ID H3DR44_TETNG Unreviewed; 1659 AA.
AC H3DR44;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD9 {ECO:0000313|Ensembl:ENSTNIP00000022993.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000022993.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000022993.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; 99883.ENSTNIP00000022993; -.
DR Ensembl; ENSTNIT00000023235.1; ENSTNIP00000022993.1; ENSTNIG00000003825.1.
DR GeneTree; ENSGT00940000155706; -.
DR InParanoid; H3DR44; -.
DR OMA; TIGMSHI; -.
DR TreeFam; TF313572; -.
DR Proteomes; UP000007303; 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: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; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 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; 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; 2.
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:UP000007303};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 142..185
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 242..418
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 445..601
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1214..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1659 AA; 188783 MW; FC3E412241976503 CRC64;
QKRRSNRQVK RKKYAEELEA RLSDDEVKVI VKAKKTNPAS KESGHQLFVE NPTEEDAAVV
DKIMSSRIVK QEVSPGVLIE IEEFFVKYKN YEYYLFCLPH VYYSLNTKKN KEQCXKRFKM
KQAQRALLFA DMEEEPFNPD YVEVDRVLEV SYCEDKDTGE EVVYYLVKWC SLPYEDSTWE
LKDDVDLNKI EEFEQLQAVK PDSRRMKRPS VNLWKKMGHS EYRNGNTLRE YQLEGVTWLL
FNWFYIPRRN CILADEMGLG KTVLCVVFGR LVMCHNRPLE VVSVQTKYIQ TKLHNNPLAG
ILLVMLWPVC QMRNLICLPY PNLDIFCINS VGRVLRSAYR FQAVITTFEM ILGGCPELNA
IEWRCVVIDE AHRLKNKNCK LLEGFKLMNL EHKVLLTGTP LQNTVEELFS LLHFLSQHAF
PQKTFHAGVC SHLQAMVQSA GKLVLIDKLL PKMKAGGHKV LIFSQMVRCL DILEDYLIQR
RYLYERIDGR VRGNLRQAAI DRFSKPDSER FVFLLCTRAG GLGINLTAAD TCIIFDSDWN
PQNDLQAQAR CHRIGQNKAV KVYRLITRNS YEREMFDRAS LKLGLDKAVL QSMSGRDNSL
GGGTGSGVSL PSSLLSKIPH SSVLDNESKS LCEEGQMRTQ RQQWMLITAI LVQEIGKKKK
TDHCRKWLLQ MGLLNQEVWR KQLEEVENFD LAKSEHVTAD IIVHSFHSPA SKTEYFRLHY
CILNIQISRH PSLAHHASHC PTVAQSLLAM IMHHRANKND RMFIRLCSNM TSCKAWDLQL
HTQDFLILGA HECMLYLQLV AMYMEAQSST VMHFIHLKVL LRVRMLYYLK QEVIGSLAQS
VLDGADSSEI KIWVPDLDNS ELPALWWDAI SDKCLLLGVF KHGYEKYNTI RADPALCFVE
RVGRPDEKAI AAEQRGNDFM DGDVDDPEYK PAPALLKDDM EKTDPLGFLM CKELCLCVSD
VVPQTESETI YWPSPSVLTA RLRRLITASQ RFTKSRQILQ IHQTQSQPTM ILSTPLYPLP
SAFNDTLNPK MAAKIERQQR WTRREEADFY RVVSTFGVVF DPNLGRFDWT KFRAMARLHK
KTDESLQKYL CAFAAMCRRV CRLPPKEGVS DSVVDPSLNI QPITEERASR TLYRVELLRQ
VREQVLCHPL LYDRLSLCQM SSDLPVWWEA GTHDRDLLIG AAKHGVSRTD YHILRDPELS
FMVAQRKYSQ TKESCAPTSL LHPQSQALLT GSPLPPPAQR DAEPCSIVPK VEPQSEGEEG
LEEKPVLQVQ DNEQQMAAAR TKPLTPNSSE RKSKKASKRG RREARRGSES DSGGSSSSSS
SHSGSTEDSE SEGEEGKKKA TSVKGFDEDS VASLSTTQDE TQVAENGITN NSSHPLQEGG
YMLAASYWPK DRVIINRLDS ICQAVLKGKW PETRRVYEPG GAVASFYTTK LLDNANSLCE
DPSASPQGSK VTKHVAENKE FSVKLNEEGG LKLTFQKQGQ MRLNGVLDSQ PLVKKRRGRR
KNVEGMDLLF MNKSRVPVPE QGPQDTESRV PVINLKDGTR LAGDDAPRRK DLEQWLNEHP
GFVADTGAFI PDGRPKQKRH RCRNPNKIDV NSLTGEERVQ IINRRNARKG YLPESMFDRI
LTGPIVPEEV SRRGRRPKNP LAKAAATATN PSASALGLN
//
