SCONB_TALMQ
ID SCONB_TALMQ Reviewed; 660 AA.
AC B6Q4Z5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Probable E3 ubiquitin ligase complex SCF subunit sconB;
DE AltName: Full=Sulfur controller B;
DE AltName: Full=Sulfur metabolite repression control protein B;
GN Name=sconB; ORFNames=PMAA_022220;
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: Component of the SCF(sconB) 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:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the SCF(sconB) E3 ubiquitin ligase complex.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat MET30/SCONB/SCON-2 family.
CC {ECO:0000305}.
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DR EMBL; DS995899; EEA27338.1; -; Genomic_DNA.
DR RefSeq; XP_002143853.1; XM_002143817.1.
DR AlphaFoldDB; B6Q4Z5; -.
DR SMR; B6Q4Z5; -.
DR STRING; 441960.B6Q4Z5; -.
DR PRIDE; B6Q4Z5; -.
DR EnsemblFungi; EEA27338; EEA27338; PMAA_022220.
DR GeneID; 7021680; -.
DR KEGG; tmf:PMAA_022220; -.
DR VEuPathDB; FungiDB:PMAA_022220; -.
DR HOGENOM; CLU_000288_103_1_1; -.
DR OrthoDB; 617388at2759; -.
DR PhylomeDB; B6Q4Z5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..660
FT /note="Probable E3 ubiquitin ligase complex SCF subunit
FT sconB"
FT /id="PRO_0000397255"
FT DOMAIN 175..221
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 340..379
FT /note="WD 1"
FT REPEAT 381..419
FT /note="WD 2"
FT REPEAT 421..457
FT /note="WD 3"
FT REPEAT 459..500
FT /note="WD 4"
FT REPEAT 542..586
FT /note="WD 5"
FT REPEAT 587..626
FT /note="WD 6"
FT REPEAT 629..660
FT /note="WD 7"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 74016 MW; 94D0EEEC15AAC584 CRC64;
MHNENSVLRD AKESLFNPTP RKQGLPEDNT MTPYNGVRSI FDNSSDSHQL TDDHTHQERA
ISKAKLANEN IAPFLAKHIP SQYAPLGTGI SKSAGPPPRP DLKCRRQADE PSMDHLQWEL
QSLPQSDQQG IAHVWSLFSA APAKQRELML RGILAQCCFP QLSLISSSVR DLIRIDFITA
LPPEISFKIL SYLDTASLCR AAQVSRGWKC LADDDVVWHR MCEQHIHRKC TKCGWGLPLL
ERKRLRASKE QIEKRALGVS VIPEASVTVQ SVDATSGVKR TAEDLEASDS QTVKRQRLPI
EEDTNIYKTN FRPWKDVYKD RFKVGTNWKY GRCSVKVFKG HTNGVMCLQF EDNILATGSY
DTTIKIWDME TGEELRTLTG HTSGIRCLQF DETKLISGSI DRTLKVWNWR TGECISTYTG
HLGGIIGLHF QNSILASGST DKTVKIWNFE DKSTFLLRGH SDWVNAVRVD SCSRTVLSAS
DDCTVKLWDL DSKQCIRTFQ GHVGQVQQVI PLPREFEFEE GHDASHEEDS NASVSGDESP
SSQVSCSPTA AFFEGDRPAP PRYILTSALD STIRLWETYT GRCLRTFFGH LEGVWALSAD
TLRIVSGAED RMVKIWDPRT GKCERTFTGH SGPVTCVGLG DSCFVTGSED CEVRIYSFKN