ID A0A072PHL0_9EURO Unreviewed; 1083 AA.
AC A0A072PHL0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=A1O9_08688 {ECO:0000313|EMBL:KEF55035.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF55035.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF55035.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF55035.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEF55035.1}.
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DR EMBL; AMGV01000008; KEF55035.1; -; Genomic_DNA.
DR RefSeq; XP_013257625.1; XM_013402171.1.
DR AlphaFoldDB; A0A072PHL0; -.
DR STRING; 1182545.A0A072PHL0; -.
DR GeneID; 25283599; -.
DR VEuPathDB; FungiDB:A1O9_08688; -.
DR HOGENOM; CLU_000288_103_3_1; -.
DR OrthoDB; 587035at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
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; 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; 7.
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; 4.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000027920};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 479..526
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 731..770
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 801..820
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 847..886
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 887..928
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 929..968
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 969..1007
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 110..144
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 120051 MW; DAC999402CECD59E CRC64;
MEEEGNMVSP TQDLPQPRFR SHSSARPPNS REIQPYTADT EQNALLGQFS FAPATQTTVV
TTTTTTTTKF PPFLMRPPRR MHELDLKHYP LAASPTPASL RNIHFEIAGK ATVFREAEDT
TLALEQLEAE RQSLRHANGT LQTIQSFLPW ASNSDEAMPN APPLESRPHR RPASPESITD
NEERFLHPDP SATSHYPPTS VRSDPRRDQD LRRSRFRMQD TQPSNPITPD SLHRSLRGNR
RRTARDASTA LRNGLALLPS PSTEQTANFP SAQATTPKSN QHQAPMLEEM LTIPTDGTIG
SRPNHRETSQ DTIVPTPPID DLPESSSARS TSWRALSSVP ARLHVAESPS INDGSLPSPS
LSPVTAAATL QNPGYFADVD SSSEGASQHE MASSLTPVER RSSNSFSAPS TLEASLLHPS
QSQRLAFSQA SVTEIPAMLD YFEAIPDELK SYVMHQLLRR CPKPTLQVIA DAVNPALKCD
FLSVLPAELA LTVLKYLDVR SLTRAAQVSK KWRQMINGDE RAWKELFDAD GFTLPDGELQ
QAITEGWGWQ DPYGVEGFER NLGNQTNIKS ETEANSSSPS ASQSKGITGL LRRSKRKAAT
MLSGRNKQAK RKDFSREDSI DVMSIDWMSQ MSTAEGPYNA ANAAILAVPY PNIGFPSLKG
LHLYKSLYRR HHLIRKNWMD EDTKPQHLAF RAHDTHVVTC LQFDTDKILT GSDDNNINVY
ETKTGILRAI LTGHEGGVWA LQYEGNTLVS GSTDRSVRVW NIQQARETQV FRGHTSTVRC
LQIVSPVKVG ETAEGKPIMV PRQPLIITGS RDSTLRVWRL PRPEDPTFIQ AENESDADDC
PFFVRTLTGH QHSVRAIAAY ADTLVSGSYD CTVRVWKIST GETIHRLQGH TQKVYSVVLD
HKRNRCISGS MDNMVRIWDL NTGSLKYTLE GHTSLVGLLD LNCDKLVSAA ADSTLRIWDP
ENGQCKATLT AHTGAITCFK HDGQKVISGS DKTLKLWNIR TGECTKDLLS DLSGVWQVKF
NERRCVAAVQ RDGLTYIEVL DFGAARDGVP EHNRGRRIVV DADGCEANND DVRYLDLDGT
AEG
//
