DUO1_CANGA
ID DUO1_CANGA Reviewed; 212 AA.
AC Q6FU23;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=DASH complex subunit DUO1;
DE AltName: Full=Outer kinetochore protein DUO1;
GN Name=DUO1; OrderedLocusNames=CAGL0F06963g;
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: Component of the DASH complex, a microtubule-binding
CC subcomplex of the outer kinetochore that is essential for proper
CC chromosome segregation. The DASH complex mediates the formation and
CC maintenance of bipolar kinetochore-microtubule attachments by forming
CC closed rings around spindle microtubules and establishing interactions
CC with proteins from the central kinetochore (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The DASH complex oligomerizes to form rings that encircle the
CC microtubules. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Chromosome, centromere, kinetochore
CC {ECO:0000250}. Note=Associates with the mitotic spindle and the
CC kinetochore. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DASH complex DUO1 family. {ECO:0000305}.
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DR EMBL; CR380952; CAG59195.1; -; Genomic_DNA.
DR RefSeq; XP_446271.1; XM_446271.1.
DR AlphaFoldDB; Q6FU23; -.
DR SMR; Q6FU23; -.
DR STRING; 5478.XP_446271.1; -.
DR EnsemblFungi; CAG59195; CAG59195; CAGL0F06963g.
DR GeneID; 2887579; -.
DR KEGG; cgr:CAGL0F06963g; -.
DR CGD; CAL0131332; CAGL0F06963g.
DR VEuPathDB; FungiDB:CAGL0F06963g; -.
DR eggNOG; ENOG502S4KM; Eukaryota.
DR HOGENOM; CLU_114619_0_0_1; -.
DR InParanoid; Q6FU23; -.
DR OMA; WIKIQSQ; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042729; C:DASH complex; IEA:EnsemblFungi.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IEA:InterPro.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:EnsemblFungi.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IEA:EnsemblFungi.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:EnsemblFungi.
DR InterPro; IPR013960; DASH_Duo1.
DR Pfam; PF08651; DASH_Duo1; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..212
FT /note="DASH complex subunit DUO1"
FT /id="PRO_0000215592"
FT REGION 150..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..148
FT /evidence="ECO:0000255"
FT COMPBIAS 155..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 212 AA; 23577 MW; 67F158C868397EDC CRC64;
MSESLDNSAI NQLIPEIFDQ MRHNAARTRD AKKPSAMVEE SGSITTQSLL RELETLDKVI
ATIRSIDSVV KGALPSHMNK IHHVCKSTNK MLDNWINIQS QAGYAHHIMD SRTGSKTGSN
SNEEVVEQYK QEIAELQKSI KMEEDKLIPA QVKGNGNGPT GQRLYGNSYR QPTGRVTKAT
ALRNARNRPS GIPQISSRLT RPTASSNLKR QR