ID A0A1B8AFC9_FUSPO Unreviewed; 894 AA.
AC A0A1B8AFC9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=BAH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPOA_10911 {ECO:0000313|EMBL:OBS19187.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS19187.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS19187.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS19187.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) 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:OBS19187.1}.
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DR EMBL; LYXU01000004; OBS19187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8AFC9; -.
DR STRING; 36050.A0A1B8AFC9; -.
DR OMA; QKWINAC; -.
DR Proteomes; UP000091967; 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; 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; IPR018359; Bromodomain_CS.
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 PRINTS; PR01217; PRICHEXTENSN.
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; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Reference proteome {ECO:0000313|Proteomes:UP000091967}.
FT DOMAIN 81..151
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 281..351
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 393..512
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..58
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 101194 MW; A51A203E9A1821FA CRC64;
MSTRRTNATE VRESIEAKTA STDIEMKDAV DNDVDAEGDP DVDMDAEGDE DAEGEVDDEG
RPDMYRLIHN LSTYLCSVED DGEQLAAGFQ RIPNRRALPD YFEIISEPIA FSTIRGKTQK
KQYSSFAEFV KDVAQICHNA QVYNRPSAPI FGAAVRLRET LVRELQKLVE RGHITASDTQ
LPDLGELPPA EESPPAEDDE DDEDEDDDED EDDEEDDDDD SEDEGGRPRG RRRRASGRKD
QDKDYEDDSH KRRGRPPSVL TPNEARITSI LKGLRKPRDA AGHLLVHPFE RLPDKAAVPD
YYTTIQNPIA LDNIKRKVKR KKYQNVDQVL QDLNLMFENA KRYNEDDSEV YRAAVELQNE
AQLLAEQEKA KPDDDFRDED GKLPLAEIQY NEQSWKVGDW VHIRNPNDLA KPTVAQIYRT
WQDRAGQRWI NACWYYRPEQ TVHRHEKHFY EHEVVKTGQY RDHQIEDVLD HCFVMFVTRF
NKGRPRGFPR GKEIYTWASC VPDEVRDKDY EMDLYDVPRR MRKIPSPIKH LLREDAKETD
ELPKPTWGSP NAPPIVGAVH RRPREINESP PPEPTPPPQA MSAIPLSDAG TDAGRRASML
SVPGAMPGDH SARHPSMSYP GGPSPSPVPY NAHMTPHFQP VTPGAQPQQV HQTPVPIPHP
PHLGPQPQVS VRPVQYQHQP QHQQAGYTQS FAPNYGQPVP PMHQQTPMGN HITPAYNQAP
APPVARSPMA PTPGMPVQSG NAYNPPRPPE VYALPDSMND ALQQELRQTF QHDSAGRVLF
FTAPPLERSH KGISHESAGL GHSVKYLAGR KEWLAEREKK RKERDEKTGE ISQKRTEKDA
ADAHEAGKAI VAQASDVMAK WLEQYEHDTQ RWTTQTGLEG WRDATKANKG RGAV
//
