ID   DPP5_ASPFN              Reviewed;         725 AA.
AC   B8NBM3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 69.
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; ORFNames=AFLA_045980;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED52896.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; EQ963476; EED52896.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002378060.1; XM_002378019.1.
DR   AlphaFoldDB; B8NBM3; -.
DR   SMR; B8NBM3; -.
DR   STRING; 5059.CADAFLAP00005925; -.
DR   ESTHER; aspor-Q9Y8E3; Prolyl_oligopeptidase_S9.
DR   MEROPS; S09.012; -.
DR   EnsemblFungi; EED52896; EED52896; AFLA_045980.
DR   eggNOG; KOG2100; Eukaryota.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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; IPR011659; PD40.
DR   InterPro; IPR001375; Peptidase_S9.
DR   Pfam; PF07676; PD40; 1.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..725
FT                   /note="Probable dipeptidyl-peptidase 5"
FT                   /id="PRO_0000397818"
FT   ACT_SITE        563
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        646
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        678
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
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        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        383
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        610
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   725 AA;  80384 MW;  AD5C7FD79F5D666E CRC64;
     MGALRWLSIA ATASTALALN PEGLISAPRR SEAIPNPSGD VAVFSQSQYS FKTHKTTSQW
     NVLDLKSGDI KLLTNDSDVS EIVWLGSDDS TVLYVNGTNA DIPGGVELWV SDISDFANGY
     KAASLPASFS GFKVVTTDSG DVRYVAYAES WANGTAYNEE LVAKPLSSAR IYDSIYVRHW
     DYYLTTRFNA VFSGTLKKSE GKGKATYKAD GDLKNLVSPV KNAESPYPPF GGASDYDLSP
     DGKWVAFKSK AHDIPRANYT TAYIFLVPHD GSKTAVPING PDSPGTPEGV KGDAGSPVFS
     PDSKKIAYWQ MADESYEADH RTLYVYTVGS EETIPSLAAD WDRSLDSVKW ADDDNLIIGV
     EDAGRSRLFS IPADAGDDYK PKNFTDGGVV SAYYQLPDST YLVTSTAIWT SWNVYIASPE
     KGVIKTLATA NKIDPELKGL GPEIVDEFYY EGNWTKIQAF VIYPENFDKS KSYPLLYYIH
     GGPQSSWLDS WSTRWNPKVF ADQGYVVVAP NPTGSSGFGD ALQDAIQNQW GGYPYEDLVK
     GWEYVNENFD FIDTDNGVAA GASYGGFMIN WIQGSDLGRK FKALVSHDGT FVADAKVSTE
     ELWFMQHEFN GTFWDNRENY RRWDPSAPER ILKFSTPMLI IHSDLDYRLP VSEGLSLFNI
     LQERGVPSRF LNFPDENHWV QNKENSLVWH QQVLGWLNKY SGVEESNEDA VSLDDTVIPV
     VDYNP