: Q0H904
Secondary accession number(s): A3FG82, Q4WPJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: April 16, 2014
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries