ID U4L853_PYROM Unreviewed; 741 AA.
AC U4L853;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN ORFNames=PCON_09037 {ECO:0000313|EMBL:CCX09444.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX09444.1};
RN [1] {ECO:0000313|EMBL:CCX09444.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX09444.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX09444.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(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; HF935465; CCX09444.1; -; Genomic_DNA.
DR AlphaFoldDB; U4L853; -.
DR STRING; 1076935.U4L853; -.
DR eggNOG; KOG2100; Eukaryota.
DR OMA; ELWFMEH; -.
DR OrthoDB; 5471261at2759; -.
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; 1.
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: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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 524..733
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 310..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 81726 MW; 0284409A13902213 CRC64;
MAYALLEILS TVRASIFPVD RMMFLTTSIM KWSLLAPAVA LAVNATLTPE QAIPLLAATN
LIEAPSRSTA TPNKAGKLAF FTTGHYSLTN HNSTTSLNLL DIQSGKISTI LENTVNVGEI
VWIDDQQLLY VNGSSPDTPG GIELWVTSIH DFSKGRYKAA SIPAPLANLK AVKTKSGDIN
FLMTGKAYAN GTAYNSKLSP KAHSSARVYD SIYVRHWDVY LTPEKYALFS GTLKGPDSYK
FDGKLNNLHK GIKGLETPVQ PFGGSGDFDI TTDGKTVAFL SKAPELPVAN YTTSYIYTVP
FDGSSTAKAV NGPDSKGAPK NARGASASPV FSPDGKTLAY LQMDGATYES DRNKIYTTKV
KSGSIRAIAH NWDRSPSSIV FSNDGKTLFF NVEEHGRQKI FSLPASAGEK ADPKKITNEG
QVDSFYQISD NHLLISNSSL VQSKGYSVVN TSGKEDPKVL FDPRTTDSQL AGLDDSQVDE
FWYKGNWTEI HGWIIKPTGF DPKKKYPLAF LIHGGPQGSW VNGWSRRWNP AAFANQGYVA
VAINPTGSTG YGQDLTDAIQ NNWGGAPYDD LVKGFEYLGK TYDYIDTNNA VAAGASYGGY
MINWIQGQPL GRKFKALVCH DGVYSTLDQY HTEELWFMQH DFNGTLWDNR DNYERWDPAR
HAKNWATPQL VIHNDLDYRL PVSEGIAQFN ILQERGVPSR FLNFPDENHW VVNSENLLVW
MTEIFGWINR WSGTKGTVST S
//