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Database: UniProt
Entry: A0A022QLI3_ERYGU
LinkDB: A0A022QLI3_ERYGU
Original site: A0A022QLI3_ERYGU 
ID   A0A022QLI3_ERYGU        Unreviewed;       742 AA.
AC   A0A022QLI3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYU29562.1};
GN   ORFNames=MIMGU_mgv1a001898mg {ECO:0000313|EMBL:EYU29562.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU29562.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU29562.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; KI631203; EYU29562.1; -; Genomic_DNA.
DR   RefSeq; XP_012846779.1; XM_012991325.1.
DR   AlphaFoldDB; A0A022QLI3; -.
DR   GeneID; 105966744; -.
DR   KEGG; egt:105966744; -.
DR   eggNOG; ENOG502QPQR; Eukaryota.
DR   OMA; RAIRANT; -.
DR   OrthoDB; 11910at2759; -.
DR   PhylomeDB; A0A022QLI3; -.
DR   Proteomes; UP000030748; 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   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; IPR003137; PA_domain.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-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; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF786; SUBTILISIN-LIKE PROTEASE SBT1.7; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 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:UP000030748};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..742
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001506958"
FT   DOMAIN          30..118
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          141..569
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          365..445
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          642..738
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        208
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        528
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   742 AA;  78844 MW;  09EFE7B2A9EF03EF CRC64;
     MGYYTLFLTL TCVLCFNTIF VRSKDSNLQT YIVHVELPSF PTLTTSSLLT EDLQAYYQTF
     LASTLSASSP STDEPSIIYS YHNVFHGFSA RLSPEQVKAM EKKPGFISAR PQKTLSLHTT
     HSPNFLGLNQ NTGFWRDSNY GRGMIIGVLD SGVNPNHPSF NDDGMPPPPA RWRGRCEFNS
     TIARCNNKLI GARFFTIGDG TPSDEDGHGT HTASTAAGNF VPGANVFGNA NGTAAGVAPL
     AHVATYKVCT TTCEESDIVA AMDAAIDDGV DIISLSLGGP AQDFFGENIA VGAFSAIERG
     IFVSASAGNN GPFYGTAQNG APWILTVGAS SVDRKIRATA VLGNNEELDG ESTFQPSDFP
     TTLLPLFYSP NDSFCSPASL RSLDLQGMIV LCDNGGGIGR IAKGRAVRAA GGAAMVIVNQ
     QRQGFTTNSD SHVLPATHLS YTDGLRVKAY LNSTASPTAT ISFKGTVIGD DRAPQVAAFS
     ARGPNPPSPG ILKPDIIGPG HNILAAWHVS VENNTGTNSN FNIISGTSMS CPHLSGVAAL
     LKSVHPDWSP AAIKSAIMTT ADLVNLAGNP IEDQTQSRAD VFAIGSGHVN ILKATDPGLV
     YDMGPQDYVP YLCGLNYTDQ QVAVIVNRVV RCAEISSIPE AELNYPSFSV VIGNTSTTYN
     RTVTNVGEAN SVYTVRAALP LVDVRVEPTT LQFSAINQTL TYQTTFTRSS GNATIVNVYV
     QGFLTWTSAK HTVRSPIVGF VE
//
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