DAM1_KLULA
ID DAM1_KLULA Reviewed; 313 AA.
AC Q6CVK1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=DASH complex subunit DAM1;
DE AltName: Full=Outer kinetochore protein DAM1;
GN Name=DAM1; OrderedLocusNames=KLLA0B11429g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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 DAM1 family. {ECO:0000305}.
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DR EMBL; CR382122; CAH02431.1; -; Genomic_DNA.
DR RefSeq; XP_452038.1; XM_452038.1.
DR AlphaFoldDB; Q6CVK1; -.
DR SMR; Q6CVK1; -.
DR STRING; 28985.XP_452038.1; -.
DR EnsemblFungi; CAH02431; CAH02431; KLLA0_B11429g.
DR GeneID; 2896917; -.
DR KEGG; kla:KLLA0_B11429g; -.
DR eggNOG; ENOG502S08R; Eukaryota.
DR HOGENOM; CLU_065404_0_0_1; -.
DR InParanoid; Q6CVK1; -.
DR OMA; LYGLMCN; -.
DR Proteomes; UP000000598; Chromosome B.
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:0042802; F:identical protein binding; IEA:EnsemblFungi.
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; IPR013962; DASH_Dam1.
DR PANTHER; PTHR28113; PTHR28113; 1.
DR Pfam; PF08653; DASH_Dam1; 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..313
FT /note="DASH complex subunit DAM1"
FT /id="PRO_0000127660"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 110..139
FT /evidence="ECO:0000255"
FT COMPBIAS 268..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 34528 MW; 8A0E29E10F669F35 CRC64;
MSQRPNTPQR DRPTEYRLSL SSNASSRRSS LGNNGRDQHA SNQTMIEKYV LPQLQELSDS
MVTLDGNMTH MNFIHESIAD LNEALSALLY GLMCNSWCVD FPNISHDTPH ELKLIQRLEE
LKQERQALQA KLKPKELTKG SILPLSRQPL SRGSQMLYRD ENVPGSTASS NVNIDINDDE
DNTAASFVSN PTTFKPQMIS SVGASTDFMG KQTVGSASSK LRRRSILHQI RNNAAIGTIP
NTLTGITPGE RKRSLAVSAK RIPILAGSST TAGSASSANR ESTNTEPALP NRVVRTRQRT
YNPKNLASRP PFR