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A2QEK7 (DAPB_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Probable dipeptidyl-aminopeptidase B

Short name=DPAP B
EC=3.4.14.5
Gene names
Name:dapB
ORF Names:An02g11420
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length901 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline By similarity.

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

Vacuole membrane; Single-pass type II membrane protein By similarity. Note: Lysosome-like vacuoles By similarity.

Sequence similarities

Belongs to the peptidase S9B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 901901Probable dipeptidyl-aminopeptidase B
PRO_0000412136

Regions

Topological domain1 – 7676Cytoplasmic Potential
Transmembrane77 – 9721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain98 – 901804Vacuolar Potential
Compositional bias120 – 1256Poly-Ser

Sites

Active site7391Charge relay system By similarity
Active site8161Charge relay system By similarity
Active site8491Charge relay system By similarity

Amino acid modifications

Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation6251N-linked (GlcNAc...) Potential
Glycosylation7931N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A2QEK7 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: F058BA27F2450237

FASTA901101,294
        10         20         30         40         50         60 
MSSPRPSTSS TSSDSGLSVD TTAYPEESKY TSTAPGAGGL SDENRYRDVE EGEAGADEPF 

        70         80         90        100        110        120 
LPSAKKQAAS GSRTSRLIWG LVILCVAGWL WGLVLFVTQN RSAQQSVSEA LQSHESGAIS 

       130        140        150        160        170        180 
GSSSSGKPVT LEQVLTGQWL PRSHAVSWIA GPNGEDGLLV EQGEDQGKGY LRVDDIRSRK 

       190        200        210        220        230        240 
GDATSQESRV LMEKAIVQVD GRTIFPVSTW PSPNLNKVLL LSEREKNWRH SFTGKYWIFD 

       250        260        270        280        290        300 
VATQTAQPLD PSNPDGRVQL AIWSPTSDMV AFVRDNNLYL RKLSSKEVVP ITKDGGADLF 

       310        320        330        340        350        360 
YGIPDWVYEE EVFSGNSVTW WSGDGKYVAF LRTNETAVPE FPVQYYLSRP SGKRPPPGLE 

       370        380        390        400        410        420 
DYPEVREIKY PKAGAPNPVV SLQFYDVEKQ EVFSIEAPDN FEDDDRIIIE IVWGTEGKIL 

       430        440        450        460        470        480 
VRATNRESDV LKVFLFDTKA RTSKLVRVEN VADIDGGWVE PTQYTWFIPA DPSNGRPHDG 

       490        500        510        520        530        540 
YLDTVIHEGY EHLGYFTPLD NSEPILLTQG EWEVVDAPTA VDLRKGIVYF ISTKESPTER 

       550        560        570        580        590        600 
HLYQVNLDGS NLKPLTDTSK PGYYDVSFSH GTGYALLSYR GPSIPWQAIV NTETDELKYE 

       610        620        630        640        650        660 
ETIEDNAGLA RMVDSYALPT EIYQNVTIDG FTLQVVERRP PHFNPAKKYP VLFYLYNGPR 

       670        680        690        700        710        720 
SQTVDRKFNI DFQSYVASSL GYIVVTVDGR GTGFSGRKTR CIVRGNLGYY EAYDQITTAK 

       730        740        750        760        770        780 
LWGEKPYVDE TRMSIWGWSY GGFMTLKTLE QDAGQTFQYG MAVAPVTDWR HYDSIYTERY 

       790        800        810        820        830        840 
MHTPAHNPNG YDNTSITDMT ALQQTVRFLV IHGASDDNVH IQNTLVLVDK LDLAGVQNYD 

       850        860        870        880        890        900 
LHFYPDSDHS INFHNAHRMV YERLSSWLVN AFNDEWHRIA DPVPDDSMWE KVKRSLPMLV 


K 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM270029 Genomic DNA. Translation: CAK37870.1.

3D structure databases

ProteinModelPortalA2QEK7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00002590.

Protein family/group databases

MEROPSS09.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANGAT00002663; CADANGAP00002590; CADANGAG00002663.

Phylogenomic databases

HOGENOMHOG000189891.
OrthoDBEOG72VHFG.

Family and domain databases

Gene3D2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDAPB_ASPNC
AccessionPrimary (citable) accession number: A2QEK7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: March 6, 2007
Last modified: June 11, 2014
This is version 42 of the entry and version 1 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

Peptidase families

Classification of peptidase families and list of entries