SCONB_NEUCR
ID SCONB_NEUCR Reviewed; 650 AA.
AC Q01277; Q7RVH3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Probable E3 ubiquitin ligase complex SCF subunit scon-2;
DE AltName: Full=Sulfur controller 2;
DE Short=SCON2;
DE AltName: Full=Sulfur metabolite repression control protein 2;
GN Name=scon-2; ORFNames=B13M15.090, NCU08563;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=7724564; DOI=10.1073/pnas.92.8.3343;
RA Kumar A., Paietta J.V.;
RT "The sulfur controller-2 negative regulatory gene of Neurospora crassa
RT encodes a protein with beta-transducin repeats.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3343-3347(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF LEU-122; ILE-127; LEU-130; GLU-133;
RP VAL-138; LEU-142; ASP-143; LEU-147; VAL-153; TRP-157 AND TRP-167.
RX PubMed=9482900; DOI=10.1073/pnas.95.5.2417;
RA Kumar A., Paietta J.V.;
RT "An additional role for the F-box motif: gene regulation within the
RT Neurospora crassa sulfur control network.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2417-2422(1998).
CC -!- FUNCTION: Component of the SCF(scon-2) 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:9482900}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the SCF(scon-2) E3 ubiquitin ligase complex.
CC {ECO:0000250}.
CC -!- INDUCTION: Expressed only under low-sulfur conditions and expression is
CC under the control of the cys-3 transcriptional activator.
CC {ECO:0000269|PubMed:7724564}.
CC -!- SIMILARITY: Belongs to the WD repeat MET30/SCONB/SCON-2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA33589.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; U17251; AAA68968.1; -; Genomic_DNA.
DR EMBL; BX897673; CAE85499.1; -; Genomic_DNA.
DR EMBL; CM002238; EAA33589.2; ALT_INIT; Genomic_DNA.
DR PIR; T46660; T46660.
DR RefSeq; XP_962825.2; XM_957732.2.
DR AlphaFoldDB; Q01277; -.
DR SMR; Q01277; -.
DR STRING; 5141.EFNCRP00000004632; -.
DR EnsemblFungi; EAA33589; EAA33589; NCU08563.
DR GeneID; 3878980; -.
DR KEGG; ncr:NCU08563; -.
DR HOGENOM; CLU_000288_103_1_1; -.
DR InParanoid; Q01277; -.
DR OMA; KMCEQHI; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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; -; 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; 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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..650
FT /note="Probable E3 ubiquitin ligase complex SCF subunit
FT scon-2"
FT /id="PRO_0000051209"
FT DOMAIN 124..170
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 292..320
FT /note="WD 1"
FT REPEAT 332..360
FT /note="WD 2"
FT REPEAT 372..400
FT /note="WD 3"
FT REPEAT 411..441
FT /note="WD 4"
FT REPEAT 453..488
FT /note="WD 5"
FT REPEAT 528..564
FT /note="WD 6"
FT REPEAT 576..604
FT /note="WD 7"
FT REPEAT 616..644
FT /note="WD 8"
FT REGION 200..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 122
FT /note="L->D: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 127
FT /note="I->D: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 130
FT /note="L->D: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 133
FT /note="E->A: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 138
FT /note="V->D: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 142
FT /note="L->D: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 143
FT /note="D->I: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 147
FT /note="L->E: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 153
FT /note="V->D: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 157
FT /note="W->G: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
FT MUTAGEN 167
FT /note="W->G: Leads to constitutive sulfur system
FT repression."
FT /evidence="ECO:0000269|PubMed:9482900"
SQ SEQUENCE 650 AA; 72189 MW; 7473859C99F1B028 CRC64;
MSSVLMSKTV TPFLREHIPS IYAPIGKPGN QETARAENPN SKYCYRHHPD SKCRRAADKA
KMVMIQSELD KLTSADQQAV THVWSLFSAA PARHRDLMLQ GILSQLCFPQ LSFVSREVNE
ALKIDFISAL PVELAQKVLC YLDTVSLTKA AQVSQRWRTL ADSDAVWVRM CEQHVNRKCT
KCGWGLPLLE RKKLRNYTRQ RQLAKGGPQG RVTELADSHD SQDRSVNQHG KRPAAEAEEE
DPIKKRQCMA AAEASKAVTQ PKTRSWKAVY RDRWQVSYNW KNSRYKLSVL KGHENGVTCL
QLDDNILATG SYDTTIKIWN IETEECIRTL VGHTAGIRAL QFDDSKLISG SLDHTIKVWN
WHTGECLSTF AAHTDSVISV HFDGHLLASG SSDKTVKIFD FNSKETYCLK GHSDWVNSTH
VDIKSRTVFS ASDDTTIKLW DLDTRQVIRT YEGHVGHVQQ VLILPPEYEP DEEVLNGASQ
DNQDAMSVSS GGSGSPSMSH AQIERAGSPG SHSSSHNLLP SSLPSGDEDV RHLYGSAFVA
DESRPLPPRY FMTGGLDSTM RLWDSATGRC LRTLFGHLEG VWSLAGDTIR VISGANDGMV
KTWEPRSGKC DATYTGHCGP VTCVGLSDSL MASGSEDGTI RLHSFKPCRQ
