ID A0A0V0S6Z9_9BILA Unreviewed; 696 AA.
AC A0A0V0S6Z9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
DE Flags: Fragment;
GN Name=Prep {ECO:0000313|EMBL:KRX22407.1};
GN ORFNames=T07_5510 {ECO:0000313|EMBL:KRX22407.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22407.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22407.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22407.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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, 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:KRX22407.1}.
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DR EMBL; JYDL01000032; KRX22407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0S6Z9; -.
DR Proteomes; UP000054630; 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; 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; 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.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 17..403
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 468..691
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX22407.1"
SQ SEQUENCE 696 AA; 79529 MW; 811DDAC89B3D7EC8 CRC64;
LKNQFSNMFD KPVHDYPLAR RDEQIQDDYH GTIIKDPYRW LENPYSTETQ TFLCNPESLF
AKIRQRILYY ENYPKYGCYR IAGDYYFYLY NSGLEQHNRL YITNDWKVPG KLFTDVNEND
TEFTTSMKMF SASKDGTLLA FGVTQKGSDW TTVKFRKIPS GELLDDKLEN LRYTSLVWSS
DAKGIFYTTF ANSVAEAVGT CPDKNEFHTL YYHVLGTDQK DDLVVLRFPL NPILMIDATM
SDNEQFLLCT IYEGCSTQTF LYLCDMTTDQ SKADLKAKAK YEFVGVYDSC LIFVTDDNAP
MHKLIKVDIQ KNNEITTILE EVESKRIGFA RIVNHKFLLI DYIENVKDVM YIYDLQTAEQ
IGTLDLPFCT VSSISSRQYL DEFFLKCSSF SLAGMIMHYK INDDGTYVKT IVHSHEFSEN
MQVKQIFYDS KDGTKVPMYI ISKKDMQLNG QNPTILYGYG GFKIALMPSF SVSTMLFVND
FGGVFAIANT RGGGEFGKAW HLAGLKNNRQ NVFDDFIAAA EYLISLNYTR PSLLAIQGGS
CGGMMVAACA NQRPDLFGCL IAQVGVMDML RFQNFTIGRA WTVEFGCSEC KEEFEYLVKF
SPLHNIRSPL APVQYPATLL FTADHDDRVV PCHSLKFMAE LYYQLKDCAH QTNPLLIHID
TDSGHNFNSM SAQKRIDEIV KVLIFIAKVM NLSLNA
//
