ID M7UC63_BOTF1 Unreviewed; 858 AA.
AC M7UC63;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative pheromone processing endoprotease protein {ECO:0000313|EMBL:EMR91245.1};
GN ORFNames=BcDW1_66 {ECO:0000313|EMBL:EMR91245.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR91245.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR EMBL; KB707674; EMR91245.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UC63; -.
DR SMR; M7UC63; -.
DR STRING; 1290391.M7UC63; -.
DR MEROPS; S08.070; -.
DR HOGENOM; CLU_002976_2_1_1; -.
DR Proteomes; UP000012045; 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};
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..858
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004086330"
FT TRANSMEM 720..743
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 650..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..824
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 858 AA; 94264 MW; 5B35C2F754322CD0 CRC64;
MKLHTLIGLF GLGVWANAVN LRPRNYDAHD YYVLHLDSTA DPVQVAGRLG LSHDGQLGEL
EDHHVFSTHK QDEDVVHTAL KMRKRRKREL SDFDILDTVR YAQKQKLKAR MEKRGLMRPA
PEGYEIDERQ DTTPPVDAAV AKQQAVQKAL GIQDPIFKDQ WHLYNPVQVG HDVNVTDVWM
QNITGTGSIV AIVDDGLDMY SNDLKANYYA EGSYDFNENT LEPKPRLSDD KHGTRCAGEV
SAVKNDVCGV GVAYDSKIAG IRILSKMITD ADEAVAMNYA YQHNQIYSCS WGPPDDGRSM
DAPGILIKRA MVNAVQKGRG GLGSIYVFAS GNGAANEDNC NFDGYTNSIY SITVGAIDRK
GLHPYYSEKC SAQLVVTYSS GSGDSIHTTD VGTNTCSDAH GGTSAAAPLA AGIFALVLQI
RPDLSWRDMQ YLVMSTALPV DLETGEWQTT TIGKKFSHTF GYGKIDTWAT IEAAKDFKNV
KPQAWFYSPW IHVNQAIPQG DDGLSVSFEV TKEMLQEANL ERLEHVQVTM NIAHTKRGDL
SVDLVSPDKL VSHLSASRRY DSEPEGYDDW TFMSVVHWGE SGIGTWTITV RDTFVNEHNG
TFTDWHLKLW GESIDAEKAI VLPMPTEHDD DNHAEIATTT IAGVTSAATA APTNPAAPTG
ELPSVPSDHP DRPINAKPSG TEDELTSPTS TAPAESETTA PSTWIPSFLP TFGVSSKTQI
WIYGALGLIA AFCAGLGVYL YMARRKRLRN NPRDEWEFDL LEDDEAEALA GNTEMSMKKG
GKRRAGELYD AFAAGSDDED DEYRDGGDER EKKLYEDDGE SEGTGSGSGH HVVGDDDDED
SDDESAVNVK DEKKPLNK
//
