ID A0A2J8KJR8_PANTR Unreviewed; 1710 AA.
AC A0A2J8KJR8; H2QR99;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD1 {ECO:0000313|Ensembl:ENSPTRP00000029279.4,
GN ECO:0000313|VGNC:VGNC:3950};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000029279.4, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000029279.4, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000029279.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; AACZ04045959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_517850.3; XM_517850.5.
DR STRING; 9598.ENSPTRP00000029279; -.
DR PaxDb; 9598-ENSPTRP00000029279; -.
DR Ensembl; ENSPTRT00000031693.4; ENSPTRP00000029279.4; ENSPTRG00000017103.4.
DR GeneID; 461968; -.
DR CTD; 1105; -.
DR VGNC; VGNC:3950; CHD1.
DR GeneTree; ENSGT00940000156579; -.
DR InParanoid; A0A2J8KJR8; -.
DR OMA; WVQIRDD; -.
DR OrthoDB; 5482994at2759; -.
DR TreeFam; TF313461; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000017103; Expressed in thymus and 21 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0000228; C:nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IEA:Ensembl.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR CDD; cd18661; CD2_tandem_CHD1-2_like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR040793; CDH1_2_SANT_HL1.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF7; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 272..364
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 389..452
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 493..663
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 792..943
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1710 AA; 196786 MW; E318D3C084F91ED7 CRC64;
MNGHSDEESV RNSSGESSQS DDDSGSASGS GSGSSSGSSS DGSSSQSGSS DSDSGSESGS
QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA ILKKQQQQQQ QQQHQASSNS
GSEEDSSSSE DSDDSSSEVK RKKHKDEDWQ MSGSGSPSQS GSDSESEEER DKSSCDETES
DYEPKNKVKS RKPQNRSKSK NGKKILGQKK RQIDSSEEDD DEEDYDNDKR SSRRQATVNV
SYKEDEEMKT DSDDLLEVCG EDVPQPEEEE FETIERFMDC RIGRKGATGA TTTIYAVEAD
GDPNAGFEKN KEPGEIQYLI KWKGWSHIHN TWETEETLKQ QNVRGMKKLD NYKKKDQETK
RWLKNASPED VEYYNCQQEL TDDLHKQYQI VERIIAHSNQ KSAAGYPDYY CKWQGLPYSE
CSWEDGALIS KKFQACIDEY FSRNQSKTTP FKDCKVLKQR PRFVALKKQP SYIGGHEGLE
LRDYQLNGLN WLAHSWCKGN SCILADEMGL GKTIQTISFL NYLFHEHQLY GPFLLVVPLS
TLTSWQREIQ TWASQMNAVV YLGDINSRNM IRTHEWTHHQ TKRLKFNILL TTYEILLKDK
AFLGGLNWAF IGVDEAHRLK NDDSLLYKTL IDFKSNHRLL ITGTPLQNSL KELWSLLHFI
MPEKFSSWED FEEEHGKGRE YGYASLHKEL EPFLLRRVKK DVEKSLPAKV EQILRMEMSA
LQKQYYKWIL TRNYKALSKG SKGSTSGFLN IMMELKKCCN HCYLIKPPDN NEFYNKQEAL
QHLIRSSGKL ILLDKLLIRL RERGNRVLIF SQMVRMLDIL AEYLKYRQFP FQRLDGSIKG
ELRKQALDHF NAEGSEDFCF LLSTRAGGLG INLASADTVV IFDSDWNPQN DLQAQARAHR
IGQKKQVNIY RLVTKGSVEE DILERAKKKM VLDHLVIQRM DTTGKTVLHT GSAPSSSTPF
NKEELSAILK FGAEELFKEP EGEEQEPQEM DIDEILKRAE THENEPGPLT VGDELLSQFK
VANFSNMDED DIELEPERNS KNWEEIIPED QRRRLEEEER QKELEEIYML PRMRNCAKQI
SFNGSEGRRS RSRRYSGSDS DSISEGKRPK KRGRPRTIPR ENIKGFSDAE IRRFIKSYKK
FGGPLERLDA IARDAELVDK SETDLRRLGE LVHNGCIKAL KDSSSGTERT GGRLGKVKGP
TFRISGVQVN AKLVISHEEE LIPLHKSIPS DPEERKQYTI PCHTKAAHFD IDWGKEDDSN
LLIGIYEYGY GSWEMIKMDP DLSLTHKILP DDPDKKPQAK QLQTRADYLI KLLSRDLAKK
EALSGVGSSK RRKARAKKNK AMKSIKVKEE IKSDSSPLPS EKSDEDDDKL SESKSDGRER
SKKSSVSDAP VHITASGEPV PISEESEELD QKTFSICKER MRPVKAALKQ LDRPEKGLSE
REQLEHTRQC LIKIGDHITE CLKEYTNPEQ IKQWRKNLWI FVSKFTEFDA RKLHKLYKHA
IKKRQESQQN NDQNSNLNPH VIRNPDVERL KENTNHDDSS RDSYSSDRHL TQYHDHHKDR
HQGDSYKKSD SRKRPYSSFS NGKDHRDWDH YKQDSRYYSD REKHRKLDDH RSRDHRSNLE
GSLKDRSHSD HRSHSDHRLH SDHRSSSEYM HHKSSRDYRY HSDWQMDHRA SSSGPRSPLD
QRSPYGSRSP FEHSVEHKNT PEHTWSSRKT
//
