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Probable E3 ubiquitin ligase complex SCF subunit scon-2 (Sulfur controller 2) (SCON2) (Sulfur metabolite repression control protein 2)

 SCONB_NEUCR             Reviewed;         650 AA.
Q01277; Q7RVH3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 135.
RecName: Full=Probable E3 ubiquitin ligase complex SCF subunit scon-2;
AltName: Full=Sulfur controller 2;
Short=SCON2;
AltName: Full=Sulfur metabolite repression control protein 2;
Name=scon-2; ORFNames=B13M15.090, NCU08563;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=7724564; DOI=10.1073/pnas.92.8.3343;
Kumar A., Paietta J.V.;
"The sulfur controller-2 negative regulatory gene of Neurospora crassa
encodes a protein with beta-transducin repeats.";
Proc. Natl. Acad. Sci. U.S.A. 92:3343-3347(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12655011; DOI=10.1093/nar/gkg293;
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the
Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[4]
FUNCTION, DOMAIN, AND MUTAGENESIS OF LEU-122; ILE-127; LEU-130;
GLU-133; VAL-138; LEU-142; ASP-143; LEU-147; VAL-153; TRP-157 AND
TRP-167.
PubMed=9482900; DOI=10.1073/pnas.95.5.2417;
Kumar A., Paietta J.V.;
"An additional role for the F-box motif: gene regulation within the
Neurospora crassa sulfur control network.";
Proc. Natl. Acad. Sci. U.S.A. 95:2417-2422(1998).
-!- FUNCTION: Component of the SCF(scon-2) E3 ubiquitin ligase complex
involved in the regulation of sulfur metabolite repression,
probably by mediating the inactivation or degradation of the metR
transcription factor. {ECO:0000269|PubMed:9482900}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Component of the SCF(scon-2) E3 ubiquitin ligase complex.
{ECO:0000250}.
-!- INDUCTION: Expressed only under low-sulfur conditions and
expression is under the control of the cys-3 transcriptional
activator. {ECO:0000269|PubMed:7724564}.
-!- SIMILARITY: Belongs to the WD repeat MET30/SCONB/SCON-2 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAA33589.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U17251; AAA68968.1; -; Genomic_DNA.
EMBL; BX897673; CAE85499.1; -; Genomic_DNA.
EMBL; CM002238; EAA33589.2; ALT_INIT; Genomic_DNA.
PIR; T46660; T46660.
RefSeq; XP_962825.2; XM_957732.2.
ProteinModelPortal; Q01277; -.
SMR; Q01277; -.
PRIDE; Q01277; -.
EnsemblFungi; EAA33589; EAA33589; NCU08563.
GeneID; 3878980; -.
KEGG; ncr:NCU08563; -.
EuPathDB; FungiDB:NCU08563; -.
HOGENOM; HOG000166480; -.
InParanoid; Q01277; -.
KO; K10259; -.
OMA; TQCCFPQ; -.
OrthoDB; EOG092C10HM; -.
UniPathway; UPA00143; -.
Proteomes; UP000001805; Chromosome 3, Linkage Group III.
GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IEA:EnsemblFungi.
GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
GO; GO:0030674; F:protein binding, bridging; IEA:EnsemblFungi.
GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
GO; GO:0006270; P:DNA replication initiation; IEA:EnsemblFungi.
GO; GO:0000209; P:protein polyubiquitination; IEA:EnsemblFungi.
GO; GO:0030174; P:regulation of DNA-dependent DNA replication initiation; IEA:EnsemblFungi.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:EnsemblFungi.
GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblFungi.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 3.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
Pfam; PF12937; F-box-like; 1.
Pfam; PF00400; WD40; 6.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50998; SSF50998; 2.
SUPFAM; SSF81383; SSF81383; 2.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS00678; WD_REPEATS_1; 2.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Complete proteome; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation pathway; WD repeat.
CHAIN 1 650 Probable E3 ubiquitin ligase complex SCF
subunit scon-2.
/FTId=PRO_0000051209.
DOMAIN 124 170 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 292 320 WD 1.
REPEAT 332 360 WD 2.
REPEAT 372 400 WD 3.
REPEAT 411 441 WD 4.
REPEAT 453 488 WD 5.
REPEAT 528 564 WD 6.
REPEAT 576 604 WD 7.
REPEAT 616 644 WD 8.
MUTAGEN 122 122 L->D: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 127 127 I->D: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 130 130 L->D: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 133 133 E->A: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 138 138 V->D: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 142 142 L->D: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 143 143 D->I: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 147 147 L->E: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 153 153 V->D: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 157 157 W->G: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
MUTAGEN 167 167 W->G: Leads to constitutive sulfur system
repression. {ECO:0000269|PubMed:9482900}.
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


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