ID A0A225VCN3_9STRA Unreviewed; 743 AA.
AC A0A225VCN3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=PHMEG_00025230 {ECO:0000313|EMBL:OWZ03102.1};
OS Phytophthora megakarya.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ03102.1, ECO:0000313|Proteomes:UP000198211};
RN [1] {ECO:0000313|Proteomes:UP000198211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT of cacao black pod achieved similar genome size and gene model numbers by
RT different mechanisms.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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:OWZ03102.1}.
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DR EMBL; NBNE01005729; OWZ03102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225VCN3; -.
DR EnsemblProtists; OWZ03102; OWZ03102; PHMEG_00025230.
DR OrthoDB; 7264at2759; -.
DR Proteomes; UP000198211; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024, ECO:0000313|EMBL:OWZ03102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198211};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 69..453
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 516..727
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 743 AA; 85201 MW; CFFD68B7CAB30A47 CRC64;
MSRLSALNLT IGVSTAAALY MVRLRRTAYS TLSKRVRPPV LEKRPKMVPF GAVAGQNRGL
TPMKPILHLE DPYFYVRDDS RKNEEVLEHL RKENDYTDVK TKHLSNVRAN IYDELLSHVQ
ETDEDYPHPH GPYLYYNRTV KGSSYSYHCR KAKTENAKEE LLLDENEIAK GHNHCQVASV
SASPDHRYLA YMVDFSGYET YTGYVKDLQT GELLPDRIEN ISSLRWGRDA SVLYYATQDE
AHRQNKLWCH KMGSKDADEL LYTEDDEIYS AYFQKARSGK YMFLLSSSSE TSEVSFIDLE
NPSNPPQLIA KRQKGLIYGV DHFGDSFYIV TNKDKATNFK LMKTSVNTPS LENWVDVFPY
DESIKVDDID CFKDFMVMEG RQGGYSQLWI IVPEGDKHAR RQITFKESSY TVAGSVNRDF
DTDKYRFVYS SMTTPWTTFD YDVNTRESKL LKEKPVPNYD RSLYKTERLE AKASDGTMVP
ISLVYRSDLR SQDRQPLHLY GYGSYEIPID PSFVSSILPL LDRGVIYAIA HIRGGGEMGR
TWYEDAKYKK KINTFSDFIS CAEHLVQTGY TSPSKMTCEG RSAGGLLMGA VLNMRPDLFT
AAIAGVPFVD VMNTMSDATI PLTTGEWEEW GNPNEKAYFE YMLSYSPYEN VTQQAYPNIL
VTSGLYDPRV AYWEPTKWVA KLRDMKSDQN EVLLKMDLSS GHFSASDRYH YLKEKAFDLS
YLLDHLKAIK EDDKKTPKTA AKL
//
