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Database: UniProt
Entry: A0A3B3T3X3_9TELE
LinkDB: A0A3B3T3X3_9TELE
Original site: A0A3B3T3X3_9TELE 
ID   A0A3B3T3X3_9TELE        Unreviewed;      1404 AA.
AC   A0A3B3T3X3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Bromodomain adjacent to zinc finger domain 1B {ECO:0000313|Ensembl:ENSPKIP00000037026.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000037026.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000037026.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR   Ensembl; ENSPKIT00000017980.1; ENSPKIP00000037026.1; ENSPKIG00000015274.1.
DR   GeneTree; ENSGT00940000156831; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0090535; C:WICH complex; IEA:InterPro.
DR   GO; GO:0140801; F:histone H2AXY142 kinase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15628; PHD_BAZ1B; 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; IPR047174; BAZ1B.
DR   InterPro; IPR047256; BAZ1B_PHD.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR018501; DDT_dom.
DR   InterPro; IPR028942; WHIM1_dom.
DR   InterPro; IPR028941; WHIM2_dom.
DR   InterPro; IPR013136; WSTF_Acf1_Cbp146.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46802; TYROSINE-PROTEIN KINASE BAZ1B; 1.
DR   PANTHER; PTHR46802:SF1; TYROSINE-PROTEIN KINASE BAZ1B; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF10537; WAC_Acf1_DNA_bd; 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; SM00249; PHD; 1.
DR   SUPFAM; SSF47370; Bromodomain; 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; PS51136; WAC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00475}; 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:PRU00175}.
FT   DOMAIN          24..130
FT                   /note="WAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51136"
FT   DOMAIN          566..630
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   DOMAIN          1127..1177
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1130..1174
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1290..1360
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          148..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1188..1219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          499..541
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          799..841
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        148..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..773
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1192..1219
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1404 AA;  161482 MW;  B4B70C2812429D28 CRC64;
     MAPLLGRKPY PLIKPIAERP GPGEDVYIIE HTKEAFRNKE EYEARLQKYS ERIWTCKSTG
     SSQLTHKEAW EEEQEVTELL KEEYPAWFEK PVLEIVHHNT VSLDKLVDQA WLEILTKYAV
     DEECDFLVGK EKSLRVKVVK VHPLEKSEEE TPEKKLDGAC DSPSSDKENA SQENQKKDSS
     KEEDGKRESL CERARRSPRK LPTNLKEEKK KWVMPKFLPH KYDVKLINED KVISNVPVDS
     LFRTERPPNK EIMRYFIRHT ALRLGTGESS PWVVEDELVK KYSLPSKFSD FLLDPHKYFA
     ENPTAKRRSL STSELKKKKK MNGSPLKVKN SGTPKKFGDG GEAGDVILLT PGFQKGPKSS
     KKQGDKKQSE PKKSRKSGVR NSSNQKTKKD GKGVKSPKMK QMTLLDVAKN RSSVSPKKKA
     RSTQGTPKLG KPLPPMALHL LRYYKENKGK EDKKSALSSL ISKAAKVLTP EDRGRLPEEV
     RVMVQKRWEL LEQKRRWAAM SEEERQDELR RKREELKEKL REKAKERREK EMLVRREQQR
     RYEDQELEGK SLPNFRLVDM AEGIPNTLFG DVAMVADFLN CYSDLLMPDD QYTVTAAGLM
     EALGTERGGF FYLNRVLVIL LQTLLQDELA EGYRELDMAL SDIPLTMHSA SELVRLCLRP
     QDACADGSTS EDSADPDPDD AVSTEILEKL ETSEVFELSP QEKAVLLVAL CHRILMTYSV
     EDHVEAMQQR SAELWKERLA TLKEVNDRKR AEKQKRKEEM EAKGKEGGGK KDPPKAKSLP
     PPAESEPDDL ISTVKSRRLQ TIQAKKEKEE QERINKERMV KEAEEERVRK QKAAAERTFQ
     EGIRKAKLVL RRVPLGTDRN HNRYWLFSDV VPGLYIEKGW VHESINYSFT PSPEEVKEEP
     SVEGETPRRH FRLACHVASS VETSVPKHGQ NLWFVCDTTR ELEELMGSLH PQGVRESELK
     SRLQYRYQDI LRSICLARKP NLGLKTCDGQ QELLKYLRSD IMEVASRLQK GGLGYMDDIS
     EFEEKVRSLE NLKDFGECVI TLQESVIKKF LQGFMAPKQK KKRKQAGEES SKAEEPDEEK
     KLSEEARVAT AVERWKTAIR EAQTFSRMHV LLGMLDACIK WDLSAENARC KVCRKKGEDD
     KLILCDECNK PFHLFCLRPV LYSIPDGEWL CPACLPAGAR RCSRGRNYKE ESEEEEDSEE
     ESEEEEDDPQ EEEEEEDDDF KLLFHTLQGR LSRGPRPLCE PSRASSFPSL IIAVAXPPPP
     PTQVRQSSRM GGRRHNVELE KCEDVLQKLI KYRCSWPFRE PVSPEEAEDY LDIISHPMDF
     QTMLQKFAEG QYRHSSDFLE DMKLVFSNAE EYNQPGSVVL SCMAKTEQTF VELLHRMVPG
     LSYLRRRPRR RQGSRPLGCS IMVP
//
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