SCONB_ASPFN
ID SCONB_ASPFN Reviewed; 706 AA.
AC B8NGT5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=AFLA_138030;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963478; EED51039.1; -; Genomic_DNA.
DR RefSeq; XP_002379815.1; XM_002379774.1.
DR AlphaFoldDB; B8NGT5; -.
DR SMR; B8NGT5; -.
DR STRING; 5059.CADAFLAP00007680; -.
DR EnsemblFungi; EED51039; EED51039; AFLA_138030.
DR VEuPathDB; FungiDB:AFLA_138030; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_1_1; -.
DR OMA; KMCEQHI; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IEA:EnsemblFungi.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:EnsemblFungi.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:EnsemblFungi.
DR GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblFungi.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
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; SSF50978; SSF50978; 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..706
FT /note="Probable E3 ubiquitin ligase complex SCF subunit
FT sconB"
FT /id="PRO_0000397247"
FT DOMAIN 203..249
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 377..414
FT /note="WD 1"
FT REPEAT 417..456
FT /note="WD 2"
FT REPEAT 458..494
FT /note="WD 3"
FT REPEAT 496..537
FT /note="WD 4"
FT REPEAT 589..632
FT /note="WD 5"
FT REPEAT 635..672
FT /note="WD 6"
FT REPEAT 675..706
FT /note="WD 7"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 79479 MW; E7690312C8E2183F CRC64;
MQSDDRSVRE GSDSSQTFLM KMAQPTGELT HPSQQQQQQL LQQQSFRSIF GGASDTAEEI
DTETDSNHRR PHSFGAAATT PAKLANKNVA PFLVKHIPEQ YGPLGSRRTD KLEDLSSPNS
KFCYRHRPDL KCRRQADEPS MDKLQRELET LPPSDQQGIA HVWSLFSAAP AKHRKLILQG
IMAQCCFPQL SFVSATVRDL IRIDFLTALP PEISFKILCY LDTTSLCKAA QVSSRWRALA
DDDVVWHRMC EQHIHRKCKK CGWGLPLLER KRLRESKREI ELRATTWDVS GPAQNAGGAE
CSAPHADDVI TQKRKADSSD DETAIVKRHC SSLDARPEPD EDYYTTRYRP WKEVYKDRFK
VGTNWKYGRC STKVFKGHTN GVMCLQFEDN ILATGSYDAT IKIWDTETGE ELRTLRGHQS
GIRCLQFDDT KLISGSMDRS LKVWNWRTGE CISTYTGHRG GVIGLHFDAT ILASASVDKT
VKIWNFEDKS TFLLRGHTDW VNAVRVDTTS RTVFSASDDC TVRLWDLDTK ACLRTFHGHV
GQVQQVVPLP REFEFEDHDA ECDNDNMSTT SGDTESNSLQ ATLGLESNAT ETSVFGPSFD
NGRPAPPRYI VTSALDSTIR LWETTTGRCL RTFFGHLEGV WALGADTLRI VSGAEDRMVK
IWDPRTGKCE RTFTGHSGPV TCIGLGDSRF ATGSEDCEVR MYSFRN
