CHD1L_DANRE
ID CHD1L_DANRE Reviewed; 1026 AA.
AC Q7ZU90;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1-like;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q86WJ1};
GN Name=chd1l; ORFNames=zgc:56084;
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 MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2003) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86WJ1}.
CC Note=Localizes at sites of DNA damage. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC050498; AAH50498.1; -; mRNA.
DR RefSeq; NP_956607.1; NM_200313.1.
DR AlphaFoldDB; Q7ZU90; -.
DR SMR; Q7ZU90; -.
DR STRING; 7955.ENSDARP00000022305; -.
DR PaxDb; Q7ZU90; -.
DR PRIDE; Q7ZU90; -.
DR GeneID; 393283; -.
DR KEGG; dre:393283; -.
DR CTD; 9557; -.
DR ZFIN; ZDB-GENE-040426-892; chd1l.
DR eggNOG; KOG0385; Eukaryota.
DR InParanoid; Q7ZU90; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q7ZU90; -.
DR Reactome; R-DRE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DRE-5696400; Dual Incision in GG-NER.
DR PRO; PR:Q7ZU90; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031053; ALC1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR031916; LIG3_BRCT.
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; PF16759; LIG3_BRCT; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS50172; BRCT; 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; Reference proteome.
FT CHAIN 1..1026
FT /note="Chromodomain-helicase-DNA-binding protein 1-like"
FT /id="PRO_0000332143"
FT DOMAIN 47..212
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 340..494
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 697..870
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 930..1023
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 606..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..666
FT /note="Required for helicase activity"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT REGION 877..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 540..668
FT /evidence="ECO:0000255"
FT MOTIF 163..166
FT /note="DEAH box"
FT COMPBIAS 625..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1026 AA; 116249 MW; 68EA14BD66BC8A2B CRC64;
MSTFLRAVRD NIPEKDKSEL TENDLKKWGL GAIHLRPYQL DGVKWLSLCM KNQQGCILGD
EMGLGKTCQT ISLLAYARGS LKMNGPFLVL CPLAVLENWR QELERFCPSL SVICYTGDKE
KRAELQQNLK SDPRFHVLLT TYEMCLKDAR YLKSWKWKIL VVDEAHRLKN QESLLHQTLK
EFTVGFRVLL TGTPIQNNLQ EVYSLLTFIQ PSVFLPEAVE DFVNAYADIQ TEPALVDELH
QVLQPFLLRR VKAEVAAELP KKTELVVFHG LSALQKRYYK AILMRDLDAF RTDQSTKTRL
LNVLMQLRKC VDHPYLFDGV EPEPFEMGEH LVEASGKLSL LDSMLAYLQE GGHHVLLFSQ
MTRMLDILQD YLEYRGYSYE RLDGSVRGEE RNLAIKNFST KDVFIFLLST KAGGVGMNLT
AADTVIFVDG DFNPQNDLQA AARAHRIGQT RPVKVIRLLG RDTIEEIIYS RAVSKLRLTD
TVIEEGRFSL LDQAQSAASG LQLSEILKFG VDKLLSSEES SVQDVDLQLI LGQSRDGQWL
TDEEHAKLNE SNEEEDEDME GQNHMYYFEG KDYSKDPSAE DEKTFELLLE KQFAEMEDAE
KEGRALRNKA GVSLSGPLIN PARKKRPLTE AELEERRQKR QAAAAKRAKL QEERKKQQEE
LNYKKKMAWW DSCGYRSLCL PRVDSEGEDM EPDEDDHVSF SSTDSDHTAI RYVLGDVTHP
QADREDAIIV HCVDDSGHWG RGGLFTALGL RSDEPRKQYE LAGDMKDLEL GNVLLFPVDD
KQSRLCGRDY LALIVAQQRD KANKLSGIRL TALDEGLKKI YKAAKQKKAS VHLPRIGHST
KGFNWYGTER LIRKHLATRG IFTSIYYYRR GSSHATVSST ASTTTPSSSK PAASSPSESP
HSSSPPANRE GLTKSAELST TSHEGPGAPG LADFMRGVHV YFYNMAATEK KKLTRYLITY
DGDEEDLMSS HVTHIVGEVE SPVHKQELQD LLHQYPQALL VKKNWLESCF ASQRKVSVSK
YVIRLT
