SCONB_NEOFI
ID SCONB_NEOFI Reviewed; 689 AA.
AC A1DHW6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=NFIA_089300;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027696; EAW18973.1; -; Genomic_DNA.
DR RefSeq; XP_001260870.1; XM_001260869.1.
DR AlphaFoldDB; A1DHW6; -.
DR SMR; A1DHW6; -.
DR STRING; 36630.CADNFIAP00006688; -.
DR EnsemblFungi; EAW18973; EAW18973; NFIA_089300.
DR GeneID; 4587428; -.
DR KEGG; nfi:NFIA_089300; -.
DR VEuPathDB; FungiDB:NFIA_089300; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_1_1; -.
DR OMA; KMCEQHI; -.
DR OrthoDB; 617388at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006702; 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; 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..689
FT /note="Probable E3 ubiquitin ligase complex SCF subunit
FT sconB"
FT /id="PRO_0000397253"
FT DOMAIN 186..232
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 358..395
FT /note="WD 1"
FT REPEAT 398..437
FT /note="WD 2"
FT REPEAT 439..475
FT /note="WD 3"
FT REPEAT 477..518
FT /note="WD 4"
FT REPEAT 572..615
FT /note="WD 5"
FT REPEAT 616..655
FT /note="WD 6"
FT REPEAT 658..689
FT /note="WD 7"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 77242 MW; B87ACA25A35F4994 CRC64;
MDAHELSFRD GHGSSTSTMK DECASEEKAL YLPGDSSFAS VFGPSETVED VETGPESTQD
KPHSFNTQKP IREKLAGKNV APFLARHIPE QYAPLGSQTG QPVEISSANS KYCYRHRPDL
KCRRQADEPT MDKLQRSDQQ GIAHAWSIFS AAPAKHRKLI LQGIMAQCCF PQLSFISATV
RDLIRIDFLT ALPPEISFKI LCYLDTTSLC KAAQVSRRWR ALADDDVVWH RMCEQHIHRK
CKKCGWGLPL LDRKRLRESK REIERRAATW DVSEQPAETE SNSATIDTAA SGSKRKPESD
KEDTAMVKRQ CTSIVSQSEQ NEDYFKTRYR PWKEVYKDRF KVGTNWKYGR CSIRVFKGHS
NGIMCLQFED NILATGSYDA TIKIWDTETG EELRTLKGHR SGIRCLQFDD TKLISGSMDH
TLKVWNWRTG ECISTYSGHR GGVVGLHFDA TILASGSVDK TVKIWNFEDK STCLLRGHTD
WVNAVRVDSA SRTVFSASDD CTVKLWDLDT KSCIRTFHGH VGQVQQVVPL PREFEFEDHD
VECENDNVSV TSGDSPAASP QAIPGFDAQT SDTPSSAFGP AFDDGRPSPP RYIVTSALDS
TIRLWETSSG RCLRTFFGHL EGVWALAADT LRIVSGAEDR MVKIWDPRTG KCERTFTGHS
GPVTCIGLGD SRFATGSEDC EVRMYSFQT
