ID A0A183CA04_GLOPA Unreviewed; 1018 AA.
AC A0A183CA04;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
DE AltName: Full=Post-proline cleaving enzyme {ECO:0000256|ARBA:ARBA00029698};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000970300};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_000970300}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228}.
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DR AlphaFoldDB; A0A183CA04; -.
DR WBParaSite; GPLIN_000970300; GPLIN_000970300; GPLIN_000970300.
DR Proteomes; UP000050741; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 2.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1018
FT /note="Prolyl endopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008147327"
FT DOMAIN 82..490
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT REPEAT 569..601
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 604..623
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 622..745
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 800..1012
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 1018 AA; 115440 MW; 4FFA4A7B378591FA CRC64;
MFLLPTLFLI WFDTLNGQKP IGWSIGEQKL KTENLFPPKN DFDDGQTTFK GDKVEKKAAT
IFSPEDSYCE SFNVDIHPDE YPIARRNESV VERICEQKVM DPYRWMENPD RAETKQFVTE
LNDLSRPFLE KAFFRSQFRK KMKQLFDQKA YGCISKHGDF YYYAYSEGTQ KQSAIYRQQT
LSSQKELFLD PNQFSSDGTA AIVQSAFSRD GQIMAYTVAD KGSDLSTIRF RDVKGNDLPD
KIRNVKQSSL AWMPNNKGIF YSKYAQRKRA TNETQVTKDE FHSLFYHRMG TKAEKDVLIA
DFRELDDPTL SISGSVSRDG RFLFVYVYDK DSANTVYYLD LKAVNYKIQR KPALSLLIHD
TRAFFIILDY DHESESALVL TDHTAPNRKL IRIGMSTAIL GCAHWDTVIA EDPDRTLDSV
VPVAGDKLLV VYIEDTYLYV HHYATGKLHY RIPLGIGTVN QCYGDRDDTE AFFSFNSFLE
PPTFYRADFS LVEKTGHAAK TVEIYNARKK LLEIRWAAKK EALIETDAES SAAGAQLLRS
SAEGDVEILG SLLGLENAVQ LVQGTRNKFG ATALHLAAGN GREKALRMLL EAGGRAQTEA
GDDDGETALH WAAREGHVEI LDYDHESESA LVLTDHTAPN RKLIRIGMST AILGCAHWDT
VIAEDPDRTL DSVVPVAGDK LLVVYIEDVK TYLYVHHYAT GKLHYRIPLG IGTVNQCYGD
RDDTEAFFSF NSFLEPPTFY RADFSLVEKT RDGTKVPIFI ISRNDTKRDG SNPALLYGYG
GFNIPLLPSY SSHRNIFVKH FRGVVAIANI RGGGEYGERW HECGARSHKQ NVFDDFIGAA
EFLIEQKYTS PRKLAIQGGS NGGLLVAACS QQRPELFGAV INQVGVMDML RFHKFTVGSY
WINEYGDPEK PDEFEYIYKY SPLHNIRLSR GIQWPATLLM TADHDDRVVP SHTLKYAAQL
YHYLKKPEVK LIQRNPVIAR VETDAGHGAG KPRDKVIDEL SDIMSFLQRV LQLKWYDD
//
