ID   A0A0L9V9X7_PHAAN        Unreviewed;       731 AA.
AC   A0A0L9V9X7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN   ORFNames=HKW66_Vig0094000 {ECO:0000313|EMBL:KAG2400746.1},
GN   LR48_Vigan09g036100 {ECO:0000313|EMBL:KOM51702.1};
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM51702.1, ECO:0000313|Proteomes:UP000053144};
RN   [1] {ECO:0000313|Proteomes:UP000053144}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX   PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA   Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA   Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA   Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA   Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT   "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT   high starch and low fat accumulation and domestication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN   [2] {ECO:0000313|EMBL:KOM51702.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:KOM51702.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAG2400746.1, ECO:0000313|Proteomes:UP000743370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAG2400746.1};
RA   Xiang H.;
RT   "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the peptidase S9A family.
CC       {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR   EMBL; JABFOF010000004; KAG2400746.1; -; Genomic_DNA.
DR   EMBL; CM003379; KOM51702.1; -; Genomic_DNA.
DR   RefSeq; XP_017437024.1; XM_017581535.1.
DR   AlphaFoldDB; A0A0L9V9X7; -.
DR   STRING; 3914.A0A0L9V9X7; -.
DR   EnsemblPlants; KOM51702; KOM51702; LR48_Vigan09g036100.
DR   GeneID; 108343327; -.
DR   Gramene; KOM51702; KOM51702; LR48_Vigan09g036100.
DR   KEGG; var:108343327; -.
DR   OMA; DGCKNAN; -.
DR   OrthoDB; 7264at2759; -.
DR   Proteomes; UP000053144; Chromosome 9.
DR   Proteomes; UP000743370; 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; IPR002471; Pept_S9_AS.
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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368024};
KW   Protease {ECO:0000256|RuleBase:RU368024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW   Serine protease {ECO:0000256|RuleBase:RU368024}.
FT   DOMAIN          14..429
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          497..726
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   731 AA;  82934 MW;  4ECF84BCF57B2B20 CRC64;
     MTSLSALNIS LQYPPARRDD TVLEDYHGVK IADPYRWLED PDAEEVKEFV QEQVKLTDSV
     LQKCETREKL REAITKLFDH PRYHAPFRRA DKYFYFHNTG LQAQDILYVQ ESLEGEAEVL
     LDPNGFSEDG TVSLSTLSVS EDGKYLAYAL SSSGSDWTTI KLLRIEDRNV EPDTLLWVKF
     SSISWTHDNK GFFYSRYPAP KDREVEHAGT ETNANLHHQL YYHFLGTDQS EDILCWRDPE
     NPKYSFGGGV TDDGQYILLH ISEGCDPVNK LYYCDLSKIP NGLESFRNGN TLLPFVKLID
     NFDAQYEAIA NDDTVFTFLT NKDAPKYKLV RVDLKEPTTW IDVVQESEKD VLESACAVNG
     NQLIVSYLSD VKYVLQVRDL KTGSFLHQLP IDIGSVSEVS GRREDSVVFI SFTSFLTPGI
     IYQCNLGTEI PDMRIFREIV VPGFDRSEFH VKQDFVSSKD ATKIPVFIVA KRDIILDGSH
     PCLLYGYGGF NISITPYFSV SRIVITRHLG VVFCIANIRG GGEYGEEWHK AGSLARKQNC
     FDDFISAAEY LVSTGYTQPK KLCIEGGSNG GLLVGACINQ RPDLFGCALA HVGVMDMLRF
     HKFTIGHAWT SDYGCSEKEE EFHWLIKYSP LHNVRRPWEQ HTDQSIQYPS TMLLTADHDD
     RVVPLHTLKL LATMQHVLCT SLEQSLQTNP IIGRIDCKSG HGAGRPTQKM IDEAADRYSF
     MARMLEAHWI E
//