Unreviewed, UniProtKB/TrEMBL Q9HFH0 (Q9HFH0_PENFN)

Names and origin

Protein names

Recommended name:
    Endo-1,4-beta-xylanase RuleBase RU004392V0
    EC=3.2.1.8

Gene names

Name:

xynC EMBL CAC15487.1

Organism

Penicillium funiculosum EMBL CAC15487.1

Taxonomic identifier

28572 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. RuleBase RU004392V0
Pathway	Glycan degradation; xylan degradation. RuleBase RU004392V0
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family. RuleBase RU003433V0

Ontologies

Keywords
Biological process	Xylan degradation RuleBase RU003433V0
Domain	Signal
Molecular function	Glycosidase RuleBase RU003433V0 Hydrolase
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential EMBL CAC15487.1
	Chain	17 – 223	207	Potential EMBL CAC15487.1		PRO_5000066092
	Chain	34 – 223	190	XYNC EMBL CAC15487.1		PRO_5000066093

Sequences

	Sequence		Length	Mass (Da)
	Q9HFH0-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 428CD224C8F13C77	FASTA	223	24,045
	10 20 30 40 50 60 MKLFLAAIVL CATAATAFPS ELAQRAAGDL SKRQSITTSQ TGTNNGYYYS FWTNGGGEVT 70 80 90 100 110 120 YTNGDNGEYS VTWVDCGDFT SGKGWNPANA QTVTYSGEFN PSGNAYLAVY GWTTDPLVEY 130 140 150 160 170 180 YILESYGTYN PSSGLTSLGQ VTSDGGTYDI YSTQRVNQPS IEGTSTFNQY WSVRTEKRVG 190 200 210 220 GTVTTANHFA AWKALGLEMG TYNYMIVSTE GYESSGSSTI TVS

References

[1]	"A family 11 xylanase from Penicillium funiculosum is strongly inhibited by three wheat xylanase inhibitors." Furniss C.S., Belshaw N.J., Alcocer M.J., Williamson G., Elliott G.O., Gebruers K., Haigh N.P., Fish N.M., Kroon P.A. Biochim. Biophys. Acta 1598:24-29(2002) [PubMed: 12147340] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases." Payan F., Leone P., Porciero S., Furniss C., Tahir T., Williamson G., Durand A., Manzanares P., Gilbert H.J., Juge N., Roussel A. J. Biol. Chem. 279:36029-36037(2004) [PubMed: 15181003] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-223.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ278385 Genomic DNA. Translation: CAC15487.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TE1	X-ray	2.50	B	34-223	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH11. Glycoside Hydrolase Family 11.

Family and domain databases

InterPro

IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]

Gene3D

G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.

Pfam

PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]

PRINTS

PR00911. GLHYDRLASE11.

PROSITE

PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9HFH0_PENFN

Accession

Primary (citable) accession number: Q9HFH0

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2001
Last sequence update:	March 1, 2001
Last modified:	May 5, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)