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Database: UniProt
Entry: A0A022RBR4_ERYGU
LinkDB: A0A022RBR4_ERYGU
Original site: A0A022RBR4_ERYGU 
ID   A0A022RBR4_ERYGU        Unreviewed;       753 AA.
AC   A0A022RBR4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MIMGU_mgv1a001832mg {ECO:0000313|EMBL:EYU37178.1};
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:EYU37178.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU37178.1, 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; KI630559; EYU37178.1; -; Genomic_DNA.
DR   RefSeq; XP_012837786.1; XM_012982332.1.
DR   AlphaFoldDB; A0A022RBR4; -.
DR   STRING; 4155.A0A022RBR4; -.
DR   GeneID; 105958324; -.
DR   KEGG; egt:105958324; -.
DR   OMA; WFSHETP; -.
DR   OrthoDB; 11910at2759; -.
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:SF463; OS12G0427600 PROTEIN; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..753
FT                   /note="Peptidase S8/S53 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001504973"
FT   DOMAIN          27..118
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          141..572
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          391..452
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          652..749
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        536
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   753 AA;  80159 MW;  659E1FE6B33E852E CRC64;
     MATMFLLAAI FIFTFHSASS SNTSYQTYIV HVDLPPTEED GFSGQSNLET WYHSFLPPSS
     EAATSDSDNH YTPSSRIVHM YRNVITGFAA KLSPEEVKEM EKKPGFMHAR PHKKYQLHTT
     HSPNFLGLHQ GVGAWPASNY GNGVIIGVID TGITPGHPSF NDQGMPPPPP KWKGKCELSG
     TLSCNNKLIG ARNFASYFPG PPIDNFGHGT HTASTAAGNF VSGANVFGQA NGTASGIAPL
     AHLAIYKVGS HENGTDVLFD SDLLAGMDAA IEDGVDVLSL SLAGDSVSHT SPFHEDVVAI
     GAFSAVKRGI FVTCSAGNDG PSHSSLYNTA PWILTVGAST TDRKIKATAL LGNGEAYEGE
     SFYQPEEGGS SSEELLPLVY GALCGSELLG EIGVKGKVVL CEIGTFNNGQ DVKDAGGAAM
     IGINDETDDY YTEPIPHVLP ATLVNYEAAL KIKAYIEDAN SSTPTSAILF GGTVIGDKTA
     PMVTPFSSRG PNLVSPGIIK PDIIGPGANI LAAWPVSIDN NIKEKTATYN MVSGTSMSCP
     HLSGVAALVK SAHPDWSPAM VKSAIMTSST QTNLGNIPIL DQRHQPADVF AVGAGHVNPP
     AALNPGLVYD ISARDYISYL CFLYTERQVA AIVNRKIDCS SKSEYSGVPE AQLNYPSFSV
     VLGQDIGYAY SRTVTNVGEA ESTYYAKIEC FPGVSIFVEP TVLSFTEVKQ QLTYEVYFSR
     TEFTTNGSYV QGSISWVSTK HVVRIPVSVK LVL
//
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