ID A0A1Z5KTI1_FISSO Unreviewed; 744 AA.
AC A0A1Z5KTI1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=FisN_2Hh175 {ECO:0000313|EMBL:GAX29616.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX29616.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX29616.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX29616.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
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:GAX29616.1}.
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DR EMBL; BDSP01000293; GAX29616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5KTI1; -.
DR InParanoid; A0A1Z5KTI1; -.
DR OrthoDB; 7264at2759; -.
DR Proteomes; UP000198406; 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; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF13; 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, ECO:0000313|EMBL:GAX29616.1};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 8..239
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 532..738
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 744 AA; 82926 MW; DC1C1CF6E49EC38B CRC64;
MSTTTVSTAE DPYIWLEEVE SEQSLDFARS ANAACLAALG NPEEKGTYAR VLQILESDDR
IPHVTHFGVN DDGEPILFNF WKDAKNPKGL WRYTTLSSYK KTSDIEWTTV LDVDALAEKD
GISWVWGGSR PLPRSRDPVY SKDRVTRALI VLSRGGSDAT HVKEFDLTTN DFVTDQPFQL
PEAKSRVSYK SRNVLLVGTD TGPDSLTDSG YPRTVREWVR GTDLLTDAKV VFEGETTDVS
VSAFISDERI WGGGIYEVYS RAMTFYTSKY FVRSVQFEHL LAPDERGPYV SDPPDFVELD
VQDDANISFL GKLLVITLRS DWEPVVGGPV YKKGSVIYTD AETFLQKGRT GCEYKILFEP
TERTAYEYYS VTKNYLILST MDNVKSRLQF YKIEDGGSRL TLIEGGSQEA QIRDVGIRPI
DPYSGSDEFW FTTSDFVTPS TLFLADASRM ETTNGESDAF IVEHVKSLPP QFDASGLVVS
QCTATSKDGT QIPYFIVRKE DTVLNGKNPT LLYGYGGFEV SLGPHYVATQ GVAWLERGGV
YVEANIRGGG EFGPSWHQAG LKANRNKCYE DFIAVGEHLI ETKVCSPKTL AVRGGSNGGL
LVGNMYTMRP DLFGAIHCAV PLLDMKRFHT LLAGASWMAE YGNPDTDDWE FLQKYSPYHN
IKEGTEYPPI LVTTSTRDDR VHPAHARKFV KKLMDGSNGK LPVYYYENIE GGHGGAADAK
QSAFMTALAY DFMFDTLSKN AMEL
//