ID R0GQE0_9BRAS Unreviewed; 845 AA.
AC R0GQE0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CARUB_v10027793mg {ECO:0000313|EMBL:EOA14555.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA14555.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; KB870812; EOA14555.1; -; Genomic_DNA.
DR RefSeq; XP_006281657.1; XM_006281595.1.
DR AlphaFoldDB; R0GQE0; -.
DR STRING; 81985.R0GQE0; -.
DR GeneID; 17874746; -.
DR KEGG; crb:17874746; -.
DR eggNOG; ENOG502QSVR; Eukaryota.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000029121; 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; IPR023827; Peptidase_S8_Asp-AS.
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:SF439; SUBTILISIN-LIKE PROTEASE SBT2.3; 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; PS00136; SUBTILASE_ASP; 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:UP000029121};
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..845
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004351592"
FT DOMAIN 36..148
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 174..662
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 745..838
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 59..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..86
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 624
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 845 AA; 90898 MW; AE1FB2E63F3B2ACA CRC64;
MLVKFGFLLL VISFGFLSNT TLGQQDDDDD DDDTAVYIVT LKQPPLVHLF EEQELKQIRQ
THKKSKLKPK PQPRNNSRKR HGRSKIPSVA QSHDSFLRKT LKGEKYIKLY SYHYLINGFA
LFVSSQQAEK LSMRREVANI VLDYSVRTAT TYTPQFMGLP QGAWVKEGGF EIAGEGVVIG
FIDTGIDPKH PSFDDNDSNS RRSYPTPKHF SGICEVTPDF PSGSCNRKLI GARHFAQSAV
TRGVFNSSED YASPYDGDGH GTHTASIAAG NHGVPVIVSN HNFGNASGIA PRAFISVYKA
LYKGFGGFAA DVVAAIDQAA QDGVDILSLS ITPNRKPPGV ATFFNPIDMA LLSAVKAGIF
VVQAAGNTGP AAKSMSSFSP WIFTVGASSH DRVYSNSLIL GNNVTIPGIG FSIPTDDGKM
YKMISAFHAV NNSTSVDNDM YVGDCQDYEN FDQDLVSGNL LICSYSARFV IGLSTIKQAL
DVAKNLSAIG VVFYMDPYVL GFQINPTPMD MPGIIIPSAE DSKTLLKYYN TSLQRDGSTK
EIVSFGAVAA IEGGLNANFS DRAPKVMYYS ARGPDPEDNS FNDADILKPN LVAPGNSIWG
AWSSASTDST EFEGEKFAMM SGTSMAAPHV AGVAALIKQT YPQFTPSQIA SALSTTALLD
DNKGGPIMAQ RSFSNPDQSL YTATPFDMGS GFVNATAALD PGLIFDTSFD DYMSFLCGIN
GSDPVVFNYT GLHCSANNAT ISGFDLNLPS VTVSTLSGTQ TFQRSIRSIA GNETYNVGWS
PPYGVSMKVS PNMFSIGMGE TQLLSVTLNA TKNSSSSSFG RIGLFGNRGH IVNIPVTVIE
KIALS
//
