ID   SKP1_NEOFI              Reviewed;         158 AA.
AC   A1CZG3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=NFIA_037050;
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: 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; DS027686; EAW24133.1; -; Genomic_DNA.
DR   RefSeq; XP_001266030.1; XM_001266029.1.
DR   AlphaFoldDB; A1CZG3; -.
DR   SMR; A1CZG3; -.
DR   STRING; 36630.CADNFIAP00003614; -.
DR   EnsemblFungi; EAW24133; EAW24133; NFIA_037050.
DR   GeneID; 4592491; -.
DR   KEGG; nfi:NFIA_037050; -.
DR   VEuPathDB; FungiDB:NFIA_037050; -.
DR   eggNOG; KOG1724; Eukaryota.
DR   HOGENOM; CLU_059252_4_0_1; -.
DR   OMA; PLKSADM; -.
DR   OrthoDB; 1412723at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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..158
FT                   /note="E3 ubiquitin ligase complex SCF subunit sconC"
FT                   /id="PRO_0000397268"
FT   REGION          100..158
FT                   /note="Interaction with the F-box domain of F-box proteins"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   158 AA;  18141 MW;  296A2931F94EE074 CRC64;
     MTTVTLTSSD GVDITVDRDV AERSILIKNM LEDLGESDEA IPIPNVNEVV LKKVIEWCTH
     HKNDPPSTGD DDDSRRKTTD IDEWDQKFMQ VDQEMLFEII LAANYLDIKA LLDVGCKTVA
     NMIKGKSPEE IRKTFNIQND FTPEEEDQIR RENEWAEE