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Database: UniProt
Entry: A0A251UXG5_HELAN
LinkDB: A0A251UXG5_HELAN
Original site: A0A251UXG5_HELAN 
ID   A0A251UXG5_HELAN        Unreviewed;       791 AA.
AC   A0A251UXG5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative peptidase S8, subtilisin-related protein {ECO:0000313|EMBL:OTG27804.1};
GN   ORFNames=HannXRQ_Chr04g0104051 {ECO:0000313|EMBL:OTG27804.1};
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:OTG27804.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
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).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; CM007893; OTG27804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251UXG5; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr04g0152171; mRNA:HanXRQr2_Chr04g0152171; HanXRQr2_Chr04g0152171.
DR   Gramene; mRNA:HanXRQr2_Chr04g0152171; mRNA:HanXRQr2_Chr04g0152171; HanXRQr2_Chr04g0152171.
DR   InParanoid; A0A251UXG5; -.
DR   OMA; NIMHITI; -.
DR   Proteomes; UP000215914; Chromosome 4.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02120; PA_subtilisin_like; 1.
DR   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 2.60.40.2310; -; 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; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034197; Peptidases_S8_3.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795:SF425; OS04G0430700 PROTEIN; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          61..132
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          160..606
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          678..784
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        237
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        566
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   791 AA;  86987 MW;  C106625F8409A2B3 CRC64;
     MSLNIMHITI RQSKLHILRY ICFHFTTYSS QMAQPMNVVF IFTLIVISIT SSSSTDDHQA
     YIVHMDKSMM PSPFSNHHHW YTSVLSSLSD EAPATHLYTY YHVMDGFSAV LTMSQLKQLQ
     KMPAHLATFE EKLGQLHTTR TPTFLGLKKE AGLWPVSGFG EDMIIGIIDS GIWPESKSFH
     DEGMPEAPSR WRGKCEAKGF CNKKLIGARS FSQGMKHLKE KISKTDDYDS PRDFLGHGTH
     TSSTAAGSRV QFANYFGYAN GTATGIAPKA QLAMYKVGFF NDSFEAAATD TLAGMDQAIE
     DGVDLMSLSL GFPETPFYQN PIAIGAFAAM EKGILVSCAA GNSGPRAYTV LNAAPWITTV
     GAGTVDRDFV AYVTPGGQSY GTLIGKSVFP KNLLVEKVHI YYGYGNRSKE SCAYNALDPK
     DVKGKYIFCE IDDAKSLFEF IELETKGAAG AIISSDMGDF LFADSFTFPF VVLERKLGKL
     LKKYIINTKN ASINVKYGET LLGVKPAPQV AYFSSRGPSR QSPWILKPDI LAPGVDILAA
     WAPNRESAQI GDDYLFSDFK LESGTSMACP HVVGVAALLK SIHRDWSPAA IRSAMMTTAD
     ILDNNNDIII DMITSKPGTS LDYGAGHVNP NNAMDPGLFY DIQPHDYINY LCAMGYTPHE
     IRIISKKPEV NCANATLDLN YPSFILILNN TNTTRYTFQR TLTNVGMSSC SYRAEVNTPP
     TGMNVVVKPS MIYFKGKYST AKFEVIVDVD ISAANRIKGG YFGNSVYLTW LEVNGHHVVR
     SPIVSAFDAS S
//
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