ID H6C4Y1_EXODN Unreviewed; 894 AA.
AC H6C4Y1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Histone-lysine N-methyltransferase ASH1L {ECO:0000313|EMBL:EHY58558.1};
GN ORFNames=HMPREF1120_06567 {ECO:0000313|EMBL:EHY58558.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY58558.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY58558.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY58558.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JH226134; EHY58558.1; -; Genomic_DNA.
DR RefSeq; XP_009159019.1; XM_009160771.1.
DR AlphaFoldDB; H6C4Y1; -.
DR STRING; 858893.H6C4Y1; -.
DR GeneID; 20311206; -.
DR VEuPathDB; FungiDB:HMPREF1120_06567; -.
DR eggNOG; KOG1827; Eukaryota.
DR HOGENOM; CLU_007728_0_0_1; -.
DR InParanoid; H6C4Y1; -.
DR OMA; QKWINAC; -.
DR OrthoDB; 1334586at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0016586; C:RSC-type complex; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:UniProt.
DR CDD; cd04717; BAH_polybromo; 1.
DR CDD; cd05522; Bromo_Rsc1_2_II; 1.
DR CDD; cd04369; Bromodomain; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037382; Rsc/polybromo.
DR InterPro; IPR048047; RSC1/2_bromodom.
DR PANTHER; PTHR16062:SF19; PROTEIN POLYBROMO-1; 1.
DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; Bromodomain; 2.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Methyltransferase {ECO:0000313|EMBL:EHY58558.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Transferase {ECO:0000313|EMBL:EHY58558.1}.
FT DOMAIN 99..169
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 313..375
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 418..537
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..632
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 101774 MW; 92A3F271000D5326 CRC64;
MAQAASAEPA ASKPEQSDEA QIEVKTEAKE EDTRDEKAHA EGEAGEEQDD AEAGEGQDGA
EVEEEQDGAE RPVSNEQYKA LKNITDVLTN HKIKLKGDED HFPSMLFRRI PNRRNLPDYH
EIIKDPVALS TLKGKIQRKQ YTGIPEFVRD FALIVHNAQI YNRPNSAPVR DVFELQKVFK
EELQKLVDEG LVKQEETVFP DLGEIPAATP EPDPVSEEED NDDAQEDDEE DEEEGDDSDD
DRRRRKSRKG GRASISGRKG GEETDEKLNE GDLHKRRGRP PKVDTPMEAR IKAILKGIRK
PKDKAGNMKI RHFERLPDKT EYPEYFLAIK DPIAVDTIKK KAKRKKYQSL EQFMKDLDLM
FNNAKQFNED GSEIYQDAVE LQAEAHKLLE IEKAKPDEEY LMEDGRRPLP SGILHKNELW
KVGDWVHIQN PNDVTKPIVA QIYRTWEDPE GQKWINACWY YRPEQTVHQY EKHFFPNEVV
KTGQYRDHRI EEVVDRCFVM FFTRYSRGRP RNIDPTKEVY VCEARYNEEK HKFNKIKTWA
SCLPDEVRDK DYEMDLFDTP RKIKKVPSPL KHLLKDDMKE TDETPSPTWG HPNAPPIIGA
IHKQPRDENQ SPPPEPTPPP PPTPPPQPVR PPSASTMQNI QSRPSMDRQT STGSAGNLQP
QLTRPSPSVA TPHMAASYPK QSISPAPQYG HRQTLYQQPQ HQHQHPQLQP NIAPQTPSTP
QQQPLPSYVP QQQLHPPPPN LATAAAAHHT APYGPGHAST PVAPNYVRPT QVQQQPAMYA
HAPNAVGVGE QRASEVYVLS ELANASIPKR IRDRFPQDDQ GRILFFTKPP VIHDWTVRGR
DGEPLVHTEK YLAAKVERDK IIATRKRARQ DDKVKVAAAS SFKRVKETRG PAVA
//
