B0Y6E0 (XYNC_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable 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
ORF Names:	AFUB_066600

Organism

Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]

Taxonomic identifier

451804 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Neosartorya fumigata

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 EDP50325.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	extracellular region Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	endo-1,4-beta-xylanase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 316	297	Probable endo-1,4-beta-xylanase C		PRO_0000393189
Sites
	Active site	155	1	Proton donor By similarity
	Active site	252	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	270 ↔ 276		By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0Y6E0 [UniParc]. Last modified March 23, 2010. Version 2. Checksum: 4FDDF1F05E93AF30	FASTA	316	34,476
	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 QTHLGALTAL 250 260 270 280 290 300 ASSGVSEVAI TELDIAGASS QDYVNVVKAC LDVPKCVGIT VWGVSDRDSW RSGSSPLLFD 310 SNYQPKAAYN AIIAAL

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CEA10 / CBS 144.89 / FGSC A1163.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS499598 Genomic DNA. Translation: EDP50325.1. Sequence problems.
3D structure databases
ProteinModelPortal	B0Y6E0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUBT00006610; CADAFUBP00006482; CADAFUBG00006610.
Phylogenomic databases
eggNOG	COG3693.
HOGENOM	HOG000019847.
Enzyme and pathway databases
UniPathway	UPA00114.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001000. Glyco_hydro_10. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00331. Glyco_hydro_10. 1 hit. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM00633. Glyco_10. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNC_ASPFC

Accession

Primary (citable) accession number: B0Y6E0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	March 23, 2010
Last modified:	May 1, 2013
This is version 31 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program