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Database: UniProt
Entry: A0A3B4G4D8_9CICH
LinkDB: A0A3B4G4D8_9CICH
Original site: A0A3B4G4D8_9CICH 
ID   A0A3B4G4D8_9CICH        Unreviewed;      2291 AA.
AC   A0A3B4G4D8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=CHD7 {ECO:0000313|Ensembl:ENSPNYP00000016608.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000016608.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000016608.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   STRING; 303518.ENSPNYP00000016608; -.
DR   Ensembl; ENSPNYT00000017021.1; ENSPNYP00000016608.1; ENSPNYG00000012490.1.
DR   GeneTree; ENSGT00940000153649; -.
DR   Proteomes; UP000261460; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031223; P:auditory behavior; IEA:Ensembl.
DR   GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
DR   GO; GO:0021602; P:cranial nerve morphogenesis; IEA:Ensembl.
DR   GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR   GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR   GO; GO:0120054; P:intestinal motility; IEA:Ensembl.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
DR   GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR   GO; GO:0014029; P:neural crest formation; IEA:Ensembl.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR   GO; GO:0048840; P:otolith development; IEA:Ensembl.
DR   GO; GO:0048935; P:peripheral nervous system neuron development; IEA:Ensembl.
DR   GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR   GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0060319; P:primitive erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0046549; P:retinal cone cell development; IEA:Ensembl.
DR   GO; GO:0009303; P:rRNA transcription; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   GO; GO:0048798; P:swim bladder inflation; IEA:Ensembl.
DR   GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR   GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR   GO; GO:0007632; P:visual behavior; IEA:Ensembl.
DR   CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR   CDD; cd17995; DEXHc_CHD6_7_8_9; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 3.40.5.120; -; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
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; IPR006576; BRK_domain.
DR   InterPro; IPR037259; BRK_sf.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
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; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR   PANTHER; PTHR46850:SF3; DNA HELICASE; 1.
DR   Pfam; PF07533; BRK; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00592; BRK; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF160481; BRK domain-like; 2.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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          182..224
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          280..454
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          602..772
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          985..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1428..1621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2205..2291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..909
