ID F9FRN6_FUSOF Unreviewed; 992 AA.
AC F9FRN6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Zn(2)-C6 fungal-type domain-containing protein {ECO:0000259|PROSITE:PS50048};
GN ORFNames=FOXB_09067 {ECO:0000313|EMBL:EGU80418.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU80418.1};
RN [1] {ECO:0000313|EMBL:EGU80418.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU80418.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU80418.1}.
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DR EMBL; AFQF01002526; EGU80418.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FRN6; -.
DR STRING; 660025.F9FRN6; -.
DR PaxDb; 5507-FOXG_02695P0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd00067; GAL4; 1.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR47785:SF4; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR PANTHER; PTHR47785; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG)-RELATED-RELATED; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 917..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 340..370
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 401..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 118
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 261
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 992 AA; 109725 MW; 3A5810BC029AAFEF CRC64;
MTGKHGIPAL PLRCLRVSRK ILGPRRRPDT SEAIAHRPEV TRRSKLQLNA PWNLARISQG
HARNDGLRRY RYDATAGSGT YVYLVDSGIN FSHAEFSGRA FRGANFVLGS PDDDELGHGT
HIAGIIGGKT YGVAKSCTMI SVKVGVNWAT KDAIAKGIAD RSVINVSAGG LYNASVNVTV
KNATDARITV VVAAGNHAAF AGAFSPASAD TAITVAASGP DDCRAPFSNY GPCVDMFAPG
AHIASAWNYV DNGMKYESGT SAAAAHVTGL TAYFISSENL RGFKAVRERI LGASLNGVIT
DTRYSSNRLA YNDNHTIAAA LDLVHNLVTS SPNTPRVIQA CVNCRMRKTR CDAAQPRCGL
CASQNVDCVY RDAKQPKIDY NTQVLLERMQ LLEDRILLST SSSQAQRAPP EASPMSHHDP
QPDNLHDSTT ESREPVFEVQ IPLSHTANAN HVFSWSLVQT LLSENSTDQQ ELPSYADATE
VFFQEQQSSK HPSTTSQPLS SWKLYDSSYF SSSRDDSIAR LHDLIHLYFT KVNIFFPLLS
KSNILNIFEM VTAREVYGND ETATVDMPQY GLLLVVLCLA LLSSSGQSDI CIEKNRRYSQ
PFSNSSNIPE DQLRSELWCK TRLILGYVST DMSLEAAQAN MLASIYMGAS GAVAEAFHWA
HATAVKCESM ARLQAKNESI SDGFRRLYWI SFIYECDFIS EISIVSPSGI ARYEDKIPYP
AFTAENHPIS PSVPESSEAN SIRSQEELVA FQITTNSAIR RFLNTVNSVV YDDKEQFRTR
RSNYASWLLR ISEDLWSHHS AIYRNLPEFL LSNPSQDVPM TGADTSSPAS LQSPTARIQG
IPVGNNSWNI LRLKGRYYAG QYIIHRPFIE FIVLNIDNFE SHPCKDAVLK RSKSCLDGCT
GFIKVFDVQT VNSLTCLFPT GMVTFTMTII LMVATIFPIF KDLLPDDVED VILGGKRNLA
RFSQSVAEFS WHIEILERLD VARRNRIVRH EE
//
