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Database: UniProt
Entry: A0A0C9TKP5_PAXIN
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Original site: A0A0C9TKP5_PAXIN 
ID   A0A0C9TKP5_PAXIN        Unreviewed;       497 AA.
AC   A0A0C9TKP5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Merops: S08.UPA {ECO:0000313|EMBL:KIJ08392.1};
GN   ORFNames=PAXINDRAFT_18477 {ECO:0000313|EMBL:KIJ08392.1};
OS   Paxillus involutus ATCC 200175.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX   NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ08392.1, ECO:0000313|Proteomes:UP000053647};
RN   [1] {ECO:0000313|EMBL:KIJ08392.1, ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ08392.1,
RC   ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN819633; KIJ08392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9TKP5; -.
DR   HOGENOM; CLU_011263_1_4_1; -.
DR   OrthoDB; 380531at2759; -.
DR   Proteomes; UP000053647; 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; 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:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 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   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:UP000053647};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..497
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002204267"
FT   DOMAIN          54..134
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          180..405
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        182
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        214
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        384
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   497 AA;  52707 MW;  5A278AAD79374365 CRC64;
     MSHFTTVAFL AASLASTVLA SPLSTSSYNT QRRPYLGLAP LAEVEHSHGT VNNSYIVVLK
     DDVPASLMQN HLNFLQTAHH SDSFLGDGVA TGLRHVYDTH IKGYAGEFTD GVLEQIRRMP
     EVDYVERDQI VRTMEIETLK TQKGSPWGLA RISHRSRLTF GTFSRYEYDP QGGEGVDAYV
     IDTGINIHHV EFEGRASWGK TIPTNDVDED GNGHGSHCAG TIASRKYGVA KKANLIAVKV
     LGSNGSGTMS DVVAGVAWAS QQAQLRAQAA RAEFAATGKT SHKGSVANMS LGGGVSTALD
     TIVNRAVAAG LHFAVAAGND NQDACKSSPA SAEKAITVAA STLADERAYF SNYGTCVNVF
     APGLNILSTY TGSPNAIATL SGTSMASPHV AGLVAYLLSI YPSVTFHPPL ATSFVPTALN
     VEDTYASFYS IARVTLPYWI SQYLPAPDFF SPIPKSNGPI LSPAELRSAI EFLSTPNIIA
     DSGKGTPNLL VFNNATA
//
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