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Database: UniProt
Entry: C8V637_EMENI
LinkDB: C8V637_EMENI
Original site: C8V637_EMENI 
ID   C8V637_EMENI            Unreviewed;       823 AA.
AC   C8V637;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   SubName: Full=SCF ubiquitin ligase subunit CulC, putative (AFU_orthologue AFUA_6G08220) {ECO:0000313|EMBL:CBF75050.1};
GN   ORFNames=ANIA_03939 {ECO:0000313|EMBL:CBF75050.1};
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:CBF75050.1, 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   -!- 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}.
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DR   EMBL; BN001302; CBF75050.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8V637; -.
DR   STRING; 227321.C8V637; -.
DR   EnsemblFungi; CBF75050; CBF75050; ANIA_03939.
DR   VEuPathDB; FungiDB:AN3939; -.
DR   eggNOG; KOG2166; Eukaryota.
DR   HOGENOM; CLU_004747_7_1_1; -.
DR   InParanoid; C8V637; -.
DR   OMA; MFKDMTI; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   GO; GO:0031463; C:Cul3-RING 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: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: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; 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:CBF75050.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          442..689
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          366..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   823 AA;  94189 MW;  34D2F1B5876788BD CRC64;
     MVMRARQKIR APRKGIPVSG DEFEKNWKDL STSLKKIHTK DASELSFEQL YRNAYSIVKI
     QRAEDLYERT KELEKEWLCG EVQKRVVAAI TPRLLLAKEA VDMQDQFTEA TERRETGERF
     LSALSEVWED HQICMKMITD VLMYMDRVVA LRKVSIYAAA MALFRDHVLR SPVSSSNNAV
     VADVLKSTVL FMIQLERSGH MIDRALIHSC IKMLEGLYET EAEEESSKLY LTSFEPDYLE
     ASAAFYRAEG KRLLETVDAA TFCAVVSARI AEEKERCQYT ISLLSESKIK EIVDNELIRN
     NLAEVVNFEG TGVRVMLDHD RIDNLSKIYA LSARVDPKKT HLTAAVQKRI VEMGNEINNA
     SFALAQAPAQ PKSTGTDAGQ KKEKEKEKPV NQVTSSAIKW VDDILALKKK FDGIWKDAFG
     SDQVLQSAIT ASFSSFLNST PRSSEFLSLF FDENLKKGVK GKTDNEVDAL LENGITLLRY
     IKDKDRFEAY YKKHLSRRLL MKRSMSMDAE RQMISKMKME VGNQFTQRLE AMFRDMTISE
     DLTASYKQFV REQGDPDKKR FELDINVLTS TMWPMEIMSS SRDGQVELPC IIPKEVETVK
     QSFEKFYLDK HSGRKLSWQP SMGTADIKAT FHRSNGKVQR HELNVSTYAM FILLLFNDIP
     IGESLTFEEI QARTRIPDND LIRNLQSLAV APKTRVLKKV PMSRDVKPTD KFYFNNDFQS
     PFMKVRIGVV SGGANKVESQ DQRKETEEKM NNERGGSIEA AIVRIMKQRK TLIHSNLISE
     VLSQLSARFV PDVNMVKRRI ESLIDREYLE RVSEDPPTYG YVA
//
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