ID C3YNT4_BRAFL Unreviewed; 2045 AA.
AC C3YNT4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=BRAFLDRAFT_82621 {ECO:0000313|EMBL:EEN58044.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN58044.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN58044.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN58044.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GG666535; EEN58044.1; -; Genomic_DNA.
DR RefSeq; XP_002602032.1; XM_002601986.1.
DR STRING; 7739.C3YNT4; -.
DR eggNOG; KOG0384; Eukaryota.
DR InParanoid; C3YNT4; -.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR CDD; cd18661; CD2_tandem_CHD1-2_like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR040793; CDH1_2_SANT_HL1.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
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; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 375..466
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 555..642
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 684..860
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 881..1056
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1753..2045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..281
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1841..1860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1868..2045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2045 AA; 231804 MW; 630550DAE82803D9 CRC64;
MFGSLSYGAG VERVGGRTQS HIPAASPSLT TVEGLPEAEF DGNFLPPDIS TTFQDPDTGS
NKVSQPQNIP PYTLENGDNS REQPSSAESG DSSSDESNSG SEDSNDEDQS KSGSSSSSQS
GSSSDSGSQS ESESKSGSGS GSSSQSESGN ESTKGDNQDE EEEDGDESND QATDNKDQAG
KMPKKDRLAD LKQMWDEYPD MYGVRRSSRA RKEPSRYNVG TEESDEDNED EDDDEDNRKR
RKNISAKSRR KRKSSENWEA ENSDSDDDDD DDDDDDDNDS GSSDDYTVKR RAKPAARPAA
RPQARVRGKA PIKGKSAANN QGRKRAGSLS EREQKRLSRR KAAANVSYKE ESPDATDSDD
LMEIAAKEEE NDDAEAIERV LNHRTGKKGS TGAITTMYAA DAAVANKPPD PEADETETQY
LIKWKDWSHL HNTWESEATL AEQKVKGIKK LENYMKKKND LQQWKDQASP EDLECQSEMN
ESLALCYKGL PTMPDYKGLP INPCPLYPCR KDHLNQASPE DLEYLECQKD QASPEDLEYL
ECQSEMNEDL LSAYQQVERI IGMAYPAAPP AYPAAPQPLE HGLQSQQPAK NSASGFPDYL
VKWQGLPYSE CSWEDGELIS MYFPDAVDGY NVRNKSQKIP GKMTAKVLKQ RPRFVALKKQ
PLYLGGTERL ELRDYQLDGL NWLAHSWCKT NSVILADEMG LGKTIQTISF LSYLFNTHAL
YGPFLLVCSV RPLVPLSTMA AWQCEFSNWA PDMNVIVYLG DVMSRNKIRE YEWCHPGNKK
LKFNCLLTTY EILLKDKSFL GGVEWACLVV DEAHRLKNDD SLLYKTLKGF DSNHRLLITG
TPLQNSLKEL WALLFFIMPA RWILTKNYKA LTKGMKGNTS SFLNIMMELK KCCNHSFLVR
PPEDPPPGQS LVTQLLRSSG KLFLLDKLLV RLRDTGHRVL IFSQMVRMLD ILAEYLTMRH
FPFQDFCFLL STRAGGLGIN LATADTVIIF DSDWNPQNDI QAQSRAHRIG QRKQVCTSTP
FNKEELSAIL KFGAEELFKE NEGEEEEMPV NIYRLVTKGS VEEDIIERAK KKMVLDHLVI
QRMDTSGRTV LSKSSAPGST STPFNKEELS AILKFGAEEL FKENEGEEEE MPEMDIDDIL
RRAETAEMVD DAGAGHELLS QFKVANFSTM EEELPEAAGK TWEDIIPAAD RQKVDDEEKQ
RELIEMHLPP RQRKFVTKLQ YGSESEGSTR RGRKRKRASS SSESDSDSDA DTKPRKRGRP
RTVPRDTIKG FSDPEVRRFV KSYKKFGMPL TRLEAIAGDA ELQEKSYADL KRLGDLLHDG
CVKAIEEYEK QMKENPEFDG KKRGPTLKLS TVTVNAPSIL RHEEEMLPLA KAIPDDPEDR
KKFRLPCRAK LAHWDVDWAV EEDSALLVGI YEYGMGSWDT VQMDPELNLS DKKLAHWDVD
WAVEEDSALL VGIYEYGMGS WDIVQMDPEL NLSDKILLDE DKKPQAKHLQ SRAEYLIRLL
NKDQLKKEAL AEGKVIKKER RPRMPKQPKD PTTVKRPKAK VKFVERKENE APLDEPNLDS
EDHREPLEEG EVEDSNDKTD IKEPVVKKVK RAKKPKTPKI VKEPSSKTTT AKPKDKNKKD
PLNADLDPDA SHSVLEDMDD LDKETFNMCK ERMRPVKKAL KQLDKPEEGL TEEEQLNHTR
QCLLKIGDRI MECLKEWTEA EEVKKWRNNL WIFVSQFTEF DARKLFKLYK HAVRRGRRRK
SFDLEVLSLN LPKKQTKEKP KPAVSSNSSV VKKEPSDSQH AHGAGKRPPG SSDRTSGWGS
DSASRDSFTS NGPWPGTSAS SSYGHTAGRS GAGGGADRWG HDRYQPGRDP FRERHRGEVS
SAYNRTGSRD YDSHRTRDSR YNADHRWDRD RDRDRERDHR DRDRGDRDYR SSRDHRDSRD
SSRGDSSSRH HRAGNKEDGG SHRSTRPDSS GERDQRLHHS QSDHKRRKRD DSWSSADDKK
KRKDSGHGGG GVHRSSTQEH RTREDTKDHR ALIEHRSPLE HRSPLEHRSP LDHGDRSNER
TDSRH
//
