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Database: UniProt
Entry: C8VRE7_EMENI
LinkDB: C8VRE7_EMENI
Original site: C8VRE7_EMENI 
ID   C8VRE7_EMENI            Unreviewed;       880 AA.
AC   C8VRE7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Ubiquitin ligase subunit CulD, putative (AFU_orthologue AFUA_5G12680) {ECO:0000313|EMBL:CBF90329.1};
GN   ORFNames=ANIA_10008 {ECO:0000313|EMBL:CBF90329.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF90329.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA   Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA   Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; BN001308; CBF90329.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8VRE7; -.
DR   STRING; 227321.C8VRE7; -.
DR   EnsemblFungi; CBF90329; CBF90329; ANIA_10008.
DR   VEuPathDB; FungiDB:AN10008; -.
DR   eggNOG; KOG2167; Eukaryota.
DR   HOGENOM; CLU_004747_7_0_1; -.
DR   InParanoid; C8VRE7; -.
DR   OMA; NYQEQTW; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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:CBF90329.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          510..753
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          1..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   880 AA;  100047 MW;  75B7ACC7260A7F02 CRC64;
     MQQNSRSPPE QRSGKRKATG KRKFPDQGEL SQQPRHQQAT ISELLHRNQA QNQAQEQDDE
     HLPPTNKRVR PSSSSIAANQ PESGDMYSFS TAEPKPNGPN TGGLTLSNST LQARPGTSSH
     QSNFTPHTGA RRLVVKNLRT GPRLNQDSYF DKVWGQLDAA LSAIFSGGKP EISLEELYKG
     AENVCRQGRA TILAKRLQER CRQHVTGKLH GSLVDKAQMA YNIETLRSVV EAWKEWQSML
     ITVRWIFYYL DQSFLLHSKE HPVIREMGLQ QFRQHIYSDP TLQEKILQGA CDLVSADRSD
     ENGIVADSSL LRNAIELFHS LDVYVSGFEP VLVSGSKDFF SLWAQQEATG YLASYVENSH
     RLIEREMNRC EQFSFNRTTK QKLSESLDQT LVTDQESVLL SQKDVLGLLR IGNKIALGQL
     YTLLERRDLG AKLKGAFSTY IVEEGTGIVF DESEADMVVR LLSFKKQLDD IWNESFRRNE
     GLGHALRESF ESFMNKGRKS DATGGTDNPK TGEMIAKYVD RLLRGGWRLA PTREAENMPL
     ADEDAEINRQ LDQVLDLFRF VHGKAVFEAF YKNDLARRLL MGRSASDDAE KSMLARLKTE
     CGSSFTHNLE SMFKDMEVAR DEMSAYNSIK RERQTPLPVD LHVSVLSASA WPTYPDVQVR
     IPPEIATAIS DFEKFYDTKY NGRKLAWKHQ LAHCQLRARF PNGNKELVVS SFQAIVLLLF
     NELPEGGTLN YRQIQEATTL SDQELTRTLQ SLACAKYRVL SKKPKGRDVS PTDEFSYNAS
     FTDPKFRIKI NQIQLKETKE ENKTTHERVA ADRHYETQAA IVRIMKSRKT ITHAELVAEV
     IKATRSRGVL EPADIKKNIE KLIEKDYMER EDGNRYQYVA
//
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