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Database: UniProt
Entry: A0A0F4GPW5_9PEZI
LinkDB: A0A0F4GPW5_9PEZI
Original site: A0A0F4GPW5_9PEZI 
ID   A0A0F4GPW5_9PEZI        Unreviewed;       905 AA.
AC   A0A0F4GPW5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Ubiquitin ligase subunit CulD like protein {ECO:0000313|EMBL:KJX99288.1};
GN   ORFNames=TI39_contig364g00016 {ECO:0000313|EMBL:KJX99288.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX99288.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX99288.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX99288.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJX99288.1}.
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DR   EMBL; LAFY01000356; KJX99288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GPW5; -.
DR   STRING; 1047168.A0A0F4GPW5; -.
DR   OrthoDB; 5474206at2759; -.
DR   Proteomes; UP000033647; Unassembled WGS sequence.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; IPR016157; Cullin_CS.
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:SF126; CULLIN 4, ISOFORM A; 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; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:KJX99288.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033647};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          511..778
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          1..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   905 AA;  102571 MW;  4AEA3AF023DF431C CRC64;
     MNPPRNVPSA TSNRTASSPT DRKRKHSNRS VAGDDTSSQQ HNFQPRPQKR QKSPESFQPS
     TPSGKRRRHD HIPTPPSRTN LAFSEMYTFN STRSPAQNSG GVVDLTNGSS PPSPQARRTS
     MSGRRTGLNP NTGAKKLVVK NLKSNTSWDS KAYLEKIWGQ LDEALALMFK DGQDGFSKED
     LYRGVENVCR QGGASTLFSR LENRCKSHIE RDVREPLLEK AGLDNVTVLK AVLLEWARWT
     EQMSTIRAIF FFLDRSYLLS SSKPTLDQFI PQLFREVVFS NITLKPKIVD GICDLIMVDR
     TKPESLDQDL FKRSVDMLHS LSTYSASFEP SLLGRSQHFV AEWSDQMISE KTVPEYVALS
     DKLIAREMQR CEEFDLDSST KRELLTLLED HLIQQKEADL TDYEAVSSLL ETNAVADLTK
     LYALLKRRRL GSNLRPSFDK WVDTTGTSIV FANQADDMVI HLLSLKRRLD YIWQTAFQRD
     ESLGHGLRET FAIFINKTKK GEATHGTDNT KVGEMIAKYV DQLLRGGAKA IPEVFSARRS
     SSLTASVVPT IAAPEQDNED DDVDEDAEIN IQLDQVLDLF RFVQGKAVFE AFYKKDLARR
     LLMARSASAD AERSMLTRLK TECGSGFTQN LEQMFKDVEL AREEMQSYKQ RLEERLGFEK
     GKKVDLSVNI LSAAAWPTYP DIPVIIPANI KRAIDDFELH YKSKHTGRKL DWKHALAHCQ
     MKATFGKGSK ELVVSSFQAI VMLLFNGLGD GDQLSYSHIL SETGLPEAEV KRTLQSLACA
     KLRPLTKHPR GKEINDTDTF SVNLTFEHPK YRVKINQVQL KETKEENKET HMRVAEDRNF
     ECQAAIVRIM KSRKTISHQE LVSEVIKATV SRGVLGMGDI KKNIDRLIEK DYMEREEGNM
     YSYIA
//
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