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Database: UniProt
Entry: A0A1L7WRQ1_9HELO
LinkDB: A0A1L7WRQ1_9HELO
Original site: A0A1L7WRQ1_9HELO 
ID   A0A1L7WRQ1_9HELO        Unreviewed;       847 AA.
AC   A0A1L7WRQ1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Probable KEX1 protease {ECO:0000313|EMBL:CZR55454.1};
GN   ORFNames=PAC_05342 {ECO:0000313|EMBL:CZR55454.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR55454.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR55454.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR55454.1};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
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DR   EMBL; FJOG01000006; CZR55454.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7WRQ1; -.
DR   STRING; 576137.A0A1L7WRQ1; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000184330; 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:UP000184330};
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..847
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012656859"
FT   TRANSMEM        715..738
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          480..615
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          641..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..820
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        232
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        404
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   847 AA;  92865 MW;  FF2D6DF68D24BACE CRC64;
     MRLHSVLGLI GLGYLASASN LRARNYDAQD YYVLHLDPTT PPAQVAVELG LTHEGKLGEL
     EDHHIFSCHK QDDDVVHTAL KERRRRKRSI GGSDLLDGVK FAQKQKMKAR MEKRGIIPPR
     PAGYAAPIEE RQTSPEDAAL IKQAAVATQL GILDPIFAEQ WHLFNTVQIG HDVNVTDVWM
     QGITGHNATV AIVDDGLDMY SDDLKDNYFA EGSYDFNDNQ LEPKPQLADD RHGTRCAGEV
     SAVKNNVCGV GVAWDSKIAG IRILSKLITD ADEAIAMNYA FQKNQIYSCS WGPPDDGRSM
     DAPGILIKRA MLNAVQNGRG GLGSIYVFAS GNGAANEDNC NFDGYTNSIY SITVGAIDRK
     GLHPYYSEKC SAQLVVTYSS GSGDAIHTTD VGTNACYSGH GGTSAAAPLA AGIFALVLQI
     RPDLTWRDMQ YLVMQTALPI DIDTGEWQTT SIGRKFSHTF GYGKIDSWAT VEAAKTFKNV
     KPQAWFYSPW IHVNQAIPQG DQGLAVSFEV TADMLKAANL ERLEHVTVTM NVDHTRRGDL
     SVELVSPDKI ISHLAATRRL DTAPEGYDDW TFMSVVHWGE SGIGTWTIIV KDTMVNEHNG
     TFVDWHLKLW GESIDASKAT LLPMPSEHDD DNHDQVISTT TIAGATTSVT PVSTPTSMMA
     NPTDHPDRPT KPKPSGTTED ENTPTTSSSP AATTSASSWL PSFFPTFGGS SKKQIWIYGA
     AALILVFCSA LGIYLYMARR KRLRNNPRDE WEFDLLEEDE TEGLTGGGKK GAKKGGKRRA
     GELYDAFAAG SDESDTEYLD DNEGGDEREK KLYESDDEGK HVIGDDEDED EEGHNEKSHQ
     GEHLLRK
//
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