ID A0A2I3TD11_PANTR Unreviewed; 2051 AA.
AC A0A2I3TD11;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD3 {ECO:0000313|Ensembl:ENSPTRP00000087124.1,
GN ECO:0000313|VGNC:VGNC:9234};
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:ENSPTRP00000087124.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000087124.1, 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:ENSPTRP00000087124.1}
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; AC192612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPTRT00000091509.1; ENSPTRP00000087124.1; ENSPTRG00000008714.5.
DR VGNC; VGNC:9234; CHD3.
DR GeneTree; ENSGT00940000158001; -.
DR Proteomes; UP000002277; Chromosome 17.
DR Bgee; ENSPTRG00000008714; Expressed in lymph node and 20 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd18055; DEXHc_CHD3; 1.
DR CDD; cd00084; HMG-box_SF; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR036910; HMG_box_dom_sf.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF9; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 432..479
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 509..556
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 589..646
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 684..720
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 801..985
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1117..1282
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..170
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..343
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..505
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2051 AA; 232304 MW; 5B9A81B8522916E4 CRC64;
MASPLRDEEE EEEEMVVSEE EEEEEEEGDE EEEEVEAADE DDEEDDDEGV LGRGPGHDRG
RDRHSPPGCH LFPPPPPPFS DAFCFEDKDD IRLLPSALGV KKRKRGPKKQ KENKPGKPRK
RKKRDSEEEF GSERDEYREK SESGGSEYGT GPGRKRRRKH REKKEKKTKR RKKGEGDGGQ
KQVEQKSSAT LLLTWGLEDV EHVFSEEDYH TLTNYKAFSQ FMRPLIAKKN PKIPMSKMMT
ILGAKWREFS ANNPFKGSAA AVAAAAAAAA AAVAEQVSAA VSSATPIAPS GPPALPPPPA
ADIQPPPIRR AKTKEGKGPG HKRRSKSPRV PDGRKKLRGK KMAPLKIKLG LLGGKRKKGG
SYVFQSDEGP EPEAEESDLD SGSVHSASGR PDGPVRTKKL KRGRPGRKKK KVLGCPAVAG
EEEVDGYETD HQDYCEVCQQ GGEIILCDTC PRAYHLVCLD PELDRAPEGK WSCPHCEKEG
VQWEAKEEEE EYEEEGEEEG EKEEEDDHME YCRVCKDGGE LLCCDACISS YHIHCLNPPL
PDIPNGEWLC PRCTCPVLKG RVQKILHWRW GEPPVAVPAP QQADGNPDVP PPRPLQGRSE
REFFVKWVGL SYWHCSWAKE LQLEIFHLVM YRNYQRKNDM DEPPPLDYGS GEDDGKSDKR
KVKDPHYAEM EEKYYRFGIK PEWMTVHRII NHSVDKKGNY HYLVKWRDLP YDQSTWEEDE
MNIPEYEEHK QSYWRHRELI MGEDPAQPRK YKKKKKELQG DGPPSSPTND PTVKYETQPR
FITATGGTLH MYQLEGLNWL RFSWAQGTDT ILADEMGLGK TIQTIVFLYS LYKEGHTKGP
FLVSAPLSTI INWEREFQMW APKFYVVTYT GDKDSRAIIR ENEFSFEDNA IKGGKKAFKM
KREAQVKFHV LLTSYELITI DQAALGSIRW ACLVVDEAHR LKNNQSKFFR VLNGYKIDHK
LLLTGTPLQN NLEELFHLLN FLTPERFNNL EGFLEEFADI SKEDQIKKLH DLLGPHMLRR
LKADVFKNMP AKTELIVRVE LSPMQKKYYK YILTRNFEAL NSRGGGNQVS LLNIMMDLKK
CCNHPYLFPV AAMESPKLPS GAYEGGALIK SSGKLMLLQK MLRKLKEQGH RVLIFSQMTK
MLDLLEDFLD YEGYKYERID GGITGALRQE AIDRFNAPGA QQFCFLLSTR AGGLGINLAT
ADTVIIFDSD WNPHNDIQAF SRAHRIGQAN KVMIYRFVTR ASVEERITQV AKRKMMLTHL
VVRPGLGSKA GSMSKQELDD ILKFGTEELF KDENEGENKE EDSSVIHYDN EAIARLLDRN
QDATEDTDVQ NMNEYLSSFK VAQYVVREED KIEEIEREII KQEENVDPDY WEKLLRHHYE
QQQEDLARNL GKGKRVRKQV NYNDAAQEDQ GEDCPRWRRQ SKRQLRNEKD KPLPPLLARV
GGNIEVLGFN TRQRKAFLNA VMRWGMPPQD AFTTQWLVRD LRGKTEKEFK AYVSLFMRHL
CEPGADGSET FADGVPREGL SLMSLVKKKV SVFLSPKEST CAGVRRRRLE LPVQEFEHIN
GRWSMPELMP DPSADSKRSS RASSPTKTSP TTPEASATNS PCTSKPATPA PSEKGEGIRT
PLEKEEAENQ EEKPEKNSRI GEKMETEADA PSPAPSLGER LEPRKIPLED EVPGVPGEME
PEPGYRGDRE KSATESTPGE RGEEKPLDGQ EHRERPEGET GDLGKREDVK GDRELRPGPR
DEPRSNGRRE EKTEKPRFMF NIADGGFTEL HTLWQNEERA AISSGKLNEI WHRRHDYWLL
AGIVLHGYAR WQDIQNDAQF AIINEPFKTE ANKGNFLEMK NKFLARRFKL LEQALVIEEQ
LRRAAYLNLS QEPAHPAMAL HARFAEAECL AESHQHLSKE SLAGNKPANA VLHKVLNQLE
ELLSDMKADV TRLPATLSRI PPIAARLQMS ERSILSRLAS KGTEPHPTPA FPPGPYATPP
GYGAAFSAAP VGALAAAGAN YSQMPAGSFI TAATNGPPVL VKKEKEMVGA LVSDGLDRKE
PRAGEVICID D
//
