ID F9XB24_ZYMTI Unreviewed; 797 AA.
AC F9XB24;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Subtilase {ECO:0000313|EMBL:EGP87418.1};
DE Flags: Fragment;
GN Name=MgSPR2 {ECO:0000313|EMBL:EGP87418.1};
GN ORFNames=MYCGRDRAFT_10819 {ECO:0000313|EMBL:EGP87418.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP87418.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP87418.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR EMBL; CM001200; EGP87418.1; -; Genomic_DNA.
DR RefSeq; XP_003852442.1; XM_003852394.1.
DR AlphaFoldDB; F9XB24; -.
DR STRING; 336722.F9XB24; -.
DR MEROPS; S08.070; -.
DR EnsemblFungi; Mycgr3T10819; Mycgr3P10819; Mycgr3G10819.
DR GeneID; 13394146; -.
DR KEGG; ztr:MYCGRDRAFT_10819; -.
DR eggNOG; KOG3525; Eukaryota.
DR HOGENOM; CLU_002976_2_1_1; -.
DR InParanoid; F9XB24; -.
DR OMA; QIKDPIF; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000008062; Chromosome 5.
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:UP000008062};
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 696..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 469..604
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 607..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..797
FT /note="Acidic 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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGP87418.1"
FT NON_TER 797
FT /evidence="ECO:0000313|EMBL:EGP87418.1"
SQ SEQUENCE 797 AA; 88231 MW; CD0BF74B14EBC0FE CRC64;
RDYDAYDYYA VHIRSDGDPE LLSRELGLEL EGPLGYLDDH YVLRAAEKRH EYDHIHTAIE
DLKRRRRKRE AGAEKPHVLD DVLLAKKQEL HKRFPLVKRG PAEPLENLGP VDPLEGVQDE
VEDLIQEAER LGMEIAANLS IADPIYQDQW HLHNHRELGH DINVTGVWQS GITGKGSRVC
IVDDGLDMDS LDLKDNYFAK GSWDYNDPGP DPKPRLSDDH HGTRCAGEIA AARNDICGVG
VAYDAKVSGV RILSKAISDV DEAEALNYGY QENHIYSCSW GPPDNGMAME GPSVLIRRAM
IKGIQQGRGG LGSVFVFALG NGAANDDNCN FDGYTNSIYS VSVGGIDRKG KHPYYSEKCS
AQLVVTYSSG SGDAIHTTDV GENSCYVNHG GTSAAGPLVA GIFALMLEAN PKLNWRDFQY
LTAMTAVKID QDAEYQMNKA LGKEFSHAFG YGKADAWALV EAAKTWKSVK PQAWYFSPWL
HVKHGIPQGN QGLASSFEVT PDMLKTANLE RLEHVTVTMN VEHTRRGDLS VELRSPTGMV
SHIATHRRND NARAGYVDWT FMSVAHWGES GIGKWTVIVK DTNVNEHNGS FIDWKLRLWG
ESIDGEKQGL LPMPTEHDDD DHDLQPPQQA PALTTSVAVP TETGAPPGNP TDHIDRPTKP
KPTASPSPTT PAAVPSSTFF LPHIFPTFGV SPRTQIWMYG AVTMIIIFLA ALGGWFYYMR
RKRRWMNSRD DYGFEMVDRE DEDDEQAPLA SGGARKKGKR RAGELYDAFA EGSSDESEPE
EAEMFELGSD GESEDDG
//
