ID   DPP5_ASPTN              Reviewed;         723 AA.
AC   Q0C8V9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=ATEG_09875;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-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; CH476608; EAU30066.1; -; Genomic_DNA.
DR   RefSeq; XP_001218497.1; XM_001218496.1.
DR   AlphaFoldDB; Q0C8V9; -.
DR   SMR; Q0C8V9; -.
DR   STRING; 341663.Q0C8V9; -.
DR   ESTHER; asptn-dpp5; Prolyl_oligopeptidase_S9.
DR   MEROPS; S09.012; -.
DR   EnsemblFungi; EAU30066; EAU30066; ATEG_09875.
DR   GeneID; 4354286; -.
DR   VEuPathDB; FungiDB:ATEG_09875; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_008615_0_1_1; -.
DR   OMA; STRWNPK; -.
DR   OrthoDB; 265965at2759; -.
DR   Proteomes; UP000007963; 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..723
FT                   /note="Probable dipeptidyl-peptidase 5"
FT                   /id="PRO_0000397820"
FT   ACT_SITE        561
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        644
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        676
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        79
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        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        608
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   723 AA;  79627 MW;  5E6A1542A60BBE4E CRC64;
     MAALRWLSAV VAVSTTVLAI TPEQMLSAPR RGEAIPNPSG NVALFSASQY SFDTKEKSSS
     WNLLNLKTGD ITLLTDDANV SEIVWLGGDD TSLLYINGTN AEIPGGVELW VSSVKDFSKG
     YKAASLGASF SGLKAVRTRS GDIKFAVNAQ SYANGTAYNE ELATKYASTA RIYDSIYVRH
     WDTYLTTTFN AVFAGTLKKG KHQYASAGPL KNLVAPVKNA ESPYPPFGDS TDYDVSPDGK
     WVAFKSKAPD VPRANYTTAY IYLAPHDGSS TATPINGPDS PGTPEGVQGD ANYPVFSPDS
     RHLAYFQMAH KSYESDRRVL YVYTLGSKTT TPAVAGDWNR SPDSAKWLDN KHLILGSEDH
     ARVRLFGPVP IDADDDFKPQ NFTDGGAVSS YHVLPDKTVL VTGTAIWTSW NVYTASPKKG
     VIKTIASANK IDPGLAGLGP EDISEFYYDG NWTKIQSWII YPENFDSSKK YPLFFYIHGG
     PQSATPDSWS TRWNAKVFAD QGYVVVAPNP TGSTGFGQEL TDAIANNWGG APYEDLVKAW
     EYVDKNLPYV DTENGVAAGA SYGGFMINWI QGSDLGRKFK ALVCHDGTFV ADAKISTEEL
     WFIEHDFNGT FWGARDNYRR WDPSAPERIL QFSTPQLVIH SDQDYRLPVA EGLAMFNVLQ
     ERGVPSRFLN FPDENHWVLK QENSLVWHQQ MLGWLNRYSG IEEANPDAVS LDDTIIPVVN
     YNP