ID   SMRDB_DANRE             Reviewed;         954 AA.
AC   E7F1C4;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1B;
DE            EC=3.6.4.12;
GN   Name=smarcad1b; ORFNames=si:dkey-76p7.6;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: DNA helicase that possesses intrinsic ATP-dependent
CC       nucleosome-remodeling activity and is both required for DNA repair and
CC       heterochromatin organization. Promotes DNA end resection of double-
CC       strand breaks (DSBs) following DNA damage: probably acts by weakening
CC       histone DNA interactions in nucleosomes flanking DSBs. Required for the
CC       restoration of heterochromatin organization after replication (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC       Note=Colocalizes with PCNA at replication forks during S phase.
CC       Recruited to double-strand breaks (DSBs) sites of DNA damage (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; BX927385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_009303506.1; XM_009305231.2.
DR   AlphaFoldDB; E7F1C4; -.
DR   SMR; E7F1C4; -.
DR   STRING; 7955.ENSDARP00000104253; -.
DR   PaxDb; E7F1C4; -.
DR   PeptideAtlas; E7F1C4; -.
DR   Ensembl; ENSDART00000113101; ENSDARP00000104253; ENSDARG00000073721.
DR   GeneID; 563175; -.
DR   CTD; 563175; -.
DR   ZFIN; ZDB-GENE-091113-61; smarcad1b.
DR   eggNOG; KOG0389; Eukaryota.
DR   GeneTree; ENSGT00910000144252; -.
DR   HOGENOM; CLU_000315_16_3_1; -.
DR   InParanoid; E7F1C4; -.
DR   OMA; HNKYEDY; -.
DR   OrthoDB; 61251at2759; -.
DR   PhylomeDB; E7F1C4; -.
DR   TreeFam; TF105768; -.
DR   PRO; PR:E7F1C4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 10.
DR   Bgee; ENSDARG00000073721; Expressed in ovary and 18 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR009060; UBA-like_sf.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51140; CUE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chromatin regulator; Chromosome; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..954
FT                   /note="SWI/SNF-related matrix-associated actin-dependent
FT                   regulator of chromatin subfamily A containing DEAD/H box
FT                   1B"
FT                   /id="PRO_0000420485"
FT   DOMAIN          176..219
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   DOMAIN          441..609
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          786..948
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           560..563
FT                   /note="DEGH box"
FT   COMPBIAS        26..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         454..461
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   954 AA;  108122 MW;  CCF4769FC9892834 CRC64;
     MRRKKGPASS SDHEEPPESD SVIPETPETK RPSGSSLSTA ISDSDSDSDS EISGSSMMPV
     RKLRPRKRKA ASSADEYSVS DEEEEIVVKT KRRPTHSRTT RSTSQQAQPA HQKASETVTD
     IAHPSPLKTS GMAAADSVQQ RRRQQMCGSS QESDSRKGGR VSAADDSEEE GQRSKDQERM
     LRKLQRKFPH LNKNELRDVL QEHDWLIDDA LETLRMFSDL VVESEDDSSQ TSTPAKHTRR
     VAETRPQAQV TKLSSPPKPK PSRPLDGTRT SQRIAKQPIL AKYTYVSSEE ECSDSEASVV
     NGLLDSDSDQ SEETLSKLKT EILCFFQSAS VDELTLIAGC SLKKAQKITE LRPFKTWKDL
     DDAMRRRNGL SAELLAGCRE VLKEREVVKG LMSKCEEISV KLIQDVTQVM DKGPGSMTQP
     EILSSTFQLK PYQLIGLNWL VLLHQNKLSG ILADEMGLGK TIQAISFLAH LYQEGNHGPH
     LITVPASTLD NWVRELNLWC PSFKVLVYYG SADDRKYMRY EILNQIVEYN IIVSTYNLAI
     GNSSDRSLFC KLKLEYAVFD EGHLLKNMNS LRYRHLMAIN AKYRLLLTGT PLQNNLLELM
     SLLNFIMPNM FSSSTSQIAK MFSMKSSEEQ SSFERDRITH AKLIMKPFIL RRVKSEVLKQ
     LPAKEEQVEF CAMSERQQEL YSALLHKLKH SSNGEKRELT NVMMQLRKMS NHPLLHRQFY
     TTEKLKAMSK LMLKEPSHRD ADPALIKEDM EVLSDFELHR LCQQYSALHE YQLNTDVLLD
     SGKLSLLTQL LNSLKEKGDR VVLFSQFTMM LDILEVFLRH HKHRYNRLDG STPMSDRIGL
     IDQFNTDQDI FVFLLSTRAG GLGINLTSAN VVILHDIDCN PYNDKQAEGR CHRVGQTKTV
     KVIKLISKDS IEDTMLRIGE RKLKLEQEMT ATQDGEEDTL PDDMTTLLKA SLGL