ID K2RI47_MACPH Unreviewed; 734 AA.
AC K2RI47;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN ORFNames=MPH_00440 {ECO:0000313|EMBL:EKG22261.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG22261.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG22261.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG22261.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG22261.1}.
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DR EMBL; AHHD01000026; EKG22261.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RI47; -.
DR STRING; 1126212.K2RI47; -.
DR MEROPS; S09.012; -.
DR VEuPathDB; FungiDB:MPH_00440; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_008615_0_1_1; -.
DR InParanoid; K2RI47; -.
DR OrthoDB; 5471261at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..734
FT /note="Dipeptidyl-peptidase V"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003867613"
FT DOMAIN 495..702
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 734 AA; 79558 MW; D66BD2122AF98D2A CRC64;
MARAGLLPSY LALLLALLAM TIKAAKFTPE VLISAPRRSA GVPNSDGSKV LYTVSTYSFA
DHSSSAELRV LDVASGESTL VTDGDASEPT WLDGGDILVL SSGANGTTDV LVGPYDDFAN
SNYTAGNIDG SASGVKVSAL GDGKYAFVIT ALAKPDGTIY NSEKAATATS TGRYYEAIFV
RHWDSYITPN RNALWYGTLA KDGEQYSLSP LVNALKGTKL ESPVPPFGGT DNFDVSSSGI
AFVAKDPELN PAIYTKINVY IVPLSTFTES APPAPIQVET TGFEGQSTSP VFSPDGKSLA
FLRMREIQYE SDKLQLFVVP DVSKPASTIN ALSTPDNKGS WDRSPSAVTW STDGKTLYLT
AENIGRVSLY SYPTPTSNSS SSDEPTLIFN DGGVSDAHAL ENGDIFISGS NLIDNSVYFT
LTPGEEPVQV SSNSKNGALF GISRSQVSEI WFPGAANGTK IHAWVIVPSN FSSNTTWPLA
YLIHGGPQGA WEDSWSTRWN PLAFAEQGYV VVAPNPTGST GYGKALTDAI QGEWGGLPYQ
DIVNGFTYIE NNLKYVDTDR AVELGASYGG YMTNWIQGHD LGRKFKALVT HDGVFSMTAQ
LASEEIWFPE HDLEGKYWDN RQSWLEWDPS AHTDKWATPH LIIHNELDYR LTIAEGLAAF
NVLQNRGVES AFLSFPDENH WVLKPENSLV WHTAVFDWIN SRVGLPTLSE QSAYAKGTKE
EAFQNRESDL GLKV
//
