ID   BAZ1A_XENLA             Reviewed;         627 AA.
AC   Q8UVR5;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Bromodomain adjacent to zinc finger domain protein 1A;
DE   AltName: Full=ATP-utilizing chromatin assembly and remodeling factor 1;
DE            Short=xACF1;
DE   Flags: Fragment;
GN   Name=baz1a; Synonyms=acf1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11809820; DOI=10.1091/mbc.01-09-0441;
RA   MacCallum D.E., Losada A., Kobayashi R., Hirano T.;
RT   "ISWI remodeling complexes in Xenopus egg extracts: identification as major
RT   chromosomal components that are regulated by INCENP-aurora B.";
RL   Mol. Biol. Cell 13:25-39(2002).
CC   -!- FUNCTION: May play a role in transcriptional regulation.
CC   -!- SUBUNIT: Together with p18 and p20 proteins, it forms the Xenopus
CC       version of CHRAC.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Phosphorylated in mitosis.
CC   -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
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DR   EMBL; AF412332; AAL60160.1; -; mRNA.
DR   AlphaFoldDB; Q8UVR5; -.
DR   SMR; Q8UVR5; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   CDD; cd05504; Bromo_Acf1_like; 1.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR037325; Acf1_Bromo.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
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   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   2: Evidence at transcript level;
KW   Bromodomain; Coiled coil; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           <1..627
FT                   /note="Bromodomain adjacent to zinc finger domain protein
FT                   1A"
FT                   /id="PRO_0000211169"
FT   DOMAIN          518..588
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   ZN_FING         222..272
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          270..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          281..327
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        270..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..323
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   627 AA;  70209 MW;  42C17587E531D380 CRC64;
     KSKICQRLDS FPVNRFNIAD NTPPTLDFKP FRGKLLNASE SGPVSAEKQL ELRLCDLILD
     IEDRIYQGTL GAVKVPDRQL WRSALENNTL ELLNDEAKEN GSSKPINHEM EEMEIDIKQS
     AKDRLLGLKN DTPSATSTST NTPQPVNNAV RYLARALHQI EQGVERKYLK APLGDASESG
     RVQRTVLDRC GESLLSSGSF SQIFLHLSTL DRSILWSRSI LNARCKVCRK KGDGESMVLC
     DGCDRGHHIY CVRPKLKYVP EGDWFCPECH PKQRSHRLPS RHRYSMDSDE EEEEELDQKE
     EEEEEEEQEE LSESENEQED EMSEEESPPK RGRAKVQLPL KMRGGKATGK LGPKPKTGKQ
     STPKNTQPAP EGRGQGKKTR SAPSLEPTSR LSASDSPAHG VSPNSSLVNV VTVNGRGRGK
     GKGRGRGRGR LQKSADNTPA SSPFAFRPFS LDSNEPTPPG RKPRSQSLLP SQAEPKGKGK
     KRLSGDISSL EQGNRRSSGR HHGVHELSAC EQLVVELVRH DDSWPFMRLV SKNQVPDYFD
     VIQRPIALNL IREKVNKCEY KCASEFIDDV HLMWSNCFEY NHHNSNEAKA GIRLQSFFIT
     EAQNLGLEVS PNNRAPAKTP PAKRSRF