GenomeNet

Database: UniProt
Entry: Q06A37
LinkDB: Q06A37
Original site: Q06A37 
ID   CHD7_CHICK              Reviewed;        3011 AA.
AC   Q06A37;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-OCT-2019, entry version 99.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 7;
DE            Short=CHD-7;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD7;
GN   Name=CHD7;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=17149726; DOI=10.1002/bdra.20330;
RA   Aramaki M., Kimura T., Udaka T., Kosaki R., Mitsuhashi T., Okada Y.,
RA   Takahashi T., Kosaki K.;
RT   "Embryonic expression profile of chicken CHD7, the ortholog of the
RT   causative gene for CHARGE syndrome.";
RL   Birth Defects Res. A Clin. Mol. Teratol. 79:50-57(2007).
CC   -!- FUNCTION: Probable transcription regulator. Maybe involved in the
CC       in 45S precursor rRNA production (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P2D1}.
CC   -!- TISSUE SPECIFICITY: Expressed in the neural epithelium, otic
CC       placodes, optic placodes, branchial arches, and the olfactory
CC       placodes,. {ECO:0000269|PubMed:17149726}.
CC   -!- DEVELOPMENTAL STAGE: Expression is pan-neuronal at stages 8-20.
CC       Expressed throughout the rostral neural ectoderm and along the
CC       rostrocaudal axis but is absent from the more lateral, non-
CC       neuronal ectoderm. Adjacent to the neural tube, detected at the
CC       optic and otic placodes. At stage 20, expression is observed in
CC       the branchial arches and olfactory placodes in addition to brain
CC       and optic and otic placodes. {ECO:0000269|PubMed:17149726}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; DQ978381; ABI96999.1; -; mRNA.
DR   RefSeq; NP_001071054.1; NM_001077586.2.
DR   SMR; Q06A37; -.
DR   STRING; 9031.ENSGALP00000024904; -.
DR   PaxDb; Q06A37; -.
DR   GeneID; 421140; -.
DR   KEGG; gga:421140; -.
DR   CTD; 55636; -.
DR   eggNOG; KOG0383; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   HOGENOM; HOG000246942; -.
DR   InParanoid; Q06A37; -.
DR   KO; K14437; -.
DR   OrthoDB; 7181at2759; -.
DR   PhylomeDB; Q06A37; -.
DR   PRO; PR:Q06A37; -.
DR   Proteomes; UP000000539; Unplaced.
DR   Bgee; ENSGALG00000015472; Expressed in 10 organ(s), highest expression level in cerebellum.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.28.130; -; 2.
DR   Gene3D; 3.40.50.10810; -; 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; IPR000330; SNF2_N.
DR   Pfam; PF07533; BRK; 2.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00592; BRK; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF160481; SSF160481; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54160; SSF54160; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chromatin regulator; Coiled coil; Complete proteome;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; rRNA processing;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   3011       Chromodomain-helicase-DNA-binding protein
FT                                7.
FT                                /FTId=PRO_0000289965.
FT   DOMAIN      801    868       Chromo 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      883    948       Chromo 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      981   1155       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1295   1465       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     994   1001       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED     2403   2433       {ECO:0000255}.
FT   MOTIF      1106   1109       DEAH box.
FT   COMPBIAS    151    225       Gln-rich.
FT   COMPBIAS    492    560       Gln-rich.
FT   COMPBIAS    602    720       Lys-rich.
FT   COMPBIAS   1939   1945       Poly-Arg.
FT   COMPBIAS   2248   2251       Poly-Asp.
FT   COMPBIAS   2728   2738       Poly-Ala.
