Skip Header

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

Q96VT7

- DAPB_ASPNG

UniProt

Q96VT7 - DAPB_ASPNG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dipeptidyl-aminopeptidase B

Gene

dapB

Organism
Aspergillus niger
Status
Reviewed - 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.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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei739 – 7391Charge relay systemBy similarity
Active sitei816 – 8161Charge relay systemBy similarity
Active sitei849 – 8491Charge relay systemBy similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. serine-type peptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.14.5. 277.

Protein family/group databases

MEROPSiS09.006.

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

Vacuole membrane By similarity; Single-pass type II membrane protein By similarity
Note: Lysosome-like vacuoles.By similarity

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. vacuole Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 901901Dipeptidyl-aminopeptidase BPRO_0000412137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi625 – 6251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi793 – 7931N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ96VT7.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7676CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini98 – 901804VacuolarSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei77 – 9721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1506.

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.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
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:
EMBL
GenBank
DDBJ
Links Updated
AJ278532 Genomic DNA. Translation: CAC41019.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ278532 Genomic DNA. Translation: CAC41019.1 .

3D structure databases

ProteinModelPortali Q96VT7.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.006.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG1506.

Enzyme and pathway databases

BRENDAi 3.4.14.5. 277.

Family and domain databases

Gene3Di 2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view ]
Pfami PF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Characterisation of the Aspergillus niger dapB gene, which encodes a novel fungal type IV dipeptidyl aminopeptidase."
    Jalving R., Godefrooij J., Veen W.J., van Ooyen A.J., Schaap P.J.
    Mol. Genet. Genomics 273:319-325(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Entry informationi

Entry nameiDAPB_ASPNG
AccessioniPrimary (citable) accession number: Q96VT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 56 of the entry and version 1 of the sequence. [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

External Data

Dasty 3