ID A0A395GQH7_9EURO Unreviewed; 656 AA.
AC A0A395GQH7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=BO80DRAFT_364448 {ECO:0000313|EMBL:RAK97198.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK97198.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK97198.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK97198.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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; KZ824465; RAK97198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GQH7; -.
DR STRING; 1448316.A0A395GQH7; -.
DR VEuPathDB; FungiDB:BO80DRAFT_364448; -.
DR OrthoDB; 587035at2759; -.
DR Proteomes; UP000249402; 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; PTHR19849; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR19849:SF3; PROTEIN WITH WD-40 REPEAT DOMAIN; 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; 8.
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; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 128..175
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 322..361
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 362..402
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 403..442
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 443..482
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 483..522
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 523..562
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 72107 MW; 48C898CA109C6916 CRC64;
MSPRSVPEQL ATAPSRSSAA RDSVASLSSA HARSLSSSTK AGTPIPPSLL PSAPASPPTP
APSPTPHQRP PTWQTAEEED DAFLLNARIH FSSLSNARKL RFLEGILGLC DSQHLSFVSS
YVSPRLRKDP FQVFPNELCL RVLSFIDDPK TLARASQVSR RWRELLNDDI TWKNLCEKHS
YASRRMSEDE RDFVDPFHGQ PLHAVSSTQS LSGLQRRPNV SSLQSGDGLA EVSRSLSGDW
LSMSGYPTRK RRVRPLSYRS HFKQKYMVES AWNKGGRFNQ RHITPDQGVV TSLHLTPKYI
VVALDNAKIH VYDTNGDNQR TLQGHVMGVW AMVPWDDILV SGGCDREVRV WNMATGAGIY
LLRGHTSTVR CLKMSDKNTA ISGSRDTTLR IWDLATGTCK NVLVGHQASV RCLAIHGDIV
VSGSYDTTAR IWSISEGRCL RTLSGHFSQI YAIAFDGKRI ATGSLDTSVR IWDPHSGQCH
AILQGHTSLV GQLQMRGDTL VTGGSDGSVR VWSLTKMAPI HRLAAHDNSV TSLQFDSSRI
VSGGSDGRVK VWSLQTGQLL RELSTPAEAV WRVAFEDEKA VIMASRSGRT VMEVWNFSPP
PEEDGDDTVI VESAASTPGL HPTTNDSRLR ERFSDPPPSL PLSTDDDHAM PDAPLS
//
