ID H9FP75_MACMU Unreviewed; 1712 AA.
AC H9FP75;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD1 {ECO:0000313|EMBL:AFE76434.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE76434.1};
RN [1] {ECO:0000313|EMBL:AFE76434.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE76434.1}, Testis
RC {ECO:0000313|EMBL:AFI36113.1}, and Thymus
RC {ECO:0000313|EMBL:AFH30921.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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; JU332679; AFE76434.1; -; mRNA.
DR EMBL; JU474117; AFH30921.1; -; mRNA.
DR EMBL; JV046042; AFI36113.1; -; mRNA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:AFE76434.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:AFE76434.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 274..366
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 391..454
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 495..665
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 794..945
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1712
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..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..208
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1693..1712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1712 AA; 197070 MW; 277249CD09C0D661 CRC64;
MNGHSDEESV RNSSGESSQS DDDSGSASGS GSGSSSGSSS DGSSSQSGSS DSDSGSESGS
QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA MLRKQQQQQQ QQQQQHQASS
NSGSEEDSSS SEDSDDSSSE VKRKKHRDED WQMSGSGSPS QSGSDSESEE ERDKSSCDET
ESDYEPKNKV KSRKPQNRSK SKNGKKILGQ KKRQIDSSEE EEDEEDYDND KRSSRRQATV
NVSYKEDEEM KTDSDDLLEV CGEDVPQPEE EEFETIERFM DCRIGRKGAT GATTTIYAVE
ADGDPNAGFE KNKEPGEIQY LIKWKGWSHI HNTWETEETL KQQNVRGMKK LDNYKKKDQE
TKRWLKNASP EDVEYYNCQQ ELTDDLHKQY QIVERIIAHS NQKSAAGYPD YYCKWQGLPY
SECSWEDGAL ISKKFQACID EYFSRNQSKT TPFKDCKVLK QRPRFVALKK QPSYIGGHEG
LELRDYQLNG LNWLAHSWCK GNSCILADEM GLGKTIQTIS FLNYLFHEHQ LYGPFLLVVP
LSTLTSWQRE IQTWASQMNA VVYLGDINSR NMIRTHEWTH HQTKRLKFNI LLTTYEILLK
DKAFLGGLNW AFIGVDEAHR LKNDDSLLYK TLIDFKSNHR LLITGTPLQN SLKELWSLLH
FIMPEKFSSW EDFEEEHGKG REYGYASLHK ELEPFLLRRV KKDVEKSLPA KVEQILRMEM
SALQKQYYKW ILTRNYKALS KGSKGSTSGF LNIMMELKKC CNHCYLIKPP DNNEFYNKQE
ALQHLIRSSG KLILLDKLLI RLRERGNRVL IFSQMVRMLD ILAEYLKYRQ FPFQRLDGSI
KGELRKQALD HFNAEGSEDF CFLLSTRAGG LGINLASADT VVIFDSDWNP QNDLQAQARA
HRIGQKKQVN IYRLVTKGSV EEDILERAKK KMVLDHLVIQ RMDTTGKTVL HTGSAPSSST
PFNKEELSAI LKFGAEELFK EPEGEEQEPQ EMDIDEILKR AETHENEPGP LTVGDELLSQ
FKVANFSNMD EDDIELEPER NSKNWEEIIP EDQRRRLEEE ERQKELEEIY MLPRMRNCAK
QISFNGSEGR RSRSRRYSGS DSDSISEGKR PKKRGRPRTI PRENIKGFSD AEIRRFIKSY
KKFGGPLERL DAIARDAELV DKSETDLRRL GELVHNGCIK ALKDSSSGTE RTGGRLGKVK
GPTFRISGVQ VNAKLVISHE EELIPLHKSI PSDPEERKQY TIPCHTKAAH FDIDWGKEDD
SNLLIGIYEY GYGSWEMIKM DPDLSLTHKI LPDDPDKKPQ AKQLQTRADY LIKLLSRDLA
KKEALSGAGS SKRRKARAKK NKAMKSIKVK EEIKSDSSPL PSEKSDEDDD KLSESKSDGR
ERSKKSSVSD APVHITASGE PVPISEESEE LDQKTFSICK ERMRPVKAAL KQLDRPEKGL
SEREQLEHTR QCLIKIGDHI TECLKEYTNP EQIKQWRKNL WIFVSKFTEF DARKLHKLYK
HAIKKRQESQ QNNDQNSNLN PHVIRNPDVE RLKENTNHDD SSRDSYSSDR HLTQYHDHHK
DRHQGDSYKK SESRKRPYSS FSNGKDHRDW DHYKQDSRYY GDREKHRKLD DHRSRDHRSN
LEGNLKDRSH SDHRSHSDHR LHSDHRSSSE YTHHKSSRDY RYHSDWQMDH RASSSGPRSP
LDQRSPYGSR SPFEHSVEHK STPEHTWSSR KT
//
