ID U4LPI0_PYROM Unreviewed; 773 AA.
AC U4LPI0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Similar to Probable E3 ubiquitin ligase complex SCF subunit sconB acc. no. Q00659 {ECO:0000313|EMBL:CCX34076.1};
GN ORFNames=PCON_02554 {ECO:0000313|EMBL:CCX34076.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX34076.1};
RN [1] {ECO:0000313|EMBL:CCX34076.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX34076.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX34076.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the WD repeat MET30/SCONB/SCON-2 family.
CC {ECO:0000256|ARBA:ARBA00007968}.
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DR EMBL; HF936296; CCX34076.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LPI0; -.
DR STRING; 1076935.U4LPI0; -.
DR eggNOG; KOG0274; Eukaryota.
DR OMA; GIAHVWS; -.
DR OrthoDB; 587035at2759; -.
DR Proteomes; UP000018144; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 3.
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; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19872; UBIQUITIN LIGASE SPECIFICITY FACTOR/HREP PROTEIN; 1.
DR PANTHER; PTHR19872:SF10; UBIQUITIN-BINDING SDF UBIQUITIN LIGASE COMPLEX SUBUNIT; 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; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:CCX34076.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 199..245
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 381..420
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 421..460
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 461..500
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 500..541
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 665..688
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 689..728
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 84470 MW; 48B4AF2CD4CAD01C CRC64;
MPMRIPTCPE TTRRRSPRLQ SVSPRRKISN STTCDPRPTK RKRSSGLDKK TPVAVEPTAM
DCDNPELSPE IATETKESVK RDIAPFLTRH IPSQYAPQGT PEQREQQKNA GQTSNTSFCY
RHRPDLKCRR PADEPTMEQL QSSMDSLPDA DRQAVTHVWS LYSVAPAPIR RMMLQGILQA
SCFAQLSYLS TEIRELIRID FISTLPVEIS FRILSYLDTN SLCRAAQVSR NWRALADDDV
VWHKMCQQHI DRKCTKCGWG IPLMERKRLR ATAKQMAMRA KDPSLFTPAT ATNEITDSTS
ELNSNGKRPA GSDDTAIDNN PSSSPKRTCN STISASREAS SSAVLPPTPK PPQTLPWKTV
FSDRFKVEAN WRRGRCNQQI FKGHTDGVMC VQFDDAILAT GSYDTTIKIW DLATGEEIRT
LVGHTQGVRC LQFDNKKLIS GSMDGHIRIW NYHTGECLSV LSGHNGGILS LHFDNTLLVS
GSTDHTIKVW NFADKNCYSL RGHTDWVNSV RIDTDSRTVY SASDDSTIKM WDLDTRSLIR
TFTGKDGHVG HVQQVIPISL PTYQKPEPTI SSRGASPVSG AGAGTGGINT GVGGISTIGL
ASNAPPSTLP PASPPAPPMF PPSSSIAPTG LFPSISSMGG SETEADPFLI ASVFSNPSRP
PPPHMLITAS LDGTVKFWDV PTGACTNTLF GHIEGVWAVA ADTLRVVSGA QDSMVKVWDV
NTGACQRTIT GHAGPVTCVG LSDSRMVTGG DDGVVRGYLF RCEREEEGVV GEQ
//