ID   DPP5_ASPNG              Reviewed;         726 AA.
AC   Q3LS63;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Probable dipeptidyl-peptidase 5;
DE            EC=3.4.14.-;
DE   AltName: Full=Dipeptidyl-peptidase V;
DE            Short=DPP V;
DE            Short=DppV;
DE   Flags: Precursor;
GN   Name=dpp5;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Xue W., Zhao Y., Wang Y., Wang A., Tang G., Zhao W., Qin J., Sims A.H.,
RA   Wang H.;
RT   "Improvement of foreign protein production by disruption of the DppIV and
RT   DppV genes in aspergillus niger.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC       dipeptides sequentially from polypeptides having unsubstituted N-
CC       termini. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR   EMBL; DQ184681; ABA26932.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3LS63; -.
DR   SMR; Q3LS63; -.
DR   STRING; 5061.CADANGAP00009722; -.
DR   ESTHER; aspng-DPP5; Prolyl_oligopeptidase_S9.
DR   MEROPS; S09.012; -.
DR   VEuPathDB; FungiDB:An12g04700; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1150584; -.
DR   VEuPathDB; FungiDB:ATCC64974_37520; -.
DR   VEuPathDB; FungiDB:M747DRAFT_265385; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..726
FT                   /note="Probable dipeptidyl-peptidase 5"
FT                   /id="PRO_0000397819"
FT   ACT_SITE        564
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        647
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        679
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        529
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        611
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   726 AA;  79165 MW;  29A59A8D746C0B9C CRC64;
     MGALQWLSIT AAAASAVSAL TPEQMIGAPR RTEVIPNPSG DTGLFSTSQW SFDTHSESTW
     WSLIDLESGE TTTLTDDSDI EEIIWLGSDS STLLYINSTN AQVPGGVELW IADSSDFANY
     KAASLSAGFL GIKSTVTDSG DVHFILRGKS YPNGTAYNDQ LAETYPSTAR IYDSIFVRHW
     DTYLTTASHA VFSGTLQSST SDDGNVQYTS SGGLTNLVNP VKGAESPFPP FGGNDDYDLS
     PDGKWVTFKS KAPELPLANN TAAYVYLVPH DGSATAFAVN GPDSPATPEG VEGESNNPVF
     SPDSDKIAYF QMATNTYESD RNVLYVYSIA DDTITPLAKD WDRSPSSVTW VDGDNLVVAS
     QDLGRTRLFA IPGDAGTTSS PRTFTDGGSV SAQYVLSNST LLVTSSAFWT SWSVYTASPD
     EGVINTLASA NEIDPELSGL SSSDFEEFYF DGNWTTLQGW ITYPQDFDSS KKYPLAFLIH
     GGPEDAWADE WNLKWHSKVF ADQGYVVVQP NPTGSTGFGQ QLTDAIQLNW TAGAAYDDLT
     KAWQYVHDTY DFIDTDNGVA AGPSFGAFMI TWIQGDDFGR KFKALVSHDG PFIGDAWVET
     DELWFVEHEF NGTFWQARDA FHNTDPSGPS RVLAYSTPQL VIHSDKDYRI PVANGIGLFN
     TLQERGVPSR FLNFPDEDHW VTGQENSLVW YQQVLGWINR YSGVGGSNPD AIALEDTVNP
     VVDLNP