ID A0A091NXU5_HALAL Unreviewed; 1952 AA.
AC A0A091NXU5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 39.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2B {ECO:0000313|EMBL:KFP97697.1};
DE Flags: Fragment;
GN ORFNames=N329_12553 {ECO:0000313|EMBL:KFP97697.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFP97697.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFP97697.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFP97697.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR EMBL; KK644009; KFP97697.1; -; Genomic_DNA.
DR Proteomes; UP000054379; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR CDD; cd01397; HAT_MBD; 1.
DR CDD; cd15630; PHD_BAZ2B; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR037374; BAZ2A/B_Bromo.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028941; WHIM2_dom.
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; PTHR45915:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15613; WSD; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054379};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 512..587
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 832..897
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1717..1767
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1861..1931
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1781..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 665..795
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..57
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..433
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1065
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP97697.1"
FT NON_TER 1952
FT /evidence="ECO:0000313|EMBL:KFP97697.1"
SQ SEQUENCE 1952 AA; 218139 MW; CB8DCE6393EE4DE8 CRC64;
KPRKKAVESS SNSDSDSGSS SDTSSEGISS SDSDDLEEDE EEEEDQSAEE SEDDESDSEN
EAHHKNKNKV LMHSGVTDMK TDGQKPHEKS QEKRTHQQIP LVSDSQTHSS FQSQQKQPQV
LSQQLPFIFQ SSQAKEESVN KHTSVIQSTG LVPNVKPLSL VHQAKKETYL KLIVHSPDLL
KAGNKNTSEE SISLTSDVRS KREQYKQTFP AAQLKKQESS KNLKKVIAAL SSPKPTSSSP
AHQKLTSLEN NHSNPFLTNA LLGNHQPNGV IQSVIQEAPL ALTTKLKSQT KINESVAISS
SAPFSLPVNL SACGKKPTGN RTSVMPSTSP VLPGSGKDKT VSNNAVNAVK TQHRLHSAKL
VVEQFRGVDS DAPSSKDSDD SNDDDDDDED EDEDDEDDDS DDSQSESDSN SESDTEGSED
EDDEDDKDQD ESDTDTEGEK TPLKLSKTSS SAKSSSIGLA AHSTPLNLQV AKTPSSAPAA
LCPESQPAVF LGTAPSTLTP STHCGISKRR RVTDERELRV PLEYGWQRET RIRNFGGRLQ
GEVAYFAPCG KKLRQYPEVV KGVQWCLLKE EEVIPRIRAM EGRRGRPPNP DRQHSREESR
MRRRKGRPPN VGSTEFLDNT DAKLLRKLQA QEIARQAAQI KLLRKLQKQE QARAAKEAKK
QQAIMAAEEK RKQKEQIKIM KQQEKIKRIQ QIRMEKELRA QQLLEAKKKK KEEAANAKLL
EAEKRIKEKE MRRQQAVLLK HQELERHRLD MERERRRQHM MLMKAMEARK KAERLKQEKR
DEKRLNKERK LEQRRLELEM AKELKKPNED MCLADQKPLP ELPRIPGLVL DGSTFSDCLM
VVQFLRNFGK VLGFDVNVDV PSLSVLQEGL LNIGDSMGEV QDLLVKLVSA AVCDPGLVTG
YKAKTILGEH LLNVGINRDN VSEILHIFME AHCGQTELIE SLKTKAFQAH TPAQKASVLA
FLVNELACSK SVVSEIDKNI DYMSNLRRDK WMVEGKLRKL RIIHAKKTGK RDAAGGGDVG
EEQHSLETPT PGRKRRRKAG DSDYDDDDDD DSDDQADEDD EDEEDKEDKK GKKTEVCEDE
DDGDQTASVE ELEKQIEKLT KQQSQYRKKL FEASHCLRSV MFGQDRYRRR YWILPQCGGI
FVEGMESGEG LEEIAKEKEK LKKVESMHIK EEEFETEEKL HCLNTTHCEQ KEDLKEKDNT
NLFLQKPGSF SKLSKLLEVA KMSPESDIMS PKPNGSAANG CTLSYPSNSK NSLCSLQPTV
SQSTIEKSDS NNLFSPNASG TGKFYSSPLI PNDQLLKTLT EKSRQWFSLL PRIPCDDMSV
THIDTPATTT SLTPQSHPPS KSPSPVPSPL LGTSSAQSPM GLSPFALSPL QQMKTGLPIM
GLQFCGWPTG VLTSNVPFSS PLPALGSGLG LSEVNGNSFL ASSVTASTSE SPALQTEKTA
SAPSTAVEVA KPVDYPNPKP IPEEMQYGWW RITDPEDLKS LLKVLHLRGI REKALQKQIQ
KHMDYITLAC IKNKDVAIID INENEDNQVT RDVVENWSVE EQAMEMDLAI LQQVEDLERR
VASASLQVKG WLCPEPASER DDLVYREHKS ITRLRKKHDG DCAGGEEGNT SSLERTSDNP
LDIAVTRLAD LERNIERRYL KSPLSTTIQI KLDNVGTVTV PAPAPSISGD GDGTEEDIAP
GLRVWRRALS EARSAAQVAL CIQQLQKSIA WEKSIMKVYC QICRKGDNEE LLLLCDGCDK
GCHTYCHRPK ITTIPDGDWF CPACIAKASG QTLKIKKLQI KGKKSNEQKR SRKLAGDTED
EDSATTSASL KRGKTDPKKR KMDENVSVSQ LKQENFTAIK KPKRDDSKDL AICSMILSEL
ETHEDAWPFL LPVNLKLVPG YKKVIKKPMD FSTIREKLSS GQYPNLEAFS LDVRLVFDNC
ETFNEDDSDI GRAGHNMRKY FEKKWTEIFK VS
//