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Database: UniProt
Entry: R0GUT2_9BRAS
LinkDB: R0GUT2_9BRAS
Original site: R0GUT2_9BRAS 
ID   R0GUT2_9BRAS            Unreviewed;       770 AA.
AC   R0GUT2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOA39722.1};
GN   ORFNames=CARUB_v10008367mg {ECO:0000313|EMBL:EOA39722.1};
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:EOA39722.1, 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}.
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DR   EMBL; KB870805; EOA39722.1; -; Genomic_DNA.
DR   RefSeq; XP_006306824.1; XM_006306762.1.
DR   AlphaFoldDB; R0GUT2; -.
DR   STRING; 81985.R0GUT2; -.
DR   GeneID; 17897501; -.
DR   KEGG; crb:17897501; -.
DR   eggNOG; ENOG502QUSK; 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; 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:SF769; CO(2)-RESPONSE SECRETED PROTEASE; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 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:UP000029121};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..770
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004341466"
FT   DOMAIN          36..109
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          141..585
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          666..762
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        146
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        547
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   770 AA;  81253 MW;  4A5AA03C8FC539EA CRC64;
     MKGLITFSTP YLLFIYLLCI LFTTETEAGS RNGDGVYVVY MGSASSAANA YRAQILINTM
     FKRRANDLVH TYKHGFTGFA ARLTAEEAKA IAKKPGVISV FPDPNFQLHT THSWDFLKYQ
     TSVKIDSGPP STASDGSYDS IVGILDTGIW PESESFNDKD MGPIPSRWKG TCMEAKDFKS
     TNCNRKIIGA RYYKNPDDDS EYYTTRDVIG HGSHTSSTIA GSAVENASYY GVASGTAKGG
     SPNARIAMYK VCNPGGCTGS SILAAFDDAI ADGVDVLSLS LGAPAYARID LNTDPIAIGA
     FHAVEQGILV ICSAGNDGPD GGTVTNTAPW IMTVAANTID RDFESDVVLG GNKVIKGEGI
     HFANASKSPV YPLIHGKSAK NADASEGEAR ACEFGSLDQD KVKGKIVLCE NVGGSSYASA
     ARDEVKSKGG IGCVFVDDRT RAVASAYGAF PTTVIDSMEA AEIFSYLNST KDPVATILPT
     ATVEKFTPAP AVAYFSSRGP SSLTRSILKP DITAPGVAIL AAWTGNDSAI SLEGKPAAQY
     NVISGTSMAA PHVTAVASLI KSQHPTWSPS AIRSAIMTTA TQTNNDKGLI TTETGAAATP
     YDSGAGELSS TASMQPGLVY ETTETDYLNF LCYYGYNVTT IKAISKALPV NFTCPADSNL
     DLISTINYPS IGISGFKGTG NKTVTRTVTN VGGDGVAEYT VSVETPPGIT IKVTPEKLQF
     TKDGEKLTYQ VIVSATASPK QDVFGALTWS NAKYKVRSPI VISSESSRTN
//
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