ID A0A1V9ZL47_9STRA Unreviewed; 746 AA.
AC A0A1V9ZL47;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=ACHHYP_08276 {ECO:0000313|EMBL:OQR98719.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR98719.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR98719.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR98719.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR98719.1}.
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DR EMBL; JNBR01000081; OQR98719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9ZL47; -.
DR OrthoDB; 7264at2759; -.
DR Proteomes; UP000243579; 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:OQR98719.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 69..458
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 517..731
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 746 AA; 84069 MW; C0231BA2288AB204 CRC64;
MQRSAGLSIG VGLLSLGMYA VRQRRGVYQA ALAQAKRTPP VLAKKPHMVP FGNVPGEVRG
DAPMDPILYI EDPYYYVRDD TRKNKEVIAH LEKENEYAEH MTSHLKNARE NIYRELLSHV
QETDVAYPYP HGDYLYYTRT EKGSSYTYHC RKSRHDANAK EELILDENEL AKGQSHCDVG
AVSISPDHKF LAYSVDFNGY ETYQGFVKNL VTGEILSDRI ENVSGGLVWG TDASTVYYST
MDDAHRQDKI WRHTVGSSVK DELIYTEDDQ LFSAYMGKTR SGRYLLLQSS SSETSEVSFI
DLQAPAKGVT LVEKRVKGVT YSVDHQGDAF FIETNKDGAT NFKLMTTPVA TPSAAHWTDV
FPYDAAVKVD GIDCFESFSV LHGRQDGFTQ LWIVTKDAAG AFTKERMAFS DPIYTISGAP
NKEYATQTYR LTYSSPTTPF TTYDYDVGSR QMTLLKERPV PNYDRSLYAC ERIEATAEDG
TRVPMSLVYR KDKRTPGTPQ PLHLYGYGSY EICIDPTFSA TTLPLLDRGV IYVIAHIRGG
GEMGRTWYED AKYLTKAKTF SDFVSCAEHL VATKMTQPSL LTCEGRSAGG LLMGAVLNMR
PDLFQAAIAG VPFVDVMNSM CDATIPLTTG EWEEWGNPNE AKYFSYMLSY SPYENVKAQK
YPNILVTSGL FDPRVAYWEP TKWVARLRER KTDDNAILLK MDLTSGHFSA SDRYHYLREK
AFDLSYLLDQ VKCLTPDDHK APAKKD
//
