ID Q4WLM1_ASPFU Unreviewed; 1079 AA.
AC Q4WLM1;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 122.
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=AFUA_6G13030 {ECO:0000313|EMBL:EAL89143.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL89143.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL89143.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:EAL89143.1}.
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DR EMBL; AAHF01000006; EAL89143.1; -; Genomic_DNA.
DR RefSeq; XP_751181.1; XM_746088.1.
DR AlphaFoldDB; Q4WLM1; -.
DR STRING; 330879.Q4WLM1; -.
DR EnsemblFungi; EAL89143; EAL89143; AFUA_6G13030.
DR GeneID; 3508488; -.
DR KEGG; afm:AFUA_6G13030; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_3_1; -.
DR InParanoid; Q4WLM1; -.
DR OMA; TMCRAAQ; -.
DR OrthoDB; 587035at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; 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 Cell cycle {ECO:0000313|EMBL:EAL89143.1};
KW Cell division {ECO:0000313|EMBL:EAL89143.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
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 459..506
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 712..751
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 782..801
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 828..867
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 868..909
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 910..949
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 950..988
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 121..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..591
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 118727 MW; CF2AB1CEC65A198F CRC64;
MDQLDANNDL DHRAANSTIG QFSFAPATRT TVVTTTTTTT TTFPPLVIKS PRATRDLDPK
LYPLASSPTP TSLRNIKFEL GGKTVVFNEP EDATVAIKEV NETNNALKAS NGFVQSVTSY
TTSDNAQTSR RLVSARLSSQ PSNPSSAKRR PASVIDSHQS STRLRPGRLP SEPSCRQIRP
HLSSATYTAG LATPETESSS YNLSDYAMPR RRVHSAAIPR RETLLRSPLS SEVESQEVLQ
DPGAESVLGK EELRALRAKA VIWERDQHIS RHRDNASSRP APQLATPVVN GDRAAGVNTA
SQGTDYDGSE ESFQQAQTEP ASQISAIENL VANDMCLPSP SLSPVAALNA MNVDSSFESA
EDQEMDTDSS LDNNASRLSN VRHLDDSKTH NLSPSRSGNL PGASEIRRAS SLMDIPSVLD
FFDSVPEELK TYLMYQFLRR CPKPTLHFVA DVVNPALKCD FLALLPLELS LNIVKYFDVQ
TMCRAAQVSK KWRHIINSDE KTWKDLFDRD GYVLTDGELE RAIKEGWGWQ FPHGDDDWEK
DLSSSAVIKP EPDCAPGPAF SSLPGESGER ALSVSRRPKR KATRISGRKF AKRKISSSNT
DSSDSSGWRN GVTATEGPYA AANAAAAAVP YPEIGLPSLR GLHLFKSLYQ RHHSIHKGWM
KPNVKPKHIA FRAHDRHVVT CLQFDTDKVL TGSDDTNINV YDTKTGALRA TLEGHEGGVW
ALEYHGNTLV SGSTDRSVRV WDIERARCTQ IFHGHTSTVR CLQIVLPVQV GTSADGTPEM
MPKEPIIITG SRDSSLRVWK LPKPGDPVYY QSGPHADDTD CPYFIRVLTG HQHSVRAIAA
HGDTLVSGSY DCTVRVWKIS TGETIHRLQG HTLKVYSVVL DHKRNRCISG SMDNTVKVWS
LDTGSIIYNL EGHSSLVGLL DLKCDRLVSA AADSTLRIWD PETGQCKSRL SAHTGAITCF
QHDGQKVISG SDRTLKMWDV RNGECVRDLL TDLSGVWQVK FNDRRCVAAV QRDALTYIEV
SRGSVCQSAT IIINHLQVLD FGASRDGVPE DQLGRRIVVN RWGQEIGDNA DEDYDLSDG
//