ID A0A022RG84_ERYGU Unreviewed; 701 AA.
AC A0A022RG84;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Subtilisin-like protease fibronectin type-III domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=MIMGU_mgv1a024251mg {ECO:0000313|EMBL:EYU39004.1};
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:EYU39004.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU39004.1, 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; KI630460; EYU39004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022RG84; -.
DR STRING; 4155.A0A022RG84; -.
DR eggNOG; ENOG502QRA7; Eukaryota.
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; 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; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF812; SUBTILISIN-LIKE PROTEASE SBT4.1; 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:UP000030748};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 11..72
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 94..546
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 603..701
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 150..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 497
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 701
FT /evidence="ECO:0000313|EMBL:EYU39004.1"
SQ SEQUENCE 701 AA; 74175 MW; 8728BAD62F793B0B CRC64;
MGDLPKGGDL SVSSSHHTIL QTVLGSASSA KESLVYSYER SFNGFAAKLT VNEAARIAGV
VSVNPNRMLK LHTTRSWDFM GFTDGNLGPG LEGQVIIGLL DTGVWPEHPS FNDTGFGPPP
SKWKGTCQTA TNFTCNNKII GARYYKSDNS YDDDNEAPSP RDTEGHGTHT ASTAGGVELP
GTSFYGLAEG VARGGARNAR IAVYKVCWLT GCSNADVLKA FDDAIADGVD ILSVSLGSLF
PHRFFDDPIA IGSFHAMQNG ILTSNSAGNS GPDPVSVVNF APWTLTVAAS TIDRKFVANL
VLGNGLFLTG ISINSFDLNG TSYPLVWGGD AANISIGASS DNTRTCMLES DEMNYGMLAG
AIVLCENPFD AAASNIFHFN GTGVIMVDNA PQYASSYPLP ATVISPDDLR KVMQYIKTTK
YPVATILVGE AWKDAMAPIV VSFSSRGPSP YSPDILKPDV TAPGVDILAG WSPLAPPSFA
YGDTRSGVYF NVVSGTSMSC PHATAAAAYV KAAHPDWSPA VIKSAIMTTA YVMDPSQNTD
KEFAYGSGHI NPAGAVDPGL VFDASAADYI NLLCKQGYNT TTLRMLTGDN STCANTTIGR
AFDFNYPILS MYVEDGQEIT GTFKRTVTNV GPLNSTYTAT WQMPSLISVT VEPSVLEFSV
VGERKSFTVT VVGPAIKQQP IMSGAVTWSD GGSRSVRTPV V
//
