ID   SCONB_TRIVH             Reviewed;         663 AA.
AC   D4D8P3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Probable E3 ubiquitin ligase complex SCF subunit sconB;
DE   AltName: Full=Sulfur controller B;
DE   AltName: Full=Sulfur metabolite repression control protein B;
GN   Name=sconB; ORFNames=TRV_03480;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Component of the SCF(sconB) E3 ubiquitin ligase complex
CC       involved in the regulation of sulfur metabolite repression, probably by
CC       mediating the inactivation or degradation of the metR transcription
CC       factor. {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the SCF(sconB) E3 ubiquitin ligase complex.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat MET30/SCONB/SCON-2 family.
CC       {ECO:0000305}.
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DR   EMBL; ACYE01000180; EFE41798.1; -; Genomic_DNA.
DR   RefSeq; XP_003022416.1; XM_003022370.1.
DR   AlphaFoldDB; D4D8P3; -.
DR   SMR; D4D8P3; -.
DR   PRIDE; D4D8P3; -.
DR   EnsemblFungi; EFE41798; EFE41798; TRV_03480.
DR   GeneID; 9580963; -.
DR   KEGG; tve:TRV_03480; -.
DR   HOGENOM; CLU_000288_103_1_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS50181; FBOX; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 4.
DR   PROSITE; PS50082; WD_REPEATS_2; 7.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation pathway;
KW   WD repeat.
FT   CHAIN           1..663
FT                   /note="Probable E3 ubiquitin ligase complex SCF subunit
FT                   sconB"
FT                   /id="PRO_0000397257"
FT   DOMAIN          195..241
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          320..359
FT                   /note="WD 1"
FT   REPEAT          361..399
FT                   /note="WD 2"
FT   REPEAT          400..437
FT                   /note="WD 3"
FT   REPEAT          439..480
FT                   /note="WD 4"
FT   REPEAT          544..589
FT                   /note="WD 5"
FT   REPEAT          592..629
FT                   /note="WD 6"
FT   REPEAT          632..663
FT                   /note="WD 7"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  74769 MW;  11057FDC385F4F79 CRC64;
     MDTDNSTLPT EQSAVRETCD RDVTMSPRKR RRLSVSLEPE LTEPEAAGTP GERCSTADTP
     ESTASEPRSL FNSTPTEGNI APFLTKHIKD QHASRNRFAP IDSSLPRRKA DSKYCYRHRP
     DLKCRRQAAE PTVDQMQRDL STLSQNDQQS IAHFWSLFSA APSKHRNLML QGIVAQCCFP
     QLSFLSASVR DLIRIDFVTA LPPEISFKIL SYLDTASLCS AAQVSHSWRA LADDDVVWHR
     MCEQHIDRKC EKCGWGLPML DRKRLKDTKR QVQLRAAGKE IAPNQRPQQQ HRPWKAVYMD
     RFKVGTNWKY GRCTTTIFRG HTNGVMCLQF DDNILATGSY DATIKIWDIE TGKEIRTLRG
     HESTIRCLQF DDTKLISGSL DRTIKVWNWR SGECISTYTG HQGGVLCLHF DSTTLASGSK
     DNTIKIWNFH DKSTRILRGH ADWVNSVKLD TASRTVFSAS DDLTVRIWDL DTGKCIHSYA
     GHVGQVQQVL PLPREFEFKH QSNCADDRSD RLSGSESPDH RGSHGYGSNN APDQQPNTSA
     PPTEPMSPLF EALFTEDQGR PAPPRYMLTA ALDLTLRLWE VHTGRCLRTF FGHIEGVWGL
     AADTLRFVSG AQDHMAKVWD PRTGTCERTF TGHRGPVTCV SLSDSRMATG SEDSEVRMYS
     FKA