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Database: UniProt
Entry: A0A317WF80_9EURO
LinkDB: A0A317WF80_9EURO
Original site: A0A317WF80_9EURO 
ID   A0A317WF80_9EURO        Unreviewed;       752 AA.
AC   A0A317WF80;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN   ORFNames=BO94DRAFT_576280 {ECO:0000313|EMBL:PWY83892.1};
OS   Aspergillus sclerotioniger CBS 115572.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY83892.1, ECO:0000313|Proteomes:UP000246702};
RN   [1] {ECO:0000313|EMBL:PWY83892.1, ECO:0000313|Proteomes:UP000246702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY83892.1,
RC   ECO:0000313|Proteomes:UP000246702};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family.
CC       {ECO:0000256|ARBA:ARBA00010040}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWY83892.1}.
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DR   EMBL; MSFK01000018; PWY83892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WF80; -.
DR   STRING; 1450535.A0A317WF80; -.
DR   OrthoDB; 2233567at2759; -.
DR   Proteomes; UP000246702; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:PWY83892.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246702}.
FT   DOMAIN          496..720
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   752 AA;  83951 MW;  919E34CDFB332433 CRC64;
     MAENRKFTPE ALITAPRPSA AVPNDEGKLA LYTVSTYDLD SHTNFTDVKL LDLETGTSSR
     YSNNPKESSF RWLRKSFLLW QREAESKATE LWIGDANHSI RPYLAGTIDA NLDNVKTHRL
     DNGDIALVFT AAADAEQNLY NTSKTDKSHS TAREWTKSRP KRWDTYVDQY RSVIWYTVLK
     FEETSQKWHL STNGPINALR GTGLVVPLYS NSASSTDMDI SKYGILFATA KPGDSEWLET
     QKSLYFVPLS TFDETEAPTL KRIHIPDHAD IVNAPTFAPT GPLAAFLVDQ TSEEWSHKNI
     GLLNVETLTI TSFLRTTDSE SQPWDVFPDE ILWANDNSSL YLTANHQAKT RLFQVPIPTT
     SSSDTQTHLV TPTPLDIPGS ISSIHPVSTS LSNPHLLATS SSFIDQGTFT LLNPTTQTTQ
     TLHTTQTLHT TSSHGAYFNI SSNQITSITF PGGPDGHTPV QTWIIKPSWY NPNTPDKHPL
     FLFMHGGPHS ANRDAWTWRW NALLLAEQGY IVAIPNFTGS DSFGGHFAKS VSLQWGGHPY
     HDIERCFNWV EQNLSSKCDI DRAVAAGASY GGYMALYVAG QPLAKRLKAL VCHDGVFDVV
     SELLSDDLAE KEELTRSFGS PYFTNTENAA LDPASAKEIW RKYNPAEYLT NWSTPLLVIH
     SDKDYRCPST AGWAAYAVCR LKGIETRMLN FPDENHFVLG KENALVWWRT VIGWCNRFVG
     MEAGEGAVVL EEKARSEPRW LGEVVEGRVV DV
//
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