ID F9F249_FUSOF Unreviewed; 1577 AA.
AC F9F249;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_00473 {ECO:0000313|EMBL:EGU88961.1};
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:EGU88961.1};
RN [1] {ECO:0000313|EMBL:EGU88961.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU88961.1};
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.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-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:EGU88961.1}.
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DR EMBL; AFQF01000132; EGU88961.1; -; Genomic_DNA.
DR STRING; 660025.F9F249; -.
DR PaxDb; 5507-FOXG_01284P0; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
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};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1577
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013220571"
FT DOMAIN 42..135
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 191..434
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 597..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1470..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 391
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1577 AA; 172625 MW; 5BF1D1AF7FFF342A CRC64;
MKSALTLSMA AVASAASFSV GTVHDKAAPI LSSIDAETIP DSYIIKFKDH VDHAAASDHH
MWVQDTHKQG ETERLELRKR SVPFTDKTFS GLKHTFDIGD AFKGYAGHFD ESMIEKVRNH
PDVEFIERDT LVHTMVPVSQ NMITEDKCDG ETERQAPWGL ARISHRNTLN FGTFNKYLYS
SDGGEGVDAY IVDTGTNVDH VDFEGRAHWG KTIPSGDADE DGNGHGTHCS GTVAGKKYGV
AKKANVYAVK VLRSNGSGSM SDVVKGVEFA ATSHLEQKKK AKDGKRKGFK GSVANMSLGG
GKTQALDAAV NAAVRTGIHF AVAAGNDNAD ACNYSPAAAS EPVTVGASAL DDSRAYFSNY
GKCTDIFAPG LNIQSTWIGS KYAVNTISGT SMASPHIAGL LAYYLSLQPA EDSEYALASI
TPKKLKENII SVATEDALSD IPSDTPNLLA WNGGGCSDYK KIVEAGSYKV NKAAPSSRVE
EIKHAVEQEV NLVSGKLTTG AKELGSKAEK FSKKIHELVD EELEEFLKEL NLCHHIVRLN
AWRSRSFLSS GKKNRRLLSR SKSTNSVARS PIRDLESINP ARAERDANIA AVVSYQRAQD
RDSSEGMPLP RDPASFYPDR SDGTGSVIRH SLERTDSALS VHGSSNIARK KSVRFTGPLA
HPRRNFACRA NGGRDSPTKA TSAIHPFGNA NTRPSSTLSF HNERPDNFSL TRRYLEMLQP
PDTCYNPEED AASMAASYKK VRKSRSMVTS SHAETGTISS KTWSARARQP PTVPRRLPTN
SENEPLKDAM PPNASLRAST SMGFLKTRRR LAASRSSSRA DDHDLAVQLA RERFRQIQEQ
DAKKSQSSSL LRPKHTQSEG SPFRKSMRNS SNNTVVSTLS NISGSKQRGI RKTARKVSQG
LRSRLRGLFG RGKSSEDSDQ HEHEQVAVEK DSDAESCLQI GDAESTEEAS MFQVTSHVPS
LHDVPSNQQL RSRKGSVESF GDGDQHIPDD KSRVTSWTNS MTNTVTSHET FGDWERQRLS
VIKENGTHIP SSVRSIEYLE QQTRDMIADM SVDSERVYSA LMERLARKEP TDRVMQSQPG
SVKSRGTNTG DNDGQSINRQ WDCSTIRCVR PDDNIFRDNG DPSSRSSSST TEVPDYENKH
QPQTGHTSTV EHTAALNWSD DRTHSESEHT SVLLQGLESH KTITQRSSAF FASPSCQSFR
SPSPYRRALR ASQMNSEDEQ GTFQGSRYLH SLSTLCLPTR QDSSPSSGKD LQVGDTESVY
SCAGDDANPV HSASENTVGQ NETCIYNDPG PPPEVPDRLS YRQHQRDTST ASSVEWKTWL
SSKVSQLEAP LTPTKREKWN DVLPTLGHVR ENASMGSTPE HFAPTKDGAT NRSPLSNVKG
NAQTFQDGGN PARSTRQVFI GYDENAAPSY KANTYTKERP PSIPPRSRLR AVPSLPSVGS
SGYIPDTGLV KEMPRMRSLN TIGRLNSTPE ESINKRRSRT RVTGWQGSPT KSSPGVRALT
NTQPPRIGSP ALRGDFGLKY PIRSQTIERQ PGDTMMDRES DAQAMGSKTM VDLFLSSRRN
QGDGRSSGFG SSPAAFL
//
