ID A0A0J7AWD2_COCIT Unreviewed; 1041 AA.
AC A0A0J7AWD2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=CIRG_01816 {ECO:0000313|EMBL:KMP01677.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP01677.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; DS028093; KMP01677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7AWD2; -.
DR STRING; 404692.A0A0J7AWD2; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; 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; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE 3: Inferred from homology;
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 443..490
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 692..731
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 762..781
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 806..845
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 846..887
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 888..927
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 928..966
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1041 AA; 115207 MW; E250AF9D28268DC1 CRC64;
MTPSDASHRS LKTPELSEYQ SCSSRYERTD CNEISEDDSR PKPTIGQFSF APTTQTTIVT
TTTTTMTKFP PLIMHPPRVL QSLDPKQYPL AAAPTPESLR DIRFNLNGKS IVLHEPDDAP
GALAEQGQEE LKTSAGNTRS ATATTNPSAP ISSSRGRILG SRHRPFRNTK RAVSPVPFAG
SSQASNPSPS RSLVSDSLIC RHPRRRHLSS AQDPCHVTEV GLATPETESA SFALDSEIYN
PERTSQPRPP VKRQNENPPA AGESRRRSVD DGEASPLVEK PSEFPSESFG SSISSEADNP
PTQDRRLRPL VSRLLATDQS RGENIPLPSP RLSPVTAMNS LQQETSFDSA EDPATDTDSV
ADQFPKESNL AGNRRAGPKN AVGKADTDQT SPSMSLMDMP VVLGYFDSIP DELKSYFMYQ
LLRRCPKPTL QLVADVVNPA LKCDFLALLP LELCLNIVKF LDVVSMCRAS QVSKKWRHII
NSDEKTWKAH FDAAGFTLPE GELQRAIEEG WGWQYADDYE RDLRLLSRPT SEQSADSPES
ILQLKDSSSL ACPRRPKRKA ESSSPSRRQV KKQSPKDNTS RSPGISDWLH DSKVAEVPYA
AASAAALAVP YPNVGLPSLQ SLHLYKSLYQ RHHLIRKRWM DPNAKPQHLA FQAHDRHVVT
CLQFDTDKIL TGSDDTNIHV YDTKTGALRA TLEGHEGGVW ALEYHGNTLV SGSTDRSVRV
WDIEKAECTQ TFHGHTSTVR CLQILLPSQI GRRSDGSPEM MPKEPLIITG SRDSSLRVWR
LPQPGDPKYF QAGPDDSSCP YFVRALNGHT HSVRAIAAHG DTLVSGSYDC TVRVWKISTG
EAVHRLEGHT LKVYSVVLDH KRNRCISGSM DHSVKIWSLE TGTLLYNLEG HSLLVGLLDL
RADKLVSAAA DSTLRIWDPE TGQCKSTLTA HTGAITCFEH DDQKIISGSD RTLKMWDIKT
GECLKDLLSD LSGMWQVRFN DRRCVAAVQR DGLTYIEMLD FGASRDRVPI DRLGRRIVVD
RYGGEVQEEN EGTGDRDGSD E
//
