ID SCONB_ARTOC Reviewed; 674 AA.
AC C5FP68;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=MCYG_04203;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995704; EEQ31384.1; -; Genomic_DNA.
DR RefSeq; XP_002846466.1; XM_002846420.1.
DR AlphaFoldDB; C5FP68; -.
DR SMR; C5FP68; -.
DR STRING; 554155.C5FP68; -.
DR GeneID; 9224536; -.
DR VEuPathDB; FungiDB:MCYG_04203; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_1_1; -.
DR OMA; GIAHVWS; -.
DR OrthoDB; 587035at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd22147; F-box_SpPof1-like; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19872; UBIQUITIN LIGASE SPECIFICITY FACTOR/HREP PROTEIN; 1.
DR PANTHER; PTHR19872:SF10; UBIQUITIN-BINDING SDF UBIQUITIN LIGASE COMPLEX SUBUNIT; 1.
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; SSF81383; F-box domain; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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..674
FT /note="Probable E3 ubiquitin ligase complex SCF subunit
FT sconB"
FT /id="PRO_0000397252"
FT DOMAIN 212..258
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 336..375
FT /note="WD 1"
FT REPEAT 377..415
FT /note="WD 2"
FT REPEAT 416..453
FT /note="WD 3"
FT REPEAT 455..496
FT /note="WD 4"
FT REPEAT 557..600
FT /note="WD 5"
FT REPEAT 603..640
FT /note="WD 6"
FT REPEAT 643..674
FT /note="WD 7"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 75511 MW; B7F5558F0BF03F66 CRC64;
MATDTPPQLA GPPTPAMETL DRDVVMSPRK RRRLSASAEP ELTEPESDGT SGGRGAAAEA
PETAALEPKS LFNSTSTESS ITSSSTTTTT TSSSSSIAPF LAKHIRDQHA SRNRFAPADS
SLPRRKADSK YCYRHRPDLK CRRQADEPTV DQMQRDLSTL SQNDQQSIAH FWSLFSAAPS
KHRNLMLQGI VAQCCFPQLS FLSASVRDLI RIDFVTALPP EISFKILSYL DTASLCNAAQ
VSRNWRHLAD DDVVWHRMCE QHIDRKCEKC GWGLPMLDRK RLKDTKRQVQ LRAAGKEAVT
GRQQQQHRPW KAVYMDRFKV GTNWKYGRCT TTIFRGHTNG VMCLQFDDNI LATGSYDATI
KIWDIETGKE IRTLRGHEST IRCLQFDDTK LISGSLDRTI KVWSWRSGEC ISTYTGHQGG
VLCLHFDSTT LASGSKDNTI KIWNFQDKST QILRGHTDWV NAVKLDTASR TVFSASDDLT
VRIWDLDTGK CIHTYAGHVG QVQQVLPLPR EFEFKHTSHC DDDRSDRLSG SESPDHRASH
DSNHAPDLPT TSAPPTQPMS PLFEALFNED RPAPPRYMLT AALDSTLRLW EVHTGRCLRT
FFGHIEGVWG LAADTLRLVS GAQDHMTKVW DPRTGTCERT FTGHRGPVTC VSLSDSRMAT
GSEDCEVRMY SFKA
//
