ID A0A3B3VIZ7_9TELE Unreviewed; 1837 AA.
AC A0A3B3VIZ7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2B-like {ECO:0000313|Ensembl:ENSPLAP00000025006.1};
GN Name=BAZ2B {ECO:0000313|Ensembl:ENSPLAP00000025006.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000025006.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000025006.1}
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; ENSPLAT00000001953.1; ENSPLAP00000025006.1; ENSPLAG00000011684.1.
DR GeneTree; ENSGT00940000155359; -.
DR Proteomes; UP000261500; 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; cd01397; HAT_MBD; 1.
DR CDD; cd15545; PHD_BAZ2A_like; 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; 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:SF8; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B-LIKE ISOFORM X1; 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; 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 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 496..567
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 827..892
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1604..1654
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1748..1818
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1080
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1837 AA; 206843 MW; 03411E858019A9AD CRC64;
MDTKLGLASS SPVPPSFLKG SPTFSSAPPQ PTSVKYSPAH SPEGNIPFTI FGQTHQTVDE
LSNMQSCPAF DLLNSSSNCP EFVHRGKMGL STTPTHTQFK VLPKLWRPTE MENCRGGAVF
HPLLGLHPFS VPVFKTHNPA DPQLYTSGVS RWNASSSDRN LNTSPLPPKE KEKTKIHSSW
SQNSLFERAQ HQKIILTTKE KDVMKRPLET PRCDVRLSGS LSESSSEEIS SDSDNMEKDD
EDLSSDSDDS DSEKDIQVGK KAVTQMDSVK QASFVRPKCQ IWNPELLLNP HFNGVVSTAD
QDAPLALITK PRVQADSPRK RLLLAATCPP YHTPVNLSIG TKKLFDTSAS PSKSAPSGLV
SGSVEAASVL HAGWRPTKTS SCLKPVDLTR SSGFEFHSSR GSETSGNIED DEENSLNSGS
SLSDSGSNPE SDSAEDHGKE FFKAESHTDA DRSAALLNLQ ISKHLGVPAT NSLHHHGNLT
PPLTFATAGL KKKRRVTDER ALQLPLKFGW ERETRMRTVF GRLQGEVAYF APCGKKLRQY
PDVVKYLVRH GITEISRDNF SFSTKVKVGN FYEGREGPEG LQWFLMNEED ISSCIIAMNG
RRSQRTKSKH QTANNVSAAQ HHHPAYYCEP PLQDISDSKL LRKLEAQEIA RQAAQIKMMR
KLEKQAIAQA SKEAKKQQAI RAAEERRKKR EEMKIHKQQE KIKRIQHIRM EKERRAQQVL
EAKRKKKEAA ANVKMLEAEK RNQERERRRQ HMILMKAVEA RRKAEEKERL RKEKKAEKQL
NKKKKLELRR LKQKKAKELM KPKEDMCLPD HKPLPELPGI PGLILPGKTF SDCLMVLQFI
RNFGAVLKLG LNSNQITISD LQDGLLNIGN SLQKVQDLLV SMLSAAVCDP GIPAGHKCKT
LLGDHLTNVE INQDNVSEIL QIYMEAHSEQ SEVAALAHSL ETKAFQAHSP SDKAAMLAFL
VNELCCSKAV ISQIDKNIDY MTNLRKDKWA LEGKLRKLRN IHAKKTDKRH TDGGEENHTF
SSVTVHNKCK RKSRSSEEEE DEDSEDQGED YDGQEEEMRR RKMKKSETCG EEEAARHSRD
ITELDAKIQK TCKLQSEISQ KLFEASHSLR SMVVGEDRYR RRYWLLPHCG DIFVEGVENE
LEEVEKDGGR QKASVRVKEE QQEKISQRRT ENVKTKAKRQ QNNDDGLLQK SFSKLSKLFE
AAKIDQNSNI DAKDARPSQV SITEPYHSCC TPETDKTSAP SALSAAQLNN NCMTWSPQSI
LPDNQLSAVL TEKSSEWFSL LPRAPCDGSS VVSNISCPAF ISSSQLVRTE SSSSPRKNTK
AGINRLHAAD SQEAEGNRDE DLCLADCNSV DKSETTEPLN NKPACASFSP LEVAKAQDYI
CPQPVPEEML RGWWRISDVE NLQSLVNSLH NRGIRERGLQ KQIQKNMEHT SQIYANRANE
FDTKDPEKQK ISREIFEGWC VEQRAVEVDG NLLLQVEALE KNVLSANLHI QGWMPSEPQY
NSDDLVCFEH EPLSSVSLDN KKWEETRQER LSGLLMRRSN SLLDVAVIKL AHLERNIERS
NKQEVAPGMR RWHKALGKIR SSAQLSLCIQ HLQKSVVWKQ DVMKVQCQLC QKGDNDELLL
LCDGCDKGCH TYCHNPKITM VPAGAWFCSS CESGQIPPSG EQQSQTAGGK HKSSEVKQNC
KPSVKGEHVS EEVASSNNMP RKGSKEFKKR KGEGSSEPRI DSLVSCAKRA KTPNSELAVC
RVLLAELEAH QDAWPFLRPV KLKSVPGYRK VIKKPMDFFT IKEKLINNMY LNQENFVIDV
NLVFDNCQKF NEDDSEIGRA GHRMKRFFDK RWTELLH
//
