ID A0A0A0AJL6_CHAVO Unreviewed; 2127 AA.
AC A0A0A0AJL6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2B {ECO:0000313|EMBL:KGL93658.1};
GN ORFNames=N301_09945 {ECO:0000313|EMBL:KGL93658.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL93658.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL93658.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL93658.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR EMBL; KL871848; KGL93658.1; -; Genomic_DNA.
DR STRING; 50402.A0A0A0AJL6; -.
DR Proteomes; UP000053858; 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; 1.
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:UP000053858};
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 682..757
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 1007..1072
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1892..1942
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2036..2106
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1771..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..2002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 827..909
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 85..113
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..227
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..603
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1240
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2127 AA; 235194 MW; 34649825D527739D CRC64;
MESGERLTSS SVSSTAAAST PASSTPSVAS AVSKGGLSSG AATLSSAINT CEWWRTVDTH
SRPGAAFFPP LLGIPPLFAP PAQNHDSASF HSRATGKNGR SSTEKGINGS LNGNSATAAS
GVSTSVLPTS IATSAGQVKA VTSGAGGRKY NQEQSKVQLL DTRADKIKDK KPRKKAVESS
SNSDSDSGSS SDTSSEGISS SDSDDLEEDE EEEEDQSAEE SEDDESDSEN EAHHKNKNKV
LMHSGITDMK NDGQKPHEKS QEKRTHQQIP LVSDSQTHSS FQSQQKQPQV LSQQLPFIFQ
SSQAKEESVN KHTSVIQSTG LVPNVKPLSL VHQAKKETYL KLIVPSPDLL KAGNKNTSEE
SLSLTSDVRS KREQYKQTFP AAQLKKQESS KNLKKVIAAL SSPKTTSSSP AHQKLTSLEN
NHSNPFLTNA LLGNHQPNGV IQSVIQEAPL ALTTKLKSQT KINESVAISS SAPFSMPVNL
SACGKKTTGN RTPVVPSTSP VLPGSGKDKT VSNNAVNAVK TQHRLHSAKL VVEQFRGVDS
DAPSSKDSDD SNDDDDDDED EDEDDEDDDS DDSQSESDSN SESDTEGSED EDDEDDKDQD
ESDTDTEGEK TPLKLNKTSS SVKSSSVGHA AHSTPLNLQA AKTPSSAPAA LCPESQPAVF
LGTAPSTLTP STHCGISKRR RVTDERELRV PLEYGWQRET RIRNFGGRLQ GEVAYFAPCG
KKLRQYPEVV KGVQWCLLKE EEVIPRIRAM EGRRGRPPNP DRQHSREESR MRRRKGRPPN
VGSTEFLDNT DAKLLRKLQA QEIARQAAQI KLLRKLQKQE QARAAKEAKK QQAIMAAEEK
RKQKEQMKIM KQQEKIKRIQ QIRMEKELRA QQILEAKKKK KEEAANAKLL EAEKRIKEKE
MRRQQAVLLK HQELERHRLD MERERRRQHM MLMKAMEARK KAENRHHRGQ EGLLELQIGL
NKERKLEQRR LELEMAKELK KPNEDMCLAD QKPLPELPRI PGLVLDGSAF SDCLMVVQFL
RNFGKVLGFD VNVDVPSLSV LQEGLLNIGD SMGEVQDLLV KLVSAAVCDP GLVTGYKAKT
ILGEHLLNVG INRDNVSEIL QIFMEAHCGQ TELTESLKTK AFQAHTPAQK ASVLAFLINE
LACSKSVVSE IDKNIDYMSN LRRDKWMVEG KLRKLRIIHA KKTGKRDATG GGDVGEEQHS
LETPTPGRKR RRKGGDSDYD DDDDDDSDDQ ADEDDEDEED KEDKKGKKAE VCEDEDDGDQ
TASVEELEKQ IEKLTKQQSQ YRKKLFEASH CLRSMMFGQD RYKRRFWILP QCGGIFVEGM
ESGEGLEEIA KEKEKLKKVE SIHIKEEEFE TEEKLHCLNT THCEQKEDLK EKDNTNLFLQ
KPGSFSKLSK LLEVAKMPPE SDIVSPKPNG SAANGCTLSY PSNSKTSLCS LQPSVSQGAV
EKSDSNNLFT PNASGAGKFY NSPLVPNDQL LKTLTEKSRQ WFSLLPRTPC DDTSVTQIDA
PAAAASLTPQ SHPPSKSPSP VPSPLLGSTS AQSPMGLSPF ALSPLQQMKT GLPVMGLQFC
GWPTGVLTSN VPFSSPLPAL GSGLGLSEVN GNSFLASSVP ASKSDSPALQ TEKTAPAPSA
AVEVAKPVDY PNPKPIPEEM QYGWWRITDP EDLKSLLKVL HLRGIREKAL QKQIQKHMDY
ITLACIKNKD VAIIDINENE DNQVTRDVVE NWSVEEQAME MDLAILQQVE DLERRVASAS
LQVKGWLCPE PASERDDLVY REHKSITRLH KKHDGDCAGG GEGNTSSLER RSDNPLDIAV
TRLADLERNI ERRYLKSPLS TTIQIKLDNV GTVTVPAPAP SVSGDGDGTE EDIAPGLKVW
RRALSEARSA AQVALCIQQL QKSIAWEKSI MKVYCQICRK GDNEELLLLC DGCDKGCHTY
CHRPKITTIP DGDWFCPACI AKASGQTLKI KKLQIKGKKS NEQKRSRKLA GDTEDEDSAT
TSTSLKRGKT DPKKRKMDEN VSVSQLKQEN FTAIKKPKRD DSKDLAICSM ILSELETHED
AWPFLLPVNL KLVPGYKKVI KKPMDFSTIR DKLSSGQYPN LEAFSLDVRL VFDNCETFNE
DDSDIGRAGH NMRKYFEKKW TEIFKVS
//
