DCN1_ASHGO
ID DCN1_ASHGO Reviewed; 255 AA.
AC Q750Y3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Defective in cullin neddylation protein 1;
GN Name=DCN1; OrderedLocusNames=AGL194C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54297.2; -; Genomic_DNA.
DR RefSeq; NP_986473.2; NM_211535.2.
DR AlphaFoldDB; Q750Y3; -.
DR SMR; Q750Y3; -.
DR STRING; 33169.AAS54297; -.
DR EnsemblFungi; AAS54297; AAS54297; AGOS_AGL194C.
DR GeneID; 4622766; -.
DR KEGG; ago:AGOS_AGL194C; -.
DR eggNOG; KOG3077; Eukaryota.
DR HOGENOM; CLU_047042_0_0_1; -.
DR InParanoid; Q750Y3; -.
DR OMA; FTQTGEQ; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblFungi.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
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..255
FT /note="Defective in cullin neddylation protein 1"
FT /id="PRO_0000129509"
FT DOMAIN 6..43
FT /note="UBA-like"
FT DOMAIN 54..250
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
SQ SEQUENCE 255 AA; 29032 MW; 1D01CD00FBC33336 CRC64;
MSNARQRELI REFLAVTSAT SAAAETYLER NHWSLDHALD DFYTQSGGGG RAEQYSAELV
ATFERYAAGG AMDTEALVRY VGDLGFQLED VATLCLARLL KVEELTADIS RFQFLSTWHG
LGCSSLPDMR AAVDALELRL RTDAAYFRAL YAYTFGLGLD AGGRRLSVET AIAYWSLFFL
DHTYAVTVPA PRLRSWFEFL RAGDHSVSRD TWDMFPRFAQ RFPDDTELLE HYNELASWPL
VIDEYYEWVK GRNQL