ID A0A1R3H0N0_COCAP Unreviewed; 806 AA.
AC A0A1R3H0N0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CCACVL1_22195 {ECO:0000313|EMBL:OMO63889.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO63889.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO63889.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO63889.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO63889.1}.
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DR EMBL; AWWV01012863; OMO63889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3H0N0; -.
DR STRING; 210143.A0A1R3H0N0; -.
DR EnsemblPlants; OMO63889; OMO63889; CCACVL1_22195.
DR Gramene; OMO63889; OMO63889; CCACVL1_22195.
DR OMA; TAYTHDQ; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000188268; 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; 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:SF618; SUBTILISIN-LIKE PROTEASE; 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; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000188268};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..806
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012842382"
FT DOMAIN 32..122
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 150..603
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 407..478
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 682..777
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 761..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 231
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 567
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 806 AA; 85453 MW; C3FAEE9DB6667115 CRC64;
MMALPWSLVF TVLFLSFTVV SSATPAAPKT QTFIVRVDDR LKPHQFPTVE EWYTSTLESL
SSTNILSSKN PTTSQTQKST VDVLHIYKTV FYGFSVKLTP EQAEELKTCP GILSVFPDRI
HHFQTTRSPH FLGLDTAKAI TGLCRRSDYG SNVIIGLLDS GIWPERHSFD DHDMGPIPSR
WKGECVQGDQ FPKTLCNKKL IGARYFTSGY QHAFGESKKN DMKSARDAVG HGTHTASIAA
GRAINNASFL GFASGEASGI AQKARIAMYK VCGGSACMGS DILAGFDAAV ADGVDVISMS
LASDDVISYD QDVAAIAAFS AMEKGVFVSA SAGNSGSTSG TVANVAPWIT SVGAGTIDRA
FAAELHLGDG SIIKGSSLYD GEPLDNNTYW PLIYGGNATA RGYSYLPSYA CFPDSLDPNL
VRGKIVICDR GVISRVMKGV VVKKAGGIGT VVANVAPLGE GLVADAYLSP ALAVTESARA
QLLTYINSTP NANATIVFRG TQVGVKPAPV VASFSSRGPN PISIYVLKPD LIAPGVNILA
GYPDGVSPTH LPEDPRQVEF NILSGTSMSC PHVSGIAALL KGAHPDWSPA MIRSALMTTA
YTHDQDGNAL LDEMDMGVGN TWAMGAGHVD PEKALDPGLV YNLTADDYIN FLCASNLSLE
QIKAITRRDV NCSEAQNLNP WDLNYPAISV AFDPLDPSFW EVDVTRTVTN VGHATSTYTV
AITNPAGIIT TVDPPTLMFK QLGETKSYTV KIAADPSCVP PVTSQSEFGQ LSWSDGKFQG
PGGGDKPAAA APPAAQPAEV PKKSKK
//
