ID   F8N311_NEUT8            Unreviewed;       751 AA.
AC   F8N311;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN   ORFNames=NEUTE1DRAFT_72228 {ECO:0000313|EMBL:EGO52522.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO52522.1};
RN   [1] {ECO:0000313|EMBL:EGO52522.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO52522.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family.
CC       {ECO:0000256|ARBA:ARBA00010040}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL891382; EGO52522.1; -; Genomic_DNA.
DR   RefSeq; XP_009856163.1; XM_009857861.1.
DR   AlphaFoldDB; F8N311; -.
DR   MEROPS; S09.012; -.
DR   GeneID; 20829580; -.
DR   KEGG; nte:NEUTE1DRAFT72228; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_72228; -.
DR   HOGENOM; CLU_008615_0_1_1; -.
DR   OrthoDB; 5471261at2759; -.
DR   Proteomes; UP000008065; 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   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..751
FT                   /note="Dipeptidyl-peptidase V"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005678394"
FT   DOMAIN          520..729
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   751 AA;  83126 MW;  230627150B6514B6 CRC64;
     MWSLLLLHPF WNLVLSCILL ISAFPGADAS DISIAVSNMT LTATKFTPEV LLTAPRRSPA
     IPNAKGTKAL FTVTTYSFET HRKTSQIRLL DIESGQSTLL VDDLSASEPT WIGDDEFLYL
     KSGEKGNTTV LVDKIARPGS QAYEVTTIKA RISNIKIKEL TNGTVAFVCS ASATPDGQLS
     NPATAKKPYS SAKVYTSLFV RHWDEWLGED KNSLWYTALE KKNGRFTLTG NGLVNALAGS
     KLESPVPPFG GTGDFDISPT GLVFVAKDPE LNPALYTKTD LYYVPLKTFT EEQPPSPQIV
     ETPGLEGYTN SPVFSHCGRK VAFTRMRSKQ YESDKPRLVL LPDIGDLSKT EEFFASDDGE
     GAWDYRPETI LWSADDKSLY VTAEKNGRVH LWEVPSNPAD AKDTPSVIKT ADGSVNDIRL
     LAEAESSSKL LVSSTSLVDN SCYSIVNPSA NSTDIVSSNS KQGKTFGLSR SSIGDITFKG
     AGDYDVHALV VRPSNFDEKK KYPLCFLIHG GPQGAWQDGW SNRWNPAVFA EQGYVVVSPN
     PTGSTGYGMA LQNGIKGQWG GRPYEDLVKA FEHIEENMPY VDTDRAVALG ASYGGYMINW
     IQGHPLGRKF KALVCHDGVF STLNQWSTEE LFFPIHDFEG TIYDNRAGYE KWDPAQHVNE
     WAIPQLIIHS ELDYRLPITE GLAPFNVLQS KGIPSKLVMF PDENHWVLKP ENSLVWHEQV
     LAWINKYSGV EKETQEVKEI AIVEDKRQKT M
//