SCONB_EMENI
ID SCONB_EMENI Reviewed; 678 AA.
AC Q00659; C8V0Y0; Q5AZC1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 125.
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; Synonyms=mapB1; ORFNames=AN6359;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9520259; DOI=10.1007/s004380050646;
RA Natorff R., Piotrowska M., Paszewski A.;
RT "The Aspergillus nidulans sulphur regulatory gene sconB encodes a protein
RT with WD40 repeats and an F-box.";
RL Mol. Gen. Genet. 257:255-263(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION.
RX PubMed=8479426; DOI=10.1007/bf00279546;
RA Natorff R., Balinska M., Paszewski A.;
RT "At least four regulatory genes control sulphur metabolite repression in
RT Aspergillus nidulans.";
RL Mol. Gen. Genet. 238:185-192(1993).
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:0000269|PubMed:8479426}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U21220; AAC15905.1; -; Genomic_DNA.
DR EMBL; AACD01000107; EAA58743.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF69629.1; -; Genomic_DNA.
DR RefSeq; XP_663963.1; XM_658871.1.
DR AlphaFoldDB; Q00659; -.
DR SMR; Q00659; -.
DR STRING; 162425.CADANIAP00006625; -.
DR PRIDE; Q00659; -.
DR EnsemblFungi; CBF69629; CBF69629; ANIA_06359.
DR EnsemblFungi; EAA58743; EAA58743; AN6359.2.
DR GeneID; 2871261; -.
DR KEGG; ani:AN6359.2; -.
DR VEuPathDB; FungiDB:AN6359; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_1_1; -.
DR InParanoid; Q00659; -.
DR OMA; KMCEQHI; -.
DR OrthoDB; 617388at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IEA:EnsemblFungi.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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..678
FT /note="Probable E3 ubiquitin ligase complex SCF subunit
FT sconB"
FT /id="PRO_0000051210"
FT DOMAIN 178..224
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 347..375
FT /note="WD 1"
FT REPEAT 387..415
FT /note="WD 2"
FT REPEAT 427..455
FT /note="WD 3"
FT REPEAT 466..496
FT /note="WD 4"
FT REPEAT 508..543
FT /note="WD 5"
FT REPEAT 553..595
FT /note="WD 6"
FT REPEAT 607..635
FT /note="WD 7"
FT REPEAT 647..675
FT /note="WD 8"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 545
FT /note="D -> N (in Ref. 1; AAC15905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 678 AA; 76071 MW; 5A40D45A417D0E5D CRC64;
MSTEDNHDSQ ILTARHRSDA SEQSFKSLFG GPSSEDGKET EPDTHDHNHS FSNAKAPAKF
ANQNVAPFLA RHIPEQYAPL GAQSILPADL SSANSKYCYR HRPDQKCRRQ ADEPSMDKLQ
RELESLPQGD QQSISHVWSL FSAAPAKHRK LILQGIMAQC CFPQLSYISA TVRDLIRIDF
ITALPPEIAF KILCYLDTTS LCKASQVSRG WRALADDDVV WHRMCEQHIH RKCKKCGWGL
PLLDRKRLRE SKREIELRAT TWDKGVVGPR SPDASAESPP SGKRKLEDDE VAVVKRHCSS
LGSDAGVDKD SDFFKTRYRP WKEVYKDRFK VGTNWKYGRC SIKTFKGHTN GVMCLQFEDN
ILATGSYDTT IKIWDTETGE ELRTLRGHES GIRCLQFDDT KLISGSMDRT IKVWNWRTGE
CISTYTGHRG GVIGLHFDAS ILASGSVDKT VKIWNFEDKS TFSLRGHTDW VNAVRVDTSS
RTVFSASDDC TVRLWDLDTK TCIRTFHGHV GQVQQVVPLP REFEFEEHDA ECENDDLSTT
SGDADPPSIQ ASMGLEPNAA YSQSSAFGTS FDNGRAAPPR YMVTSALDST IRLWETTTGR
CLRTFFGHLE GVWALGADTL RIVSGAEDRM IKIWDPRTGK CERTFTGHSG PVTCIGLGDS
RFATGSEDCE VRMYSFQS
