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Database: UniProt
Entry: W5MK58_LEPOC
LinkDB: W5MK58_LEPOC
Original site: W5MK58_LEPOC 
ID   W5MK58_LEPOC            Unreviewed;      2443 AA.
AC   W5MK58;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
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:ENSLOCP00000008767.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008767.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000008767.1}
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   EMBL; AHAT01020892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01020893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01020894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01020895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSLOCT00000008777.1; ENSLOCP00000008767.1; ENSLOCG00000007225.1.
DR   GeneTree; ENSGT00940000155706; -.
DR   HOGENOM; CLU_000315_5_1_1; -.
DR   Proteomes; UP000018468; Linkage group LG23.
DR   Bgee; ENSLOCG00000007225; Expressed in camera-type eye and 13 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: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; cd18061; DEXHc_CHD9; 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:SF1; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 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; 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:UP000018468};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          315..381
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          414..588
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          728..884
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1002..1025
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1573..1776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1849..1877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1932..1956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2262..2319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2373..2443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1585..1618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1685..1741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1742..1764
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2275..2293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2417..2436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2443 AA;  271576 MW;  0A67CC5E0E7E8508 CRC64;
     MSSVKRPRGR PPSSKNTNGS SGHTRVLSPQ LKSGTSSSSS SSSSSSEKRQ KKKPLMEQAL
     EDKQEKANRI ISEAIAKARE RGEKNIPRVM SPESFPCSST PPRQDHKPHH AKAPPTDPPS
     RKAKGPAASR SKQKTKIGKI VIKFGKKKKR KTESSEELSD TEPLPRRCSK DDDSKRRSNR
     QVKRKKYAEE GECKVSDEEV KVIVKAKKTA SGSRKEQPVQ LFVENPSEED AAVVDKIMSS
     RIGKKEVSPG VVVEVEEFYV KYKNYSYLHC EWATEQQLVK DKRIQQKIKR FKIKQAQRAH
     FFADMEEEPF NPDYVEVDRV LEVSYCKDKD TGEPVVYYLV KWCSLPYEDS TWELKEDVDQ
     SKIEEFEQLQ AARPDPRRVE RPPASMWKKT EQSREYRNGN RLRDYQLEGV NWLLFNWYNR
     RNCILADEMG LGKTIQSITF LEEIFLTGIR GPFLIIAPLS TIANWEREFR TWTDLNVIVY
     HGSMVSRQML QQYEMYFRDS QGRVIRGAYK FHAIVTTFEM ILGGCPELNA IEWRCVIIDE
     AHRLKNKNCK LLEGFKLMSL EHKVLLTGTP LQNTVEELFS LLHFLEPLRF PSESTFMQEF
     GDLKTEEQVQ KLQAILKPMM LRRLKEDVEK KLAPKEETII EVELTNIQKK YYRAILEKNF
     SFLSKGAGQA NVPNLVNTMM ELRKCCNHPY LIKGAEEKIL EEFREVHNPA ALDFHLQAMV
     QSAGKLVLID KLLPKMKAGG HKVLIFSQMV RCLDILEDYL IQRRYLYERI DGRVRGNLRQ
     AAIDRFSKPD SDRFVFLLCT RAGGLGINLT AADTCIIFDS DWNPQNDLQA QARCHRIGQN
     KAVKVYRLIT RNSYEREMFD RASLKLGLDK AVLQSMSGRE NSVGGIQQLS KKEIEDLLRR
     GAYGAIMDEE DEGSKFCEED IDQILQRRTK TITIESEGRG STFAKASFVA SGNRTDISLD
     DPNFWDKWAK KAEIDLDTIN GRNSLVIDTP RVRKQTRPFS ATKDELAELS EPESEGDDKP
     KLRRPYDRLN GYGRTECFRV EKNLLVYGWG RWKDILLHGR FKRQLNEHDV EIICRALLAY
     CLVHYRGDDK IKSFMWDLIA PTEDGQTKEL QNHLGLSAPV PRGRKGKKVK TQPSSFDIQK
     AEWIRKHNPE HLLQDDGYKK HLKHHCNKVL LRVRMLYYLK QEVIGDQSQK VLDGVDSSET
     EIWVPEPDHS ELPAHWWDTE ADKSLLIGVY KHGYEKYNTI RADPALIFLE RVGRPDDKAI
     AAEQRANDFM DGDGDDPEYK PAPALLKDDI EDDASSPGDL VIADGGGEGG MLMEGDALYW
     PPPSALTTRL RRLITAYQRN TKNRQIQHIQ QALPAQPSAL LSTLNDNINP KIAAKIERQQ
     RWTRREEADF YRVVSTFGVV FDPEQGRFDW TKFRAMARLH KKTDDSLQKY LCAFTAMCRR
     VCRLPPREGE SVDPSISIQP ITEERASRTL YRIELLRKVR EQVLRHPQLY ERLQLCQPGP
     DLPVWWEPGA HDRDLLIGAA KHGVSRTDYH ILRDPELCFM TAQSNYSQNK GAQSRTPTPL
     LLPQYQAMVA GSPLAAQPRP PDPRTAQVEE PRQRAEHLKE EPPTSEEEGA ERKGKAEQWS
     PRSGAQTQGL VDSKAGGQVK GESERRSMVA ARTEPLTPNS VAKKQKRGSK RGRRQGRRAS
     CTDSDTERSS SCSSSRSSSS SSSSSSSSSS CSRSGSSSSS SSSSCSSGSS SSSSSSSSSS
     SEDSDSDRED RKASVAEAAK IKGFDEDSVA SLSTTQDETQ DSFLTDNGLH SSSHAFQGGY
     MLAASYWPKD RVMINRLDSI CQAVLKGAWP AARRGYEGSA VSSFYTTKLL DSPSDQGGPP
     GPREDPAQSP QMSKQEGSLK LTFQKQGLPQ KRPLEGEDGP LGQQQYLARL RELQSASDTS
     LADFTKPLPT AAGAAGPVRA NGALDGQPVV KKRRGRRKNV EGMDLLFLNK NRSTPDHVGP
     GVGGSAQASP AVVPGLGYGP SQAPVDTESR VPVINLKDGT RLAGDDAPKK KDLEQWLKEH
     PGYVADVGAF IPGLNKMTFQ DGRPRQKRHR CRNPNKIDIN SLTGEERVQI INRRNARKVG
     GAFAPPLKDL CRFLKENPEY GVPPEWADVV KRSGFLPESM FDRILTGPIV REEVSRRGRR
     PKSEMAKAAA AAANASAATL SINPLLSNGL LSGMDLSSLQ ALQQNLQSLQ SLHLTAGLMG
     LPGGLAAAGD ANNLAAMFPM MLSGMAGLPN LLGMGGLLGK PQEGAGVSED GTKKGNGGSG
     DSSSSASKTP VPTDTKGERT EGQGADQCPS DPSTSGATAP LSASAVAAAA ASSNHPLALN
     PLLLSSMLYP GMLLTPGLNL PISALSQSGV FDAQQQSTSA RPAATASGET PRGAGGSTPA
     KGQEPGEQKE NSAEEGSEKA GSSSSESEGS SSSSEDSDSS NED
//
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