ID F9G4R3_FUSOF Unreviewed; 469 AA.
AC F9G4R3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 08-NOV-2023, entry version 46.
DE RecName: Full=Protein SGT1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_13645 {ECO:0000313|EMBL:EGU75845.1};
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:EGU75845.1};
RN [1] {ECO:0000313|EMBL:EGU75845.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU75845.1};
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 SGT1 family.
CC {ECO:0000256|ARBA:ARBA00008509}.
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:EGU75845.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFQF01003424; EGU75845.1; -; Genomic_DNA.
DR AlphaFoldDB; F9G4R3; -.
DR STRING; 660025.F9G4R3; -.
DR PaxDb; 5507-FOXG_07652P0; -.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR CDD; cd06466; p23_CS_SGT1_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS_dom.
DR InterPro; IPR044563; Sgt1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45862; PROTEIN SGT1 HOMOLOG; 1.
DR PANTHER; PTHR45862:SF1; PROTEIN SGT1 HOMOLOG; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 233..323
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 386..469
FT /note="SGS"
FT /evidence="ECO:0000259|PROSITE:PS51048"
FT REGION 138..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 51626 MW; 2E3FA2C44B7D2C88 CRC64;
MSHITLAQQG LAAAEARNWD EAIEKLSTAL KASQNPAWLV ARSKALINKK RFQEALDDAN
LAWHTAYQRN KRPLLIDAHY RRAVAYFRLG QYANADACCV YAMRLVKGFP AVEKEDPAKK
NTDENGFYKV TLKDAQEESK TDDINKSQGG AAGALGAQGN DVANAKEWRI ASTLRMQILF
AMDKLPEDDP ARKLTTANKP ELKELSDVGN KKAETKESAA ATQTASKPTV PADTPVRLQE
FQNDTTMTVS IFSKGVNKEK LQVQFSPKSA HLDSIIWPSG DEKPFTLDLW GEIDTEASTY
RVTPNKVELA LKKKTPGKWA QLKGEAGDSA PDAAAAEEAE KLKVLKDARK KAMDNAAAEA
PAQEKPTDST EAKEKTPAAQ DSSKPAYPSS SRTGPKNWDT IGDDIDSDEE KDVNVFFKKL
FKDASPEQQR AMMKSFTESN GTSLSTDWDD VKNRTVETVP PEGVEAKKW
//
