ID A0A493TR94_ANAPP Unreviewed; 2113 AA.
AC A0A493TR94;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 2B {ECO:0000313|Ensembl:ENSAPLP00000028100.1};
GN Name=BAZ2B {ECO:0000313|Ensembl:ENSAPLP00000028100.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000028100.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000028100.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000028100.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR Ensembl; ENSAPLT00000047825.1; ENSAPLP00000028100.1; ENSAPLG00000015688.2.
DR GeneTree; ENSGT00940000155359; -.
DR Proteomes; UP000016666; Chromosome 7.
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; 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; IPR016024; ARM-type_fold.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
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; SM00571; DDT; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
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 683..754
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 1031..1096
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1917..1967
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2063..2113
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1796..1817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1978..2028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..604
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1980..2028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2113 AA; 233527 MW; 2908877159ADBBD2 CRC64;
MESGERLTSS SISSSAATSS PVSSTPSVPS AVSKGGLTTG AASLSSTINT CEWWRTADTH
SRSGAAFFPP LLGIPPLFAP PAQNHDSTPF HSRATGKNSR GSTEKGINGS LNGNSTTAVC
GVSTSVLSTS IAVSAGQVKT TTSGAGGRKY NQEQSKAQLL DTRADKIKDK KPRKKAVESS
SNSDSDSGSS SDTSSEGISS SDSDDLEEDE EEEEEDQSAE ESEDDESDSE NEAHHKTKNK
VLMHSGVTDM KTDGQKTLEK SQEKRTHQQI PLVSDSQTHS SFPSQQKQPQ VLSQQLPFIF
QSSQAKEESV NKHTSVIQST GLVPNVKPLS LVHQAKKETY LKLIVPSSDL LKAGNKNTSE
DSIPLTSDIR SKREQYKQTF PAAHLKKQES SKNLKKVIAA LSSSKSTSSS PAHQKLTSLE
NNHSNPFLTN ALLGNHQPNG VIQSVIQEAP LALTTKPKSQ TKINESVAIS SSTPFSLPVN
LSACGKKTAG NRTPVMPSTS PVLPGSGKDK AVSNNAVNAV KTQHRLHSPK LVVEQFRGVD
SDAPSSKDSD DSNDDDDDDE DEDEDDEDDD SDDSQSESDS NSESDTEGSE DEDDEDDKDQ
DESDTDTEGE KTPLKLNKTA SSMKSSSIGP AAHSTPLNLQ AAKAPGSAPA ALCPESQPAV
FLGTAPSTLT PSTHCGISKR RRVTDERELR VPLEYGWQRE TRIRNFGGRL QGEVAYFAPC
GKKLRQYPEV VKYLSRNGIM DISRDNFSFS AKIGVGDFYE ARDGPQGVQW CLLKEEEVIP
RIRAMEGRRG RPPNLDRQHS REESRMRRRK GRPPNVGSTE FLDNTDAKLL RKLQAQEIAR
QAAQIKLLRK LQKQEQARAA KEAKKQQAIM AAEEKRKQKE QIKIMKQQEK IKRIQQIRME
KELRAQQILE AKKKKKEEAA NAKLLEAEKR IKEKEMRRQQ AVLLKHQERE RRRQHMMLMK
AMEARKKAEE KERLKQEKRD EKRLNKERKL EQRRLELEMA KELKKPNEDM CLADQKPLPE
LPRIPGLVLA GSTFSDCLMV VQFLRNFGKV LGFDVNTEVP SLSILQEGLL NIGDSMGEVQ
DLLVKLVSAA VCDPGLVTGY KAKTILGEHL LNVGINRDNV SEILQIFMEA HCGQTELTES
LKTKAFQAHT PAQKAAVLAF LVNELACSKS VVSEIDKNID YMSNLRRDKW MVEGKLRKLR
IIHAKKTGKR DTTGGGDIGE EQQSLETPTP GRKRRRKGGD SDYDDDDDDD SDDQADEDEE
DEEDKEDKKG KKAEVCEDED DGDQTASVEE LEKQIEKLTK QQSQYRKKLF EASHCLRSMM
FGQDRYRRRY WILPQCGGIF VEGMESGEGL EEIAKEKEKL KKVESIHIKE EVFETSEEKL
HCLNTTHCER KEDLKEKDNT NLFLQKPGSF SKLSKLLEVA KMPPESDIIS PKPTGSAANG
CTLSYQSTSQ NSLCSLQPSV SQSGNEKSDS NNLFSPIPSG TGKFYNSPLI QSDQLLKTLT
EKSRQWFSLL PRIPCDDISV THIDTPATTT SLTPQSHPSS KSPSPVPSPL LGSTSAQSPA
GLSPFALPPL QQMKSGLPIM GLQFCGWSTG VLTSNVPFSS PLPAIGSGLG LSEGNGNPFL
TSSVPTSKSE SPALQTEKVA SASCTAVDVA KPVDYPNPKP IPEEMQYGWW RITDPEELKS
LHKVLHLRGI REKALQKQIQ KHMDYITMAC MKNKDVAIID INENEDNQVT RDVVENWSVE
EQAMEMDLAI LQQVEDLERR VASASLQVKG WLCPEPASER EDLVYHEHKS ITRLHKKHDG
DCAGGGEGST SSLERKSDNP LDIAVTRLAD LERNIERRYL KSPLSTTIQI KLDNVGTVTV
PAPAPSISGD GDGAEEDIAP GLRVWRRALS EARSAAQVAL CIQQLQKSIA WEKSIMKVYC
QICRKGDNEE LLLLCDGCDK GCHTYCHRPK ITTIPDGDWF CPACIAKASG QTLKIKKLQM
KGKKSNEQKK SRKLSLAGDT EDEDSATTST SLKRGKTDAK KRKMDENVSV SQLKQENFTA
IKKPKRDDSK DLAICSMILS ELETHEDAWP FLLPVNLKLV PGYKKVIKKP MDFSTIRDKL
TSGQCSTSTK ACL
//