ID A0A094ZGV4_SCHHA Unreviewed; 555 AA.
AC A0A094ZGV4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=MS3_01899 {ECO:0000313|EMBL:KGB33720.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB33720.1};
RN [1] {ECO:0000313|EMBL:KGB33720.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
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}.
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DR EMBL; KL250565; KGB33720.1; -; Genomic_DNA.
DR RefSeq; XP_012793484.1; XM_012938030.1.
DR AlphaFoldDB; A0A094ZGV4; -.
DR STRING; 6185.A0A094ZGV4; -.
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; 2.
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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 5..313
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 407..548
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 535..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 62725 MW; D9B66390B958756D CRC64;
MKTLSGPTKT FLDPNEIDPE GLTSLRNYSF SVEGTYCCYG LSFGGSDWSE LKFKTCESGK
DLPDVLKHVK FSSISWTKDE KGVFYCMYPQ HEGKADGTET TTNTDQKLMY HRLGTPQSDD
ILFLERPDHP TWNIQGEVSD CGRYLLVTLY DGCEPNNQLF YCDLEKFDLI IKKKIELIPI
VDRFEAVYEY VTNEGDSFVF RTNLDAPMYK IIKINLSNCD RQHWEDLIDH NVESLLESAV
CVNEDKLIIC HLKNVKSCLS VHKLLTGEKI SDIDISLGCV ANVTGRKRDD EAFIHFTSFL
TPGIIYSYNF SHSHPKLEVI RESKIRDVDL DQFEVKQVFY ESKDKTVVPM FLVLPKNFQQ
NNSAPCQLYG YGGFNISVTP SFSVGRLFFL MHFGGIIAVA NIRGGGLYIQ GGSNGGLLVC
ACCNQRPDLF KAAIAQVPVC DLIRFHKFTI GHAWKSDYGD PDNKKDFSNL MRISPLHNVK
IPSNPDVQYP ALLILTADHD DRVVPLHSFK FIATLQEKLC RNCRQTNPIL IRIEPKAGHG
QGKPTSKSVS LQANK
//
