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Protein

Probable dipeptidyl-aminopeptidase B

Gene

dapB

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei739Charge relay systemBy similarity1
Active sitei816Charge relay systemBy similarity1
Active sitei849Charge relay systemBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Protein family/group databases

ESTHERiaspng-DAPB. DPP4N_Peptidase_S9.
MEROPSiS09.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable dipeptidyl-aminopeptidase B (EC:3.4.14.5)
Short name:
DPAP B
Gene namesi
Name:dapB
ORF Names:An02g11420
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006706 Componenti: Chromosome 4R

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 76CytoplasmicSequence analysisAdd BLAST76
Transmembranei77 – 97Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini98 – 901VacuolarSequence analysisAdd BLAST804

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004121361 – 901Probable dipeptidyl-aminopeptidase BAdd BLAST901

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi334N-linked (GlcNAc...)Sequence analysis1
Glycosylationi625N-linked (GlcNAc...)Sequence analysis1
Glycosylationi793N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA2QEK7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi120 – 125Poly-Ser6

Sequence similaritiesi

Belongs to the peptidase S9B family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000189891.
OrthoDBiEOG092C0PZJ.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B_N.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

A2QEK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPRPSTSS TSSDSGLSVD TTAYPEESKY TSTAPGAGGL SDENRYRDVE
60 70 80 90 100
EGEAGADEPF LPSAKKQAAS GSRTSRLIWG LVILCVAGWL WGLVLFVTQN
110 120 130 140 150
RSAQQSVSEA LQSHESGAIS GSSSSGKPVT LEQVLTGQWL PRSHAVSWIA
160 170 180 190 200
GPNGEDGLLV EQGEDQGKGY LRVDDIRSRK GDATSQESRV LMEKAIVQVD
210 220 230 240 250
GRTIFPVSTW PSPNLNKVLL LSEREKNWRH SFTGKYWIFD VATQTAQPLD
260 270 280 290 300
PSNPDGRVQL AIWSPTSDMV AFVRDNNLYL RKLSSKEVVP ITKDGGADLF
310 320 330 340 350
YGIPDWVYEE EVFSGNSVTW WSGDGKYVAF LRTNETAVPE FPVQYYLSRP
360 370 380 390 400
SGKRPPPGLE DYPEVREIKY PKAGAPNPVV SLQFYDVEKQ EVFSIEAPDN
410 420 430 440 450
FEDDDRIIIE IVWGTEGKIL VRATNRESDV LKVFLFDTKA RTSKLVRVEN
460 470 480 490 500
VADIDGGWVE PTQYTWFIPA DPSNGRPHDG YLDTVIHEGY EHLGYFTPLD
510 520 530 540 550
NSEPILLTQG EWEVVDAPTA VDLRKGIVYF ISTKESPTER HLYQVNLDGS
560 570 580 590 600
NLKPLTDTSK PGYYDVSFSH GTGYALLSYR GPSIPWQAIV NTETDELKYE
610 620 630 640 650
ETIEDNAGLA RMVDSYALPT EIYQNVTIDG FTLQVVERRP PHFNPAKKYP
660 670 680 690 700
VLFYLYNGPR SQTVDRKFNI DFQSYVASSL GYIVVTVDGR GTGFSGRKTR
710 720 730 740 750
CIVRGNLGYY EAYDQITTAK LWGEKPYVDE TRMSIWGWSY GGFMTLKTLE
760 770 780 790 800
QDAGQTFQYG MAVAPVTDWR HYDSIYTERY MHTPAHNPNG YDNTSITDMT
810 820 830 840 850
ALQQTVRFLV IHGASDDNVH IQNTLVLVDK LDLAGVQNYD LHFYPDSDHS
860 870 880 890 900
INFHNAHRMV YERLSSWLVN AFNDEWHRIA DPVPDDSMWE KVKRSLPMLV

K
Length:901
Mass (Da):101,294
Last modified:March 6, 2007 - v1
Checksum:iF058BA27F2450237
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270029 Genomic DNA. Translation: CAK37870.1.

Genome annotation databases

EnsemblFungiiCAK37870; CAK37870; An02g11420.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270029 Genomic DNA. Translation: CAK37870.1.

3D structure databases

ProteinModelPortaliA2QEK7.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiaspng-DAPB. DPP4N_Peptidase_S9.
MEROPSiS09.006.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAK37870; CAK37870; An02g11420.

Phylogenomic databases

HOGENOMiHOG000189891.
OrthoDBiEOG092C0PZJ.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B_N.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDAPB_ASPNC
AccessioniPrimary (citable) accession number: A2QEK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: March 6, 2007
Last modified: November 2, 2016
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.