SCONB_ASPCL
ID SCONB_ASPCL Reviewed; 700 AA.
AC A1C7E4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=ACLA_073500;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027045; EAW14315.1; -; Genomic_DNA.
DR RefSeq; XP_001275741.1; XM_001275740.1.
DR AlphaFoldDB; A1C7E4; -.
DR SMR; A1C7E4; -.
DR STRING; 5057.CADACLAP00007022; -.
DR EnsemblFungi; EAW14315; EAW14315; ACLA_073500.
DR GeneID; 4707886; -.
DR KEGG; act:ACLA_073500; -.
DR VEuPathDB; FungiDB:ACLA_073500; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_1_1; -.
DR OMA; KMCEQHI; -.
DR OrthoDB; 617388at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006701; 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; -; 2.
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..700
FT /note="Probable E3 ubiquitin ligase complex SCF subunit
FT sconB"
FT /id="PRO_0000397245"
FT DOMAIN 195..241
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 369..406
FT /note="WD 1"
FT REPEAT 409..448
FT /note="WD 2"
FT REPEAT 450..486
FT /note="WD 3"
FT REPEAT 488..529
FT /note="WD 4"
FT REPEAT 583..626
FT /note="WD 5"
FT REPEAT 627..666
FT /note="WD 6"
FT REPEAT 669..700
FT /note="WD 7"
FT REGION 282..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 78780 MW; 13AF6C49E352561B CRC64;
MDTQRLSLRK ENGSAHSLLQ DQTGLKENTM NIPRDSSFNS IFGPSEVVDD AGTDRDFKHE
SHKFSITRAM PEKLAGKNIA PFLAKHIPEQ YAPLGSHAGE PVESSGANSR YCYRHRPDLK
CRRQADEPTM DKLQRIAKEL ETLPQRDQQG IAHAWSIFSA APAKHRKLLL QGIMAQCCFP
QLSFISASVR DLIRIDFLTA LPPEISFKIL CYLDTTSLCK AAQVSRRWRA LADDDVVWHR
MCEQHIHRKC KKCGWGLPLL DRKRLRESKR QIELRAATWD ISEQSTEDET GSPAPESASS
NAKRKPESDD EDTALVKRHC TSIVPRLEKE KDGDYFITRY RPWKEVYKDR FKVGTNWKYG
RCSVKVFKGH TNGIMCLQFE DNILATGSYD ATIKIWDTET GEELRTLRGH ESGIRCLQFD
DTKLISGSMD RSLKVWNWRT GECISTYTGH RGGVIGLHFD ATILASASVD KTVKIWNFED
KSTCLLRGHT DWVNAVRVDT NSRTVFSASD DCTIRLWDLD TKTCIRTFHG HVGQVQQVIP
LPREFEFEDH DAECENDNVS VTSGDSPAAS PRGIPGLDAG TSETQSSPFG PAFDNGRPAP
PRYIVTSALD STIRLWETST GRCLRTFFGH LEGVWALAAD TLRIVSGAED RMVKIWDPRT
GKCERTFTGH SGPVTCIGLG DSRFATGSED CEVRMYGFQS