ID A0A317XQI6_9BASI Unreviewed; 950 AA.
AC A0A317XQI6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
DE Flags: Fragment;
GN ORFNames=BCV70DRAFT_139083 {ECO:0000313|EMBL:PWY99550.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWY99550.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWY99550.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWY99550.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR EMBL; KZ819195; PWY99550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XQI6; -.
DR STRING; 1882483.A0A317XQI6; -.
DR InParanoid; A0A317XQI6; -.
DR Proteomes; UP000246740; 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; 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 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; PS00136; SUBTILASE_ASP; 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:UP000246740};
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 793..814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 558..694
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 102..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 307
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 482
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PWY99550.1"
FT NON_TER 950
FT /evidence="ECO:0000313|EMBL:PWY99550.1"
SQ SEQUENCE 950 AA; 103689 MW; 41158CE6FEFDF4B4 CRC64;
ISAASCSANG DTAQLHRRRL DPSEYPWANQ KRSVPLPAER SYHSHHYYVV ELNPRHEKDV
DPRHVAEALG AEFVERAGEL PHHWLIRSEK PLPADADLDA LAKRASSSTS KPLDSRSLQR
PDVPEHQDPI LTRWNAIRRS AHEPGFSTEH GLSKRQHAAA FSIKGVERQV VRRRHKRNVI
YDPVEMPHLY PELRDPFPEP GPAPVASPRP PPISSAKTAE MMSLYGIKDP LFANQWHLAN
DKKRGFDLNV TEVWSQNILG DGVNVCLIDD GLDMHSPDLK DNFFAAGSYD FNSHVALPEP
RESDDQHGTR CAGEIAAVKN DVCGVGVAHH SKVSGVRILS GPISDVDEAA ALNYAYQQNH
IYSCSWGPPD DGRSMDAPKG LIAKAMLNGV QNGRDGKGSI FVFAGGNGGA SDDQCNFDGY
TNSIYSMTIA AVDREGQHPY YSEMCSAIIG TSWSSGSGDH IHTTDVAWNG NNRCTAHHGG
TSAAAPLAAG VIALALSVRP ELTWRDAQHV AVRSAVMVNP EDPDWQRTQA GRHYNHKYGY
GLIDAYQFVE EAKRHQLVTP QAWYESPNVT LPATQTLITE PGTESTITIT EDDLRNANLA
ALEHVTVRVW ITHARRGDVN VELVSPHGTK SALARTRRYD DATTGFPGWS FMTLKHWDES
PVGEWKIRVY DNAHPNRVGN FYAWTMTLWG ASLDPAKAKP WNFPQDSVEY HETLAAAPNT
TIIKLPAAQT SSAQLKKPTD HLPADHGTAP GESHIDFSNS NGNGAASGGA GSELDRPEAD
TGYLTGLRKN STWVVVAGGL VLIFAGSLAA FFIMRRRKMR GRGSGLGGDR GATGGEYEYL
ATDEELAMGD LDGDVGGRGG RGPRTGRRGK AGGAEKSRRT KELYDAFAEG SSDEDGDDLY
DDDARDGRGL MGRASPADPA SKSSAQPYRD DLEDDDGDRR FALHDDDEDG
//
