(data stored in ACNUC8465 zone)

SWISSPROT: F2Z631_CANGA

ID   F2Z631_CANGA            Unreviewed;       179 AA.
AC   F2Z631;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   30-AUG-2017, entry version 40.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62380.1};
GN   Name=CBF3D {ECO:0000313|CGD:CAL0137041};
GN   OrderedLocusNames=CAGL0M01364g {ECO:0000313|CGD:CAL0137041,
GN   ECO:0000313|EMBL:CAG62380.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62380.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the SKP1 family.
CC       {ECO:0000256|SAAS:SAAS00587069}.
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DR   EMBL; CR380959; CAG62380.1; -; Genomic_DNA.
DR   RefSeq; XP_449404.1; XM_449404.1.
DR   ProteinModelPortal; F2Z631; -.
DR   STRING; 284593.XP_449404.1; -.
DR   EnsemblFungi; CAG62380; CAG62380; CAGL0M01364g.
DR   KEGG; cgr:CAGL0M01364g; -.
DR   CGD; CAL0137041; CBF3D.
DR   EuPathDB; FungiDB:CAGL0M01364g; -.
DR   eggNOG; KOG1724; Eukaryota.
DR   eggNOG; COG5201; LUCA.
DR   InParanoid; F2Z631; -.
DR   KO; K03094; -.
DR   OMA; ENKWCEE; -.
DR   OrthoDB; EOG092C54Q0; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0031518; C:CBF3 complex; IGI:CGD.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0043291; C:RAVE complex; IEA:EnsemblFungi.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:EnsemblFungi.
DR   GO; GO:0019237; F:centromeric DNA binding; IGI:CGD.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IGI:CGD.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblFungi.
DR   GO; GO:0010458; P:exit from mitosis; IEA:EnsemblFungi.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0051382; P:kinetochore assembly; IEA:EnsemblFungi.
DR   GO; GO:2000766; P:negative regulation of cytoplasmic translation; IEA:EnsemblFungi.
DR   GO; GO:0045116; P:protein neddylation; IEA:EnsemblFungi.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0007096; P:regulation of exit from mitosis; IEA:EnsemblFungi.
DR   GO; GO:0043254; P:regulation of protein complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0000921; P:septin ring assembly; IEA:EnsemblFungi.
DR   GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
DR   InterPro; IPR016897; SKP1.
DR   InterPro; IPR001232; SKP1-like.
DR   InterPro; IPR011333; SKP1/BTB/POZ.
DR   InterPro; IPR016072; Skp1_comp_dimer.
DR   InterPro; IPR016073; Skp1_comp_POZ.
DR   Pfam; PF01466; Skp1; 1.
DR   Pfam; PF03931; Skp1_POZ; 2.
DR   PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
DR   SMART; SM00512; Skp1; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF81382; SSF81382; 1.
PE   3: Inferred from homology;
DR   PRODOM; F2Z631.
DR   SWISS-2DPAGE; F2Z631.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN        7     41       Skp1_POZ. {ECO:0000259|Pfam:PF03931}.
FT   DOMAIN       53     84       Skp1_POZ. {ECO:0000259|Pfam:PF03931}.
FT   DOMAIN      129    176       Skp1. {ECO:0000259|Pfam:PF01466}.
SQ   SEQUENCE   179 AA;  20888 MW;  C51C660A4DA4071A CRC64;
     MDKKGKYVVL VSGEGEKFTV EKKIAQRSLL LKNYLNDMHE SSLDDEDEEQ DEDEDEDDEI
     VMPVPNVRSS VLQKVIEWAE HHRDSNFPDE DDDDSRKSAP VDAWDREFLK VDQEMLYEII
     LAANYLNIKP LLDAGCKVVA EMIRGRSPEE IRRTFNIVND FTPEEEAAIR RENEWAEDR
//

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