ID A0A218VBI6_9PASE Unreviewed; 3012 AA.
AC A0A218VBI6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD7 {ECO:0000313|EMBL:OWK63363.1};
GN ORFNames=RLOC_00005525 {ECO:0000313|EMBL:OWK63363.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK63363.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK63363.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK63363.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK63363.1}.
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DR EMBL; MUZQ01000013; OWK63363.1; -; Genomic_DNA.
DR STRING; 299123.ENSLSDP00000020127; -.
DR OrthoDB; 22878at2759; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18668; CD1_tandem_CHD5-9_like; 1.
DR CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR CDD; cd18059; DEXHc_CHD7; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
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; 2.
DR Pfam; PF00385; Chromo; 2.
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; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
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, ECO:0000313|EMBL:OWK63363.1};
KW Helicase {ECO:0000313|EMBL:OWK63363.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 802..869
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 884..949
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 982..1156
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1296..1466
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 94..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1839..1887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2153..2292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2826..2901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2949..3012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1854..1887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2171..2241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2259..2277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2278..2292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2841..2865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2866..2901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2951..2985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2988..3012
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3012 AA; 338159 MW; 086AE3983D35CD32 CRC64;
MADPGMMSLF GEDGNIFSEG LEGLGECGYP ENTVNPMGQQ MPMDQGFPTL QSSLHHPPAN
QNQAKLTHFD HYNQYEQQKM HLMDQPNRMI SNAPGNGIAS PHSQYHNPPV PQVPHSSGAG
GQMGVYPGMQ NERHGQPFVD SGSMWGPRAV QVPDQIRAPY QQQQQQQQPQ PTQPPQAPSG
PPGQGHPQHM QQMGNYMARG DFSMQQHGQP QQQRMNQFSQ GQEGLNQGNP FIATSGPGHL
SHVPQQNPSM APSLRHSVQQ FHHHPPTALH GESVAHSPRF SPNPPQQGAV RPQTLNFSSR
SQTVPSPTIN NSGQYSRYPY SNLNQGLVNN TGMNQNLGLT NNTPMNQSVP RYPNAVGFPS
NSGQGLMHQQ PIHPSGSLNQ MNTQTMHPSQ PQGTYASPPP MSPMKAMSNP AGTPPPQVRP
GSAGIPMEVG SYPNIPHPQP SHQPPGAMGI GQRNMGPRNM QQNRPFMGMS STSREMGGHM
