ID A0A3Q4HM05_NEOBR Unreviewed; 2812 AA.
AC A0A3Q4HM05;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD6 {ECO:0000313|Ensembl:ENSNBRP00000018197.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000018197.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000018197.1}
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; 32507.ENSNBRP00000018197; -.
DR Ensembl; ENSNBRT00000018687.1; ENSNBRP00000018197.1; ENSNBRG00000013839.1.
DR GeneTree; ENSGT00940000158986; -.
DR OMA; HMERWTH; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000013839; Expressed in muscle tissue and 4 other cell types or tissues.
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 CDD; cd18663; CD2_tandem_CHD5-9_like; 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:SF2; -; 1.
DR PANTHER; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 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; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 353..406
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 452..626
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 766..935
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1761..1800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1944..1976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2270..2321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2450..2486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2577..2657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2720..2771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1870..1890
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2278..2296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2297..2320
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2592..2631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2636..2655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2730..2767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2812 AA; 311952 MW; E064E7B191933F67 CRC64;
MFTGLLKHTP PQASAAAASS SSSDQNSNAQ TTAPTIPRGH LVVGTKDQLR LLTPVGSTVT
SNHCTTSGVH AAKHSGGAPR PPSSMSEEDD GGGGGRVKKK RKKKDKREWE KAGVECEEKE
SSKPKKRREE REPIVVSLRK SKEPKEAKEG KERKERRTKG KEGRTESETV LKNVSGVKTL
LEWRITHQNS CPYRDPGAAP VEKKKKGKRR NQELAVQEGV ESDDTTSMSA INMGGEDSQD
PLDNAKRRSG RQVKRRKYNE DLDFKVVDDD GETIAVLGAG RIAALNATAL AWQAEEPPED
EANIIEKILA VRTVKKEKDP RIHQKIKRFR TKQAQMKHLF AEPDEDLFNP DYVEVDRVLE
VAVTTDTETG EEVTHYLVKW CSLSYEEATW ELQEDLDPEK IKEFEEIQKL PADLRHIERP
SPEKWQKLER SRDYRNGNQL REYQLEGMNW LLFNWYNRKN CILADEMGLG KTIQSITFLY
EIFSMGIRGP FLIIAPLSTI TNWEREFRTW THMNVIVYHG SQISRQMILQ YEMFHRDPQG
