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Database: UniProt
Entry: S8AUH7_DACHA
LinkDB: S8AUH7_DACHA
Original site: S8AUH7_DACHA 
ID   S8AUH7_DACHA            Unreviewed;       875 AA.
AC   S8AUH7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS44621.1};
GN   ORFNames=H072_1412 {ECO:0000313|EMBL:EPS44621.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS44621.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS44621.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS44621.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPS44621.1}.
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DR   EMBL; AQGS01000041; EPS44621.1; -; Genomic_DNA.
DR   RefSeq; XP_011107404.1; XM_011109102.1.
DR   AlphaFoldDB; S8AUH7; -.
DR   STRING; 1284197.S8AUH7; -.
DR   eggNOG; KOG1827; Eukaryota.
DR   HOGENOM; CLU_332019_0_0_1; -.
DR   OMA; QKWINAC; -.
DR   OrthoDB; 1334586at2759; -.
DR   Proteomes; UP000015100; 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:0006338; P:chromatin remodeling; IEA:InterPro.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:UniProt.
DR   CDD; cd04717; BAH_polybromo; 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; IPR018359; Bromodomain_CS.
DR   InterPro; IPR037382; Rsc/polybromo.
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; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT   DOMAIN          31..101
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          266..336
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          383..502
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          122..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..198
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..603
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   875 AA;  99802 MW;  6A4B2E14709EC972 CRC64;
     MPSAAPQRAS DADLARMKAI IDTIMEFKDE NEVLIADVFM EIVSRRALPD YYRIIKSPIA
     LMTIQNKLKQ KRYAGFKDFI NDAARVFHNA KTYNRPSSQI YKDAVTLEGV LLGELNKLTK
     LEEPPLTAEE AVLPDLGPLP TTESEGEDDG TGEEGSNEGS GDEEDEEEGD GEEEDEDEEM
     EDADAPKNED DGENDSDEEE EGNRTRRSSR RTVKKSSGGD DGDEDEEKKD RKKEPKKRGR
     PPRVDAPYEC RIKGILKGIR KFRTKDDQPL HAPFEKLPDI KTTPEYYRYI TNPVAIDTLK
     KKVKRRQYDT VEGFMEDVYT MFDNAMEYNE DASEIYRTAK QLKDEAKKFY DIEIAKPDSD
     FVEANSKGNQ DREPVPYIDL KGDRFVVGDW IELVNPLDDE KHIVAQIFRV FKKRIDGLLG
     INVCWYYRPE NTVHRVNKRF FENEVAKTGQ YRDHPVDDIV GRCFVMFYTK ASRGRPKNSA
     GKNIYICEAR YNEEKCLFNR IKTWKSCIPD EVRNHPDDTE YWDKQVPLKK FESPIKHLLP
     ADAKFGDKLP KAKWIRDDAP PEGAVYIGAR RPNDSPSPEP TPPPKPKSPT PPPPPPPQAV
     PPSQPRSSRR AAVPQPQQAP ATPMAHRQYP PQQQAQLAPM PSPYGQYTPQ HQQAGYYQPP
     QPQIQPHYQQ PHSPFVSQMP TINTPGHGHA NIIQAPVADQ QDMPGEPISF TIDADWSPQV
     LDKLRLTEHG LPMFHTVIPQ NNPGHKVSFE QWGERFSSGG VPLRKLDFTL RGVVNRMKQA
     HTYGIPFDAD QQIIWKDAST ILEEFMARER AANSTAMENR NFLTAITYPL EQAVQKFLAE
     KPEGYQLNSK LYDAETLNEY KAKKRKREAE ESEAA
//
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