ID   A1CBL2_ASPCL            Unreviewed;       914 AA.
AC   A1CBL2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Ubiquitin ligase subunit CulD, putative {ECO:0000313|EMBL:EAW13130.1};
GN   ORFNames=ACLA_015720 {ECO:0000313|EMBL:EAW13130.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW13130.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW13130.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SIMILARITY: Belongs to the cullin family.
CC       {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
CC       ECO:0000256|RuleBase:RU003829}.
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DR   EMBL; DS027049; EAW13130.1; -; Genomic_DNA.
DR   RefSeq; XP_001274556.1; XM_001274555.1.
DR   AlphaFoldDB; A1CBL2; -.
DR   STRING; 344612.A1CBL2; -.
DR   EnsemblFungi; EAW13130; EAW13130; ACLA_015720.
DR   GeneID; 4706926; -.
DR   KEGG; act:ACLA_015720; -.
DR   VEuPathDB; FungiDB:ACLA_015720; -.
DR   eggNOG; KOG2167; Eukaryota.
DR   HOGENOM; CLU_004747_7_0_1; -.
DR   OMA; NYQEQTW; -.
DR   OrthoDB; 5474206at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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; 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; PS50069; CULLIN_2; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EAW13130.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT   DOMAIN          523..788
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          1..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   914 AA;  103843 MW;  4B13C267E12DB871 CRC64;
     MQNPRVAPDQ RSGKRKSTSK RKLPDQGEAS LQSQASQPQQ QQPQQTTISE LLSRNHTHGK
     AHPHQSPSSN KRPRLSPSVS DFRPLESAPE LHPPNKMYNF SNSGQNASGT FSHSAPALSS
     RTASHPLNAP SRQSNFTPHT GAKRLVVKNL RTGSRLNQDS YFDKVWTQLD AALTAVFNGG
     NPDVSLEELY KGAENVCRQG RAAVLTQRLQ DRCRAHVSGR LRDDLLTKAS GGNNVDTLRA
     VVGAWSTWQK KLVTVRWIFY YLDQSFLLHS KEYPVIREMG LRQFRDHIFS DSVLQTKILQ
     GACDLVEADR NENSTMMADI SLLREAIELF HGLDVYTTAF EPLLLTESKR FFTSWAQREA
     SGYLATFVEN AHRLIEREVN RCELFSLSRS TRQKLSALLD TNLVADQESF LLNEKDILGL
     LRDGNKDALE KLYTLLERRQ LGTKLKASFK SYIVEEGSRI VFDEDKEAQM VVSLLEFKSQ
     LDKIWANSFH RNEELGHTLR EAFATFMNQS RKSDSTGGTD NVKTGEMIAK YVDRLLKGGW
     KLPPGGDIKD VPLADEDAEI NRQLDQVLDL FRFVNGKAVF EAFYKNDLAR RLLMGRSASD
     DAEKSMLARL KTGWFPFADV SSLVSGISKL IWYAECGSTF THNLESMFKD MEVARDEMAA
     YSSIQRERKK RLPVDLNVSV LSASAWPSYP DVQVRIPAVI ATAIDDFENF YHNKYNGRKL
     TWKHQLAHCQ LRAWFGGKSK ELVVSSFQAI VLLLFNDVEE SKRLTYSEIQ DATKLSDPEL
     QRTLQSLACA KYRVLTKTPK GRDVNKTDEF AYNAEFNDPK MRIKINQIQL KETKEENKKT
     HERVAADRHL ETQAAIVRIM KSRKRSTHAE LVAEVIKATR SRGVLEVADI KSNIEKLIEK
     DYIERDDNVY QYVA
//