DCN1_CANGA
ID DCN1_CANGA Reviewed; 273 AA.
AC Q6FJR2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Defective in cullin neddylation protein 1;
GN Name=DCN1; OrderedLocusNames=CAGL0M04257g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: May contribute to neddylation of cullin components of SCF-
CC type E3 ubiquitin ligase complexes. Neddylation of cullins play an
CC essential role in the regulation of SCF-type complexes activity (By
CC similarity). {ECO:0000250}.
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DR EMBL; CR380959; CAG62508.1; -; Genomic_DNA.
DR RefSeq; XP_449532.1; XM_449532.1.
DR AlphaFoldDB; Q6FJR2; -.
DR SMR; Q6FJR2; -.
DR STRING; 5478.XP_449532.1; -.
DR EnsemblFungi; CAG62508; CAG62508; CAGL0M04257g.
DR GeneID; 2891541; -.
DR KEGG; cgr:CAGL0M04257g; -.
DR CGD; CAL0137307; CAGL0M04257g.
DR VEuPathDB; FungiDB:CAGL0M04257g; -.
DR eggNOG; KOG3077; Eukaryota.
DR HOGENOM; CLU_047042_0_0_1; -.
DR InParanoid; Q6FJR2; -.
DR OMA; FTQTGEQ; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0097602; F:cullin family protein binding; IEA:EnsemblFungi.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblFungi.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:EnsemblFungi.
DR GO; GO:0032182; F:ubiquitin-like protein binding; IEA:EnsemblFungi.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IEA:EnsemblFungi.
DR GO; GO:0045116; P:protein neddylation; IEA:EnsemblFungi.
DR Gene3D; 1.10.238.200; -; 1.
DR InterPro; IPR014764; DCN-prot.
DR InterPro; IPR042460; DCN1-like_PONY.
DR InterPro; IPR005176; PONY_dom.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR12281; PTHR12281; 1.
DR Pfam; PF03556; Cullin_binding; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51229; DCUN1; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..273
FT /note="Defective in cullin neddylation protein 1"
FT /id="PRO_0000129511"
FT DOMAIN 6..44
FT /note="UBA-like"
FT DOMAIN 62..268
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
SQ SEQUENCE 273 AA; 32739 MW; 778CD4D838998EC7 CRC64;
MVSRHEKELM KTFQSLTSCT DEGKAKRYLS ANNWNINYAL NEYYDKEVGG FTEDHMIRHQ
FKYPDELVSL FGHYAALIEE DGTQSITPDG LIDYIQDLGY NLEDLVTISL AHFLQCKNLE
NPITEKQFLY FWYNEGCYTL EQMRHYLEDC ERKLCNDWKY FTTIYNYSFD LNASKQGVVE
TDIAIEYWKL FFEENRTKLS GIIKVDQAHL DLWCKFLQDE HKKLIHKDTW QMLLLFFKKF
PSLDAIKTEY NEADAWPYTI DEFYEYLEER NVL