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Database: UniProt
Entry: K1VED7_TRIAC
LinkDB: K1VED7_TRIAC
Original site: K1VED7_TRIAC 
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
//
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