ID K1VED7_TRIAC Unreviewed; 1090 AA.
AC K1VED7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Bromodomain and PHD finger-containing protein 3 {ECO:0000313|EMBL:EKD02370.1};
GN ORFNames=A1Q2_03322 {ECO:0000313|EMBL:EKD02370.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD02370.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD02370.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD02370.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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:EKD02370.1}.
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DR EMBL; AMBO01000288; EKD02370.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VED7; -.
DR STRING; 1220162.K1VED7; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_003589_0_0_1; -.
DR InParanoid; K1VED7; -.
DR OMA; ERPEHYI; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04369; Bromodomain; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR CDD; cd05839; PWWP_BRPF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13793:SF107; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00384; AT_hook; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 127..177
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 181..293
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 506..554
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 959..1026
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 299..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..831
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1090 AA; 121677 MW; 3D9D842E6B7B9B7F CRC64;
MSTMSSASGE KTYEIPTVSF RVITDDKSLL APAGVHSEQA RSYGYNDFSD FERPEHYIRY
IEPIESELAA QVEYDMDEQD QEWLDTVNAE RKKDQSGPVS YEVFEIIMDK LEKEWFTLPE
TNMPDGDSKC AICDDGEGEN SNAIVFCDGC NLAVHQDCYG VPYIPEGQWL CRKCTVSPEN
PVSCLFCPNE GGAFKQTTTG HWAHLLCAIW IPELGVGNAI YMEPVEGVDM VPKSRWKLHC
SLCKERVGAC IQCENKSCFT AFHVTCARQA GLLMSMKLMG ADGQLKAYCE KHLPSYHETS
ESDVFEDEEE EEEVVTPPPR KRGRPRKNSI RNTSGGQPKR PRGRPPKHRK EEEEQAVVVA
DKKRKVTTKS ARAHAKSYRP GPPIVPRMIV NKLLDYIGKI SIRKKQPFVE RLCRYWSLKR
EARRGAPLLK RLHLEPWTAT TESKEQTDAE KAKNLEFLGM LRNDLEKVRM LAELVRKREK
EKLRQAQVIK EVVDSFIFPH YETLRSTMDR GELFLQPVTL EEAPDYYDVI KEPISWTQID
AKLKSVKYLN VADFKYNKSE TSFHRTASRI KKNAAPLLDA LNSIPAAGQL MPPAPEEDHA
RPRSLRDRPR GGARHAALDL RFRGREGAAS APFSQEAEDN VCRRAHKKFE QAEERYKERL
SMGGGSTRVS RAAAAATIPE SPPPTTGRRK ASEETSETSR RSQPGVVGVT SVPAMSERER
RQAEKNLDLI AESLDSKDEY ERFNIGWILP EGSKRRRPAP VTVPPPPKRS TSRAASSVSG
ASERNKRQRT STPIDAPASK KRKGAEPEPN KEEEKAEEED VDAEGEDEEL TPVPDSAVTP
NFPRSSLSPP PADADGEADD AASDKTAVEQ PSKSKSEKDA TPVPEKATKD EPMDVDADAD
GDTKNDPKTP KTPAGQEGST AESTPAKDRR KSLVAPKPAL PADGSDPYPP GTQEKLTSVW
AKVTSYPYFP GVVIDPRADP SIVPPSVLAL EAEETKSGRA WLVRFHDKQG SWGWMHPERI
EALGQDDEVD KMYLAGKERS RNKGFKSSHL KASCKAAYQK AMEAQDPTRT ESSGNKEKEA
EAKSEKQVSV
//