ID U3CJH2_CALJA Unreviewed; 2714 AA.
AC U3CJH2; A0A2R8MCB8; F6RZP6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD6 {ECO:0000313|EMBL:JAB18514.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB18514.1};
RN [1] {ECO:0000313|EMBL:JAB18514.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB05798.1}, and Hippocampus
RC {ECO:0000313|EMBL:JAB18514.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
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 EMBL; GAMT01006063; JAB05798.1; -; mRNA.
DR EMBL; GAMS01004622; JAB18514.1; -; mRNA.
DR STRING; 9483.ENSCJAP00000057302; -.
DR InParanoid; U3CJH2; -.
DR OrthoDB; 22878at2759; -.
DR Bgee; ENSCJAG00000017920; Expressed in testis and 6 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: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; cd18058; DEXHc_CHD6; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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:SF1; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:JAB18514.1};
KW Helicase {ECO:0000313|EMBL:JAB18514.1};
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 375..418
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 473..647
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 787..956
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2030..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2220..2239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2321..2350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2376..2422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2548..2602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2640..2714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2030..2050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2548..2564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2565..2584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2714 AA; 305734 MW; 465448FA42C86842 CRC64;
MKMKIQKKEK QLSNLKVLNH SPMSDASVNF DYKSPSPFDC STDQEEKIED DPSHCLPPKD
LYTAEEEAAT LFPRKMTSHN GMEDSGGGGT GVKKKRKKKE PGDQEGAAKG SKDREPKPKR
KREPKEPKEP RKAKEPKKAK EHKEPKQKDG AKKTRKPREA SGTKEAKEKR SCADCTARTK
SKKASKEQGP TPVEKKKKGK RKSETTVESL ELDQGLTNPS LRSPEESTES TDSQKRRSGR
QVKRRKYNED LDFKVVDDDG ETIAVLGAGR TSALSASTLA WQAEEPPEDD ANIIEKILAS
KTVQEVHPGE PPFDLELFYV KYRNFSYLHC KWATMEELEK DPRIAQKIKR FRNKQAQMKH
IFTEPDEDLF NPDYVEVDRI LEVAHTKDAE TGEEVTHYLV KWCSLPYEES TWELEEDVDP
AKVKEFESLQ VLPEIKHVER PASDSWQKLE KSREYKNSNQ LREYQLEGMN WLLFNWYNRK
