ID A0A452SGU7_URSAM Unreviewed; 1784 AA.
AC A0A452SGU7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 2B {ECO:0000313|Ensembl:ENSUAMP00000031678.1};
GN Name=BAZ2B {ECO:0000313|Ensembl:ENSUAMP00000031678.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000031678.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000031678.1}
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; ENSUAMT00000035332.1; ENSUAMP00000031678.1; ENSUAMG00000024238.1.
DR GeneTree; ENSGT00940000155359; -.
DR Proteomes; UP000291022; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
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 409..484
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 668..733
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1547..1597
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1693..1763
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..901
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1784 AA; 199452 MW; DBCA4894C8143426 CRC64;
PRKKAMESSS NSDSDSGTSS DTSSEGISSS DSDDLEEDEE EEDQSIEESE DDDSDSESEA
QHKSNNQVLL HGISDPKAEG QKATEKAQEK RIHQPLPLVS ESQTHSSFQS QQKQPQVLSQ
QLPFIFQSSQ AKEESVNKHT SVIQSTGLVS NVKPLSLVNQ AKKETYMKLI VPSPDVLKAG
NKNTSEESSP LTSEMRSKRE QYKQTFPAQL KKQESSKSLK KVIAALSNPK PTSSSPAHPK
QTVENNHPNP FLTNALLGNH QPNGVIQSVI QEAPLALTTK TKMQSKINEN IATASSTPFS
SPVNLSTSGR RTASNQTAVI PSASPVVHPQ GKEKAVSNNA SMVKTQHHAH PAASLVEQFR
GTDSDIPSSK DSEESNEDEE EDDEEEDEED DEDDESDDSQ SGTSKRRRVT DERELRIPLE
YGWQRETRIR NFGGRLQGEV AYYAPCGKKL RQYPEVIKGM QWCLLKEEDV IPRIRAMEGR
RGRPPNPDRQ RAREESRMRR RKGRPPNVGS AEFLDNTDAK LLRKLQAQEI ARQAAQIKLL
RKLQKQEQAR VAKEAKKQQA IMAAEEKRKQ KEQIKIMKQQ VCLCERERRR QHMMLMKAME
ARKKAEEKER LKQEKRDEKR LNKERKLEQR RLELEMAKEL KKPNEDMCLA DQKPLPELPR
IPGLVLSGST FSDCLMVVQF LRNFGKVLGF DVNIDVPNLS VLQEGLLNIG DSMGEVQDLL
VRLLSAAVCD PGLITGYKAK TALGEHLLNV GVNRDNVSEI LQIFMEAHCG QTELTESLKT
KAFQAHTPAQ KASVLAFLIN ELACSKSVVS EIDKNIDYMS NLRRDKWVVE GKLRKLRIIH
AKKTGKRDTS GGIDLGEEQH PLGTPTPGRK RRRKGGDSDF DDDDDDDSDD QADEDDEDEE
DKEDKKGKKT DICEDEDEGD QAASVEELEK QIEKLSKQQS QYRRKLFDAS HSLRSMMFGQ
DRYRRRYWIL PQCGGIFVEG MESGEGLEEI AKEREKLKKA ESIQIKEEIF ETSEDTLNCS
NPDHCEQKED PKDNTNLFLQ KPGSFSKLSK LLEVAKMPPE SDVMTPKPNS STNGCALSYQ
NSGKHSLGSI QSTATQSNME KTDSNNLFST GSSGPGKFYS PLPNDQLLKT LTEKNRQWFS
LLPRTPCDDT SLTHADVAAA SVVTPQSQPP STSPSPAPAP LLGSSSAQTP VGLNPFAVSP
LQMKSGVSMM GLQFCGWPTG VLASNIPFPS PLPSLGSGLG LSEGNGNSFL NPNVASSKSE
SPVPQNEKVS ATQPAPVEVA KPVDFPSPKP IPEEMQFGWW RIIDPEDLKA LLKVLHLRGI
REKALQKQIQ KHLDYITQAC IKNKDVAIIE LNENEENQVT RDIVENWSVE DQAMEMDLSI
LQQVEDLERR VASASLQVKG WMCPEPASER EDLVYFEHKS FSKLCKEHDG EFTGEEESSA
HALERKSDNP LDIAVTRLAD LERNIERRYL KSPLSTTIQI KLDNVGTVTV PAPAPSISGD
GDGIEEDIAP GLRVWRRALS EARSAAQVAL CIQQLQKSIA WEKSIMKVYC QICRKGDNEE
LLLLCDGCDK GCHTYCHRPK ITTIPDGDWF CPACIAKASG QTLKVKKLHV KGKKTNESKK
GKKVTLTGDT EDEDSASTNS SLKRGNKDLK KRKMEENTSV NLSKQESFTS VKKPKRDDSK
DLALCSMILT EMETHEDAWP FLLPVNLKLV PGYKKVIKKP MDFSTIREKL SSGQYPNLET
FAVDVRLVFD NCETFNEDDS DIGRAGHSMR KYFEKKWTDI FKVS
//
