ID   A0A1W2TWG7_ROSNE        Unreviewed;       726 AA.
AC   A0A1W2TWG7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN   ORFNames=SAMD00023353_0403800 {ECO:0000313|EMBL:GAP92971.1};
OS   Rosellinia necatrix (White root-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX   NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP92971.1};
RN   [1] {ECO:0000313|EMBL:GAP92971.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W97 {ECO:0000313|EMBL:GAP92971.1};
RA   Kanematsu S.;
RT   "Draft genome sequence of Rosellinia necatrix.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family.
CC       {ECO:0000256|ARBA:ARBA00010040}.
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DR   EMBL; DF977449; GAP92971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2TWG7; -.
DR   STRING; 77044.A0A1W2TWG7; -.
DR   OMA; IFNWIRY; -.
DR   OrthoDB; 5471261at2759; -.
DR   Proteomes; UP000054516; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF11; DIPEPTIDYL-PEPTIDASE 5-RELATED; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF07676; PD40; 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   Aminopeptidase {ECO:0000313|EMBL:GAP92971.1};
KW   Hydrolase {ECO:0000313|EMBL:GAP92971.1};
KW   Protease {ECO:0000313|EMBL:GAP92971.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054516};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..726
FT                   /note="Dipeptidyl-peptidase V"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010719060"
FT   DOMAIN          504..713
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          291..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   726 AA;  79709 MW;  6B61B61DBFE40D1B CRC64;
     MAFKKVVVFA LGTVLPWANA LTIEGMLGAP RRSTANVNPS GKWALFTATS YDWDAQKSST
     TWNLLDVASG KVKLAPFGSD VSEVVWIGDT DTSILYINGT NDNVAGGVTL YTADIGAKTF
     SPTLVASLEA PFQGLKAVQT KSGDINFVVN TLANWNDGSA YNPELATASL SSGAIFDANY
     IRHWDVYITP ERYAVFSGKL ALGKECATRG KKCHSLKGGV KNLLLGINAT VTRPETPVQP
     FGDQGDYDLS PDGQTVAFLT KAPELSKANH TASYIYLVPH DGSKAPVSVN GPGTSAPANA
     KGASGAPHWS PDGKKLAYIQ QDGVAYESDR YKLYVATVSG LNAKVSAVAE DWDSSPSSLQ
     WTPNGKDLWV ASELHASTRL FVVPYNAKSS FVPKNFTGPD TNLADFTILP NGRALVSAAA
     SWTSRVFYTQ APGKDKKILF TANEVDPELK GLKPDSVSNF WVENDDGDKI QTFVFYPTDF
     DPNKKYPLAF IIHGGPQSSQ GDSWSTRWNL RLWAEQGFVV TTVQFTGTPS YGQAFTDKIQ
     NNWGGTPYTD LVTVFEHLKH NVPYVDTDRA VAAGASFGCY MTNWIQGHAL GREFKALVCH
     DGKVNQVAAY ATDELWFIQH DSNGTIWDDR ENYELWDPLM HARDFATPEF IIHSDGDYRV
     SVTEGIQTFN ILQSLGVPSR FLHFPDETHW ISNRHNSVLW HSSIFNWIRY WVGLDEELIQ
     DGVVHM
//