ID   PEPC_ASPNG              Reviewed;         533 AA.
AC   P33295;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Subtilisin-like serine protease pepC;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=pepC;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=8449413; DOI=10.1016/0378-1119(93)90745-o;
RA   Frederick G.D., Rombouts P., Buxton F.P.;
RT   "Cloning and characterisation of pepC, a gene encoding a serine protease
RT   from Aspergillus niger.";
RL   Gene 125:57-64(1993).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M96758; AAA32702.1; -; Genomic_DNA.
DR   PIR; JU0146; JU0146.
DR   AlphaFoldDB; P33295; -.
DR   SMR; P33295; -.
DR   STRING; 5061.CADANGAP00005548; -.
DR   Allergome; 3130; Asp n 18.0101.
DR   Allergome; 83; Asp n 18.
DR   VEuPathDB; FungiDB:An07g03880; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1143957; -.
DR   VEuPathDB; FungiDB:ATCC64974_45980; -.
DR   VEuPathDB; FungiDB:M747DRAFT_312795; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027126"
FT   CHAIN           ?..533
FT                   /note="Subtilisin-like serine protease pepC"
FT                   /id="PRO_0000027127"
FT   DOMAIN          43..136
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          145..450
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REGION          496..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        181
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        379
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        320..351
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   533 AA;  56949 MW;  0DC26E79BE8E8CC1 CRC64;
     MKGILGLSLL PLLTAASPVF VDSIHNEAAP ILSATNAKEV PDSYIVVFKK HVTSELASAH
     HSWVQDIHDS QSERTELKKR SLFGLGDEVY LGLKNTFDIA GSLIGYSGHF HEDVIEQVRR
     HPDVDYIERD SEVHTMEGAT EKNAPWGLAR ISHRDSLTFG NFNKYLYASE GGEGVDAYTI
     DTGINVDHVD FEGRATWGKT IPTNDEDLDG NGHGTHCSGT MAGKKYGVAK KANLYAVKVL
     RSSGSGTMSD VVSGVEYAVQ AHIKKAKDAK NGKVKGFKGS VANMSLGGGK SKTLEDAVNA
     GVEAGLHFAV AAGNDNADAC NYSPAAAEKA ITVGASTLAD ERAYFSNYGE CTDIFAPGLN
     ILSTWIGSNY ATNIISGTSM ASPHIAGLLA YFVSLQPSSD SAFAVEELTP AKLKKDIIAI
     ATEGALTDIP SNTPNVSHAA VGIYKRNELT QKFSSLPGTV VVPRTTPTSL AAVATRSPLP
     RTASRTVLRV SFTRPKSCSP RSLVPSTARS RMPSSHRSEL VLSRRRSEDL VFF