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Entry: A0A0P1BEB4_9BASI
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ID   A0A0P1BEB4_9BASI        Unreviewed;      1287 AA.
AC   A0A0P1BEB4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Phd finger and bah domain protein {ECO:0000313|EMBL:CEH14168.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH14168.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH14168.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CCYA01000240; CEH14168.1; -; Genomic_DNA.
DR   STRING; 401625.A0A0P1BEB4; -.
DR   OrthoDB; 1409291at2759; -.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15571; ePHD; 1.
DR   CDD; cd15497; PHD1_Snt2p_like; 1.
DR   CDD; cd00202; ZnF_GATA; 1.
DR   Gene3D; 2.30.30.490; -; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR029617; Snt2.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR47672; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR   PANTHER; PTHR47672:SF1; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00249; PHD; 3.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          54..187
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          224..276
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          874..1006
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          848..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1199..1267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1287 AA;  139063 MW;  2A079219F1EFF537 CRC64;
     MTAAPLASSS SSRVPVASTS SSSTTGEDAA TSRTSNGSFK QQAPVTRVTV RNGLTIGIND
     YVYLSVPWAP GAGEPFIIAR VMEFVLASSS RSGAAALLSS SGTLQLRANV FLRTRDISHR
     VSNDPRLLVG TMKSDVYALE NVRGLCEVRH RDLLGDAPEV SAWKKKDDHF YFHQIYDGYI
     HRFYDVIPTE KIKNAPPAVL NLLRSRYSFI VAEVGMTPDL CDALRGCAVC HRWASSPESV
     RCDTCKKFFH MRCLTPPLAS KPAKGYSWTC APCSKRHEQD VESTISGGLS ASALAAGTSS
     LSRLPGTQGA IRGVPSGNGV KARGPGRGRA SGIGTPTDPS PDSSPAPVAR TIDDIRGTRC
     FNRWPYRYFG QHTEAKDVLD PHDSIYPRAA TRLGPKYQAA PPSWKEQLEL GLGVQGRTSD
     DAEGGGAGNG LPIEEGGPPP KKKGGRPPKR KRPEAERSDT PQAQLTPTLS TVKLPADPPA
     RDFERGTDES VEVIWQPQLK PGKIVDAFFI GARQLFAHIP AHDVDFMDRA LQVLASRAGN
     PALGLQALSA STPEDFRQVH WSQKETRQFD QVMKDYNADM RQLKKAVPTK TYGEIVRQFY
     SWKCKRLREV LDKEAQEEAE LASKTGKVVR KSGAQSLAPA PTPPSTRAVS PSLSVFGDAS
     ISNPTCYMCS THQSQVWYKG PYSWPNRYLC THCGLYWRKY AAESTSTQEL VAINTRQKAA
     ALNAAGDEEL GVQPPAKSAK MSKTASARAA AARTTPPTRA APVAPPPPPP KPDPIKCVMC
     DKMEPKKTLQ QCRQCTLSVH KGCFGLTDEE VAAEWWQCEA CSNEKALDAA LTPGCVLCPS
     LPRAKSIGTT DAADQGDKAL SRARKGGVDA NGTDESATGT PTVLDAVKPT EGNNWVHLIC
     AAFIPEIVFT DPARLRLVEG VGNLQWWRYN SECDLCKTRF GACVSCAEPS CRKTMHVSCA
     WTAQPSVCML FDFTAVKVSR KDIVPTASFK GESGHINAML WCKEHKHIGE SKKPTTHQLT
     DIDPETGKTL LQIYAETHKH TASPGIPREV VAAADQAYAL LRRARRYDLM LSKTNTTSVV
     HGPPLASEMA RIDEEHAVQA YRPDPELLPA LTRAPAKNHK IPAGSAENVV AKRATTTPVP
     IGHLGRQATP ASSGAPPSLF GMKPKRRCAK CSAHSSPFWW PAPPSGPTKL DQLDAVGEAK
     DQPGASSGHA MKPEKRSPSI ALAERQDVDS PMRSVSEGAF EGEDQQASIK ASPVPPTPSS
     TTNDSSLPAY LCNVCAHENG MVDDALE
//
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