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Database: UniProt
Entry: A0A251VFT7_HELAN
LinkDB: A0A251VFT7_HELAN
Original site: A0A251VFT7_HELAN 
ID   A0A251VFT7_HELAN        Unreviewed;       489 AA.
AC   A0A251VFT7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative peptidase S8, subtilisin-related protein {ECO:0000313|EMBL:OTG33792.1};
DE   SubName: Full=Tripeptidyl-peptidase II {ECO:0000313|EMBL:KAF5817649.1};
DE            EC=3.4.14.10 {ECO:0000313|EMBL:KAF5817649.1};
GN   ORFNames=HannXRQ_Chr02g0038561 {ECO:0000313|EMBL:OTG33792.1},
GN   HanXRQr2_Chr02g0055561 {ECO:0000313|EMBL:KAF5817649.1};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG33792.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|EMBL:KAF5817649.1, ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5817649.1};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
RN   [2] {ECO:0000313|EMBL:OTG33792.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:OTG33792.1};
RA   Langlade N., Munos S.;
RT   "Sunflower complete genome.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF5817649.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5817649.1};
RA   Gouzy J., Langlade N., Munos S.;
RT   "Helianthus annuus Genome sequencing and assembly Release 2.";
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; MNCJ02000317; KAF5817649.1; -; Genomic_DNA.
DR   EMBL; CM007891; OTG33792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251VFT7; -.
DR   STRING; 4232.A0A251VFT7; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr02g0055561; CDS:HanXRQr2_Chr02g0055561.1; HanXRQr2_Chr02g0055561.
DR   Gramene; mRNA:HanXRQr2_Chr02g0055561; CDS:HanXRQr2_Chr02g0055561.1; HanXRQr2_Chr02g0055561.
DR   InParanoid; A0A251VFT7; -.
DR   OMA; MAAHHIN; -.
DR   Proteomes; UP000215914; Chromosome 2.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02120; PA_subtilisin_like; 1.
DR   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR034197; Peptidases_S8_3.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   PANTHER; PTHR10795:SF585; OS01G0868900 PROTEIN; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KAF5817649.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..489
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013100852"
FT   DOMAIN          29..112
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          136..489
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
SQ   SEQUENCE   489 AA;  52960 MW;  C93AB9F8C1E93124 CRC64;
     MADSFQMANY ISLCVWLLSL VVLAMSHETY IVHMDLSAKP TAFSSHHTWF SATLDSLTTT
     STHVTSSSSS KLVYSYTNAI NGFTAILSSS ELELIKNTPG YLYSIKDTTV ELDTTHSTQF
     LGLNSNSGAW PVANYGRDVI IGLVDSGIWP ESESFNDHGM SSVPSRWKGE CEVGFQFNSS
     LCNKKLIGAR YFNKGLLSNR PNLTLSMYSA RDTFGHGTHT SSTAAGGYVK HASCFGYGTG
     TATGVAPHAR VAMYKALWDE GVFVSDILAA IDQAIIDGVD VLSLSFGKDG LPLHQDPIAI
     ATFAGLEKGI FVSTSAGNNG PDLRTLHNGT PWVLTVAAST IDREFTGILT LGNGDSVTGL
     SLYPGKSSLR QLPIDFVGAC QNNFDYKKFD RKIVVCFDNN NTFFQQFFNV KRLNVSGAIF
     ITNTTGLELV MQSKYPALFL DLESGKTVMN YLQKLKNEEA KASIKFHGTH LGTKPAPSVA
     SYSSRGPSC
//
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