SCONB_ASPTN
ID SCONB_ASPTN Reviewed; 673 AA.
AC Q0CY32;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=ATEG_01402;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476595; EAU38159.1; -; Genomic_DNA.
DR RefSeq; XP_001208767.1; XM_001208767.1.
DR AlphaFoldDB; Q0CY32; -.
DR SMR; Q0CY32; -.
DR STRING; 341663.Q0CY32; -.
DR EnsemblFungi; EAU38159; EAU38159; ATEG_01402.
DR GeneID; 4316261; -.
DR VEuPathDB; FungiDB:ATEG_01402; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_1_1; -.
DR OMA; KMCEQHI; -.
DR OrthoDB; 617388at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007963; 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..673
FT /note="Probable E3 ubiquitin ligase complex SCF subunit
FT sconB"
FT /id="PRO_0000397251"
FT DOMAIN 164..210
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 342..379
FT /note="WD 1"
FT REPEAT 382..421
FT /note="WD 2"
FT REPEAT 423..459
FT /note="WD 3"
FT REPEAT 461..502
FT /note="WD 4"
FT REPEAT 556..599
FT /note="WD 5"
FT REPEAT 602..639
FT /note="WD 6"
FT REPEAT 642..673
FT /note="WD 7"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 75579 MW; 8CBFD7361144488A CRC64;
MDSTQVSFKS IFGGTPEPTD EVDAEPDPTQ HGPHSFNNVT TTSAKLADEN VAPFLAKHIP
EQYAPLGSRT GKPEDLSSAN SKYCYRHRPD LKCRRQADEP SMDKLQRDLE TLPQSDQQGI
AHIWSLFSAA PAKHRKLILQ GLMAQCCFPQ LSFVSATVRD LIRIDFLTAL PPEISFKILC
YLDTTSLCKA AQVSRRWRAL ADDDVVWHRM CEQHIHRKCK KCGWGLPLLE RKRLRESKRE
IELRATTWDI SGPSPTVTST GEQQREQSAA PESSSSGKRK QDTSDEETAV VKRQCSSLAP
DSENDDAFFK KRYRPWKEVY KDRFKVGTNW KYGRCSTKIF KGHTNGVMCL QFEDNILATG
SYDATIKIWD TETGEELRTL YGHESGIRCL QFDDTKLISG SMDRSLKVWN WRTGECISTY
TGHRGGVIGL HFDATILASA SVDKTVKIWN FEDKSTCLLR GHTDWVNAVR VDTTSRTVFS
ASDDCTVRLW DLDTKQCIRT FHGHVGQVQQ VIPLPREFEF EEHDAECEND NVSTVSDDPG
SPAPQTTFGV SSIEPASQSS MFGPSFDNGR PAPPRYIVTS ALDSTIRLWE TTTGRCLRTF
FGHLEGVWAL GADTLRIVSG AEDRMVKIWD PRTGKCERTF TGHSGPVTCI GLGDSRFATG
SEDCEVRMYS FQS
