ID   Q51714_9EURY            Unreviewed;       616 AA.
AC   Q51714;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   13-SEP-2023, entry version 83.
DE   SubName: Full=Prolyl endopeptidase {ECO:0000313|EMBL:AAA73423.1};
OS   Pyrococcus furiosus.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=2261 {ECO:0000313|EMBL:AAA73423.1};
RN   [1] {ECO:0000313|EMBL:AAA73423.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 3638 {ECO:0000313|EMBL:AAA73423.1};
RX   PubMed=7828913; DOI=10.1016/0378-1119(94)00688-O;
RA   Robinson K.A., Bartley D.A., Robb F.T., Schreier H.J.;
RT   "A gene from the hyperthermophile Pyrococcus furiosus whose deduced product
RT   is homologous to members of the prolyl oligopeptidase family of
RT   proteases.";
RL   Gene 152:103-106(1995).
RN   [2] {ECO:0007829|PDB:5T88, ECO:0007829|PDB:6CAN}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RX   PubMed=30786206; DOI=10.1021/acs.biochem.9b00031;
RA   Ellis-Guardiola K., Rui H., Beckner R.L., Srivastava P., Sukumar N.,
RA   Roux B., Lewis J.C.;
RT   "Crystal Structure and Conformational Dynamics of Pyrococcus furiosus
RT   Prolyl Oligopeptidase.";
RL   Biochemistry 58:1616-1626(2019).
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DR   EMBL; U08343; AAA73423.1; -; Genomic_DNA.
DR   PIR; JC4084; JC4084.
DR   PDB; 5T88; X-ray; 1.90 A; A/B=1-616.
DR   PDB; 6CAN; X-ray; 2.20 A; A/B=1-616.
DR   PDBsum; 5T88; -.
DR   PDBsum; 6CAN; -.
DR   AlphaFoldDB; Q51714; -.
DR   SMR; Q51714; -.
DR   ESTHER; pyrfu-Q51714; S9N_PPCE_Peptidase_S9.
DR   MEROPS; S09.002; -.
DR   BRENDA; 3.4.21.26; 5243.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5T88, ECO:0007829|PDB:6CAN};
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT   DOMAIN          2..351
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          412..615
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   616 AA;  70867 MW;  7C42561D7D187F2D CRC64;
     MEDPYIWMEN LEDERVLKII EEENKRFREF IGELSDKLFP EVWEQFSQPT IGMARITKKG
     IIASYSEKDR VVIKWFNGDV IVDSKELERE VGDEVLLQGF TTDEEGEKLA YSFSIGGADE
     GITRIIDLKT GEVIEEIKPS IWNITFLKDG YYFTRFYRKE KTPDGVNPPA ARMFWKDREG
     ERMVFGEGLT SGYFMSIRKS SDGKFAIVTL TYGWNQGEVY IGPIDNPQEW KKVYSASVPV
     EAIDVVNGKL YILTKEGKGL GKIIAIKNGK IDEVIPEGEF PLEWAVIVRD KILAGRLVHA
     SYKLEVYTLN GEKIKEITFD VPGSLYPLDK DEERVLLRYT SFTIPYRLYE FKDDLRLIEE
     RKVEGEFRVE EDFATSKDGT KVHYFIVKGE RDEKRAWVFG YGGFNIALTP MFFPQVIPFL
     KRGGTFIMAN LRGGSEYGEE WHRAGMRENK QNVFDDFIAV LEKRKKEGYK VAAWGRSNGG
     LLVSATLTQR PDVMDSALIG YPVIDMLRFH KLYIGSVWIP EYGNPEDPKD REFLLKYSPY
     HNVDPKKKYP PTLIYTGLHD DRVHPAHALK FFMKLKEIGA PVYLRVETKS GHMGASPETR
     ARELTDLLAF VLKTLS
//