ID A0A4W3GLZ9_CALMI Unreviewed; 1451 AA.
AC A0A4W3GLZ9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 1A {ECO:0000256|ARBA:ARBA00068253};
GN Name=baz1a {ECO:0000313|Ensembl:ENSCMIP00000004446.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|Ensembl:ENSCMIP00000004446.1, ECO:0000313|Proteomes:UP000314986};
RN [1] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17185593; DOI=10.1126/science.1130708;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Ancient noncoding elements conserved in the human genome.";
RL Science 314:1892-1892(2006).
RN [2] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17407382;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Survey sequencing and comparative analysis of the elephant shark
RT (Callorhinchus milii) genome.";
RL PLoS Biol. 5:E101-E101(2007).
RN [3] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
RN [4] {ECO:0000313|Ensembl:ENSCMIP00000004446.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [5] {ECO:0000313|Ensembl:ENSCMIP00000004446.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00475}.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR Ensembl; ENSCMIT00000004612.1; ENSCMIP00000004446.1; ENSCMIG00000002622.1.
DR GeneTree; ENSGT00940000158135; -.
DR Proteomes; UP000314986; Unassembled WGS sequence.
DR GO; GO:0008623; C:CHRAC; IEA:TreeGrafter.
DR GO; GO:0000228; C:nuclear chromosome; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:TreeGrafter.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:TreeGrafter.
DR GO; GO:0031445; P:regulation of heterochromatin formation; IEA:TreeGrafter.
DR CDD; cd15627; PHD_BAZ1A; 1.
DR FunFam; 3.30.40.10:FF:000300; Bromodomain adjacent to zinc finger domain protein 1A; 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; IPR047171; BAZ1A.
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; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46510; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR PANTHER; PTHR46510:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 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.
PE 3: Inferred from homology;
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000314986};
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 10..116
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 397..462
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1064..1114
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1341..1411
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 637..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 299..369
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 637..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..688
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1181
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1226
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1451 AA; 166361 MW; F39D1F258027BF87 CRC64;
MLLPLSYRTP DNDYDNNNNP CIYLIYDFFE RTILCNSLVW SCAITGKPGL TYQEALESES
RARQNLQNFP GPLVVPILYL TTLTHCSRLH ELCDDIYTYT KDRYFAGEII EVTNTNGTRQ
TCKILEVVTP PVQNGTANGH ISNRAEDVVI VISDESDNED GSTSSAHAGK KKSKVDVSLF
KYKVKPLKSE GNEIIIKAAQ MNRKKNVYSR DKLKLFLKQH CELRHSLLKV KSTTATKYKL
SEQNFSHLFP DDPLAFPFSP TSRGRGRVAK HRGSFSNVSR NFLLNFFNSA LAQKEDEIAS
DLKKRKAEVL EAKKKEKEDK EKKREELKKI LEEEKLKRKE EKERLKLEKE KVREKLREEK
KKYAEYLKEW NKPREDMECE DLKELPSPMP VKTRLPSELF GDALMVLEFL NAFGELFDLQ
DEFPDGMTLE MLEEALVGND TEGPLCELLF FFLSAIFQAH AEEEEEVAKE QLKEADTKDL
TEALDEDADS TKCAVSAVAA FAAAWPQLYQ GCTLRDLDLD SCTLSEILRL HILAAGADVT
PANAKYRYQQ QGGFDATDNA CVELRLNNPG LLKKLSNIPV YDLTAADKLK LLQALCGQLL
TLVSTRDFIE DNVEILKQAR QEFRELKAEQ HRKEREEAAA RYRKKKEERL KEQEQKIKEK
HDQLKEEEQR NSKGNAVEED ATQEELETST ESRVSAHIDR GHDTATEDEE EVGPSKRDRK
GRKSLNELKD TPSREETEES GTEKREMLAP EEEEVFKREQ QRKEKEMWEK IQIASSCTNI
VPLGRDRLYR RYWVLNSVPG LFVEEDFEGL TEDMLQPYPV KTAINNAQSQ GNPADSTEEL
HKPVNKPNRW CVYSSPEQLD QLIEALNSRG KRESCLKESL HQEKTRLTER LTNFPVERFS
IPVESKSARN SFKSAHNTND ASQLSAEKQL ELRLKDLLLD IEDRTWQGTL GGIKVCIPVL
PSAHGQRLCE LKTEARSIVS TNASTPQPVN LVVRYLAIAL LHLERGIERK FLKPPLDASD
GGKVQKTLLD RWRESLTAST SLAQVFLHLS TLDRSILWAK SLLNARCKIC HKKGDAENML
LCDGCDRGHH TYCLRPKIKT IPEDDWFCPE CRPKQRFRRP SARQRPALDS EEEVFEELEE
MEDEEEESEE EEETEVEDDE TEEEQLRRGR TRVKLQVKSK SGKGSATTVA HGQGTEPRRY
PSRSRSNTPK LTLSGAKKRR GKKVGRPKSL PNAEVKPLAR LSGRMKNSRW SEGSFIELGV
PRRRRRYRKA AARSPEYGAS TSCRLRRLSD LDNSQEEPVR KKRKYTRLVE VLKVTGNRRS
SGRNSGIHEL SVCEQLIVDL VRHEDSWPFL KLVNKAQVTD YYDIIKKPVA LNIIREKLNR
CQYNYASDFI DDVELMFTNC FEYNPRNTSE AKAGMKLQAF FHNQVEKLGL PVKPANVDHP
PQLAATKRSR I
//