FT   COMPBIAS   2782   2787       Poly-Ala.
FT   COMPBIAS   2863   2899       Thr-rich.
FT   MOD_RES    2561   2561       Phosphoserine. {ECO:0000250}.
SQ   SEQUENCE   3011 AA;  338213 MW;  E544AB2C80E7C6D7 CRC64;
     MADPGMMSLF GEDGNIFSEG LEGLGECGYP ENTVNPMGQQ MPMDQGFPSL QSSLHHPPAN
     QNQAKLTHFD HYNQYEQQKM HLMDQPNRMI SNAPGNGIAS PHSQYHNPPV PQVPHGSGAS
     GQMGVYPSMQ NERHGQPFVD SGSMWGPRAV QVPDQIRAPY QQQQQQPQPT QPPQAPSGPP
     GQGHPQHMQQ MGNYMARGDF SMQQHGQPQQ QRMNQFSQGQ EGLNQGNPFI ATSGPGHLSH
     VPQQNPSMAP SLRHSVQQFH HHPPTALHGE SVAHSPRFSP NPPQQGAVRP QTLNFSSRSQ
     TVPSPTINNS GQYSRYPYSN LNQGLVNNTG MNQNLGLTNN TPMNQSVPRY PNAVGFPSNS
     GQGLMHQQPI HPSGSLNQMN TQTMHPSQPQ GTYASPPPMS PMKAMSNPAG TPPPQVRPGS
     AGIPMEVGSY PNIPHPQPSH QPPGAMGIGQ RNMGPRNMQQ NRPFMGMSST PREMGGHMRP
     NGCPGVGLAD PQAIQERLIS GQQLPSQQQS FQQQMPTCPP MQPHPGIHHQ SSPPPHPHHQ
     PWAQLHQSPQ NTPQKVPVLQ HSPSEPFLEK PVPDMTQVSG PNTQLVKSDD YLPSVEPQPQ
     QKKKKKKNNH IAAEGPSKSF GKEDFPGGLD SQNLSRNSVD CSQEDKKKKK KPKAKKEPKD
     PKEPKEKKEP KTPKVPKTPK EPKEKKAKNT TPKPKTSKKT SNKKTDSESS AAKKKVNKGK
     EGSENSDLDK TPPPSPHPED EDDPGVQKRR SSRQVKRKRY TEDLEFKISD EEADDADAAG
     RDSPSNTSQS EQQESADAEG PVVEKIMSSR SVKKKMENGE EVEIEEFYVK YKNFSYLHCQ
     WASVEELDKD KRIQQKIKRF KAKQGQNKFL SEIDDELFNP DYVEIDRILD FSRSTDDNGE
     PVTHYLVKWC SLPYEDSTWE LKQDIDQAKI EEFEKLMSRE PEMERVERPP ADDWKKSESS
     REYKNNNKLR EYQLEGVNWL LFNWYNTRNC ILADEMGLGK TIQSITFLYE IYLKGIHGPF
     LVIAPLSTIP NWEREFRTWT ELNVVVYHGS QASRRTIQLY EMYFKDPQGR VIKGSYKFHA
     IITTFEMILT DCPELRNIPW RCVVIDEAHR LKNRNCKLLE GLKMMDLEHK VLLTGTPLQN
     TVEELFSLLH FLEPGRFPSE TTFMQEFGDL KTEEQVQKLQ AILKPMMLRR LKEDVEKNLA
     PKEETIIEVE LTNIQKKYYR AILEKNFAFL SKGGGQANVP NLLNTMMELR KCCNHPYLIN
     GAEEKILEEF KETHNADSPD FQLQAMIQAA GKLVLIDKLL PKLKAGGHRV LIFSQMVRCL
     DILEDYLIQR RYPYERIDGR VRGNLRQAAI DRFSRPDSDR FVFLLCTRAG GLGINLTAAD
     TCIIFDSDWN PQNDLQAQAR CHRIGQSKSV KIYRLITRNS YEREMFDKAS LKLGLDKAVL
     QSMSGRENAT NGVQQLSKKE IEDLLRKGAY GALMDEEDEG SKFCEEDIDQ ILLRRTHTIT
     IESEGKGSTF AKASFVASGN RTDISLDDPN FWQKWAKKAE LDIDALNGRN NLVIDTPRVR
     KQTRLYSAVK EDELMEFSDL ESDSEEKPST KPRRPQDKSQ GYARSECFRV EKNLLVYGWG
     RWTDILSHGR YKRQLTEQDV ETICRTILVY CLNHYKGDEN IKSFIWDLIT PTADGQTRAL
     VNHSGLSAPV PRGRKGKKVK AQSSQPMLQD ADWLTTCNPD VLFQEDSYRK HLKHHCNKVL
     LRVRMLYYLR QEVIGDQADR ILEGADSSEV DVWIPEPFHA EVPADWWDKE ADKSLLIGVF
     KHGYEKYNSM RADSTLCFLE RVGMPDAKAI AAEQRGTDML ADGGDGGEFD REDEDPEYKP
     TRTPFKDEID EFANSPPEDK EESIEIHPNK HSESNSELGQ LYWPNTSTLT TRLRRLITAY
     QRSYKRQQMR QEALMKTDRR RRRPREEVRA LEAEREAIIT EKRQKWTRRE EADFYRVVST
     FGIIFDPIKH QFDWNQFRAF ARLDKKSDES LEKYFNGFVN MCRRVCRMPV KPDDEPPDLS
     TMIEPITEER ASRTLYRIEL LRKIREQVLH HPQLGERLKL CQPSLDLPEW WECGKHDKDL
     LIGAAKHGVS RTDYHILNDP ELSFLEAHKN FAQNRGTGNA NTVSSLHPVG AGCSQTPPIV
     PSTPVQEEKS TEQTESKVEG SENPAAKEKS DIKEETDIAD KDTKQDCDAE AETGSVKCEL
     KDIEMSTDVD PKSISEKGSE EDEEEKLDDD DKSEESSQPE AGAVSQGKNF DEESNASMST
     ARDETRDGFY MEDGDPSVVQ LLHERTFAFS FWPKDRVMIN RLDNICEAVL KGKWPVNRRQ
     MFDFQGLIPG YTPTAVDSPL QKRSFAELSM IGQASISGSE DITASPQLSK EDALNLSVPR
     QRRRRRRKIE IEAERAAKRR NLMEMVAQLR ESQVVSENGQ EKVVDLSKAS REATSSTSNF
     SSVTSKFILP NVSTPVSDAF KTQMELLQAG LSRTPTRHLL NGSLIDGEPP MKRRRGRRKN
     VEGLDLLFMS NKRTSLTVED AEVTKAFEED MEALPARNIP SPGQLDPDTR IPVINLEDGT
     RLVGEDAPKN KDLVEWLKLH PTYTVDMPSY VPKSADVLFS SFQKPKQKRH RCRNPNKLDI
     NTLTGEERVP VVNKRNGKKM GGAMAPPMKD LPRWLEENPE FAVAPDWTDI VKQSGFVPES
     MFDRLLTGPV VREEGASRRG RRPKSEIAKA AAAAAAVAST SGINPLLMNS LFAGMDLTSL
     QNLQNLQSLQ LAGLMGFPPG LATAAAAGGD AKNPAAMLPL MLPGMAGLPN MFGLSGLLNN
     PITATTGNAT TASGQGETED GASKAEEKKN ENEEENKDSE KSTDTVSATD SANGSVSAAT
     AATTATATTT TTTNTGLPTN PLAFNPFLLS TMAPGLFYPS MFLPPGLGGL TLPGFPALAG
     LQNAVGSNEE KATDKTEGTA FKDEENLEGS DAEESLDKTA DSSILEDEIA QGEELDSLDG
     GEEIENNEND E
//
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