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E3QKD2 (DAPB_COLGM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 16. 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 attributes

Sequence length921 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.

Ontologies

Keywords
   Cellular componentMembrane
Vacuole
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionAminopeptidase
Hydrolase
Protease
Serine protease
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

vacuolar membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 921921Probable dipeptidyl-aminopeptidase B
PRO_0000412144

Regions

Topological domain1 – 108108Cytoplasmic Potential
Transmembrane109 – 12921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain130 – 921792Vacuolar Potential
Compositional bias64 – 8320Asp-rich

Sites

Active site7681Charge relay system By similarity
Active site8451Charge relay system By similarity
Active site8781Charge relay system By similarity

Amino acid modifications

Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation5771N-linked (GlcNAc...) Potential
Glycosylation8271N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
E3QKD2 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: 92129EF1EB01470B

FASTA921103,378
        10         20         30         40         50         60 
MDAPATASRQ PIAEEPRMSQ ESSLSTVSTT SLVFDRLHEH NEKSYHSSSQ RRRAPSASRG 

        70         80         90        100        110        120 
GYADHPDDDD DDDESYKEAD TNDLETGPFL APASVMMRRV GVDRGLKKVI LILAAAFLFA 

       130        140        150        160        170        180 
WGAALFVFLS NKSYKHASTI DHDPSATSRG SGKPVTLDQV ISGFWYPTSH SISWIEGPNG 

       190        200        210        220        230        240 
EDGLLLEQGA RGKDYLVVED VRSGNKDSQV SANVVQSRTL MKNPWINVGG RQLAPSDTRP 

       250        260        270        280        290        300 
SKDMKKVLVS TDRQRNWRYS YTALYWIFDV ETQTAEALDP EHPDGRVQLA TWSPQSNAIV 

       310        320        330        340        350        360 
FTRDNNLFLR KLDGDKKVTQ ITNDGGPEYF YGIPDWVYEE EVFATNSATW YSEDGKYVAF 

       370        380        390        400        410        420 
LRTNETGVPE YPLQYFLSRP SGKEKPPGEE TYPDEKRIKY PRAGSHNPVV DLLFFDVERG 

       430        440        450        460        470        480 
DVFSVDIDGG FADDDRLINM VLWANDKVLI KETNRVSDIM RVVLVDVVAR TGKTVNTIDV 

       490        500        510        520        530        540 
GELDGGWFEI SHTTQFIPAD PANGRPQDGY IDTVVHGNGD HIAYFSPMDN AEPVYLTGGD 

       550        560        570        580        590        600 
WEVDDGPSAV DLKNNLVYFV ATKESSIQRH VYSVHLNRSD LKPFTDTKFE SYYDISFSSG 

       610        620        630        640        650        660 
AGYALLSYQG PKIPWQKVVS TPSSPVSYEH VVEKNEDLAE NAKKYELPIL NYGTLKVDGV 

       670        680        690        700        710        720 
ELNYVERRPP HFDEKKKYPV LFQQYSGPGS QSVHKKFAVD FQSYVASALG YLVVTVDGRG 

       730        740        750        760        770        780 
TGFIGRKNRV LIRDHLGYWE AHDQIAAAQA WAAKKYVDPA RIAIWGWSYG GFNTLKTLEM 

       790        800        810        820        830        840 
DAGRTFSYGM AVAPVTDWRF YDSIYTERYM RTPQLNPSGY DQTAVSNVSA LAGNVRWLMM 

       850        860        870        880        890        900 
HGVGDDNVHY QNTLTLLDKL DLNGIENYDV HVFPDSDHGI YFHGANRIVY DKLSNWLINA 

       910        920 
FNGEWLKVAG AKPIVEPKAR V 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GG697354 Genomic DNA. Translation: EFQ31320.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFQ31320; EFQ31320; GLRG_06464.

Phylogenomic databases

OrthoDBEOG72VHFG.

Family and domain databases

Gene3D2.140.10.30. 1 hit.
InterProIPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPB_COLGM
AccessionPrimary (citable) accession number: E3QKD2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 16 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