DAM1_DEBHA
ID DAM1_DEBHA Reviewed; 294 AA.
AC Q6BWK6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=DASH complex subunit DAM1;
DE AltName: Full=Outer kinetochore protein DAM1;
GN Name=DAM1; OrderedLocusNames=DEHA2B10582g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382134; CAG85417.2; -; Genomic_DNA.
DR RefSeq; XP_457413.2; XM_457413.1.
DR AlphaFoldDB; Q6BWK6; -.
DR STRING; 4959.XP_457413.2; -.
DR EnsemblFungi; CAG85417; CAG85417; DEHA2B10582g.
DR GeneID; 2913340; -.
DR KEGG; dha:DEHA2B10582g; -.
DR VEuPathDB; FungiDB:DEHA2B10582g; -.
DR eggNOG; ENOG502S08R; Eukaryota.
DR HOGENOM; CLU_092107_0_0_1; -.
DR InParanoid; Q6BWK6; -.
DR OMA; PKIHYPV; -.
DR OrthoDB; 1397508at2759; -.
DR Proteomes; UP000000599; Chromosome B.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042729; C:DASH complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IEA:InterPro.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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..294
FT /note="DASH complex subunit DAM1"
FT /id="PRO_0000127659"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 121..163
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 33059 MW; DDD1D449B1A2B8E9 CRC64;
MASSPRPTTP NSQKKRSGRR QSHRSSGAYN ILPQSPKIHY PVDPDNLPLE APGNTEKFES
LSDALEELDV NMTNLQSIHE AISDGFNESF ASFLYGLSIT MWCVDFPGCP SRNQWEKLKL
VEGLDDRISE LAEKIRSHRE ENERLKNRLA SNVVESTEEV ENHSDSHENR KPQHSHRVGK
GPTRQVDEGD DTYMTNEGSF VVNPSAPSAT RIPQPVKTAP RRFTKHTPPP PPPPPPADTS
MHSSYRGPNL NQPPRYMRGL FDSTNRPTTP SNNRSKRVAN PNRIQKATGR PPFR
