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Database: UniProt
Entry: A0A161YJK2_9PEZI
LinkDB: A0A161YJK2_9PEZI
Original site: A0A161YJK2_9PEZI 
ID   A0A161YJK2_9PEZI        Unreviewed;       414 AA.
AC   A0A161YJK2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Serine protease (Subtilase) {ECO:0000313|EMBL:KZL73137.1};
GN   ORFNames=CT0861_11127 {ECO:0000313|EMBL:KZL73137.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL73137.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL73137.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL73137.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) 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       ECO:0000256|RuleBase:RU003355}.
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:KZL73137.1}.
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DR   EMBL; LFIV01000048; KZL73137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161YJK2; -.
DR   STRING; 708197.A0A161YJK2; -.
DR   OrthoDB; 380531at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 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; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
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   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   PANTHER; PTHR43806:SF69; PROTEINASE T; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000076552};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..414
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007829854"
FT   DOMAIN          39..106
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          144..376
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        146
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        177
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        333
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   414 AA;  42177 MW;  2C2F3853476950DA CRC64;
     MHAATLLALL PLAAVAAPSR RAQPAPVIKP RGATLVADKY IVRLKNEAKT GALQSVMSAF
     SADADHVYNF GNALRGFSST LNATEIEKLQ NDPDVDFIEQ DAIVTIKATQ RNAPWGLARL
     SSAQPGSTTY SYDESAGEGT CAYIVDTGID VEHPDFEGRA TFLANYADNS DTDGQGHGTH
     VAGTVGSATY GVAKKTKLFA VKVLDSNGEG TNSAVIAGMD FVASDAAGQE GCAKGVVVNM
     SLGGQSSTAV NQAAAAIVKA GHFLAVAAGN EAADASTSSP ASEQSVCTVG ATASDDSLAE
     YSNFGAVVDI LAPGSEIKST WPGGSTNTIS GTSMASPHIA GLAAYLLGLG SAPSDPVELC
     SYIAETALDG VVGQVPRRTV NRLANNGFAG NGTAKATDGS VVGRQLNKRF SIRA
//
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