ID   TAY1_YARLI              Reviewed;         406 AA.
AC   Q6C9I6;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=telomere-associated protein 1 {ECO:0000303|PubMed:20923774};
GN   Name=TAY1 {ECO:0000303|PubMed:20923774}; OrderedLocusNames=YALI0D10923g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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).
RN   [2]
RP   FUNCTION, TELOMERE-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=20923774; DOI=10.1074/jbc.m110.127605;
RA   Kramara J., Willcox S., Gunisova S., Kinsky S., Nosek J., Griffith J.D.,
RA   Tomaska L.;
RT   "Tay1 protein, a novel telomere binding factor from Yarrowia lipolytica.";
RL   J. Biol. Chem. 285:38078-38092(2010).
RN   [3]
RP   FUNCTION, DOMAIN, TELOMERE-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=22815473; DOI=10.1074/jbc.m112.385591;
RA   Visacka K., Hofr C., Willcox S., Necasova I., Pavlouskova J., Sepsiova R.,
RA   Wimmerova M., Simonicova L., Nosek J., Fajkus J., Griffith J.D.,
RA   Tomaska L.;
RT   "Synergism of the two Myb domains of Tay1 protein results in high affinity
RT   binding to telomeres.";
RL   J. Biol. Chem. 287:32206-32215(2012).
CC   -!- FUNCTION: Telomere-binding protein that mediates telomere clustering by
CC       promoting formation of head-to-head dimers of DNA molecules through the
CC       telomeric tracts. Binds specifically 5'-TTAGTCAGGG-3' repeats in
CC       subtelomeric regions. {ECO:0000269|PubMed:20923774,
CC       ECO:0000269|PubMed:22815473}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC       Chromosome, telomere {ECO:0000269|PubMed:20923774,
CC       ECO:0000269|PubMed:22815473}.
CC   -!- DOMAIN: The presence of both Myb domains is required for high affinity
CC       telomeric DNA-binding. {ECO:0000269|PubMed:22815473}.
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DR   EMBL; CR382130; CAG80864.1; -; Genomic_DNA.
DR   RefSeq; XP_502676.1; XM_502676.1.
DR   AlphaFoldDB; Q6C9I6; -.
DR   STRING; 284591.Q6C9I6; -.
DR   EnsemblFungi; CAG80864; CAG80864; YALI0_D10923g.
DR   GeneID; 2910717; -.
DR   KEGG; yli:YALI0D10923g; -.
DR   VEuPathDB; FungiDB:YALI0_D10923g; -.
DR   HOGENOM; CLU_678276_0_0_1; -.
DR   InParanoid; Q6C9I6; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   Pfam; PF00249; Myb_DNA-binding; 2.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS51294; HTH_MYB; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   1: Evidence at protein level;
KW   Chromosome; DNA-binding; Nucleus; Reference proteome; Telomere.
FT   CHAIN           1..406
FT                   /note="telomere-associated protein 1"
FT                   /id="PRO_0000433237"
FT   DOMAIN          147..206
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          234..288
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   DNA_BIND        175..202
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          20..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   406 AA;  46861 MW;  C60AD9307F4F1E83 CRC64;
     MSHFGDHVGI DPAIMKQYSE HHNGSHDNDD KDKEDKEKQN TEAVAAAAVQ LDASLLASGI
     LDDFEKAKKE EEEANGNNNA SNDQQNASDR HVGDMLEQHS QQHQQSQEHD TSYINTYIED
     KVPLTSVLIP GDRRVSDREA SDRIAATTRR VRLRWTQEET ADLMEGCKVH GVGNWKKILT
     DPRFRFNNRT AVDLKDRFRT CFPEDYRRLY PNARSRKFGK KTNVMAVNDD LVKVNRKERR
     VFTPEEDERL LNGFMKHGPS WSNIQRDNEL GLFERRSTDL RDRFRNAFPL EYAAAGFKAR
     GPKRRPVVEA THGNTLQTIF SASDGSEMSP RKYHRVQEQM DRQPVMRVHP QAPMDQGVDR
     DHMTQQFTQE LQPQAHSRKQ QGGDGLKEEV FAAAQNQSYN NYYYQK