ID A0A022QM74_ERYGU Unreviewed; 708 AA.
AC A0A022QM74;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Subtilisin-like protease fibronectin type-III domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MIMGU_mgv1a002151mg {ECO:0000313|EMBL:EYU28709.1};
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:EYU28709.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU28709.1, 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; KI631311; EYU28709.1; -; Genomic_DNA.
DR RefSeq; XP_012847558.1; XM_012992104.1.
DR AlphaFoldDB; A0A022QM74; -.
DR STRING; 4155.A0A022QM74; -.
DR GeneID; 105967508; -.
DR KEGG; egt:105967508; -.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR OMA; TCAEDCM; -.
DR OrthoDB; 11910at2759; -.
DR PhylomeDB; A0A022QM74; -.
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:SF836; SUBTILISIN-LIKE PROTEASE SBT4.3 ISOFORM X1; 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 9..73
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 95..542
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 597..700
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 103
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 163
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 491
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 708 AA; 75359 MW; E611BDB82F85577D CRC64;
MGNLVATNRS AEAYHTKMLE EVVGSRFAAQ SLVRSYKRSF NGFAAYLTPQ EHEKLAGHEE
VVSIFPSTTY KLQTTRSWDF IGFPENVTRN PTIESDTIIG VIDSGIWPES QSFTDKGFGP
VPKKWKGVCS GGTNFTCNNK IIGARYYNTM SPNDTTARDN VGHGSHTSSI AAGVPVRGAS
FYGIAEGTAR GGAPSARIAV YKVCHKDSCG AVDLLAALDD AIADGVDIIT ISLGGDPLEL
KSDVIAIGSF HAAQHGVLVV QSAGNGAAKA TVASVAPWIF SVGASSTDRG IITRVALGNG
SILTGKSVNS FDFEGKSFPL AYGKDVTIKC NESSAMDCAP DCIVPSLVKG KIVLCRMYDF
TFEVYNAGAL GIIFNEESFL PDNEVDDDSD VAPIAAIGLK RKDFNVVEGY FNSTKSSEVN
ILTSETTKNL DAPRVAGFSS KGPSTIIPDI LKPDITAPGM EILAAYSPLA SPSEYDSDHR
SVNYNIISGT SMSCPHVAGA AAYVKSFRPN WSPSAIKSAL MTTARKLDPT KDQYAEFAYG
AGQIDPIKAV DAGLVYETST QDYITFLCNL GYDSATIKNM FKANTTCPAK PATTIKDLNY
PSMTSQIKTA KGSKSAVTFS EKFTRTVTNV GAGKSTYKAT ASAGPGYNIS VTPSVLTFAA
TNEKKTFEVV VSGKIDYGKM LSASLEWSDG VHLVRSPIVV FPDNFFDS
//
