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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
 
 
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