ID K3V7G8_FUSPC Unreviewed; 784 AA.
AC K3V7G8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=FPSE_12114 {ECO:0000313|EMBL:EKJ67743.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ67743.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ67743.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ67743.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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:EKJ67743.1}.
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DR EMBL; AFNW01000621; EKJ67743.1; -; Genomic_DNA.
DR RefSeq; XP_009263506.1; XM_009265231.1.
DR AlphaFoldDB; K3V7G8; -.
DR EnsemblFungi; EKJ67743; EKJ67743; FPSE_12114.
DR GeneID; 20370731; -.
DR KEGG; fpu:FPSE_12114; -.
DR eggNOG; KOG4177; Eukaryota.
DR eggNOG; KOG4266; Eukaryota.
DR HOGENOM; CLU_368436_0_0_1; -.
DR OrthoDB; 2247221at2759; -.
DR Proteomes; UP000007978; Chromosome 2.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR24178:SF9; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT REPEAT 62..94
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 95..127
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 131..163
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 164..196
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 278..310
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 311..343
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 468..707
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 370..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 474
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 528
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 688
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 784 AA; 87447 MW; 10139ED8CDA942EC CRC64;
MTPEDYAKYL REHRLDPENR PKDRGEAIHS AILDKRVYIA IELLNLYPED CLEARSQKGS
PRWRTPLHNA CEHNRTLVVK ELLDKGADSN ARSFHRLTPL IFAVEAENHE IVKLLVEKGT
DVNLQSDAKT NERSALHVAA NVVSPDILLT LLHNGADPKL VTKNGNTPLH FAVRSGCASA
AALLLFHGAS PTATNEKGES PINLIENLGK DDHGKFTHIF ECAQKKGDFG DLFNQHLRRN
APIDIVSALH WAISHDLDGA VAYLLHVEPH AVEARLSSGW YPLHVAARGG HEKCVAVLLG
HEAKVDCKTK TGWTPLMMAA EKGDRKVLRI LLNYDADRSA TNANKDTAWK IARHHGHRFP
MLLAVRHVSP SNIDREGKET DGESRLAPPK ERPHCRTPSP SPRDVSEDTG EMFALTDAKS
DEASTETPQN SEYFEDFLKT LEQTWYHKIQ WNPEDDVENP RKDWTGPVKI AILDTGIDLS
HQDFNQRAKR RTKIGLKHVS EKTQRERIKA CKNFTDGPEH DVTDNDGHGT HIAGLIMTIA
PRAELYIAKV SSPQRPENKD ESPKRRGKES HPIQEALKWA IENEVNIINM SLGFSELGSL
ELTKTLRDAD GKGISVFAAA SNHGNRNPIA WPARDRRLAI CVGSNDEMSK LSTFAPSTNS
KFPIFVTYGE NIYSHWPGGG YRKMSGTSVS TPIAVGMAAM IIAFLNKTNE WGQDDKAGLL
GRIKEWRIRG TEGMGRVLEN MCRDINGLKL LSPKLMWEDD TVPDPKPIQI LAFLSFFEGR
EIAG
//