SCONB_ARTBC
ID SCONB_ARTBC Reviewed; 663 AA.
AC D4AM37;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 53.
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=ARB_04727;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
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}.
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; ABSU01000002; EFE35793.1; -; Genomic_DNA.
DR RefSeq; XP_003016438.1; XM_003016392.1.
DR AlphaFoldDB; D4AM37; -.
DR SMR; D4AM37; -.
DR STRING; 663331.D4AM37; -.
DR EnsemblFungi; EFE35793; EFE35793; ARB_04727.
DR GeneID; 9521921; -.
DR KEGG; abe:ARB_04727; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_1_1; -.
DR OMA; KMCEQHI; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008866; 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 Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..663
FT /note="Probable E3 ubiquitin ligase complex SCF subunit
FT sconB"
FT /id="PRO_0000397244"
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..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..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..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 74866 MW; 97CF3B9FA48291B5 CRC64;
MDADNSTLPT EQSAVRETCD RDVTMSPRKR RRLSVSLEPE LTEPEAAGTP GERCSTADTP
ESTASEPRSL FNSTPTEGNI APFLTKHIKD QHASRNRFAP IDSSLPRRKA DSKYCYRHRP
DLKCRRQAVE 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 RGSHGYRSNN APDQQPNTSA
PPTEPMSPLF EALFTEDQGR PAPPRYMLTA ALDLTLRLWE VHTGRCLRTF FGHIEGVWGL
AADTLRFVSG AQDHMAKVWD PRTGTCERTF TGHRGPVTCV SLSDSRMATG SEDSEVRMYS
FKA