ID   SWI6_CRYNH              Reviewed;         222 AA.
AC   J9VQZ0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 2.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Chromatin-associated protein SWI6 {ECO:0000305};
GN   Name=SWI6 {ECO:0000303|PubMed:31955845};
GN   ORFNames=CNAG_03458 {ECO:0000312|EMBL:AFR96683.2};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN   [1] {ECO:0000312|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000312|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
RN   [2] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH DMT5, AND DISRUPTION PHENOTYPE.
RX   PubMed=31955845; DOI=10.1016/j.cell.2019.12.012;
RA   Catania S., Dumesic P.A., Pimentel H., Nasif A., Stoddard C.I., Burke J.E.,
RA   Diedrich J.K., Cook S., Shea T., Geinger E., Lintner R., Yates J.R. III,
RA   Hajkova P., Narlikar G.J., Cuomo C.A., Pritchard J.K., Madhani H.D.;
RT   "Evolutionary Persistence of DNA Methylation for Millions of Years after
RT   Ancient Loss of a De Novo Methyltransferase.";
RL   Cell 180:263.277.e20-263.277.e20(2020).
CC   -!- FUNCTION: Recognizes and binds histone H3 tails methylated at 'Lys-9',
CC       leading to epigenetic repression (By similarity). Localizes DMT5 to
CC       heterochromatin characterized by trimethylation of histone H3 tails at
CC       'Lys-9' (PubMed:31955845). {ECO:0000250|UniProtKB:P40381,
CC       ECO:0000269|PubMed:31955845}.
CC   -!- SUBUNIT: Interacts with DMT5. {ECO:0000269|PubMed:31955845}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40381}.
CC   -!- DISRUPTION PHENOTYPE: Mildly decreases methylation of the fifth carbon
CC       of cytosine (5mC) in DNA. {ECO:0000269|PubMed:31955845}.
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DR   EMBL; CP003827; AFR96683.2; -; Genomic_DNA.
DR   RefSeq; XP_012050961.1; XM_012195571.1.
DR   EnsemblFungi; AFR96683; AFR96683; CNAG_03458.
DR   GeneID; 23886963; -.
DR   VEuPathDB; FungiDB:CNAG_03458; -.
DR   HOGENOM; CLU_045874_5_0_1; -.
DR   Proteomes; UP000010091; Chromosome 8.
DR   GO; GO:0000792; C:heterochromatin; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR017984; Chromo_dom_subgr.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR008251; Chromo_shadow_dom.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF01393; Chromo_shadow; 1.
DR   PRINTS; PR00504; CHROMODOMAIN.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00300; ChSh; 1.
DR   SUPFAM; SSF54160; SSF54160; 2.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
PE   1: Evidence at protein level;
KW   Nucleus.
FT   CHAIN           1..222
FT                   /note="Chromatin-associated protein SWI6"
FT                   /id="PRO_0000454228"
FT   DOMAIN          28..87
FT                   /note="Chromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   222 AA;  25068 MW;  76486C0A2A7F53EA CRC64;
     MPVIKKEELS QKKDLESEEE DSGLEDEYEV EKVIKHRGKG KNIEFLVRWK GYGPEYDTWE
     PTENVASAEE AVAAYWETQD KTATAPRKRG RQEAYTASQT SITPKPESSK QAAKKARTST
     AENGIKASVD KGEGNDGASD DDIDRQYSGS LDKYSDLKSW ENVVQNIETV EQGEGGQLIV
     YATMKGGEKV TIPTELAYKK CPLKCLYFYQ KHLKWRPVDE NE