ID A0A3P9BLG7_9CICH Unreviewed; 1416 AA.
AC A0A3P9BLG7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 1B {ECO:0000313|Ensembl:ENSMZEP00005010767.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005010767.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005010767.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005010767.1}
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; ENSMZET00005011144.1; ENSMZEP00005010767.1; ENSMZEG00005008055.1.
DR GeneTree; ENSGT00940000156831; -.
DR Proteomes; UP000265160; LG14.
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}; Reference proteome {ECO:0000313|Proteomes:UP000265160};
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:PRU00175}.
FT DOMAIN 24..130
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 584..648
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1139..1189
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1142..1187
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1289..1359
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 148..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 516..553
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 816..860
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..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1416 AA; 162167 MW; 6003F167326C7DCE CRC64;
MAPLLGRKPY PLAKPLAEPP GPGEEVYIIE HTKEAFRNKE EYEARLQRYN ERIWTCKSTG
SSQLTHKEAW EEEQEVTELL QEEYPKWFEK PVLEMVHHNT VSLDKLVEMA WVEILTKYAV
GEECDFLVGK EKSLRVTVVK IHPLENTEGE SGEKKLEGAC DSPSSDKENA SQENQRKEPP
PREENRRESL SDRARRSPRK LPTAMKEERK KWAMPKFLPH KYDVKLINED KVICDVPADS
LYRTERPPTK EIMRYFIRHY ALRLGMGESA PWVVEDELVK KFNLPSKFND FLLDPHKVSL
NPSTKRKSLS SPEGKPNKKL KTKDALGMPL SPTIWGHMQV SQLKIKMNGS PLKVKNSGTP
KKGEGKGSAP STPKSGKKSG DKKEGKKTGK SGEKKLNVLK ASKKDGKAGA KGPKMKQMTL
LHLAKSGAAG SPKKRARSSG IGTPKLGKPL HPMALHLLRY YKENKGKEDK KNSLSSLISK
AAKTLSPDDR SRLPEELKEL VQKRWELLEQ KKRWAAMSEE EKKEEMKKRR EELKEKLREK
AKERREKEML VRREQSRRYE DQEIEGGKPL PAFKLVDMPE GLPNTLFGNV AMVVDFLHCY
SGLLMPNDQY PITAAALMEA LAGERSGFLY LNRVLVVLLQ TLLQDELAEG YSELDMPLSE
IPLTMHSASE LARLCLRPCD AHGEESGQGS EDSGAMGGYD DVVTSEFLDK LETTEVFELS
PEEKVTLLVA LCHRILMTYS VEDHVDAMQQ RSAELWKERL AMLKEANDRK RAEKKRRKEM
ENKGEKKKEG SSKKEVKKEV KVEPEPEDMI SSVKSRRLMA MQAKKEKEEM DRQNKERMEK
EAEEERMRKQ RAAAERAFQD GITKARQVMR RTPLGTDRNH NRFWLFSDVV PGLYIEKGWV
HESIDYRTEK DDGSVDGAVS EGAQQGAAPD VCIETTVPKQ GQNLWFICDS SAELEELVES
LHSQGVRESE LKSNIQSRYQ EILHSIHLTR KARLGLRTCD GYAELLKYLR SDIQEVASRL
QKGGLGYLDD NVDIEDKVNN MESLKDFGEC IITIQACVIK KFLQGFMAPK QKKKKKQAGE
ESSKAEEVDE EKRLAEEARV ATAVEKWKTA IREAQTFSRM HVLLGMLDAC IKWDMSAENA
RCKVCRRKGD DEKLILCDEC NKAFHLFCLR PALYRVPNGE WLCPACQPTV ARRGSRVRNY
KQDSDEEDDE EESEEEDSEE EDEDEEENDY KAMGHSCEYF TEKIRLKKKN CNSLTKFKFT
PTVRQSSQTG VSRQVLELER CEEILKKLMK YRYSWPFREP VSSEEAEDYL DIISQPMDYQ
TMLGKFSQGS YRHAQDFLED VKLVFSNAEE YNQQGSTVLS CMVKTEQTFT ELLQKLLPGL
SYIRRRSRKP ICNLATGVQS KMDQSKGQRC EKSVET
//
