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Database: UniProt
Entry: A0A010RJD2_9PEZI
LinkDB: A0A010RJD2_9PEZI
Original site: A0A010RJD2_9PEZI 
ID   A0A010RJD2_9PEZI        Unreviewed;       639 AA.
AC   A0A010RJD2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=WD domain-containing protein {ECO:0000313|EMBL:EXF80501.1};
GN   ORFNames=CFIO01_08221 {ECO:0000313|EMBL:EXF80501.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF80501.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF80501.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF80501.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the regulatory network controlling carbon source
CC       utilization through ubiquitination and deubiquitination involving creA,
CC       creB, creC, creD and acrB. Required to prevent the proteolysis of the
CC       CreB deubiquitinating enzyme in the absence of carbon catabolite
CC       repression. CreB deubiquitinating enzyme stabilized in a complex with
CC       the CreC leads to the expression of genes such as those in the proline
CC       and quinate pathways. {ECO:0000256|ARBA:ARBA00037241}.
CC   -!- SUBUNIT: Interacts with creB. {ECO:0000256|ARBA:ARBA00038682}.
CC   -!- SIMILARITY: Belongs to the WD repeat creC family.
CC       {ECO:0000256|ARBA:ARBA00038107}.
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:EXF80501.1}.
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DR   EMBL; JARH01000435; EXF80501.1; -; Genomic_DNA.
DR   RefSeq; XP_007595838.1; XM_007595776.1.
DR   AlphaFoldDB; A0A010RJD2; -.
DR   STRING; 1445577.A0A010RJD2; -.
DR   KEGG; cfj:CFIO01_08221; -.
DR   eggNOG; KOG2394; Eukaryota.
DR   HOGENOM; CLU_016971_1_1_1; -.
DR   OrthoDB; 1513505at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR14107:SF16; AT02583P; 1.
DR   PANTHER; PTHR14107; WD REPEAT PROTEIN; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   REPEAT          436..477
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          111..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   639 AA;  69246 MW;  4058237FD770E355 CRC64;
     MFVLPPPPRY PSHSGAYGAI GAGIAPMIET NNILSNPEGP EYQFLVGEGT YVLKECLHLA
     TPPPHPSEAP VVNPNPLATT PQPASAGTKL SLISLDVRAA PPFFYNKGAS TSTTLSSSLG
     GDIQEHPNEG RYSTEAGLSS DGGDGRGASL SDGVAPPTSS LTMVSAPAFG DGNTALAPAN
     TKDAAKKKVA KPKNNMTKSN SSFISRVIVN ESLAKKLQER PTDGVFAFAN INRAFQWLDL
     SSPTKADYLT KILFTKAHCL CHDVNPITKN IAHIDVIMGF STGEIIWWEP VSQRYTRLNK
     NGIINGTPVS EIRWIPGSES LFLAAHMDGS LVVYDKDKED AQFSPEEEQL ATTNGSSTNG
     ESDSSTNGVN HNLKIQINKS VHSKNQKTNP VASWKLSNQR INAFAFSPDN RHLAVVSEDG
     SLRIIDYLKE ELLDLYNSYY GGFICITWSP DGKYVLTGGQ DDLISIWSVV DSAIVARCQG
     HQSWVTSVAF DPWRCDDRNY RFGSVGEDCR LCLWDFNVGM LHRPKAASVH HRGSVSSRFA
     NPLQRQETTN TSASRIRSNS TLSGGAVDED GSSIVHPVEP RARIAMLPPV SSKAVDTHPL
     CWLEFTEEAI ITSCKNGHIR TWNRPTDAPV PTEGASQPS
//
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