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Database: UniProt
Entry: A0A0C3P1M9_PISTI
LinkDB: A0A0C3P1M9_PISTI
Original site: A0A0C3P1M9_PISTI 
ID   A0A0C3P1M9_PISTI        Unreviewed;       783 AA.
AC   A0A0C3P1M9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Bromo domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M404DRAFT_1003270 {ECO:0000313|EMBL:KIO01239.1},
GN   M404DRAFT_1006035 {ECO:0000313|EMBL:KIN97398.1};
OS   Pisolithus tinctorius Marx 270.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO01239.1, ECO:0000313|Proteomes:UP000054217};
RN   [1] {ECO:0000313|EMBL:KIO01239.1, ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIO01239.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIN97398.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KIO01239.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIO01239.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KN832029; KIN97398.1; -; Genomic_DNA.
DR   EMBL; KN831990; KIO01239.1; -; Genomic_DNA.
DR   STRING; 870435.A0A0C3P1M9; -.
DR   HOGENOM; CLU_007728_1_0_1; -.
DR   OrthoDB; 1334586at2759; -.
DR   Proteomes; UP000054217; 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; 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; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF47370; Bromodomain; 2.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054217}.
FT   DOMAIN          26..96
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          390..515
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          116..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  85990 MW;  95EEFEA9F02CB4F1 CRC64;
     MAITSTQKSA IEDIINILVA ATPSRGKRKM ADMFLDLVDR SDWPEYYEVI PEPRCINGVR
     ANVEKNRYKD PLNAYTDLSL VFWNALFYNE PGSQIATDAE TLKNILVTEW QKRTVLPSPR
     LSPPPASPQK VHKALASAQP QLGQPAAAAA IKPDPSNSKL APSQLASSPE MDVDVNGMSP
     EPEGQSEEAG MGSVAGDGDG DSETIIRQLE QSLPRWDGFG DSGWMSEINK DRLLDLVVAI
     KSHKDVVGNR LAVALEAVPE EPTSPLLSYQ SHLSLKIMEG RVRSGSYESA KAFDLDMARL
     FEKARRWHEP CTEPYGHVLL LQRLYHALTS SSPPSGPPYT STTNFASIRA GPGTARPLHS
     TDSEGVPGVT TFRVSNKDRT FVEEVHYKGW SVRLADWLHL SNPDDPSRPI VGQVFKPWLS
     DDPAKKGQPG VTVCWYYRPE QTFHPAHTMF MEKEVFKTSH FADHPVEDVI EKIACQFTAR
     HIRGRPRPPF WYPGWPLYVC HSRYNDRERL FVKIKNWSSC IPEEVRKKEE FMPIYAFERL
     VYPPKVGSPF VGGKNTVKGP GGIGEPVERA EGEKIEGGGT GRKRAKRNNA ATAEGTAVAG
     TSSSATLIRP AATLAGTSSA LPSYYSQQAG QAQKAHGAAT GTDAKDRTML TAAGNLSVPP
     VVDKLPPETT KYFDRSPETN ELLWFGAPPL NVARPPAVKH SLTYLHFLAR KRKEMDKSES
     NADADAADNA IMDVDHSDNN GAEGSNRGGP HRATAKRLRG TVPPTVTEMM KTALDAVSGQ
     LEQ
//
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