ID   SCONB_ASPOR             Reviewed;         705 AA.
AC   Q2UFN8; Q5KU02;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=AO090026000133;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sano M., Takase K., Yamamoto M., Machida M.;
RT   "Analysis of sulfur regulatory netwok in Aspergillus oryzae.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAD83608.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB070844; BAD83608.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP007159; BAE59627.1; -; Genomic_DNA.
DR   RefSeq; XP_001821629.1; XM_001821577.1.
DR   AlphaFoldDB; Q2UFN8; -.
DR   SMR; Q2UFN8; -.
DR   STRING; 510516.Q2UFN8; -.
DR   EnsemblFungi; BAE59627; BAE59627; AO090026000133.
DR   GeneID; 5993657; -.
DR   KEGG; aor:AO090026000133; -.
DR   VEuPathDB; FungiDB:AO090026000133; -.
DR   HOGENOM; CLU_000288_103_1_1; -.
DR   OMA; KMCEQHI; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000006564; Chromosome 3.
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   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..705
FT                   /note="Probable E3 ubiquitin ligase complex SCF subunit
FT                   sconB"
FT                   /id="PRO_0000397250"
FT   DOMAIN          202..248
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          376..413
FT                   /note="WD 1"
FT   REPEAT          416..455
FT                   /note="WD 2"
FT   REPEAT          457..493
FT                   /note="WD 3"
FT   REPEAT          495..536
FT                   /note="WD 4"
FT   REPEAT          588..631
FT                   /note="WD 5"
FT   REPEAT          634..671
FT                   /note="WD 6"
FT   REPEAT          674..705
FT                   /note="WD 7"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        3
FT                   /note="S -> F (in Ref. 1; BAD83608)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="S -> F (in Ref. 1; BAD83608)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   705 AA;  79353 MW;  2CDF2379330B5BB6 CRC64;
     MQSDDRSVRE GSDSSQTFLM KMAQPTGELT HPSQQQQLQL QQQSFQSIFG GASDTTEEID
     TETDSNHRRP HSFGAAATTP AKLANKNVAP FLVKHIPEQY GPLGSRRTDK LEDLSSPNSK
     FCYRHRPDLK CRRQADEPSM DKLQRELETL PPSDQQGIAH VWSLFSAAPA KHRKLILQGI
     MAQCCFPQLS FVSATVRDLI RIDFLTALPP EISFKILCYL DTTSLCKAAQ VSSRWRALAD
     DDVVWHRMCE QHIHRKCKKC GWGLPLLERK RLRESKREIE LRATTWDVSG PAQNAGGAEC
     SAPHADDVIT QKRKADSSDD ETAIVKRHCS SLDARPEPDE DYYTTRYRPW KEVYKDRFKV
     GTNWKYGRCS TKVFKGHTNG VMCLQFEDNI LATGSYDATI KIWDTETGEE LRTLRGHQSG
     IRCLQFDDTK LISGSMDRSL KVWNWRTGEC ISTYTGHRGG VIGLHFDATI LASASVDKTV
     KIWNFEDKST FLLRGHTDWV NAVRVDTTSR TVFSASDDCT VRLWDLDTKA CLRTFHGHVG
     QVQQVVPLPR EFEFEDHDAE CDNDNMSTTS GDTESNSLQA TLGLESNATE TSVFGPSFDN
     GRPAPPRYIV TSALDSTIRL WETTTGRCLR TFFGHLEGVW ALGADTLRIV SGAEDRMVKI
     WDPRTGKCER TFTGHSGPVT CIGLGDSRFA TGSEDCEVRM YSFRN