ID E4ZRP2_LEPMJ Unreviewed; 787 AA.
AC E4ZRP2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN ORFNames=LEMA_P035630.1 {ECO:0000313|EMBL:CBX93889.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the peptidase S9C family.
CC {ECO:0000256|ARBA:ARBA00010040}.
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DR EMBL; FP929116; CBX93889.1; -; Genomic_DNA.
DR RefSeq; XP_003837329.1; XM_003837281.1.
DR AlphaFoldDB; E4ZRP2; -.
DR STRING; 985895.E4ZRP2; -.
DR EnsemblFungi; CBX93889; CBX93889; LEMA_P035630.1.
DR GeneID; 13284434; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_008615_0_1_1; -.
DR InParanoid; E4ZRP2; -.
DR OMA; YPVRYWD; -.
DR OrthoDB; 5471261at2759; -.
DR Proteomes; UP000002668; Genome.
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:SF11; DIPEPTIDYL-PEPTIDASE 5-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 568..776
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 345..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 87083 MW; C91C9EC347EA2A15 CRC64;
MTDGKKRVCC TVRYRQPARS RDPAGNARMA DRINVAQHLD IQISLLPFLE LGSLPFIDLV
QLSFYEAGRI CNGSLPEYCR SIGRDWRLLL LSTVRRGAAE PSPDGSVALF TYSQYSFEEH
SGSSGLNQID LKTGDISESG WNASEINEFV WLPGTETGIL YINGTNEEVP GGVTLWMGDF
KSPNTSTMVA SLDAPYSGLR VANTSSGDLH FLVHSMAYPN GTAVNPETEV VPHSTARLYS
NIYARHWDTW LTKNRYAVFA GALSANNSYA LAGTGLRNLN HGINFTTTQP ETPIQPFGDS
SDYAISPDGS MYAFVSKAPQ LNKANYTASY AYVGSFASSE PPVAFNGPES EAAQAGHKGA
SGQPSFSKDS SKLAYIQQDE DYYESDRWIL YTVDVSVEGN GVSVSNWKSL SAGFDRWVQG
PLTWAEDDQS IFVTAEDYGR VKVFNFPIDA DESFVPEPMT SNTSVSSFSV LPSGSLFVTG
TAVWTPTEYY TVTNGTKHTL FDASQVDPNL AGLGAHSFSE IFFNASNPAQ KDPLHAIVVK
PSNYMENQTY PLAFLIHGGP QGAWLNSWSN RWNPQVWADQ GYIVVAPNPT GSTGFGQALT
DAVQGAWGSW PYEDLVNAWN YVDTNMNWID TANGFAAGAS YGGYMTNWIQ SHDLGRKFKA
LVTHDGISNT QGAWASEELW FIRHDYNGSI WESDAYNKWN PQNHIANWST PQFVIHNTLD
YRLPESDGLS LFNILQARGV PSRFLNFPDE NHWVLKQENS LVWHEEIFNW VNHYSKGEPL
NDEPVGY
//