ID A0A0D1ZV47_EXOME Unreviewed; 937 AA.
AC A0A0D1ZV47;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=PV10_01558 {ECO:0000313|EMBL:KIV97854.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV97854.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV97854.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV97854.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847520; KIV97853.1; -; Genomic_DNA.
DR EMBL; KN847520; KIV97854.1; -; Genomic_DNA.
DR RefSeq; XP_016229427.1; XM_016365778.1.
DR RefSeq; XP_016229428.1; XM_016365779.1.
DR STRING; 212818.A0A0D1ZV47; -.
DR GeneID; 27319403; -.
DR VEuPathDB; FungiDB:PV10_01558; -.
DR HOGENOM; CLU_000288_103_0_1; -.
DR OMA; HSKGIAC; -.
DR OrthoDB; 337075at2759; -.
DR Proteomes; UP000054302; 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; 7.
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:UP000054302};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 83..129
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 315..354
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 356..399
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 401..431
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 489..528
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 529..568
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 153..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 103045 MW; 3FD04CB7E6C1AED1 CRC64;
MDSYRGRSIS SSSASFRLDE GFSEETASQN ESSRITPSTD RFQAWVLSQN EESRAEIAYE
VLRTLRTSSI AAVVERLTPL LHMDPLEKLP PEITCQIFSY LDASTLMTAS LASRTWRARV
MDTMLWQDLY KSQGWGIDTT EVKAFENTHL SITRHGTRRR LPRPGQPQLK KRATSDWLQS
RGRQGSADVS QWREQHGTIE ADSDMPSDPD DQEMQDAPNS LANSPQRPNK RHSNDSGDEM
DYVSSSPALP HPPNNRKKVP PETEPPFKSR LITYDSNGGE KLNWLNLYKQ RQRLEQNWTN
GQYTTFQLPH PSYPREAHTE CVYTIQFFGK WLVSGSRDRS LRVWDLETRR LRGKPLLGHS
QSVLCLQFDP TEQEDVIISG SSDSSVIVWR FSTGERIHKI PSAHEESVLN LRFDHRYLVT
CSKDRKIKIW NRKHLTAADP DYPQHSRQSS ARLPSYIVNL DEVEPSLLEA RIANGSIRAL
QPYTLLMTLE GHGAAVNAIQ INGDLIVSAS GDRLIRVWNV KDGRLLRSLQ GHHKGIACVQ
FDSKRIVSGS SDNTVRIYDP FTSAEVAELK GHTNLVRTVQ AGFGDMPGAD DASTAREVEK
KFLQAVANGT VPDDRQYFRR VRNGEFGSSR MALNSKLPPG GGGSKWGRIV SGSYDETIII
WRKNAQGDWV ESQRLRQVAH TPDGARPRPS QPPNVAATLP PLPNTLAAPM PPQAPHLTQG
QSSSSNVGSS SNANHQAVLA ATQVMQQAVG SGMAGLGSGL LNAFGAASTA GLGTWRTSST
NARVSVTSSV GPIQGQSPST VLPDAAASIS QTVQHALTQA PAQEPSVNQP QRSNISNSSG
PTPGPQPQPQ GSSATSQPGA QVTNNHHHQH HNNNTGGQAP VPNQHHPVAP ASVSRVFKLQ
FDARRIVCCS QDSRIVGWDF ANGDPDIAEA AKFFVGP
//
