ID M7T8F5_EUTLA Unreviewed; 686 AA.
AC M7T8F5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN ORFNames=UCREL1_10124 {ECO:0000313|EMBL:EMR62940.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR62940.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S9C family.
CC {ECO:0000256|ARBA:ARBA00010040}.
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DR EMBL; KB707331; EMR62940.1; -; Genomic_DNA.
DR RefSeq; XP_007797966.1; XM_007799775.1.
DR AlphaFoldDB; M7T8F5; -.
DR KEGG; ela:UCREL1_10124; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_008615_0_1_1; -.
DR OMA; YPVRYWD; -.
DR OrthoDB; 5471261at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..686
FT /note="Dipeptidyl-peptidase V"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004085513"
FT DOMAIN 482..678
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 686 AA; 75579 MW; 339A02300DD1F037 CRC64;
MKRISRSLAA VALATLSRVS ALTPEGLISA NRYSDAAPNP SGEFALFTVS KYSFDTKETS
SVWKKLDLAT GDISVWYEGS DISEVVFVGS DPTSIIYVNG TNEEDNGGIS LYSANALELE
KAKLVASLPA PYSGLKAAQT DSGDIHFLVY SKAYPNGTAY NEALASTSAS TARIYNSIYV
RHWDTWLTAD RNAVFGGVLK GGNGSYALSG DLTNYVTGIS NVTSAESPYD QSDQNDYDIS
PDGSAIVFLT KDISLPLANY TSTQIYYVPF GGSAEDAVPI NPRGGTKYPD AQGASSTPRF
SPSGKKIAYL QQNGIYYESD RNILYVADAD PEDFNVTSLA LDWDRSPDTV VWSKDSETIF
VAAPDLGRER IFPIPLSAGD SYEPKNITNE GVPTAFYVLP DESILVSDSK IWTSRDIYTV
TPEGEVTQTY FQANLVDPEL AGLGPEILSE FYYETNSTEI KQQSWIVYPE NFDESINVNP
GGSVVIAPNP TASSGFGQNL TDAIQGNWGS LPYWDLVHTW DYVNETLDYV DTSRGIEAGA
SFGGYMTNWI QGHELGRRFK ALVTHDGSTS TLNQYASEEL WFMNHDFQGP FNETGLKPGS
PYYDWNPLLY VDNWQTVHND LDFRLPVSEG ILLFNMLQTK GVPSKFLNFP DENHWVISPE
NSLVWHTEIF KWINYYSGIS NATSPY
//