RPNGCPGVGL ADPQAIQERL ISGQQLPSQQ QSFQQQMPTC PPMQPHPGIH HQSSPPPHPH
HQPWAQLHQS PQNTPQKVPV LQHSPSEPFL EKPVPDMTQV SGPNTQLVKS DDYLPSIEPQ
PQQKKKKKKN NHIAAEGPSK GFGKEDFPGG LDSQNLSRNS VDCSQEDKKK KKKPKAKKEP
KDPKEPKEKK EPKTPKVPKT PKEPKEKKAK NTTPKPKTSK KASNKKQDSE ASAAKKKVKG
KEGSENSDLE KTPPPSPHPE DEDDSGVQKR RSSRQVKRKR YTEDLEFKIS DEEADDADAA
GRDSPSNTSQ SEQQESADAE GPIVEKIMSS RLVKKKMENG EEVEVEEFYV KYKNFSYLHC
QWASVEELDK DKRIQQKIKR FKAKQGQNKF LSEIDDELFN PDYVEVDRIM DFSRSTDDNG
EPVTHYLVKW CSLPYEDSTW ELKQDIDQAK IEEFEKLMSR EPEMERVERP PADDWKKSES
SREYKNNNKL REYQLEGVNW LLFNWYNTRN CILADEMGLG KTIQSITFLY EIYLKGIHGP
FLVIAPLSTI PNWEREFRTW TELNVVVYHG SQASRRTIQL YEMYFKDPQG RVIKGSYKFH
AIITTFEMIL TDCPELRNIP WRCVVIDEAH RLKNRNCKLL EGLKMMDLEH KVLLTGTPLQ
NTVEELFSLL HFLEPGRFPS ETTFMQEFGD LKTEEQVQKL QAILKPMMLR RLKEDVEKNL
APKEETIIEV ELTNIQKKYY RAILEKNFAF LSKGGGQANV PNLLNTMMEL RKCCNHPYLI
NGAEEKILEE FKETHNADSP DFQLQAMIQA AGKLVLIDKL LPKLKAGGHR VLIFSQMVRC
LDILEDYLIQ RRYPYERIDG RVRGNLRQAA IDRFSRPDSD RFVFLLCTRA GGLGINLTAA
DTCIIFDSDW NPQNDLQAQA RCHRIGQSKS VKIYRLITRN SYEREMFDKA SLKLGLDKAV
LQSMSGRENS TNGVQQLSKK EIEDLLRKGA YGALMDEEDE GSKFCEEDID QILLRRTHTI
TIESEGKGST FAKASFVASG NRTDISLDDP NFWQKWAKKA ELDIDALNGR NNLVIDTPRV
RKQTRLYSAV KEDELMEFSD LESDSEEKPS TKPRRPQDKS QGYARSECFR VEKNLLVYGW
GRWTDILSHG RYKRQLTEQD VETICRTILV YCLNHYKGDE NIKSFIWDLI TPTADGQTRA
LVNHSGLSAP VPRGRKGKKV KAQSSQPMLQ DADWLTTCNP DILFQEDSYR KHLKHHCNKV
LLRVRMLYYL RQEVIGDQAD KILEGADSSE VDVWIPEPFH AEVPADWWDK EADKSLLIGV
FKHGYEKYNS MRADAALCFL ERVGMPDAKA IAAEQRGTDM LADGGDGGEF DREDEDPEYK
PTRTPFKDEI DEFANSPPED KEESIELHPS KHSESNAELG QLYWPNTSTL TTRLRRLITA
YQRSYKRQQM RQEALMKTDR RRRRPREEVR ALEAEREAII TEKRQKWTRR EEADFYRVVS
TFGVIFDPVK HQFEWNQFRA FARLDKKSDE SLEKYFNGFV NMCRRVCRMP VKPDDEPPDL
STLIEPITEE RASRTLYRIE LLRKIREQVL HHPQLGERLK LCQPSLDLPE WWECGKHDKD
LLIGAAKHGV SRTDYHILND PELSFLEAHK NFAQNRGTGN ANIVSSVNPL GAGCSQTPPV
VPCTPVPEEK TTEQTESKVE GSENPAAKEK SEIKEETDTT DKDTKPDCDA EAEPGSVKCE
LKDIEMNTDV DPKSISEKGS EEDEEEKLED DDKSEESSQP EAGAVSQGKN FDEESNASMS
TARDETRDGF YMEDGDPSVV QLLHERTFAF SFWPKDRVMI NRLDNICEAV LKGKWPVNRR
QMFDFQGLIP GYTPTAVDSP LQKRSFAELS MVGQASVSGS EDLTASPQLS KEDALNLSVP
RQRRRRRRKI EIEAERAAKR RNLMEMVAQL RESQVVSENG QEKVVDLSKA SREATSSTSN
FSSVTSKFIL PNVSTPVSDA FKTQMELLQA GLSRTPTRHL LNGSLIDGEP PMKRRRGRRK
NVEGLDLLFM SNKRTSLTVE DAEVTKAFEE DMEALPARNI PSPGQLDPDT RIPVINLEDG
TRLVGEDAPK NKDLVEWLKL HPTYTVDMPS YVPKSADVLF SPFQKPKQKR HRCRNPNKLD
INTLTGEERV PVVNKRNGKK MGGAMAPPMK DLPRWLEENP EFAVAPDWTD IVKQSGFVPE
SMFDRLLTGP VVREEGASRR GRRPKSEIAK AAAAAAAVAS TSGINPLLMN SLFAGMDLTS
LQNLQNLQSL QLAGLMGFPP GLATAAAAGG DAKNPAAMLP LMLPGMAGLP NMFGLSGLLN
NPITATTGNA TTASGQGETE DGASKAEEKK NENEEENKDS EKSTDTVSAT DSANGSVSAA
TAATTATATT TTTTNTGLPT NPLAFNPFLL STMAPGLFYP SMFLPPGLGG LTLPGFPALA
GLQNAVGSNE EKATDKTEGA AFKDEENLEG SDAEESLDKT ADSSVLEDEI AQGEELDSLD
GGEEIENNEN DE
//