NTIPGVLKFH GLITTFEMIM ADCPELKKLH WRCVVIDEAH RLKNRNCKLL EGLKLMNLEH
KVLLTGTPLQ NSVEELFSLL NFLEPLQFPS ESTFLEEFGD LKTDEQVKKL QAILKPMMLR
RLKDDVEKNL APKEETIIEV ELTNIQKKYY RAILEKNFSF LSKGANQHNM PNLINTMMEL
RKCCNHPYLI TGAEEKILES FKKSHSPEAP DFQLQAMIQA AGKLVLIDKL LPKLLAGGHK
VLVFSQMVRC LDILEDYLIQ RRYTYERIDG RVRGNLRQAA IDRFCKPDSD RFVFLLCTRA
GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQSKA VKVYRLITRN SYEREMFDKA
SLKLGLDKAV LQDINRKGSL NGVQQLSKLE VEDLLKKGAY GALMDEEDEG SKFCEEDIDQ
ILQRRTQTIT IQSEGKGSTF AKASFISSGN RTDISLDDPN FWQKWAKIAE VEIDSKSEKE
SLVIDTPRVR KQTRHYNSFE DDELMEFSEL DSDSEERPCR TRRLGERSRR YLRAECFRVE
KNLLIFGWGR WKDILNHGRF KWHLTERDME VICRALLVYC LRHYKGDDKI KSFIWDLITP
TKEGQDQALV NHSGLSAPVP RGRKGKKLKN QLNVTEVKNA DWLVHCNPEV VLQDESYKKH
LKQHCNKVLL RVRMLYYLKV EVLGEAATQG LEGVPASKLE VPLPDIDYIE IPVSWWDAEA
DKSLLIGVHK HGYERYNAMR ADPDLCFLER VGMPDVTALS SEQGGGEVAS DVADSKSSPE
TILVMCFLLS SLPLSLSLHV VQARPLWPTG PALTARLRRL ITAYQRFTLR REPLLRHDFI
HHAGGPLAWQ LGEDLRRCSV VATEPDPLFL EWQRRWTRRE QADFYRTVSS FGVVYDPERK
AFDWSQFRAL ARLERKTDES LERYFNSFVN MCRTACKLPP RKEEGLVDPA VIVEPLTEER
AARTLYRIEL LRKIREQVLR HPLLSARLQL CRPSLYLPVW WESGKHDRDL LIGAARHGLS
RTDFYILNDP QLSFLEAHRN YVRGHPLPHP HCCLYDSGLG RHSPQPPEYP HQSSHHHHHH
HHSLGIVPGP RGDFLDCPPL DETLELGTLQ HDTMSADSLH GGKVSKDALN GFPFNSAAGG
QSMLNSYGVG GTDLDSKLRS DVLVGEQGSS EETGLMAPSV ELDQLQAPWD STDHTSPAHH
MFNESDPILG PSTLETGFLE EEDEEAQGGD RGGEEGGTLE ECLGLPPSSP PSHPSAGDSV
EPLSSSYMLF KVGFTSLADH TDLSASPPLP YVPPPPLSLS DITAHEPQDG LGHSDVSESL
TNPVEDGDDR EESTGFEFDD KEEEEVEDLS RETLEQNVEK QRESSEIKPE AKPEVLGFTA
LSEVKTETKH EMLEADSTVL TPKLEQNDGL VETSESAELK GQVKEERPST PGFSASPRFA
APISVCEIPD SLHETREPTI AQLLQEKALY SFSEWPKDRV IINRLDSICH AILKGKWPSS
SEQYDSPAAL AANSCLANSL AQHHQHRAGF LSTTASGSVP TQARERLVAP AFLPELKRAG
GRRSFDYEAA AAAAAKVLAG KSASSCHTAV TTSSSSDKAP VVAPPSHRTG AILINGWQEA
AIDLTKSSGE ISTTSNIGTN EAVVAPGISH LNAGAGSSHK IPPPPPITAP LPGPVGIDMA
GILQAGLIHP VTGQIVNGSL RGDDSMRRRR GRRRNVEALY SEFTKSRGLH LPESQGRVEV
ISHSSVSSST SSPSPSPSER PAGPPTPSSS STPTPTQTPP QPEIVAIDRE AAGKGLIEWL
RQNPGYTMDL PAFAHSGAGL LHGFVERPKQ RRHRCKDPTK LDINSLTGEE RVPVVHRGTG
RRLGGAMAPA IKELSRWLDA NSEYYVAPDW ADVVKHSGFL PEGKFSRILT EPVNKDPSSR
RRGRRPRSEM PKPLLSVSDS SSPGLGPPLF MNGGLIGSMD SMVAMQNLRS GIPGIPISGI
MAAGFPHGFP AAVSAGGAGG SAEDAKNGLS MLPMMLHGIP HPHGAAIPQH ALFSVGTMMA
HTPPPPSPHP SSSSSSSTSS SSSASAVKVT TTTAPSATEA ASPSSTTPAE REGSAPAAGG
EKDRTREEKG AAEANKRPVV AEAAAIITST TRAHLSSAHL GAGTGSHLTF NPFLIPGMSH
GLLYPHMFLP HGGIMALPAM PPGAVDSSPG SPKRRKKRGR EEVEREEERE KAATGDGEER
ESTDKAGLKD SPLPALSSCL LCCSPFSAEQ QCKICAVSVS QCPCKDFYYD DD
//
