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Database: UniProt
Entry: A0A1R3I1N1_9ROSI
LinkDB: A0A1R3I1N1_9ROSI
Original site: A0A1R3I1N1_9ROSI 
ID   A0A1R3I1N1_9ROSI        Unreviewed;       736 AA.
AC   A0A1R3I1N1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=COLO4_25546 {ECO:0000313|EMBL:OMO76496.1};
OS   Corchorus olitorius.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO76496.1, ECO:0000313|Proteomes:UP000187203};
RN   [1] {ECO:0000313|Proteomes:UP000187203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
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., Yahiya A.S., Khan M.S.,
RA   Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA   Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA   Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA   Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA   Shommy N.S.;
RT   "Corchorus olitorius 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:OMO76496.1}.
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DR   EMBL; AWUE01019079; OMO76496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3I1N1; -.
DR   STRING; 93759.A0A1R3I1N1; -.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000187203; 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:SF783; CUCUMISIN-LIKE ISOFORM X1; 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:UP000187203};
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..736
FT                   /note="Peptidase S8/S53 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013091157"
FT   DOMAIN          34..111
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          132..581
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          638..735
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        140
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        532
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   736 AA;  78730 MW;  8EEFB0B3324AAF0E CRC64;
     MEGKKFLLNC LLLHGLMILA MLTTTAVSQP NKKSYIVYMG DKPKDGSSTS SLHSSILQEA
     FGSDSITKSV HCRYKRSFSG FVVELTEEEA VKMSRMKGVV SVFPNEKREL HTTRSWNFLG
     FSQQVERSVT ESDVIIGVLD TGIWPESDSF NDEGFGPPPS KWNGSCETAG GNFTCNNKII
     GAQYYRSDGY FGSSDIISPR DSEGHGTHTA STAAGRLVNG ASLFGLGSGT ARGGVPSARI
     AVYKICWSDG CYDADILQAF DDAIADGVDI ISLSVGGKYA KEYFEDSIAI GAFHAMRNGV
     LTVNSAGNRG PRPATITNFS PWSLSVAAST IDRKFFTKVQ LGDNRVYQGV SVNTFDLNNQ
     MFPLIYGGDA PNITGNYSRD SSRFCEPNSL DSNMVNGKIV LCDSYGNLTA PFYAGAAGAV
     MRGSAPSDNA DLFPLPASYL KRVDGRRVFT YINSASAPTA TIFKSNEAND SLAPYVVSFS
     SRGPNPITPD ILKPDISAPG VDILAAWTLA SPASGVTGDT RFVPFNIISG TSMACPHVSG
     SAAYVKSFHP SWSPSAIKSA LMTTAIPMSS ELNTDAEFAY GSGEVNPVEA VNPGLIYDAE
     EIDYIKFLCG QGYGTQFLQL VTRDNTTCSE ATNGTVWDLN YPSFALNTSG STKVSGVFTR
     TVTNVGSAMS EYIANVTVET ESLEINVNPS VLSFTSLGQK LSYTLTINGT IDGSMVSASL
     VWDDGEHMVR SPIIVV
//
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