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Q4WX13 (DAPB_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. 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:AFUA_3G07850
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length919 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 – 919919Probable dipeptidyl-aminopeptidase B
PRO_0000412135

Regions

Topological domain1 – 9292Cytoplasmic Potential
Transmembrane93 – 11321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain114 – 919806Vacuolar Potential

Sites

Active site7571Charge relay system By similarity
Active site8341Charge relay system By similarity
Active site8671Charge relay system By similarity

Amino acid modifications

Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential
Glycosylation6431N-linked (GlcNAc...) Potential
Glycosylation8111N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WX13 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 41A93F5575C44F80

FASTA919103,079
        10         20         30         40         50         60 
MRRSDGHEET SEFLPMTHSR SVSAASQTST DSSLSTESLF PREQKPFPNA MGGMALADDD 

        70         80         90        100        110        120 
KYRDLEDGEA EQSEPFLSSS KKAATGGGRA RRIFWILVLL CLGGWLLAFV LFLTGGRANY 

       130        140        150        160        170        180 
QTASDALQAH GADSALGSTS TSSGKPVTLH QVLGGQWNPR YHAIGWVAGP NNEDGLLVEK 

       190        200        210        220        230        240 
GGDEKQGYLR VDDIRSRKGN NTGRESRVLM RKPIVHVDGQ AIVPSNVWPS PDLKKVLLIS 

       250        260        270        280        290        300 
EQQKNWRHSF TGKYWVLDVD SQTAQPLDPS APDGRVQLAL WSPASDAVVF VRDNNLYLRR 

       310        320        330        340        350        360 
LSSDSVVAIT KDGGENLFYG VPDWVYEEEV ISGNSVTWWS NDAKYIAFFR TNETSVPEFP 

       370        380        390        400        410        420 
VQYYISRPSG KKPLPGLENY PDVREIKYPK PGAPNPVVDL QFYDVEKNEV FSVQVADDFA 

       430        440        450        460        470        480 
DDDRIIIEVL WASEGKILVR STNRESDILK VYLIDTQSRT GKLVRSEDVA GLDGGWVEPS 

       490        500        510        520        530        540 
QSTRFVPADP NNGRPHDGYI DTVPYNGYDH LAYFSPLDNP NALMLTSGEW EVVDAPAAVD 

       550        560        570        580        590        600 
LQRGLVYFVG TKEAPTQRHV YRVQLDGSNL NPLTDTSKPG YYDVSFSHGT GYALLTYKGP 

       610        620        630        640        650        660 
SIPWQAIINT HGDEITYEDR IEDNAQLTKM VEAYALPTEV YQNVTVDGYT LQVVERRPPH 

       670        680        690        700        710        720 
FNPAKKYPVL FYLYGGPGSQ TVDRKFTVDF QSYVASSLGY IVVTVDGRGT GFIGRKARCI 

       730        740        750        760        770        780 
VRGNLGFYEA HDQIATAKMW AAKSYVDETR MAIWGWSFGG FMTLKTLEQD AGRTFQYGMA 

       790        800        810        820        830        840 
VAPVTDWRFY DSIYTERYMH TPQHNPNGYD NSTITDMAAL SESVRFLVMH GASDDNVHLQ 

       850        860        870        880        890        900 
NTLVLIDKLD LSNVENYDVQ FYPDSDHSIY FHNAHMMVYH RLSDWLVNAF NGEWHLIAKP 

       910 
VPDESMWERM KRSLRLLSP 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000002 Genomic DNA. Translation: EAL92790.2.
RefSeqXP_754828.2. XM_749735.2.

3D structure databases

ProteinModelPortalQ4WX13.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00005369.

Protein family/group databases

MEROPSS09.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00005369; CADAFUAP00005369; CADAFUAG00005369.
GeneID3512523.
KEGGafm:AFUA_3G07850.

Phylogenomic databases

HOGENOMHOG000189891.
KOK01282.
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_ASPFU
AccessionPrimary (citable) accession number: Q4WX13
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: April 17, 2007
Last modified: June 11, 2014
This is version 58 of the entry and version 2 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