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Database: UniProt
Entry: N1JDP0_BLUG1
LinkDB: N1JDP0_BLUG1
Original site: N1JDP0_BLUG1 
ID   N1JDP0_BLUG1            Unreviewed;       862 AA.
AC   N1JDP0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=KEX1 protease {ECO:0000313|EMBL:CCU77974.1};
GN   ORFNames=BGHDH14_bgh04181 {ECO:0000313|EMBL:CCU77974.1};
OS   Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS   (Oidium monilioides f. sp. hordei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX   NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU77974.1, ECO:0000313|Proteomes:UP000015441};
RN   [1] {ECO:0000313|EMBL:CCU77974.1, ECO:0000313|Proteomes:UP000015441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH14 {ECO:0000313|EMBL:CCU77974.1};
RX   PubMed=21148392; DOI=10.1126/science.1194573;
RA   Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA   Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA   Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA   Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA   Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA   Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA   Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA   Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA   Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA   Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA   Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA   Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT   "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT   extreme parasitism.";
RL   Science 330:1543-1546(2010).
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:CCU77974.1}.
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DR   EMBL; CAUH01003938; CCU77974.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1JDP0; -.
DR   STRING; 546991.N1JDP0; -.
DR   EnsemblFungi; BLGH_00216-mRNA-1; BLGH_00216-mRNA-1; BLGH_00216.
DR   eggNOG; KOG3525; Eukaryota.
DR   HOGENOM; CLU_002976_2_1_1; -.
DR   InParanoid; N1JDP0; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000015441; Unassembled WGS sequence.
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:UP000015441};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..862
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004107145"
FT   TRANSMEM        723..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          479..614
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          648..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          796..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..700
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..810
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..835
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..862
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        231
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        403
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   862 AA;  95480 MW;  4F47F7CAFB4B0FA4 CRC64;
     MRLHSLLCLV GLGQLCSATT KRARDYNTQD YYVLHIESGI PPSQVAARLE LVYEGELGNL
     ADHHIFSSHK QEEDIVQISL NKRRQFKRNY NDIDMLDGVR FAQKQRVKPR MEKRGLVAPN
     PRDHKAWTER RDTPVPELVA KQSEVANKLD IRDPIFNDQW HLLNVVQQGH DVNVTGVWLQ
     GVTGHNATVA IVDDGLDMYS DDLKENYFSE GSYDFNDNSL EPKPQLSDDR HGTRCAGEVS
     AVRNNVCGVG VAWSSKVAGI RILSKQISDA DEAVALNYAY ERNQIYSCSW GPPDDGKSMD
     APGILIKRAM LNAVQNGRGG LGSIYVFASG NGAANEDNCN FDGYTNSIYS ITVGAIDRKG
     LHPYYSEKCS AQLVVTYSSG SGDAIHTTDV GSNQCYSGHG GTSAAAPLAA GIFALALQVR
     PDLTWRDMQY LVMETALPID LDTGEWQTTS IGLKYSHTYG YGKIDTWATI EAAKTYQKVQ
     PQAWFFAPWI HVNQEIPQGD AGLAVSFEVT QEMLSNANLK RLEHVTVTIN IKHGKRGDLS
     TDLVSPAKIV SHLSVVRRQD SSNKGYDDWT FMSVAHWGEA GVGTWTIIVK DTEVNKFNGT
     FVDWHLKLWG ECIDSSKATI LPMPSDHDDD NHDQVIISTT TIAASTTSLI SVPTPSSEPV
     ANPTDHPERP QKPPKPTETA DKTTPPTAAP DTSNEPAPNV SAVPSTWLPS FFPTFGVSPK
     TQIWIFGAAA LILIFCFGLA IYFFIARRKH LRNNPRDEWE FDLLEDDEAE GLNGVKANGR
     GRMRRAGELY DAFAAGSEDE SDENYADDDE GGDEREKRLY EDEDEEGGKH VIGDYDDDSD
     EDENQDETGS ILGEKEQKFT RK
//
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