CHD1_CHICK
ID CHD1_CHICK Reviewed; 1719 AA.
AC B6ZLK2;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1;
DE Short=CHD-1;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD1;
GN Name=CHD1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH SSRP1.
RX PubMed=19625449; DOI=10.1091/mbc.e09-01-0065;
RA Okada M., Okawa K., Isobe T., Fukagawa T.;
RT "CENP-H-containing complex facilitates centromere deposition of CENP-A in
RT cooperation with FACT and CHD1.";
RL Mol. Biol. Cell 20:3986-3995(2009).
CC -!- FUNCTION: ATP-dependent chromatin-remodeling factor which functions as
CC substrate recognition component of the transcription regulatory histone
CC acetylation (HAT) complex SAGA. Regulates polymerase II transcription.
CC Also required for efficient transcription by RNA polymerase I, and more
CC specifically the polymerase I transcription termination step. Regulates
CC negatively DNA replication. Not only involved in transcription-related
CC chromatin remodeling, but also required to maintain a specific
CC chromatin configuration across the genome. Required for maintaining
CC open chromatin and pluripotency in embryonic stem cells (By
CC similarity). Required for centromeric localization of CENPA
CC (PubMed:19625449). {ECO:0000250|UniProtKB:P40201,
CC ECO:0000269|PubMed:19625449}.
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 -!- SUBUNIT: Component of the SAGA complex (By similarity). Interacts with
CC SSRP1. {ECO:0000250, ECO:0000269|PubMed:19625449}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19625449}.
CC Chromosome, centromere {ECO:0000269|PubMed:19625449}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
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DR EMBL; AB465210; BAH03306.1; -; mRNA.
DR AlphaFoldDB; B6ZLK2; -.
DR SMR; B6ZLK2; -.
DR STRING; 9031.ENSGALP00000023555; -.
DR PaxDb; B6ZLK2; -.
DR PRIDE; B6ZLK2; -.
DR VEuPathDB; HostDB:LOC374195; -.
DR eggNOG; KOG0384; Eukaryota.
DR InParanoid; B6ZLK2; -.
DR PhylomeDB; B6ZLK2; -.
DR PRO; PR:B6ZLK2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR040793; CDH1_2_SANT_HL1.
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; IPR025260; DUF4208.
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; IPR000330; SNF2_N.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF13907; DUF4208; 1.
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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 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 1: Evidence at protein level;
KW ATP-binding; Centromere; Chromosome; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1719
FT /note="Chromodomain-helicase-DNA-binding protein 1"
FT /id="PRO_0000388771"
FT DOMAIN 268..360
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 385..448
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 489..659
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 788..939
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 610..613
FT /note="DEAH box"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 502..509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1719 AA; 197526 MW; E08417D4D35F5AE5 CRC64;
MNGHSDEESV RNSSGESRSD DDSGSASGSG SGSSSGSSSD GSSSQSGSSD SESGSESGSQ
SESESDTSRE KKQVQAKPPK ADGSEFWKSS PSILAVQRSA VLKKQQQQQK AASSDSGSEE
DSSSSEDSAD DSSSETKKKK HKDEDWQMSG SGSVSGTGSD SESEEDGDKS SCEESESDYE
PKNKVKSRKP PSRIKPKSGK KSTGQKKRQL DSSEEEEDDD EDYDKRGSRR QATVNVSYKE
AEETKTDSDD LLEVCGEDVP QTEEDEFETI EKFMDSRIGR KGATGASTTI YAVEVDGDPN
AGFEKSKELG EIQYLIKWKG WSHIHNTWET EETLKQQNVK GMKKLDNYKK KDQETKRWLK
NASPEDVEYY NCQQELTDDL HKQYQIVERI IAHSNQKSAA GYPDYYCKWQ GLPYSECSWE
DGALIAKKFQ ARIDEYFSRN QSKTTPFKDC KVLKQRPRFV ALKKQPSYIG GHESLELRDY
QLNGLNWLAH SWCKGNSCIL ADEMGLGKTI QTISFLNYLF HEHQLYGPFL LVVPLSTLTS
WQREIQTWAP QMNAVVYLGD ITSRNMIRTH EWMHPQTKRL KFNILLTTYE ILLKDKSFLG
GLNWAFIGVD EAHRLKNDDS LLYKTLIDFK SNHRLLITGT PLQNSLKELW SLLHFIMPEK
FSSWEDFEEE HGKGREYGYA SLHKELEPFL LRRVKKDVEK SLPAKVEQIL RMEMSALQKQ
YYKWILTRNY KALSKGSKGS TSGFLNIMME LKKCCNHCYL IKPPDDNEFY NKQEALQHLI
RSSGKLILLD KLLIRLRERG NRVLIFSQMV RMLDILAEYL KYRQFPFQRL DGSIKGELRK
QALDHFNAEG SEDFCFLLST RAGGLGINLA SADTVVIFDS DWNPQNDLQA QARAHRIGQK
KQVNIYRLVT KGSVEEDILE RAKKKMVLDH LVIQRMDTTG KTVLHTGSTP SSSTPFNKEE
LSAILKFGAE ELFKEPEGEE QEPQEMDIDE ILKRAETREN EPGPLTVGDE LLSQFKVANF
SNMDEDDIEL EPERNSRNWE EIIPESQRRR IEEEERQKEL EEIYMLPRMR NCAKQISFNG
SEGRRSRSRR YSGSDSDSIT ERKRPKKRGR PRTIPRENIK GFSDAEIRRF IKSYKKFGGP
LERLDAVARD AELVDKSETD LRRLGELVHN GCIKALKDNS SGQERAGGRL GKVKGPTFRI
SGVQVNAKLV ISHEEELAPL HKSIPSDPEE RKRYVIPCHT KAAHFDIDWG KEDDSNLLVG
IYEYGYGSWE MIKMDPDLSL TQKILPDDPD KKPQAKQLQT RADYLIKLLN KDLARKEAQR
LAGAGNSKRR KTRNKKNKMK ASKIKEEIKS DSSPQPSEKS DEDDDEEDNK VNEIKSENKE
KSKKIPLLDT PVHITATSEP VPISEESEEL DQKTFSVCKE RMRPVKAALK QLDRPEKGLS
EREQLEHTRQ CLIKIGDHIT ECLKEYTNPE QIKQWRKNLW IFVSKFTEFD ARKLHKLYKH
AIKKRQESQQ HNDQNISSNV NTHVIRNPDV ERLKETTNHD DSSRDSYSSD RHLSQYHDHH
KDRHQGDAYK KSDSRKRPYS AFSNGKDHRD WDHYKQDSRY YSDSKHRKLD DHRSRDHRSN
LEGNLKDSRG HSDHRSHSDH RIHSDHRSTS EYSHHKSSRD YRYHSDWQMD HRASGSGPRS
PLDQRSPYGS RSPLGHRSPF EHSSDHKSTP EHTWSSRKT
