ID   DPP5_ASPCL              Reviewed;         724 AA.
AC   A1CSW4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=ACLA_080850;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027060; EAW06401.1; -; Genomic_DNA.
DR   RefSeq; XP_001267827.1; XM_001267826.1.
DR   AlphaFoldDB; A1CSW4; -.
DR   SMR; A1CSW4; -.
DR   STRING; 5057.CADACLAP00007735; -.
DR   ESTHER; aspcl-dpp5; Prolyl_oligopeptidase_S9.
DR   MEROPS; S09.012; -.
DR   EnsemblFungi; EAW06401; EAW06401; ACLA_080850.
DR   GeneID; 4700146; -.
DR   KEGG; act:ACLA_080850; -.
DR   VEuPathDB; FungiDB:ACLA_080850; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_008615_0_1_1; -.
DR   OMA; STRWNPK; -.
DR   OrthoDB; 265965at2759; -.
DR   Proteomes; UP000006701; 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; IPR001375; Peptidase_S9.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..724
FT                   /note="Probable dipeptidyl-peptidase 5"
FT                   /id="PRO_0000397817"
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        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
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   724 AA;  79926 MW;  44AFD7DF4D204FA4 CRC64;
     MGALTWLSVV AAAASTALAM TPEKMISAPR RSEVIPNPSG EIGVFSTSQY SFEKHKRSSW
     WSLLDLKTGQ SKILTNDSSV SEILWLGTDD STLLYVNGTN ADVPGGVELW VTQVSSFTNG
     YKAASLPAAF SGFKTVTTKS GDIRFVAYAQ SYANGTAYNE ELVEKPLSSA RIYDSIYVRH
     WDSYLTTTFN AVFSGTLKKG NNKKGYTLDG AVKNLVSPVR NAESPYPPFG GASDYDLSPN
     GKWVAFKSKA PELPKANFTT AYIYLVPHDG SEKAFAINGP DSPGTPKGIK GDANSPVFSP
     NSEKLAYLQM KDETYEADRR VLYVYSIGSK KTIPSVAGNW DRSPDSIKWT PDGKTLIVGS
     EDKGRSRLFA IPATARDDFK PKNFTDGGAV SAYYFLPDRS LLVTGTAIWT NWNVYTASPA
     KGVIKTLASA NEIDPELKGL GPSDVSEIYF KGNWTDIHAW VVYPENFDKS KKYPLAFLIH
     GGPQGSWADS WSSRWNPKTF ADQGYVVVAP NPTGSTGFGQ KLTDEIQNNW GGAPYDDLVK
     CWEYVNKNLP FVDTEHGIAA GASYGGFMVN WIQGNDLGRR FKALVSHDGT FVADAKISTD
     ELWFMQREFN GTFWDARDNY RRFDPSAPEH IRQFGTPQLV IHNDKDYRLA VAEGLSLFNV
     LQERGVPSRF LNFPDENHWV VNPENSLVWH QQVLGWINKY SGIEKSNPGA VSLDDTIVPV
     VNYN