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DAM1_ASHGO
ID   DAM1_ASHGO              Reviewed;         339 AA.
AC   Q75EQ0;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=DASH complex subunit DAM1;
DE   AltName: Full=Outer kinetochore protein DAM1;
GN   Name=DAM1; OrderedLocusNames=AAR029W;
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, AND SEQUENCE REVISION TO C-TERMINUS.
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 DAM1 family. {ECO:0000305}.
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DR   EMBL; AE016814; AAS50394.2; -; Genomic_DNA.
DR   RefSeq; NP_982570.2; NM_207923.2.
DR   AlphaFoldDB; Q75EQ0; -.
DR   STRING; 33169.AAS50394; -.
DR   EnsemblFungi; AAS50394; AAS50394; AGOS_AAR029W.
DR   GeneID; 4618458; -.
DR   KEGG; ago:AGOS_AAR029W; -.
DR   eggNOG; ENOG502S08R; Eukaryota.
DR   HOGENOM; CLU_065404_0_0_1; -.
DR   InParanoid; Q75EQ0; -.
DR   OMA; LYGLMCN; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0042729; C:DASH complex; IBA:GO_Central.
DR   GO; GO:1990537; C:mitotic spindle polar microtubule; IBA:GO_Central.
DR   GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
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; IBA:GO_Central.
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..339
FT                   /note="DASH complex subunit DAM1"
FT                   /id="PRO_0000127656"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          120..150
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        14..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   339 AA;  36698 MW;  23F92A4389C3F0AE CRC64;
     MSKESVRESK AATEYRLSIS SNPGSRRSSF GGSSEHPAGS GIGNNKASNG ELREATLVDT
     LLLPQVQELK DSMITLDANL THMNFIHESL VDLNESVSAL LYGLMCNSWC VDFPNMPHHT
     ARELGISKEL ARLKEEKQQL LADLQGTAQA PSLVLKEKEP NTSKQKFQLP KPPMVSTRSV
     VAPVRTISEE EEDDNTAASF VSNPTVMGQP PHAPPPVARS NNAKGRRRYS ILQQIRNHDL
     TGQKHMVANL GGTVKARAAT HPIPESAGEK RKSLAVSAVR IGNNKRLQTS RPPSGGRDVT
     MARKRSGTQP AILNTNSITH SSTGAVPASS AQGRRPPFR
 
 
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