NCILADEMGL GKTIQSITFL SEIFLRGIHG PFLIIAPLST ITNWEREFRT WTEMNAIVYH
GSQISRQMIQ QYEMVYRDAQ GNPLSGIFKF HVVITTFEMI LADCPELKKI HWSCVIIDEA
HRLKNRNCKL LEGLKLMALE HKVLLTGTPL QNSVEELFSL LNFLEPSQFP SETAFLEEFG
DLKTEEQVKK LQSILKPMML RRLKDDVEKN LAPKQETIIE VELTNIQKKY YRAILEKNFS
FLTKGANQHN MPNLINTMME LRKCCNHPYL INGAEEKILE DFRKTHSPDA PDFQLQAMIQ
AAGKLVLIDK LLPKLIAGGH KVLIFSQMVR CLDILEDYLI QRRYTYERID GRVRGNLRQA
AIDRFCKPDS DRFVFLLCTR AGGLGINLTA ADTCIIFDSD WNPQNDLQAQ ARCHRIGQSK
AVKVYRLITR NSYEREMFDK ASLKLGLDKA VLQDINRKGG TNGVQQLSKM EVEDLLRKGA
YGALMDEEDE GSKFCEEDID QILQRRTHTI TIQSEGKGST FAKASFVASG NRTDISLDDP
NFWQKWAKIA ELDTEAKNEK ESLVIDRPRV RKQTKHYNSF EEDELMEFSE LDSDSDERPT
RSRRLNDKAR RYLRAECFRV EKNLLIFGWG RWKDILTHGR FKWHLNEKDM EMICRALLVY
CVKHYKGDEK IKSFIWELIT PTKDGQAQTL QNHSGLSAPV PRGRKGKKTK NQLLIPELKD
ADWLATCNPE VVLHDDGYKK HLKQHCNKVL LRVRMLYYLK AEILGEAAEK AFEGTPAREL
DVPLPDIDYM EIPVDWWDAE ADKSLLIGVF KHGYERYNAM RADPALCFLE KVGMPDEKSL
SAEQGVTDGT SDIPERGNTD KEDNAEDKVD GLQKQTESSS DGGDGIFGEK KDDSRAAQDG
SDPDKSPWPV SSALTARLRR LVTVYQRCNR KELCRPEILG PGNQGYWVQE EMFRRTSEMD
LINKEAQKRW TRREQADFYR TVSSFGVVYD QEKKTFDWTQ FRIISRLDKK SDESLEQYFY
GFVAMCRNVC RLPTWKDGAP PDTTIYVEPI TEERAARTLY RIELLRKVRE QVLKCPQLHE
RLQLCRPSLY LPVWWECGKH DRDLLIGTAK HGLNRTDCYI MNDPQLSFLD AYRNYAQHKR
SDTQAPGNLC CLYQTNSKLY ESLTYTQMSR TSETLENEPE NLVKVESRDD HLSLPDVTCE
NFISKVQDVI SINHDESLLP ESLESMIYGK KVLGKEPGSF RESPSTNTES TKDVITISTS
KGGNCQPGGH EAEIASSPAF MGSLEAERVA QANIKNGKHL LMSISKEGEL CCNEAGQRPE
SIDQLEAKCL ASPSLNPGNE SGFVDMCSLN VCDSKRNLPS DQQLIDLLEN KSLESKLILS
QNHSDEEEEE ENEEENFAMA AGMGERSEIL QLMEPTTDIS REKSQGFHVD ETMKGSLEAA
NQTHGLQRAF PLPAACECHC KHMERWMHGL ENDEFEIETP KTYNPDLFRS KTNTIALEGE
PTAIPSELFK VKHELLKEPW KESAEGQKVF PTYPLEGSEL KSEDIDFENK DDYERDGNCH
SQDYPGKYSE EESKSSTSGI AGDIGDELQE ARAPTIAQLL QEKTLYSFSE WPKDRVIINR
LDNICQVVLK GKWPSSQQYE PSGTLPTPIL TSSAGSRTSL SEPEVAEHSF SNGAALAAQI
QKESFLAPVF TKDEQKHRRP YEFEVERDAK ARGLEQFSAT HGHTPIILNG WHGESAIDLS
CSSEGSPGGT SPFSVSSSTP KIGAISSLQG ALGMDLSGIL QAGLIHPVTG QIVNGSLRRD
DAAMRRRRGR RKHVEGGMDL IFLKEQTLQA GILEVHEDPG QATLSTTHPE GPGPATSATE
PATAASSQAE KAIPNKSLLD WLRQQADYSL EVPGFGANFS DKPKQRRPRC KEPGKLDVSS
LSGEERVPAV PKEPGLRGFL PENKFNHTLA EPVLRDTGPR RRGRRPRSEL LKAPSIVADS
PSGMGPLFMN GLIAGMDLVG LQNMRNMPGI PLTGLVGFPA GFATMPTGEE VKSTLSMLPM
MLPGMAAVPQ MFGVGGLLNA PMATTCTSTA PASLSSTTKS GTAVTEKTAE DKPSSHDVKT
DPLAEDKPGP GPFSDQSEPA ITTSSPVAFN PFLIPGVSPG LIYPSMFLSP GMGMALPAMQ
QARHSEIGLE SQKRKKKKTK GDNPNSHPEP APSCEREPSS DQNCTEPSAP LPTEREHVAQ
AGEGALKDSN NDTN
//
