ID   HSK3_ASHGO              Reviewed;          68 AA.
AC   Q753W8;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=DASH complex subunit HSK3;
DE   AltName: Full=Outer kinetochore protein HSK3;
GN   Name=HSK3; OrderedLocusNames=AFR204W;
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.
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: 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 HSK3 family. {ECO:0000305}.
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DR   EMBL; AE016819; AAS53575.1; -; Genomic_DNA.
DR   RefSeq; NP_985751.1; NM_211105.1.
DR   AlphaFoldDB; Q753W8; -.
DR   SMR; Q753W8; -.
DR   STRING; 33169.AAS53575; -.
DR   EnsemblFungi; AAS53575; AAS53575; AGOS_AFR204W.
DR   GeneID; 4622012; -.
DR   KEGG; ago:AGOS_AFR204W; -.
DR   eggNOG; KOG4853; Eukaryota.
DR   HOGENOM; CLU_193155_0_0_1; -.
DR   InParanoid; Q753W8; -.
DR   OMA; QCNKNIV; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0042729; C:DASH complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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; IPR042332; Hsk3.
DR   InterPro; IPR013183; Hsk3-like.
DR   PANTHER; PTHR28289; PTHR28289; 1.
DR   Pfam; PF08227; DASH_Hsk3; 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..68
FT                   /note="DASH complex subunit HSK3"
FT                   /id="PRO_0000084078"
FT   COILED          3..39
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   68 AA;  7971 MW;  84B217EB8906CA6E CRC64;
     MDQTKRRHYS QLSQQLQLLQ KNLEATTQHV ETMSVQCNEH LVNKLGKIQA SWFIGGNRCF
     EQELLGKR