CHD1L_BOVIN
ID CHD1L_BOVIN Reviewed; 897 AA.
AC Q3B7N1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1-like;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q86WJ1};
GN Name=CHD1L;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA helicase which plays a role in chromatin-remodeling
CC following DNA damage. Targeted to sites of DNA damage through
CC interaction with poly(ADP-ribose) and functions to regulate chromatin
CC during DNA repair. Able to catalyze nucleosome sliding in an ATP-
CC dependent manner. Helicase activity is strongly stimulated upon
CC poly(ADP-ribose)-binding. {ECO:0000250|UniProtKB:Q86WJ1}.
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 Evidence={ECO:0000250|UniProtKB:Q86WJ1};
CC -!- SUBUNIT: Interacts (via macro domain) with PARP1; interacts only when
CC PARP1; interacts only when PARP1 is poly-ADP-ribosylated (PARylated)
CC (By similarity). Interacts with CIAO1 (By similarity).
CC {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86WJ1}.
CC Note=Localizes at sites of DNA damage. Probably recruited to DNA damage
CC sites by PARylated PARP1. {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- DOMAIN: The macro domain mediates non-covalent poly(ADP-ribose)-binding
CC and recruitment to DNA damage sites (By similarity). Mediates auto-
CC inhibition of ATPase activity by interacting with the N-terminal ATPase
CC module, encompassing the helicase ATP-binding domain and helicase C-
CC terminal domain (By similarity). PARP1 activation upon DNA damage and
CC poly(ADP-ribose)-binding release the auto-inhibition by the macro
CC domain and trigger ATPase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; BC107534; AAI07535.1; -; mRNA.
DR RefSeq; NP_001032909.1; NM_001037820.1.
DR AlphaFoldDB; Q3B7N1; -.
DR SMR; Q3B7N1; -.
DR STRING; 9913.ENSBTAP00000027762; -.
DR PaxDb; Q3B7N1; -.
DR PRIDE; Q3B7N1; -.
DR GeneID; 524787; -.
DR KEGG; bta:524787; -.
DR CTD; 9557; -.
DR eggNOG; KOG0385; Eukaryota.
DR InParanoid; Q3B7N1; -.
DR OrthoDB; 61251at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031053; ALC1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR47157; PTHR47157; 1.
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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; DNA damage; DNA repair; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..897
FT /note="Chromodomain-helicase-DNA-binding protein 1-like"
FT /id="PRO_0000332140"
FT DOMAIN 60..225
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 353..515
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 704..897
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 558..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..675
FT /note="Required for helicase activity"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT REGION 689..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 640..677
FT /evidence="ECO:0000255"
FT MOTIF 176..179
FT /note="DEAH box"
FT COMPBIAS 561..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..708
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
SQ SEQUENCE 897 AA; 101394 MW; 75F0FA7EA39E37A4 CRC64;
MERVGAATPE GDMPGFLLAL QSKSRAEAPR ARVQEQDLRQ WGLTGIHLRP YQLQGVNWLA
QCFHCQNGCI LGDEMGLGKT CQTIALFIYL AGRLNDEGPF LILCPLSVLS NWKEEMERFA
PGLSCVTYAG DKDKRACLQQ DLKQESRFHV LLTTYEICLK DASFLKSFPW SVLVVDEAHR
LKNQSSLLHK TLSEFSVVFS LLLTGTPIQN SLQELYSLLS FVEPDLFSKE QVEDFVQRYQ
DIEKESESAS ELYKLLQPFL LRRVKAEVAT ELPRKTEVVI YHGMSALQKK YYKAILMKDL
DAFENETAKK VKLQNVLSQL RKCVDHPYLF DGVEPEPFEI GDHLIEASGK LHLLDKLLAF
LYSKGHRVLL FSQMTQMLDI LQDYLDYRGY SYERVDGSVR GEERHLAIKN FGQQPIFTFL
LSTRAGGVGM NLTAADTVIF FDSDFNPQND LQAAARAHRI GQNKSVKVIR LIGRDTVEEI
VYRKAASKLQ LTNTIIEGGH FTLGAQKPAA DADLQLSEIL KFGLDKLLSS EGSTMHEIDL
KSILGETEDG HWVSDALPTA EEGSREPEEG KNHMYLFEGK DYSKEPSKED RESFEQLVNL
QKTLLEKTSQ EGRLLRNKGS VPIPGLVEGS TKRKRILSPE ELEDRRKRRQ EAAAKRKRLL
EEKRKKKEEA EHKKKMAWWE SNNYQSFCLP SEESEPEDGE DESSAQLEYE DPDSTSIRYV
SGDVTHPQAG AEDAVIVHCV DDSGRWGRGG LFTALETRSA EPRKRYELAG KMKDLSLGGV
LLFPIDDKES RNEGQDLLAL IVAQHRDRAN VLSGIKMAAL EEALKKIFLA AKKRKASVHL
PRIGHATKGF NWYGTERLIR KHLASRGIPT YIYYFPRSKA AILHLQASSS SSGQLVS
