ID A0A9W3BQG6_BIOGL Unreviewed; 2462 AA.
AC A0A9W3BQG6;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2B-like isoform X3 {ECO:0000313|RefSeq:XP_055901761.1};
GN Name=LOC106072824 {ECO:0000313|RefSeq:XP_055901761.1};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|Proteomes:UP001165740, ECO:0000313|RefSeq:XP_055901761.1};
RN [1] {ECO:0000313|RefSeq:XP_055901761.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR RefSeq; XP_055901761.1; XM_056045786.1.
DR GeneID; 106072824; -.
DR Proteomes; UP001165740; Chromosome 11.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd15545; PHD_BAZ2A_like; 1.
DR FunFam; 3.30.40.10:FF:000199; Bromodomain adjacent to zinc finger domain 2B; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.890.10; Methyl-cpg-binding Protein 2, Chain A; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; IPR028942; WHIM1_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; TOUTATIS, ISOFORM E; 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; 2.
DR Pfam; PF15612; WHIM1; 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; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP001165740};
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 548..620
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 852..917
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 2121..2171
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2175..2222
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2369..2439
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 92..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2257..2350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 689..733
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 112..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..307
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1080
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1091
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1612
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1916..1929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2267..2281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2289..2299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2320..2330
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2331..2340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2462 AA; 274194 MW; 268DA5CC32145FB4 CRC64;
MSKEEKKSSP SPSHGLLFDP SHLLGVHPLA ASGFPFPHLG PLSNPYSLLG QPPRFPALFG
GLGGIPNPLH AAALSHSLAA ASYFGLSKHH NEINSPPAPS PIPTAHKRGR SSRASTSSYK
QSSRLSPSST SPHTPSSPYL PPWSINGSTL PYSNLGAEPK SKSSSSSKRQ KLSAKSESRE
SSHSAPHAHQ QPHSSPLLTI PSAHSVQDHK PSTEKTDAFA FDPRAMITPY QMSPELAYMS
QSLFLHRPEL GLPSHFLASA AASLPAHVAS SSSSSSAVKN KEAGQRSSPS VPSSSKHSSS
KISSSSSKVD RSKVEKDRPT HHAESSKKHQ TTSNGIKNVD SKSAEPLDCT ADDKNLSDLA
IHMLDGDRKK QIAEHIRKRV GMYDLDEDIV RHGTKHSDWP YAEPSGEHRH NSDITEKQRD
LHLAEVHKNN DMLLEDLSVP HSSGKKLNLK LDSYLGKCDI TESESHKREE PLHNKSSYGE
ESMSSTLDES CESIGHSEHE ESKLDNSSAS ENVDVGSHSG SDSEDSGKNV AEGSTDEGSP
NKKKPPTQLD ERELIIPLEH GWNRQTIING MGRRGIVGEV LYFAPCGKKM KTIPDVMRYL
ERNPNSDLGR EHFSFNTKVN IGHFYEVRGG PDSQPVPLSD AEVLEKIEMS RGKRARMQML
ARQRREKAAR EQAMAQQVMD LKLKRRMELQ VLERRKEKEQ HKINKQQEKI RLQEQLRKER
ELKAQQIVEA RNRRQRELEE MRLADALQRN KERDMKRQQL VIMKEQERER RRQHLLLLKG
LEQRKRLEEK QTKERLREEK LHEKIKQKEI KLHQRRVEME IAMELKKPVE DMELKNAKPI
PEFPRIKSKL AGRPIADCLM AVEFLNNFGL ALNLEKSSIP TLESLERGIL NESDEDIEEF
MSLIMHLLRF ALDDVGVPNP KEAVTKLHQK ITEMEMTDTT MSEILRIFLK ARGEKEMMEW
LTEKPMEALN PTKKAAILAF LCNELLTSKV IANEIDKHMD AINNLRRDKW VVEGQLRQLR
VFQARKFNKI HKSTDRRPAI NSSISQDEDT MNSSKIGSDE DDDKDEEDDK EDDEGSESDE
SSSVITNSSS SNMPFEPVDE NLTKEESDKK IEKLRKQHAA YRQKVFRASL RLRAINIGQD
RYKRTYWILP LTGGVYVEGM ESGVPEDYVA EQAKKEEVKE QVTGSTDDES SDDTVMQVKK
ENCDPAVSGT GEKTADDCTT AREEERENFM GETICTELSP ACLDKVKVNL ASKLEDMSES
IHQSKLDSCD EDSTSMTVDE APSSFPYHVT SQTYTSINLT SFDKNLATSD KNLASSEKNL
ASYDSIQALI ANSPSQNVMM PCKLSPMVTN SASKDATDNT LDKKNDPMLK SPTNTITISK
PELSGSISEP ATYKHAFVSD ILKVPKIGGV DRGTLVTLLN NSIQQAYQEE ESESNSEMTS
TLVTTSSTPI LTSMPTVSPS LPSLLTSSLL FSAIPKLPQQ AHSATLDLTC KPKGQAPLES
SVITSTPVPA HSKPVNPQSL PPFHPSAQAN HLLDLPPPAA HSGYTKTPAL PPPGPPLPFT
QSPYHPNFSH YPFGPTSASE TLSSLASIVS PPPAHHNPVT TSSISSPLTT SSVQQPLTPS
FSPAKNVFPK LEKNDKDPLY SSSELLQQAA THVLRSAESV KSSPLSTITK SASLKTLSED
NDAVTSEVVD HKLWFSILPR MPCDELSLTQ RLPGQSPSLS QQSQQSISAS LSALTTYMNS
PTNANFDVLL PHIQSNPGLL SSDLLFTSIF NSPMTPSPSP TPCSTPGVDS AGEFKVPPPP
DMNLSSYPWE VLRAVQGEAQ PIPKRLQHGW WRIYDLAMLK EVMTCMLNRG IREKNLQRSI
HRYLDYAKLH CEFDTVKTEP ETTPDASQNN SDVKIKTEKQ SDDCQDDTST EPSAESEAKL
EEPAEEKVPV TENAAAVENA AATGAKEEVA VQTDKSSCDI NDFNPPDDPD WWSVSCLHQI
ELAALEEVEA LEERIFQASL QAKQGWKPNK DNSIIIVDRS VKSVADNESY PLDVAISRLL
ELEANIERRY LKPPLIRSVQ LNLSSLSQNE RCDGDFGESE SIPPGLLLWR QAVVGSESPA
QLSLCTQLLA KSISWEKSIM RVTCQICSKD DNEAELLLCD GCDKGYHTYC FKPKMDNIPD
GDWYCFECVS KASGTPHCVV CGAPGGRIVG CSKCPRHIHL ECLDPPLPRM PKRWQCCNCV
NEKGSSKRSK KRKESLPTVQ RISITKLVVK EEPIDAEEMS MASSSSCHTS PPVSFGSSSP
EKSARKNSVK SQETPQQQGA DKKKRKRKDK EEDLTSPPPP KKKKEKKEKK EKKSQEKVEE
LNGAVEENED NQANNKDLII CGKLLSELEK HEDGWPFLKP VNKKQFPSYK KYIKFPMDFA
TARGKIKSKE YKHRQEFAAD MRLIFNNCET FNEDDSDVGQ AGFKLRQFFE SRWLDMFPDD
AP
//
