ID   SKP1_ARTBC              Reviewed;         164 AA.
AC   D4ARL8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=E3 ubiquitin ligase complex SCF subunit sconC;
DE   AltName: Full=Sulfur controller C;
DE   AltName: Full=Sulfur metabolite repression control protein C;
GN   Name=sconC; Synonyms=skpA; ORFNames=ARB_06761;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3
CC       ubiquitin ligase complexes, which mediate the ubiquitination and
CC       subsequent proteasomal degradation of target proteins. Controls sulfur
CC       metabolite repression, probably by mediating the inactivation or
CC       degradation of the metR transcription factor (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC       ligase complexes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR   EMBL; ABSU01000006; EFE34361.1; -; Genomic_DNA.
DR   RefSeq; XP_003015001.1; XM_003014955.1.
DR   AlphaFoldDB; D4ARL8; -.
DR   SMR; D4ARL8; -.
DR   STRING; 663331.D4ARL8; -.
DR   EnsemblFungi; EFE34361; EFE34361; ARB_06761.
DR   GeneID; 9520724; -.
DR   KEGG; abe:ARB_06761; -.
DR   eggNOG; KOG1724; Eukaryota.
DR   HOGENOM; CLU_059252_4_0_1; -.
DR   OMA; PLKSADM; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IEA:EnsemblFungi.
DR   GO; GO:0043291; C:RAVE complex; IEA:EnsemblFungi.
DR   GO; GO:0017117; C:single-stranded DNA-dependent ATP-dependent DNA helicase complex; IEA:EnsemblFungi.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0101026; P:mitotic nuclear membrane biogenesis; IEA:EnsemblFungi.
DR   GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; IEA:EnsemblFungi.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0060542; P:regulation of strand invasion; IEA:EnsemblFungi.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IEA:EnsemblFungi.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR016897; SKP1.
DR   InterPro; IPR001232; SKP1-like.
DR   InterPro; IPR036296; SKP1-like_dim_sf.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR016072; Skp1_comp_dimer.
DR   InterPro; IPR016073; Skp1_comp_POZ.
DR   PANTHER; PTHR11165; PTHR11165; 1.
DR   Pfam; PF01466; Skp1; 1.
DR   Pfam; PF03931; Skp1_POZ; 1.
DR   PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
DR   SMART; SM00512; Skp1; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF81382; SSF81382; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..164
FT                   /note="E3 ubiquitin ligase complex SCF subunit sconC"
FT                   /id="PRO_0000397258"
FT   REGION          106..164
FT                   /note="Interaction with the F-box domain of F-box proteins"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   164 AA;  18680 MW;  BBC83BC303BAA7CF CRC64;
     MASTATNKIT LTSSDGVEVT IERQVAERSI LIKNMLEDLG DSGEPIPIPN VNESVLKKVI
     EWCEHHKGDP PSTGDDDVDS RRKTTDIDEW DQKFMQVDQE MLFEIILAAN YLDIKALLDV
     GCKTVANMIK GKSPEEIRKT FNIQNDFTPE EEDQIRRENE WAEE