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Database: UniProt
Entry: A0A1Q3BRC5_CEPFO
LinkDB: A0A1Q3BRC5_CEPFO
Original site: A0A1Q3BRC5_CEPFO 
ID   A0A1Q3BRC5_CEPFO        Unreviewed;       767 AA.
AC   A0A1Q3BRC5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidase_S8 domain-containing protein/PA domain-containing protein/Inhibitor_I9 domain-containing protein {ECO:0000313|EMBL:GAV70577.1};
GN   ORFNames=CFOL_v3_14075 {ECO:0000313|EMBL:GAV70577.1};
OS   Cephalotus follicularis (Albany pitcher plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX   NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV70577.1, ECO:0000313|Proteomes:UP000187406};
RN   [1] {ECO:0000313|Proteomes:UP000187406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA   Fukushima K., Hasebe M., Fang X.;
RT   "Cephalotus genome sequencing.";
RL   Submitted (APR-2016) 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:GAV70577.1}.
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DR   EMBL; BDDD01000823; GAV70577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3BRC5; -.
DR   STRING; 3775.A0A1Q3BRC5; -.
DR   InParanoid; A0A1Q3BRC5; -.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000187406; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
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; IPR046450; PA_dom_sf.
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:SF850; SUBTILISIN-LIKE PROTEASE SBT5.4; 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; SSF52025; PA domain; 1.
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:UP000187406};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..767
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013338114"
FT   DOMAIN          29..99
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          139..614
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          387..468
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          667..762
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        218
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        555
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   767 AA;  82839 MW;  B77FA44133A55E38 CRC64;
     MWFPKISFLV LLFTLFSLLH APAFAIKKSY IVYLGSHAHG PQVTTADLDG VTESHYEFLG
     SFLGSKDKAR DAIFYSYKRH INGFAATLEE EEADEIAKHV PVFLNKGKKL HTTHSWDFML
     LEKEGVIHSS SVWNQARFGE DTIIANLDTG VWPESDSFSD KGFGPIPSKW KGKCEDDTPT
     GVKCNRKLIG ARYFNKGYEA YGGKLNSTNK SARDDEGHGT HTLSTAGGNF VPGANVFGLG
     NGTAKGGSPK ARVAAYKVCW APINGSECFD ADIMAGFDAA IHDGVDVISV SLGGDPTDYF
     NDGLAIGAFH AVKNGIVVVC SAGNSGPIDG SVSNVAPWMI TVGASTLDRE FQAFVELRNG
     KRLKGTSLSR PLPKDTFYPL ISGSQAKAAD ATDEDALRCL PETLDPKKVK GKILACLRGG
     SARVDKGYQA LMAGAAGMIL CNDKLSGNEI IADPHVLPAS QITYEDGLEV IAYIDSTDDP
     LAYITAPSAQ TGIKPAPFMA SFSSRGPNTV TPQLLKPDIT APGVNIIAAY TEASSPTDEA
     FDKRKTPYNT ESGTSMSCPH VSGVAGLLKT LHPEWSPAAI RSAIVTTART RDNTMNPMVD
     GSFEEATPFS YGHGHIRPNR AMDPGLIYDL NVNDYLDFLC ASGYRKTMLQ PFSDGHYKCP
     QTAHLRDFNY PSITVHALEE SATVTRRVKN VGSPGTYAVN IRNPLGISVS VEPTTLTFKD
     VGEEKSYNVT LTVKWRENDE AYVFGGLTWT DGKHYVRSPI VVSTESD
//
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