ID A0A452S7F0_URSAM Unreviewed; 1928 AA.
AC A0A452S7F0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 2A {ECO:0000313|Ensembl:ENSUAMP00000028105.1};
GN Name=BAZ2A {ECO:0000313|Ensembl:ENSUAMP00000028105.1};
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:ENSUAMP00000028105.1, 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:ENSUAMP00000028105.1}
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 STRING; 9643.ENSUAMP00000028105; -.
DR Ensembl; ENSUAMT00000031392.1; ENSUAMP00000028105.1; ENSUAMG00000021587.1.
DR GeneTree; ENSGT00940000159490; -.
DR OMA; GMIMWER; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
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; cd15629; PHD_BAZ2A; 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; IPR017956; AT_hook_DNA-bd_motif.
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; IPR028940; PHD_BAZ2A.
DR InterPro; IPR028942; WHIM1_dom.
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:SF5; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2A; 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; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00384; AT_hook; 4.
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: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 553..624
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 866..931
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1700..1750
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1833..1903
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1779..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 748..787
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1928 AA; 213145 MW; D36D9F66A4D3D6F3 CRC64;
MEANDHFNFT GLPPAPAASG LKPSPSSGEG LYTNGSPMNF PQQGKSLNGD VNVNGLSTVS
HTTTSGILNS APHSSSTSHL HHPSVAYDCL WNYSQYPSAN PGNNLKDPPL LSQFSGGQYP
LNGILGGSRQ PSSPSHNTNL RAGSQEFWAN GTQSPMGLNF DSQELYDSFP DQNFEVMPNG
PPSFFTSPQT SPMLGSSIQT FAPSQEVGSG IHPDEVAEKE LTSVVAENGT GLVGSLELEE
EQPELKMCGY NGSVPSVESL HQEVSVLVPD PTVSCLDDPS HLPDQLEDTP ILSEVSLEPF
NPLAPEPVSG GLYGIDDTEL MGTEDKLPLE DSPVISALDC PSLNNATAFS LLADDSQTSA
SIFASPTSPP VLGESVLQDN SFDLNNGSDA EQEEMETQAS DFPPPLTQPA SDQSSTIQLH
PATSPAVLPT VSPAVSLAVS PAASLEISPE VSPVASPAVS PEISPVISPA AFPAVSPTSS
AALPPVSSEV SLTGSPVTSP KVSPAASPVA VLPTASPADK DVSTFPETTT DLEEITGEGV
TTSGSGDVLR RRIATPEEVR LPLQHGWRRE VRIKKGSHRW QGETWYYGPC GKRMKQFPEV
IKYLSRNVVH NVRREHFSFS PRMPVGDFFE ERDTPEGLQW VQLSAEEIPS RIQAITGKRG
RPRNTEKAKT KEVPKVKRGR GRPPKVKIAE LLNKTDNRLL KKLEAQETLN EEDKAKMSKI
KKKMKQKVQR GECQPTIQGQ VRASESFLSG LELSLQSAEK EKVKTKQEKL KEKVKREKKE
KVKMKEKEEV AKGKSACKAD KALAVQRRLE ERQRQQMILE EMKKPTEDMC LTDHQTFPLK
EPPRYPDCCL QPLPDFSRIP GLILPSGAFS DCLTIVEFLH SFGKVLGFDP AKDVPSLGVL
QEGLLCQGDS LGEVQDLLVR LLKAALYDPG LPSYCQSLKI LGEKVSEIPL TRDNVSEILR
CFLMAYGVEP ALCDSLRTQP FQAQPPQQKA AVLAFLVHEL NGSTLIINEI DKTLESMSSY
RKNKWIVEGR LRRLKTALAK RTGRPEIEMQ GPEEGLGRRR SSRIMEETSG MEEEEEEETI
ATVHGRRGRR DGEVDATASS IPELERQIEK LSKRQLFFRK KLLHSSQMLR AVSLGQDRYR
RRYWVLPYLA GIFVEGTEES LVPEDMIKQE TDSLKVAARP APSPAPSSLK KELAGSSTSA
STPTRARGRP RKTKPGSLQP RHLKSPSRDQ GSEQPDAQLQ PEIQPHPQLQ AQPQLQPPPQ
LQLHPQPQNG FLEPEGSPLS LGQSQHDLSQ SAFLSWLSQT QSHGSLLSSS VLTPDSSPGK
LDPTPSQPLE EPEPDEAESV PDAQAPWFNF SAQMPCNAAP TPPPAVSEDQ PALSPQQPAS
SKPMNRPGAA NPCSPIQLSS TPLPGMASRR RTGDSGGTPQ SLTGLGQPKR RGRPPSKFFK
QMEQRYLTQL TAQPVPPEMG SGWWCIQDPE TLDATLKALH PRGIREKALH KHLNKHRDFL
QEVCLRPSTD PIFEPSQLPA FQEGMISWSP KEKTYETDLA VLQWVEELEQ RVILSDLQIR
GWTCPSPDST REDLAYCEHL PDSQEDMTWR GRVREGLAPQ RKATNPLDLA VMRLAALEQN
VERRYLREPL WPAHEVVLEK ALLSTPPGAP QCATTEISYE ITPRIRAWRQ TLERCRSAAQ
VCLCLGQLER SIAWEKSVNK VTCLVCRKGD NDEFLLLCDG CDRGCHIYCH RPKMEAVPEG
DWFCAVCLAQ QVEGGFTQKP GFPKRGQKRK SSYELNFPES DSRRRRVLSR GRESPAVPRY
SDEGLSPSKR RRFSMRNHHS DLTFCEIILM EMESHDAAWP FLEPVNPRLV SGYRRIIKNP
MDFSTMRERL LRGGYTSSEE FAADALLVFD NCQTFNEDDS EVGKAGHIMR RFFESRWEEF
YQGKQANL
//
