ID A0A0R3RFI2_9BILA Unreviewed; 1590 AA.
AC A0A0R3RFI2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2B {ECO:0000313|WBParaSite:EEL_0000012001-mRNA-1};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000012001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000012001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 1147741.A0A0R3RFI2; -.
DR WBParaSite; EEL_0000012001-mRNA-1; EEL_0000012001-mRNA-1; EEL_0000012001.
DR Proteomes; UP000050640; Unplaced.
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; cd15545; PHD_BAZ2A_like; 1.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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:SF2; IP14655P-RELATED; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 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; 2.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
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; 2.
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 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 334..406
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 665..729
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1281..1331
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1335..1390
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1464..1534
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 78..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 906..933
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 79..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1590 AA; 177179 MW; 187F9B9E9F0114D4 CRC64;
MGDQAQQNFL ALLAAQAATQ NNVPMGLLFP NLNFGMANTV DMMFWNMAQL SQPGLLLQQQ
QQPQESFEEV FRRMATASAR SANIATGRQQ TSREADNTDS SESVLRPTGH FVSDVASTSS
ANVGIPTSSF PDSPTKGLEP GEIPKRRDGS RTRNGMSSQL SPASSSSSSS TGGVPLNSNL
LEASARCYAA LAASASQQQQ QQQSELIAAV LQSAVNYEKA RARAATTSSA AATASPSGSS
SGTQILKRTA LTHQHSNTGL SSCRKDESHR SCVVSAKVAS HEAMLTAPSS ARFTDSPLDL
SFHKSKNGAT GERSRIFSEH ASGADSDGSR KRTQADAALI RIPLKSGWRR QTCIRTISAS
GVRGDVIYYA PCGKKLGSYA EVTRYLTKKN IKDIGRENFS FSCKVIVGEY ILFKDDEDGS
KVPDRVSEER ILAEIANCSA TNTVRRTSGT HVKATLSSGT IEPSGTAAIS SDKNLPKLTD
DNALKQLHRQ FLRRQGEQQM YAQLLLTFGQ HVQQQRQFHQ QQQQQQKQQS SVITVEGKTA
ADEPEIKKLK VHFYFVVAFF TQLDHSESTA LRHVTPSVIP VAIPVIATTA ANIVSSHIAT
TTSNAAIAVC TAPSQEAKQP KIELSEEEKQ EERLKALRLP TDDLLIEEAR KLPTLDSIEN
LTVSASVFAN VLMVDEFVRN FGHVLKIDLN ALPTLNEFLA GLQNHPNHLK SFLLLTKILL
QLVLEYPGLP SGIAGRTPLG QALKDVGVHR ENYSELLKMF LLSRDEDGKK LGTKLECCSF
ECLDPESKAA ILAFLCNELL YCRNVVRDIE SNMEEMTRLK GEKWLREGKS RALRAVQTRK
RAALRRLRHD IRDDDPSSSR AGTPGSEPSD VSEEVEPALQ PSRLKALTPG LGQCDVLTEE
EEAMTVDELD EYIGKLNSEA EELRERHNTL INRVRIQPIG QDRFHRFYWV LPRLGVPLVE
SIASSGLHNP AVNVDITCRQ DPPSIIEDPQ NFIDPDVIAC VEDILDTLCG NEERPDRGKK
VRLRRLDNKC KRGWWMISNG KLMEQLRGAF HGRGIRERVL HRLLIKDNFT FTPSTQLKLE
SVNRPLTNNE INKAMIVRLA AHISSFEQKV VAANVHCRPM FPPGDSRDDD TESEDSVDAW
TLDDGYVLMD EAEVNEGCQL FEWNDFKALK DRLLEVERSI ERRSTIPAEK ILRAQQQNNQ
NGSSGDASSI MDVSEVQSEA SDSISSNGPF DGAAITVDES GNTELLQRWR DYVQEARTGG
QIMFALQALD SAIAWEKSIM KASCQICRTS ENESQLLLCD ACDMGYHMYC FRPRIAAVPD
GEWYCPLCVQ RACRKVVCLL CAKWNRPNSQ PFEPIIVCSK CYNGYHASCF DRPPTVNDPK
QWTCPGCLNA DGFSTELANS LLNGDVEIAL AQQEGQEKQT SCVQEDASGR QEPPRHRRRM
TPADYDFPLD MMKNLFNTML DELWARPESG PFQYPVDTKE VPFYKKVIKR PMDLNQIRMN
VESNKYMTQE SFIEDLEQIF ENCRTFNEDE SPIGQSGVTL HKFYLKRWKQ LRYNYSKRLK
RLKNPRLVHS VTLLPSSSPQ HISKNSEQPS
//