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Database: UniProt
Entry: A0A1Q3C3H3_CEPFO
LinkDB: A0A1Q3C3H3_CEPFO
Original site: A0A1Q3C3H3_CEPFO 
ID   A0A1Q3C3H3_CEPFO        Unreviewed;       744 AA.
AC   A0A1Q3C3H3;
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:GAV74779.1};
DE   Flags: Fragment;
GN   ORFNames=CFOL_v3_18259 {ECO:0000313|EMBL:GAV74779.1};
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:GAV74779.1, 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:GAV74779.1}.
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DR   EMBL; BDDD01001274; GAV74779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3C3H3; -.
DR   STRING; 3775.A0A1Q3C3H3; -.
DR   InParanoid; A0A1Q3C3H3; -.
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:SF768; 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; 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}.
FT   DOMAIN          1..83
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          110..591
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          362..446
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          644..740
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        189
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"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:GAV74779.1"
SQ   SEQUENCE   744 AA;  80187 MW;  53350317ABD7C814 CRC64;
     VYLGAHTHGP GPTEIDLNRV TDSHYQLLGS YLGSNEKAQE QIFYSYTRHI NGFAAFLEEE
     EAVEIAKNPN VVSVFLNKGK KLHTTRSWDF LGVEKDEGSS SSIWRNARFG EDVIIANLDT
     GVWPESKSFS DEGMGPVPSK WQGTCQDDVR KKFPCNRKLI GAKYFNKGYA AFVGHLDSSY
     QTTRDIMGHG SHTLSTAAGG FVPGANVLGH GNGTAKGGSP KARVAAYKVC WPPVGDYECF
     DADILAGFDA AISDGVDILS VSLGGDPVDF FEDGISIGAF HAVKKGIVVV TSAGNNGPVA
     GSVSNVSPWM FTVGASKIDR TFTNYVALGN NHPSKPAHLK GESLSSGNLP SKKFYPLVDG
     PTAKLANASI DKARLCAAGT LDPKKVKGKI LLCFRGETAR LDKGWQAAQA GAVGMILGND
     VANGNELVAD PHFLPASHLT YEDGETVFEY VHSTKAPMAY MTNVETIVGT ELAPVMAAFS
     SRGPNLIEPT ILKPDITAPG MDIIAAFSEA VAPSDLVYDK RRIPFNIMSG TSMSCPHVSG
     IVGLLKTLHP RWSPAAIKSA IMTTARTQGN NMRPMMDSNN RKATSFAYGA GHVRPNRAMD
     PGLVYDLTVD DYLNFLCAHG YNKSQINLFS GKPYVCPKSF ILENFNYPSI TIPGFNRTAT
     VSRTVKNVGS PGTYVASIKA PKGIVVSVSP ASLKFEKIGE EKTFDVIFRA DSRFKSDSDF
     VFGHLLWSDG KHYVRSPLVV KHNK
//
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