ID Q0UUZ4_PHANO Unreviewed; 831 AA.
AC Q0UUZ4;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN ORFNames=SNOG_04420 {ECO:0000313|EMBL:EAT88180.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT88180.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR EMBL; CH445330; EAT88180.1; -; Genomic_DNA.
DR RefSeq; XP_001794838.1; XM_001794786.1.
DR AlphaFoldDB; Q0UUZ4; -.
DR STRING; 321614.Q0UUZ4; -.
DR MEROPS; S08.070; -.
DR EnsemblFungi; SNOT_04420; SNOT_04420; SNOG_04420.
DR GeneID; 5971706; -.
DR KEGG; pno:SNOG_04420; -.
DR VEuPathDB; FungiDB:JI435_044200; -.
DR eggNOG; KOG3525; Eukaryota.
DR HOGENOM; CLU_002976_2_1_1; -.
DR InParanoid; Q0UUZ4; -.
DR OMA; AINFAYQ; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
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:UP000001055};
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..831
FT /note="P/Homo B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004178410"
FT TRANSMEM 707..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..604
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 613..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 393
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 831 AA; 92100 MW; E4A4F3D629621C1F CRC64;
MRILNLWNLL SAASLATAAQ HLPPRNYSSH DYYAVHIDPT SSPLDVAAHL GLTYEGPLSS
LAEHHVFKAP KHDNDIIDEA RQDLKRRRRK REIGYESHPL DSVRFTQKQK IKPRHWKRSV
IPERQDRAGI QITDAIRTQR EIAGKLEIHD PIFEEQWHIF NVKDTRQRHQ RITGKGVTAC
VVDDGLDYDS NDLKDNFFAE GSHDYNDHED LPTPKLSDDR HGTRCAGEIA AGRNDACGVG
LAYDAKISGV RILSGDITDM DEALAINYEM QKNFIYSCSW GPPDDGKTMQ APGILIEKAM
VTAVQQGRGG KGSIYVFAAG NGAASDDNCN FDGYTNSIYS ITVGAIDKNN QHPYYSEACS
AQLVVTYSSG GGDSIHTTDV GANKCTSQHG GTSAAGPIGV GVYALLLEAR PDLTWRDVQW
LTVMTAVPFD TPSDWTKTAL DRMYSHQFGY GKLDAWAIVE KSKDWKLVKP QAWFWSPWMH
VKKAIPEGDH GLASVFEVTA DMLKEANLER VEHITLTMNV KHQRRGDLLV QLHSPTGMIS
HLSTARRDDE DIRGYQDWTF MSVAHWGESG VGNWTVIIKD VISGNNKKGT FVDWKLRLWG
ESIDAAKAKL LPIPTEHDDD DHDKIEDHPA HTTSVSVPAG TKPTMTGNPS DHPDRPVNQK
PSQTLADVQQ TVTATSSPTA PTASSTPAEN LLPSIFPTFG VSKRTQIWIY GSLALIIVFV
IGLGAYLFIA RRKRLRDSRD SYEFEVLDDI EDREDTGMLG AAAGRKKHAR RGGELYDAFA
GESDEDLLSD EDGDEGPYRD RDGDRFNEKF EAADESDEGT GSSSSSAGKR Q
//
