ID   A0A0N0RS32_9BASI        Unreviewed;       721 AA.
AC   A0A0N0RS32;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN   ORFNames=Malapachy_0070 {ECO:0000313|EMBL:KOS13329.1};
OS   Malassezia pachydermatis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS13329.1, ECO:0000313|Proteomes:UP000037751};
RN   [1] {ECO:0000313|EMBL:KOS13329.1, ECO:0000313|Proteomes:UP000037751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS13329.1,
RC   ECO:0000313|Proteomes:UP000037751};
RA   Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT   "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT   pachydermatis CBS1879.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC         H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043665};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC         Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043831};
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:KOS13329.1}.
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DR   EMBL; LGAV01000006; KOS13329.1; -; Genomic_DNA.
DR   RefSeq; XP_017990961.1; XM_018134603.1.
DR   AlphaFoldDB; A0A0N0RS32; -.
DR   STRING; 77020.A0A0N0RS32; -.
DR   GeneID; 28726478; -.
DR   VEuPathDB; FungiDB:Malapachy_0070; -.
DR   OrthoDB; 5471261at2759; -.
DR   Proteomes; UP000037751; 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, ECO:0000313|EMBL:KOS13329.1};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037751};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..721
FT                   /note="Dipeptidyl-peptidase V"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005857615"
FT   DOMAIN          497..706
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   721 AA;  80876 MW;  FA8EB44315651022 CRC64;
     MFVRWHLPVI GAVCLAAQAI ASHVLTPELL MEAPRPASVV ANEAGTAAVI GVSTFSSQTG
     DESKALYHIP LTQARAWDEA PNVRVLTNDT TEAAFVDDDT LLYVKDNQVC QRSLHATLKG
     TACHAVAELP TSIKYLKVAR TSKNKATLVF AATVYDDGDL YAVAKHDRSK ESERWKHAKV
     YDTMFARHWD QWMDPRRRSQ LFALDVHRDP TTAAWHAKGS IRNLMRGTKL ETPVGPLGEA
     TDFSVSSNWV AFVAKDLHVP PAWHTKQQVF LVPIDGSKAP RQISSNNRHG WTGIPAISPN
     EDMVVFLQQD KDGFESDLKV LQTYSLHDGT LRTFHRDWDM SPTALTFSAD GAWLYAVVTE
     DEQRPIYRMP VDGAHLGPRT ALVTHGSVSN VVPLKHDRMV YTRSTLHHPN DVYLLHVDED
     EERALRLTNF FRWSKAHRDI DLGPKPERFT YAGSNDVPMH GWILKPPSFT KAKELGEKLP
     LAVLIHGGPE SDWNDGWSIR WNPATFAAAG FVVVTLDPSG STGFGQALTD RILEHWGDRP
     LDDVMKGVHY VLDTKSYIDR DRVVAAGASF GGYMVNMLQG HNDEKLFKAL VTHDGAFNTM
     AMAYSTDELY FAESEFGGVP WERPELLDKF SPHQFVHKWN TPHLIVHGGH DFRLSPAEGV
     SAFHALQRRG VPSRLLFFPE ESHWVQETVN AVQWHHEVLG WLQQWSAPSD ERTAPVPLVF
     Q
//