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
//