Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dipeptidyl-aminopeptidase B

Gene

dapB

Organism
Aspergillus niger
Status
Reviewed-Annotation score: -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.1 Publication

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

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.14.5 518

Protein family/group databases

ESTHERiaspng-DAPB DPP4N_Peptidase_S9

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl-aminopeptidase B (EC:3.4.14.5)
Short name:
DPAP B
Gene namesi
Name:dapB
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004121371 – 901Dipeptidyl-aminopeptidase BAdd BLAST901

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ96VT7
SMRiQ96VT7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2100 Eukaryota
COG1506 LUCA

Family and domain databases

Gene3Di2.140.10.30, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR001375 Peptidase_S9
IPR002469 Peptidase_S9B_N
IPR038554 Peptidase_S9B_N_sf
PfamiView protein in Pfam
PF00930 DPPIV_N, 1 hit
PF00326 Peptidase_S9, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit

Sequencei

Sequence statusi: Complete.

Q96VT7-1 [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 RRLSSKEVVP ITKDGGADLF
310 320 330 340 350
YGIPDWVYEE EVFSGNSVTW WSGDGKYVAF LRTNETAVPE FPVQYYLSRP
360 370 380 390 400
SGKRPPPGLE DYPEVREIKY PKAGAPNPVV SLQFYDVEKQ EVFSIEAPDD
410 420 430 440 450
FEDDDRIVIE IVWGTEGKIL VRATNRESDV LKVFLFDTKA RTSKLVRTEN
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 SQTVDRKFSI DFQSYVASSL GYIVVTVDGR GTGFSGRKTR
710 720 730 740 750
CIVRGNLGYY EAYDQITTAN 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

N
Length:901
Mass (Da):101,256
Last modified:December 1, 2001 - v1
Checksum:i3A519512C903D784
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278532 Genomic DNA Translation: CAC41019.1

Similar proteinsi

Entry informationi

Entry nameiDAPB_ASPNG
AccessioniPrimary (citable) accession number: Q96VT7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: December 1, 2001
Last modified: May 23, 2018
This is version 67 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health