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Database: UniProt
Entry: A0A286UMK2_9AGAM
LinkDB: A0A286UMK2_9AGAM
Original site: A0A286UMK2_9AGAM 
ID   A0A286UMK2_9AGAM        Unreviewed;       812 AA.
AC   A0A286UMK2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Kex {ECO:0000313|EMBL:PAV20769.1};
GN   ORFNames=PNOK_0339600 {ECO:0000313|EMBL:PAV20769.1};
OS   Pyrrhoderma noxium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX   NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV20769.1, ECO:0000313|Proteomes:UP000217199};
RN   [1] {ECO:0000313|Proteomes:UP000217199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA   Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA   Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA   Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA   Kikuchi T., Tsai I.J.;
RT   "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT   Hymenochaetales Members.";
RL   bioRxiv 0:0-0(2017).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
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:PAV20769.1}.
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DR   EMBL; NBII01000003; PAV20769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286UMK2; -.
DR   STRING; 2282107.A0A286UMK2; -.
DR   InParanoid; A0A286UMK2; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000217199; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; 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   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
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   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000217199};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        711..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          484..630
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          649..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        196
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        234
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        408
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   812 AA;  89465 MW;  1F32DA49AE2793AA CRC64;
     MSNFRRVSIR SWHILLAVAF SICVVTTSVI ASKPTKLSHD LYDYYVLEHN PAIGVSIEEC
     AESLGAEVVD SAGELHNHWL LRRQKNERST RDDGVLTQHK SLLQRRDPVS FAIKHLSRQT
     LRQRVKRAAL PAPAPQSPDD TLSLTRDIAE RLGIEDPLFK DQWHLINEEY PEHMVNAAPV
     WDMGITGKDV VSCIIDDGLE YESEDLADNF DAAGSYDFND HTELPKPRLR DDHHGTRCAG
     QIAAVKNGVC GVGIAYDSKV AGVRILSGPI SDIDEATALN FGYQNTSIYS CSWGPPDDGR
     SMDVPSILVQ KAMLNGVQRG RDGLGSVFVF ASGNGANSGD QCNFDGYTNS IYSVTVASID
     YQGQHPYYSE ACAANMVTTY SSGFDRNKHI VTTDIGRNKC TRNHGGTSAA APNAVGIFAL
     ALSARPDLTW RDIQYLCVKT AQIVNPEDPD WEPIASGQLF SYKYGFGKLD ALKFVKAAQE
     WSVVKPQTWI EAPAVQLENG SMDSNGKYSG GLPIAKDGIQ STLEITQDMI DDNNFEDLEH
     VTIRVWIDHT RRGAVEVSLV SPNGIRSVLA GKRNSDFDRD GFPGWRFMSV KHWGENPLGT
     WTLHVSDQNA KSESGSLIGW SLSLWGSSKD TSKVQTYVLK ASEELPIPFP PVVEDPVPDP
     DSTTLDPSTT KQYQKPTVTG TSVSNQDDTE STQTGSSGGT SEKMSDDTRH IIVVVASIFT
     VLLIGFGAFL IIRQLRQNRR DALERNRSGD NDVRMRLLDS DSRHLTPSES VTVLYDEEDE
     GKADAVGPSD EEQTYNDSDD DHDVDESLLR SH
//
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