ID B3SCR3_TRIAD Unreviewed; 751 AA.
AC B3SCR3;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=TRIADDRAFT_62068 {ECO:0000313|EMBL:EDV19515.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV19515.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV19515.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV19515.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR EMBL; DS985272; EDV19515.1; -; Genomic_DNA.
DR RefSeq; XP_002118032.1; XM_002117996.1.
DR AlphaFoldDB; B3SCR3; -.
DR STRING; 10228.B3SCR3; -.
DR ESTHER; triad-b3scr3; S9N_PREPL_Peptidase_S9.
DR MEROPS; S09.015; -.
DR EnsemblMetazoa; TriadT62068; TriadP62068; TriadG62068.
DR GeneID; 6759231; -.
DR KEGG; tad:TRIADDRAFT_62068; -.
DR CTD; 6759231; -.
DR eggNOG; KOG2237; Eukaryota.
DR HOGENOM; CLU_011290_0_1_1; -.
DR InParanoid; B3SCR3; -.
DR OMA; LINCNSK; -.
DR OrthoDB; 318259at2759; -.
DR PhylomeDB; B3SCR3; -.
DR Proteomes; UP000009022; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 62..451
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 515..740
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 751 AA; 85911 MW; CD6080FB3C8CEC62 CRC64;
MATVILKGSM SKLISSEWIG NIHNKFSLPY QLLSRRLKFN WPFNRKDYIS TPKAAIKPWT
ISVHGKTISD PYHWLKDQGN AAVMKYLQQE NSYAKKVMTN TKSIQSKLVR TMSDIEAQLT
VPPEILEKYE YYMKEESAAS LPIYCRRKLD SNLVDNNEEV ILDLNDLSKR HQHCCVGQLK
VSPSHRLVAY TFDTNGKENY EAHIIDLSGN QPNVIDVIRD AFAVEFASNE DSIIYTKQNY
RRRPYQVWLR AFDSRLTDRL LFQEDDEKYF LHIVCTKNHR FLTINLNSKS SSEVWALDTE
KLKSKPVLIK ERELDCECYV DHSNNHFYIL TNDKSSGKYK VMMAPDQNPG RDNWKELQAM
DKDSASDSTD TLLDDMDIFA DYCVLYQREN LEPQITIVNL HSPLQCQTFK LPIGTIASAS
NFTFSADTVR FSYSSPLIAD TFYELDMRTM ALNNLTPSTI GLDSDQYSFY ISHATSKDGC
KIPISLCHRK DIVLNSSTPL LAIVYGAYGM ELNRQFSVQN MCLLKAGWVL AFCHVRGGGE
FGRHWYYQGR QLNKMNSFYD FLACINEVQD QGYTKPTLTS CKGTSAGGLI VAHLCNNHPN
KIAAAIMKVP HVDILGTMLD QSLPLTVEEY EEWGDLNSSH VFDYICSYCP YTNIQRNLYP
SLLLTASYND NRVPYWSPVR FMAKLRAAQR DYQSQHEGAT TNNKIYHILK TNLSSGHYGT
AGDEGLKEAA FEIAFLHKAL DLPDELLNTF N
//
