ID Q51714_9EURY Unreviewed; 616 AA. AC Q51714; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 24-JUL-2024, entry version 87. DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897}; DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897}; 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). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0070012; F:oligopeptidase activity; IEA:TreeGrafter. 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 InterPro; IPR051167; Prolyl_oligopep/macrocyclase. 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}. FT DOMAIN 2..351 FT /note="Peptidase S9A N-terminal" FT /evidence="ECO:0000259|Pfam:PF02897" FT DOMAIN 413..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 //