ID A0A251NBD1_PRUPE Unreviewed; 733 AA.
AC A0A251NBD1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=PRUPE_7G143000 {ECO:0000313|EMBL:ONH96637.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONH96637.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONH96637.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR EMBL; CM007657; ONH96637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251NBD1; -.
DR EnsemblPlants; ONH96637; ONH96637; PRUPE_7G143000.
DR Gramene; ONH96637; ONH96637; PRUPE_7G143000.
DR Proteomes; UP000006882; Chromosome g7.
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; 2.
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; 2.
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:UP000006882};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 46..198
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 206..420
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 521..695
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 19..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 83788 MW; 6E52D0ADB8277070 CRC64;
MRHLLKPLRH NCRRLRWAHH RAQKAAASPS PPPRPPRPPP KPESLTFHDH SWEDPYSWMS
KLNDKVAMRH LDMYMEQEEK YTEATMSGTD RLQSKLQSEM ASRFASDLST PPLRWGPWLY
YRRVEEGKQF PVLCRRLASL NDEFISHKSP SAGFDFTSGK RIEQKLLDYN REAQRFGGYA
YEELSEVSPD HRFIAYTMIY CSMIGSTDDD FLILEEPDEN VYVNIRHTKD FRFVTVHTFS
TASSKVFLIN AADPLSGVNL VWECEGISHG ILEHHQGYLY LFTDAAKEGQ SVDYHYLLRS
HLDSSSSPRT WESVFTDDPD WVVEDLDFSH THLVVTLREG RNFRLCSVTL PLPAGKGPVH
LKELHPQFLP LPKYVSQISP GPNYDYHSSK MRFTISSPVM PDAVVDYDLS NGEWNIVQQQ
NILHERTRVL YGTASSASIN EETLNSKTSN PSNEVNSDDD QLWNGLSEFY ACEQYNVASY
DGVLLPLTVV YSRKNKKEDQ NPGLLHVHGT YGELLDKRWR SELKSLLGRG WIIAYADVRG
GGGGGKKWHH DGRRTKKINS IKDYISCANF LVDKEIVHEN KLAGWGYSAG GLVVASAINQ
SPHLFKAAIL KVPFLDPTNT LLYPILPLTA ADYEEFGYPG DIADFHAIRD YSPYDNIQKD
VLYPAVMVSS SFNTRFGVWE AAKWVARVRE LTIYDQKRPI LLNLTTDIVE ENRYLQCKES
ALESAFLIKV MES
//