Probable dipeptidyl peptidase 4 precursor - Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163)

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B0Y6C5 (DPP4_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 29. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Probable dipeptidyl peptidase 4
EC=3.4.14.5

Alternative name(s):
Dipeptidyl peptidase IV
Short name=DPP IV
Short name=DppIV

Gene names

Name:	dpp4
ORF Names:	AFUB_066450

Organism

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

Taxonomic identifier

Taxonomic lineage

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

Protein attributes

Sequence length	765 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)

Function	Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Contributes to pathogenicity. Ref.1
Catalytic activity	Release of an N-terminal dipeptide, Xaa-Yaa-\|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
Subcellular location	Secreted Ref.1.
Sequence similarities	Belongs to the peptidase S9B family.
Biophysicochemical properties	Kinetic parameters: K_M=0.38 mM for Gly-Pro pNA and Ala-Pro pNA Ref.1 K_M=0.15 mM for Arg-Pro pNA pH dependence: Optimum pH is 6.7 to 7.0.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Secreted
Domain	Signal
Molecular function	Aminopeptidase Hydrolase Protease Serine protease
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

14

Potential

Chain

751

Probable dipeptidyl peptidase 4

PRO_0000397810

Sites

Active site

1

Charge relay system By similarity

Active site

1

Charge relay system By similarity

Active site

1

Charge relay system By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

1

Y → H in AAC34310. Ref.1

Sequence conflict

1

D → G in AAC34310. Ref.1

Sequence conflict

1

A → P in AAC34310. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

B0Y6C5 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 544F27B6134F9B1B
Show »

765

85,876

        10         20         30         40         50         60 
MKWSILLLVG CAAAIDVPRQ PYAPTGSGKK RLTFNETVVK RAISPSAISV EWISTSEDGD 

        70         80         90        100        110        120 
YVYQDQDGSL KIQSIVTNHT QTLVPADKVP EDAYSYWIHP NLSSVLWATN YTKQYRYSYF 

       130        140        150        160        170        180 
ADYFIQDVQS MKLRPLAPDQ SGDIQYAQWS PTGDAIAFVR DNNVFVWTNA STSQITNDGG 

       190        200        210        220        230        240 
PDLFNGVPDW IYEEEILGDR FALWFSPDGA YLAFLRFNET GVPTFTVPYY MDNEEIAPPY 

       250        260        270        280        290        300 
PRELELRYPK VSQTNPTVEL NLLELRTGER TPVPIDAFDA KELIIGEVAW LTGKHDVVAV 

       310        320        330        340        350        360 
KAFNRVQDRQ KVVAVDVASL RSKTISERDG TDGWLDNLLS MAYIGPIGES KEEYYIDISD 

       370        380        390        400        410        420 
QSGWAHLWLF PVAGGEPIAL TKGEWEVTNI LSIDKPRQLV YFLSTKHHST ERHLYSVSWK 

       430        440        450        460        470        480 
TKEITPLVDD TVPAVWSASF SSQGGYYILS YRGPDVPYQD LYAINSTAPL RTITSNAAVL 

       490        500        510        520        530        540 
NALKEYTLPN ITYFELALPS GETLNVMQRL PVKFSPKKKY PVLFTPYGGP GAQEVSKAWQ 

       550        560        570        580        590        600 
ALDFKAYIAS DPELEYITWT VDNRGTGYKG RAFRCQVASR LGELEAADQV FAAQQAAKLP 

       610        620        630        640        650        660 
YVDAQHIAIW GWSYGGYLTG KVIETDSGAF SLGVQTAPVS DWRFYDSMYT ERYMKTLESN 

       670        680        690        700        710        720 
AAGYNASAIR KVAGYKNVRG GVLIQHGTGD DNVHFQNAAA LVDTLVGAGV TPEKLQVQWF 

       730        740        750        760 
TDSDHGIRYH GGNVFLYRQL SKRLYEEKKR KEKGEAHQWS KKSVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans." Beauvais A., Monod M., Wyniger J., Debeaupuis J.P., Grouzmann E., Brakch N., Svab J., Hovanessian A.G., Latge J.P. Infect. Immun. 65:3042-3047(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]	"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. 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	U87950 Genomic DNA. Translation: AAC34310.1. DS499598 Genomic DNA. Translation: EDP50310.1.
3D structure databases
HSSP	HSSP built from PDB template 1ORV based on UniProtKB P22411.
ProteinModelPortal	B0Y6C5.
ModBase	Search...
Protein-protein interaction databases
STRING	5085.CADAFUAP00007859.
Protein family/group databases
MEROPS	S09.008.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUBT00006595; CADAFUBP00006467; CADAFUBG00006595.
Phylogenomic databases
HOGENOM	HOG000189891.
Family and domain databases
InterPro	IPR001375. Peptidase_S9. IPR002469. Peptidase_S9B. [Graphical view]
Pfam	PF00930. DPPIV_N. 1 hit. PF00326. Peptidase_S9. 1 hit. [Graphical view]
PROSITE	PS00708. PRO_ENDOPEP_SER. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPP4_ASPFC

Accession

Primary (citable) accession number: B0Y6C5
Secondary accession number(s): O14425

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	April 8, 2008
Last modified:	April 3, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents