CHD1_BOMMO
ID CHD1_BOMMO Reviewed; 1365 AA.
AC A9X4T1;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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 Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DNA-BINDING, INTERACTION WITH HMGA, AND
RP FUNCTION.
RC STRAIN=Feng 1 X 54A;
RX PubMed=18817785; DOI=10.1016/j.jmb.2008.09.011;
RA Papantonis A., Tsatsarounos S., Vanden Broeck J., Lecanidou R.;
RT "CHD1 assumes a central role during follicle development.";
RL J. Mol. Biol. 383:957-969(2008).
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). Has a key role in chorion gene regulation and nucleosome
CC positioning. Its binding to middle chorion gene promoters is correlated
CC with H3K4 methylation and TFIID recruitment. {ECO:0000250,
CC ECO:0000269|PubMed:18817785}.
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 HMGA. {ECO:0000250, ECO:0000269|PubMed:18817785}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7KU24}.
CC Chromosome {ECO:0000250|UniProtKB:Q7KU24}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; DQ402511; ABD64154.1; -; mRNA.
DR RefSeq; NP_001106734.1; NM_001113263.1.
DR AlphaFoldDB; A9X4T1; -.
DR SMR; A9X4T1; -.
DR PRIDE; A9X4T1; -.
DR GeneID; 100134916; -.
DR KEGG; bmor:100134916; -.
DR CTD; 1105; -.
DR eggNOG; KOG0384; Eukaryota.
DR eggNOG; KOG4830; Eukaryota.
DR InParanoid; A9X4T1; -.
DR OrthoDB; 57339at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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; IPR002464; DNA/RNA_helicase_DEAH_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; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Chromosome; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1365
FT /note="Chromodomain-helicase-DNA-binding protein 1"
FT /id="PRO_0000388772"
FT DOMAIN 16..86
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 111..176
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 217..387
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 518..669
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 795..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 338..341
FT /note="DEAH box"
FT COMPBIAS 808..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..843
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1365 AA; 157689 MW; 40E55FC175954292 CRC64;
MRRGKKGVTG NVTTIYYIEE HGDPNEGCDP NDEDSTEPQY LIKWKGWSHI HNTWESEKTI
NDQKVKGLKK LENFIKKEVE ISWWRQQAGP EDIDYYECQS ELQQELVKTY NNVERIIAEQ
NRELEGGGTA HEYFCKWESL PYADATWEDA VLIEKRWPVE VEHFKSREAA KSTPSRHCPV
LKRRPKFHQI KEQPEYVGKD SSYHLRDYQM DGLNWLIHSW CKDNSVILAD EMGLGKTIQT
ICFLYYLFKS QHLYGPFLCV VPLSTMTAWQ REFQQWAPDI NVVTYIGDVS SRDIIRQFEW
SFSSSKRLKF NAILTTYEIL LKDRQFLRSF SWACLLVDEA HRLKNDDSLL YKALKEFDTN
HRLLVTGTPL QNSLKELWAL LHFIMPYKFE SWEDFEKDHE DAATKGYEKL HKQLEPFILR
RQKKDVEKSL PAKVEQILRV EMTSIQKQYY KWILTKNYSA LRKGVKGSIN TFINIVIELK
KCCNHALLTK PEDFESRASL ATSDAVEKLL RGSGKLLLLD KLLCRLKETG HRVLIFSQMV
RMLDILAEYL QRRHFPFQRL DGSIKGELRK QALDHFNAEG SQDFCFLLST RAGGLGINLA
TADTVIIFDS DWNPQNDLQA QARAHRIGQK NQVNIYRLVT ARSVEEDIVE RAKRKMVLDH
LVIQRMDTTG KTVLNKRDAS GTTANNPFNK EDLNAILKFG AEELFKDDEE NDEDPVCDID
EILQRAETRD EGPAMVGDEL LSAFKVASFT FDEEKAVNEL KKDNADEEPK DWDDIIPENV
RKTIAEAEKL KEMEDIYLPP RRKNQLQNNA DGGRRRRGRS GDGGDGDGVD GDGEAESDAS
DGEASADDDR PRKRGRPPAS HREKIKGFTD QEIRRFVKSY KKFSAPLKHL DSIACDAELQ
EKPLAELKRL GEILQERCKA VLSETAEPSE QNEGRKNNRK TFKLGGVPVN AKTLAACQDE
LAALDDFLPQ TKEERLKWQL DFRTRPANFD VEWNVSDDSK LLAGIYQYGL GSWEAIKMDS
SFEIGDKILT NEDKKPQAKH LQSRAEYLLK LIKKLLDQKN GKQKMKKPRP KRANKEPVTK
DIVEDDGSSA EDKKTKGVKN DKTEKGKLKI EEVSTHDETS NDKKEKDKKR KKDEDRKGDK
SKGRKKPRQR GNEGIPGPMH FTANNEPRAL EVLGDLDPSV FEECKEKMRP VKKALKALDN
PDQSLSETEQ VSRTRACLTQ IGTQIDLCVE AYPDSQKVEW RSNLWYFVSK FTNFDAKQLY
KLYKYGLKKN EASKQKDGKH KENVKTNNRN NHNSINHLKS FKKNSNSKQK SDTNDKKEKK
MKLEKEKTDK HDKNQHTSGV KRKLEDGECD PEPNDNKRHE RYVVD
