ID A0A139GVM0_9PEZI Unreviewed; 713 AA.
AC A0A139GVM0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cullin family profile domain-containing protein {ECO:0000259|PROSITE:PS50069};
GN ORFNames=AC579_7331 {ECO:0000313|EMBL:KXS94254.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXS94254.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXS94254.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXS94254.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the cullin family.
CC {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
CC ECO:0000256|RuleBase:RU003829}.
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:KXS94254.1}.
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DR EMBL; LFZO01001000; KXS94254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139GVM0; -.
DR STRING; 113226.A0A139GVM0; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 4.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; CULLIN; 1.
DR PANTHER; PTHR11932:SF168; CULLIN-3; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF74788; Cullin repeat-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT DOMAIN 332..579
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT REGION 250..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 81712 MW; 494C1CAE09A71EE0 CRC64;
MSETWLIFNL RSGIGWLVNF NFAYLDRIHL PTIGLNGTDV DFEVTWQILE KAFTEIHTKN
ASVLSFEELY HSMAGSPGLH GHADGCLDVH GPRLLHRSPP AFYLHQGLYN SDQEVEDEQL
YLREFEPRFL ESSARFYRQE GERLLKESDA GTYCKHAKRR IDEEGDRCRS TLLETTALKI
QKVVEDELIR NKMKGLIEME SGVRYMVDND KFHELHLVFD LEARVDPKKP ELTKALQLIV
AEMGAKINDG ASTASQAPPA PPPASEEGEG EKTKSNTKQI NQQTAAALKW VEEVLELKDR
FDNIWKTSFN EDQSISTALT RSMGENINAF SRAPEYISLF IDDNMKKGIK DRTDREVDQT
LEKAIILLRY LQDKDIFETY YKKHLCKRLL LKKSQSTEVE KQMIARMKME LGNSFTLKLE
AMFKDMTISE ELTADYRKRV AGLGDVDRTR VDLTVNILTS MTWPLEAFKS SSEDDPENNL
AQLIYPPELD RVRQGFERFY SEKHSGRKLT WQTSMGDVDV KARFPRSQRV HEVNCSTYAA
LVLLLFNKLP SGTTLTLEEI QAQTNVPLNA LKRNLQSLAV APKTRFLSKE PMSREINAND
KFKLNDDYKP ASVKIKVGVV SAGNKVEGDK ERKETEKKNN DSRGFQIEAA VVRIMKQRKM
LAHAQLLTET LNVLSSQFKP DVNMIKKRIE SLIEREYVER MDNAPVPSYK YLA
//