ID A0A286ZUW6_PIG Unreviewed; 1708 AA.
AC A0A286ZUW6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 38.
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:ENSSSCP00000035246.2,
GN ECO:0000313|VGNC:VGNC:86631};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000035246.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000035246.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000035246.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000035246.2}
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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR Ensembl; ENSSSCT00000037530.3; ENSSSCP00000035246.2; ENSSSCG00000021363.4.
DR VGNC; VGNC:86631; CHD3.
DR GeneTree; ENSGT00940000158001; -.
DR Proteomes; UP000008227; Chromosome 12.
DR Bgee; ENSSSCG00000021363; Expressed in uterus and 44 other cell types or tissues.
DR ExpressionAtlas; A0A286ZUW6; baseline and differential.
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; 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; 1.10.10.60; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
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 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 1: Evidence at protein level;
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A286ZUW6};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
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 206..253
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 283..330
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 363..420
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 458..494
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 575..759
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 891..1056
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 56..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..279
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1708 AA; 193584 MW; 5D5D4F004FC4D219 CRC64;
MPLIAKKNPK IPMSKMMTIL GAKWREFSAN NPFKGSAAAV AAAAAAAAAA VAEQVSAAVS
SATPIAPSGP PALPPPPAAD IQPPPIRRAK TKEGKGPGHK RRSKSPRVPD GRKKLRGKKM
APLKIKLGLL GGKRKKGGSS DEGPEPEAEE SDLDSGSVHS ASGRPDGPVR TKKLKRGRPG
RKKKKVLGCP AVAGEEEVDG YETDHQDYCE VCQQGGEIIL CDTCPRAYHL VCLDPELDRA
PEGKWSCPHC EKEGVQWEAK EEDDDYEEEG EEEGEKEEED DHMEYCRVCK DGGELLCCDA
CISSYHIHCL NPPLPDIPNG EWLCPRCTCP VLKGRVQKIL HWRWGEPPVA VPAPQQADGN
PDAPPPRPLQ GRSEREFFVK WVGLSYWHCS WAKELQLEIF HLVMYRNYQR KNDMDEPPPL
DYGSGEDDGK SDKRKVKDPH YAEMEEKYYR FGIKPEWMTV HRIINHSVDK KGNYHYLVKW
RDLPYDQSTW EEDEMNIPEY EDHKQSYWRH RELIMGEDPA QPRKYKKKKK ELQGDGPPSS
PTNDPTVKYE TQPRFITATG GTLHMYQLEG LNWLRFSWAQ GTDTILADEM GLGKTIQTIV
FLYSLYKEGH TKGPFLVSAP LSTIINWERE FQMWAPKFYV VTYTGDKDSR AIIRENEFSF
EDNAIKGGKK AFKMKREAQV KFHVLLTSYE LITIDQAALG SIRWACLVVD EAHRLKNNQS
KFFRVLNGYK IDHKLLLTGT PLQNNLEELF HLLNFLTPER FNNLEGFLEE FADISKEDQI
KKLHDLLGPH MLRRLKADVF KNMPAKTELI VRVELSPMQK KYYKYILTRN FEALNSRGGG
NQVSLLNIMM DLKKCCNHPY LFPVAAMESP KLPSGAYEGG ALIKASGKLM LLQKMLRKLK
EQGHRVLIFS QMTKMLDLLE DFLDYEGYKY ERIDGGITGA LRQEAIDRFN APGAQQFCFL
LSTRAGGLGI NLATADTVII FDSDWNPHND IQAFSRAHRI GQANKVMIYR FVTRASVEER
ITQVAKRKMM LTHLVVRPGL GSKAGSMSKQ ELDDILKFGT EELFKDENEG ENKEEDSSVI
HYDNEAIARL LDRNQDATED TDVQNMNEYL SSFKVAQYVV REEDKIEEIE REIIKQEENV
DPDYWEKLLR HHYEQQQEDL ARNLGKGKRV RKQVNYNDAA QEDQDNQSEY SVGSEEEDED
FDERPEGRRQ SKRQLRNEKD KPLPPLLARV GGNIEVLGFN TRQRKAFLNA VMRWGMPPQD
AFTTQWLVRD LRGKTEKEFK AYVSLFMRHL CEPGADGSET FADGVPREGL SRQQVLTRIG
VMSLVKKKVQ EFEHINGRWS MPELMPDPSA DSKRSSRASS PTKTSPTTPE ASAANSPCTS
KPATPAPSEK GEGMRTPLEK DEAENQEEKP EKNSKTGEKM EAEADTPSPA PSLGERLEPR
KVPLEDEGPG GPGEMEPEPG YRGDREKSAT ESTPGERGEE KPLDGQEQRE RPEGETGDLG
KRAEDVKGDR ELRPGPPRDE LRSNGRREEK VEKPRFMFNI ADGGFTELHT LWQNEERAAI
SSGKLNEIWH RRHDYWLLAG IVLHGYARWQ DIQNDAQFAI INEPFKTEAN KGNFLEMKNK
FLARRFKLLE QALVIEEQLR RAAYLNLSQE PAHPAMALHA RFAEAECLAE SHQHLSKESL
AGNKPANAVL HKGKGRGGPA RGRAHNAA
//