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1149..1188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1444..1518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1520..1536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1537..1564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1585..1611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2212..2227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2228..2247
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2265..2279
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2291 AA;  257221 MW;  C24C7FEA7402048B CRC64;
     LYFVSEGGAS AAKKDSKRKR EFSVNDDAEV KSPPLSPPEE EDDDGVQKRR SSRQVKRKRY
     TEDLEFRISE DDDSGDDSPS PKSPSSSSQQ QDVAEAEGPV VEKIMGMRTS KKQVSCTDPH
     PNDTNTIHRS TGCSYLHCRW ADLEELEKDK RIHQKVKRFK AKQQLNTFIT EMDDEPFNPD
     YVEVDRVLDV SESTDENGET VTLYLVKWCS LPYEDSTWEL KADIDQSKID EFERIGARTP
     NTKRVDRPPA ADWKKLEGSR EYRNGNALRE YQLEGLNWLT FNWYNSRNCI LADEMGLGKT
     IQSITFLYEI YMKGIEGPFL VIAPLSTIPN WEREFRTWTE LNVVVYHGSQ ASRKTIQAYE
     MYYRDAQGKI IKGVYRFHAV ITTFEMILAD CPELRSIPWR CVVIDEAHRL KNRNCKLLEG
     LKMMDMEHKV LLTGTPLQNT VEELFSLLNF LEPERFPSEQ TFMTEFGDLK TEEQVQKLQG
     ILKPMMLRRL KEDVEKNLAP KEETIIEVEL TNIQKKYYRA ILEKNFSFLS KGGAGGAGGG
     GASVPNLLNT MMELRKCCNH PYLINGAEEK IIEEFRDSHS CGADMPDMAL QAMIQAAGKL
     VLIDKLLPKL KAGGHRVLVF SQMVRCLDIL EDYLIQKRYP YERIDGRVRG NLRQAAIDRF
     SRPDSDRFVF LLCTRAGGLG INLTAADTCI IFDSDWNPQN DLQAQARCHR IGQSKSVKIY
     RLITRNSYER EMFDKASLKL GLDKAVLQSM SGRENANSGV QQLSKKEIED LLRKGAYGAL
     MDEEDEGSKF CEEDIDQILQ RRTHTITIES EGKGSTFAKA SFVATGNRTD ISLEDPDFWQ
     KWAKKAELDL DAINGRNTLV IDTPRVRKQT RHFSSVKEEE MLEFSELESD EDEPSKPSSK
     PRRPQDKTQG YPRSECFRVE KNLLVYGWGR WSDILAHGRF KRPLKESDVE TICRALLAYC
     LLHYRGDENI KSFIWDLITP SEDGTTRTLT NHSGLSTPVP RGRKGKKGKP QAPPPQTPRA
     DWLASCNPDH LLQEDSYKRH LKHHCNKVLL RVRMLYYLRQ EVIGDQAERI LEGADSSLSS
     APIPLPSPCH PDVNAFIMWN TCYEKYNSMR ADPALCFLER VGMPDAKAIA AEQRGSDMMA
     DGVEGEDEDP EYKPLRMPFK DDMDDFTNSP LDDKDEGVEG ENEAKSDENS QRAPASNERL
     YWPAASALTA RLRRLITAYQ RSNRREQLPA PYIQDGAGMF MAEGSPYLAK GSAYFVKGGQ
     WTRREEADFY RVVSTFGVVF DTKRQKFDWT QFRAFARLDK KTDESLEKYY YSFIAMCKRV
     CRMQVKTETE LPDPTLIIDP ITEERASRTL YRIELLRRIR EQVLPHPQLS ERLKLCQPSP
     DLPEWWECGR HDRDLLLGAS KHGVSRTDYH ILNDPTLAFL EAHQRFTSQR GEGDANNIPC
     AKIETPDEQK EHEGEIREDK DETAASQSKE IKKEEEVQPK AENEEEEVHK EEQSGEEEKL
     TNDQDKDLTE EKNGTLGDQK DTLAELQHSS PKVQPAQKTA EEEDGEEKEN PESPKSPKSA
     DTEKSPEEEE EERLDEDDKS EKSSQAEVSA ASEQKNFDEE SIASLSTSAR DETRDGFCPD
     DLPETSALQA LQDRAFGFSF WPKDRVMINR MDNICEAVLK GKWPVNRRHV FDFPGNLLPG
     HGSSATTAAA AMATESPLQR RSLAELTMAG IHTPFSGSED KTLSPQVHVS ETLSLTVPRQ
     RRRRRKKIEI EAERAAKRRN LMEMVAQLRE SHAAAESQSQ AIDLTKASPS LTSFSSALVT
     NSSLKAQMDL LQQGPATGHR ANGSLEADLP VIRRRRGRRK NVEGLELLAN VSPSARSLAS
     GNLEEEETAV SNKELGEWLR QHPTYTMDMP GFTPKNEDLL LSPFSKPKQK RHRCRNPNKI
     DINTLTGDER VPVVNRRNGR KMGGAMAPPM KELPRWLLEN PEFSIAPDWT DIVKQSGFLP
     EAMFDRLLTG PVVREEGVRR RGRRPKSEIA KAAAASLATA ASSAGGINPL LLNSLFGGMD
     LSSLQSLQSL QLAAGLMAFP PPTDPKQAAA NAAAASMLPL MLPGMGGLPN MATALPNMFS
     LGGLFGENRN EASLSEDAVA SQIPAADSSA EATINGDAAT LLAAAGMSAN TLAFNPFLLS
     TMAPGLLYPS MFLPPGLGGL SLPGFPTASN LAELQNAMAG ALGGSAGTPN VLRDQEKEDK
     KADLKAAAEE EEEEEEEDEE GGGESDLAEE KEGEMRSEAD YSALEDGGMG EEEEEAAAEE
     AAASSQKDKS D
//
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