Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A1CJQ1 (DAPB_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. 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:ACLA_035780
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length914 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 – 914914Probable dipeptidyl-aminopeptidase B
PRO_0000412132

Regions

Topological domain1 – 9191Cytoplasmic Potential
Transmembrane92 – 11221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain113 – 914802Vacuolar Potential

Sites

Active site7531Charge relay system By similarity
Active site8301Charge relay system By similarity
Active site8631Charge relay system By similarity

Amino acid modifications

Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation5651N-linked (GlcNAc...) Potential
Glycosylation6391N-linked (GlcNAc...) Potential
Glycosylation8071N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A1CJQ1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: B72E64B88D3C541D

FASTA914102,054
        10         20         30         40         50         60 
MATFSDHETS EFLPMTRPRS TSSASQTSSD SGLSSEPAFQ EDQKQPFSAP NGTTGMDNGD 

        70         80         90        100        110        120 
RYRDLEDGEA EANEPFLASS KKAATGGRAR RIFWLLVLLC FGGWLLAFVL FLTGGRANYQ 

       130        140        150        160        170        180 
SASDALQAQE PESASGSTSS GKPVTLEQVL TGQWSPRYHA ITWVAGPNDE DGLLVEKGGG 

       190        200        210        220        230        240 
EQEGYLRVDD IQSRKNKDGK GGRVLMRKPI VHVDGKLVVP GNAWPSPDLK KVLLISDQEK 

       250        260        270        280        290        300 
NWRHSFTGKY WVLDVESQTA QPLDPSLPDG RVQLALWSPK SDAVIFVREN DVYLRKLSSD 

       310        320        330        340        350        360 
RVVTVTKDGG ENLFYGVPDW VYEEEVISGR SVTWWSNDAK YVAFFRTNES AVSDFPVDYF 

       370        380        390        400        410        420 
LSRPSGKKPD PGLENYPEVR QIKYPKAGAS NPVVDLQFYD VEKNEVFSVD VADDFDNDDR 

       430        440        450        460        470        480 
IIIEVVWASE GKVLVRSTNR ESDILKVFLI DTKSRTGRVV RTEDVASLDG GWVEPSQSTR 

       490        500        510        520        530        540 
FIPADPSNGR PDDGYIDTVP YKGYDHLAYF SPLDSPKGVM LTSGDWEVVD APAAVDLQRG 

       550        560        570        580        590        600 
LVYFVAAKEA PTERHIYRVQ LDGSNMTAIT DTSKPGYFGV SFSHGAGYAL LTYNGPSVPW 

       610        620        630        640        650        660 
QAIINTHGDE ITFEERIEEN PQLTSMIEAY ALPTEIYQNV TVDGFTLQVV ERRPPHFNPA 

       670        680        690        700        710        720 
KKYPVLFYLY GGPGSQTVDR KFSIDFQSYV ASSLGYIVVT VDGRGTGHIG RKARCIVRGN 

       730        740        750        760        770        780 
LGFYEARDQI ATAKIWAAKS YVDESRMAIW GWSFGGFMTL KTLELDAGET FQYGMAVAPV 

       790        800        810        820        830        840 
TDWRFYDSIY SERYMHTPQH NPSGYANSTI TDMAALTHPV RFLVMHGTAD DNVHLQNTLV 

       850        860        870        880        890        900 
LTDKLDLSNV KNYDLHFFPD SDHSIFFHNA HAMVYDRLSS WLVNAFNGEW HRIAHPVPGE 

       910 
SMWTRFKRSL PVLV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027056 Genomic DNA. Translation: EAW09375.1.
RefSeqXP_001270801.1. XM_001270800.1.

3D structure databases

ProteinModelPortalA1CJQ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00003660.

Protein family/group databases

MEROPSS09.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00003740; CADACLAP00003660; CADACLAG00003740.
GeneID4703117.
KEGGact:ACLA_035780.

Phylogenomic databases

HOGENOMHOG000189891.
KOK01282.
OMAETKFWYQ.
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_ASPCL
AccessionPrimary (citable) accession number: A1CJQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 40 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