ID A0A179UX35_BLAGS Unreviewed; 893 AA.
AC A0A179UX35;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Probable E3 ubiquitin ligase complex SCF subunit sconB {ECO:0000256|ARBA:ARBA00015819};
DE AltName: Full=Sulfur controller B {ECO:0000256|ARBA:ARBA00032113};
DE AltName: Full=Sulfur metabolite repression control protein B {ECO:0000256|ARBA:ARBA00030034};
GN ORFNames=BDBG_07212 {ECO:0000313|EMBL:OAT11789.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT11789.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(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:0000256|ARBA:ARBA00002730}.
CC -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
CC -!- SUBUNIT: Component of the SCF(sconB) E3 ubiquitin ligase complex.
CC {ECO:0000256|ARBA:ARBA00011725}.
CC -!- SIMILARITY: Belongs to the WD repeat MET30/SCONB/SCON-2 family.
CC {ECO:0000256|ARBA:ARBA00007968}.
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DR EMBL; GG657465; OAT11789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A179UX35; -.
DR STRING; 559298.A0A179UX35; -.
DR VEuPathDB; FungiDB:BDBG_07212; -.
DR OrthoDB; 337075at2759; -.
DR Proteomes; UP000002038; Unassembled WGS sequence.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR22847:SF723; E3 UBIQUITIN LIGASE COMPLEX SCF SUBUNIT SCONB-RELATED; 1.
DR PANTHER; PTHR22847; WD40 REPEAT PROTEIN; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 211..257
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 465..504
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 506..549
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 551..581
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 639..678
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 679..718
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 12..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 99600 MW; 01D516165844610A CRC64;
MFGHARRISY LSQLHSRPRR RPRRPPRRPP RPSPGVNTKK TLRRMFPVYT SFERRIIPLL
FFPTDLVVSS SIPYTHQCPT PFSPSWSYSS PNLCYRQGDS LMERDSAAAA TAAAAGGAAH
IPKLPGGKYR GEFAPPSALG SVKLDEGYSD ETRSQAENEV AQTSDEGVSL PSWILAHSEA
DRAELAYSIL RTLRTSTVSS VVDRLTPLLH MDPVLKLPPE ITSEIFSYLD TSTLLTAALA
SRAWRERIID SRLWRHLYIQ EGWRFDMDAV RTFEQSLSKP PFSHNRKSRT RRSDTDMGQP
KLKKRVPSGW IDSRRGSRVG NNNMQDASPP WSEQHETVEA DGTSAFEMNT LPDAEGDHEM
RDASYDDHSI GSSPDQSRPP QSIDFSSVQF THKSGRADSS ARYPSFHSPL TNYNPQAKAP
HLLRTINGTS RLNWPYLYRQ RQKLEDNWRK GRFVNFQLPH PAYPSEAHTE CVYTIQFSGK
WLVSGSRDKT VRVWNLETRR LRGSPLVAHS KSVLCLQFDP SAEEDIIISG SSDRSVIVWR
FSTGEKINEL ANAHQDSVLN LRFDKRFLVT CSKDKLIKVW NRRELSPMDK DYPSFFNGAG
VRYPTYIVDT SLISPSTLEA QIANQQIKTL PPYSLLMTLD GHGAAVNAIQ IDENEIVSAS
GDRLIKVWDI HNGACLKTLI GHKKGIACVQ FDSRRIVSGS NDDTVRIYDH ASGAEVACLH
GHHGLVRTVQ AGFGDPPGAE ETLRLEAMAV DTQYWKARLR GDIPESSSSV RRQQRSCPVR
SSGSRNPNDI MALGAKIPPG GGGSSWARIV SGSYDESIIM WKKDQEGKWV IGQRLRQDEA
ARAAAANVIP DPALANQPIP PLPGQSPQGL MGPHPMSQSS QQTTPRLSGN SVQ
//
