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SKP1_TALMQ
ID   SKP1_TALMQ              Reviewed;         160 AA.
AC   B6QGB9;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=PMAA_085020;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; DS995901; EEA24504.1; -; Genomic_DNA.
DR   EMBL; DS995901; EEA24505.1; -; Genomic_DNA.
DR   RefSeq; XP_002148015.1; XM_002147979.1.
DR   RefSeq; XP_002148016.1; XM_002147980.1.
DR   AlphaFoldDB; B6QGB9; -.
DR   SMR; B6QGB9; -.
DR   STRING; 441960.B6QGB9; -.
DR   EnsemblFungi; EEA24504; EEA24504; PMAA_085020.
DR   EnsemblFungi; EEA24505; EEA24505; PMAA_085020.
DR   GeneID; 7025630; -.
DR   KEGG; tmf:PMAA_085020; -.
DR   VEuPathDB; FungiDB:PMAA_085020; -.
DR   HOGENOM; CLU_059252_4_0_1; -.
DR   OrthoDB; 1412723at2759; -.
DR   PhylomeDB; B6QGB9; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001294; 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..160
FT                   /note="E3 ubiquitin ligase complex SCF subunit sconC"
FT                   /id="PRO_0000397270"
FT   REGION          101..160
FT                   /note="Interaction with the F-box domain of F-box proteins"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   160 AA;  18509 MW;  E075830ADD7BFCAA CRC64;
     MSGQVTLQSS DSVDITVERA VAERSMLIKN LLEDLGESEE PVPIPNVNES VLKKVIEWCT
     HHKNDPQSTG EDDDNRRRTT EIDEWDQKFM QVDQEMLFEI ILAANYLDIK ALLDVGCKTV
     ANMIKGKSPE EIRKTFNIQN DFTPEEEDQI RRENEWAEDR
 
 
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