ID A0A096NI99_PAPAN Unreviewed; 2902 AA.
AC A0A096NI99;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 63.
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:ENSPANP00000012697.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000012697.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000012697.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000012697.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_009194690.1; XM_009196426.2.
DR RefSeq; XP_017808845.1; XM_017953356.1.
DR RefSeq; XP_017808846.1; XM_017953357.1.
DR RefSeq; XP_017808847.1; XM_017953358.1.
DR RefSeq; XP_017808848.1; XM_017953359.1.
DR RefSeq; XP_017808849.1; XM_017953360.1.
DR RefSeq; XP_017808850.1; XM_017953361.1.
DR STRING; 9555.ENSPANP00000012697; -.
DR Ensembl; ENSPANT00000017606.3; ENSPANP00000012697.2; ENSPANG00000019307.4.
DR GeneID; 101006068; -.
DR CTD; 80205; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000155706; -.
DR OMA; ASYWPKX; -.
DR Proteomes; UP000028761; Chromosome 18.
DR Bgee; ENSPANG00000019307; Expressed in prostate gland and 68 other cell types or tissues.
DR ExpressionAtlas; A0A096NI99; baseline.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; 2.
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 Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
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:UP000028761};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 690..753
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 773..839
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 872..1046
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1186..1337
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 104..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2050..2240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2307..2339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2733..2780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2828..2902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2062..2076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2122..2140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2141..2194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2200..2216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2221..2240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2739..2764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2765..2780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2842..2863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2902 AA; 326392 MW; D7A27BE6D181C56D CRC64;
MTDPMMDFFD DANLFGETLE GLSDDAFVQP GPVSLVDELN LGAEFEPLHI DSLNHVQSTP
AHQKMTDFEQ LNQFDSIKFH HVNQSFGSPA EHVLSPHSQF NCSPIHPQNQ PNGLFPDVSD
GSPMWGHQTS TSISSQNGSP FHQQGHSHSM HQNKSFVAHH DFALFQANEQ QTQCTSLRSQ
QNRNNLNPGQ NSLSQSKNFM NVSGPHRVNV NHPPQMTNAS NSQQSISMQQ FSQTSNPSAH
FHKCSNHQEG NFNGPSPNMT SCSVSNSQQF SSHYSFSSNH ISPNSLLQSS AVLAPNHTNQ
TLSDFTGSNS FSPHRGIKQE STQHILNPNT SLNSNNFQIL HSSHPQGNYS NSKLSPVHMN
FPDPVDSGTQ MGHFNDHVET NGFSSLEENL LHQVESQTEP FTGLDPEDLL QEGLLPHFDE
STFGQDNSSH ILDHDLDRQF TSHLVTRPSD MAQTQLQSQA RSWHSSFSNH QHLHDRNHLC
LQRQPPSSKK SDGSGTYTKL QNTQVRVMSE KKQRKKVESE SKQEKANRII SEAIAKAKER
GERNIPRVMS PENFPSASVE GKEEKKGRRM KSKPKDKDSK KTKTCSKLKE KTKIGKLIIT
LGKKQKRKNE SSDEISDAEQ MPQHTLKDQD SQKRRSNRQI KRKKYAEDVE GKQSEEEVKG
SMKIKKNSAP LPGEQPLQLF VENPSEEDAA IVDKILSSRI VKKEISPGVM IDTEEFFVKY
KNYSYLHCEW ATEEQLLKDK RIQQKIKRFK LRQAQRAHFF ADMEEEPFNP DYVEVDRVLE
VSFCEDKDTG EPVIYYLVKW CSLPYEDSTW ELKEDVDLAK IEEFEQLQAS RPDTRRLDRP
PSNIWKKIDQ SRDYKNGNQL REYQLEGLNW LLFNWYNRRN CILADEMGLG KTIQSITFLY
EILLTGIRGP FLIIAPLSTI ANWEREFRTW TDINVVVYHG SLISRQMIQQ YEMYFRDSQG
RIIRGAYRFQ AIITTFEMIL GGCGELNAIE WRCVIIDEAH RLKNKNCKLL EGLKLMNLEH
KVLLTGTPLQ NTVEELFSLL HFLEPLRFPS ESTFMQEFGD LKTEEQVQKL QAILKPMMLR
RLKEDVEKKL APKEETIIEV ELTNIQKKYY RAILEKNFSF LSKGAGQTNV PNLVNTMMEL
RKCCNHPYLI KGAEEKILGE FRDAYNPAAS DFHLQAMIQS AGKLVLIDKL LPKMKAGGHK
VLIFSQMVRC LDILEDYLIH KRYLYERIDG RVRGNLRQAA IDRFSKPDSD RFVFLLCTRA
GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQNKA VKVYRLVTRN SYEREMFDRA
SLKLGLDKAV LQSMSGRESN VGGIQQLSKK EIEDLLRRGA YGAIMEEEDE GSKFCEEDID
QILLRRTKTI TIESEGRGST FAKASFVASG NRTDISLDDP NFWQKWAKKA EIDIEAISGR
NSLVIDTPRI RKQTRPFSAT KDELAELSEA ESEGEEKPKL RRPCDRSNGY GRTECFRVEK
NLLVYGWGRW REILSHGRFK RQLNEHDVEI ICRALLAYCL VHYRGDEKIK GFIWDLITPT
EDGQTRELQN HLGLSAPVPR GRKGKKVKTQ TSSFDIQKAE WLRKYNPEQL LQDEGYKKHI
KHHCNKVLLR VRMLYYLKQE VIGSECQKVF DGVDASDIDV WVPEPDHSEV PAEWWDFDAD
KSLLIGVFKH GYEKYNTIRA DPALCFLERV GKPDDKAVAA EQRANDYMDG DVEDPEYKPA
PAIFKDDIED DVSSPGDLVI ADGDGQLMEG DKVYWPTQSA LTTRLRRLIT AYQRTNKNRQ
IQQIQPTFSV PTSVMQPIYE EATLNPKMAA KIERQQRWTR REEADFYRVV STFGVVFDPD
RGQFDWTKFR AMARLHKKTD DSLEKYLYAF MSMCRRVCRL PSKEELVDPN IFIQPITEER
ASRTLYRIEL LRKVREQALR HPQLFERLKL CHPNPDLPVW WECGPHDRDL LIGAAKHGVS
RTDYHILRDP ELSFMAAQRS YSQSKIAHSR TSTPLLQQYQ VALSASPLTS LPRLLDAKGI
ILEEMKVKSE NLKEEPQSSE EESMSSVETR TLIKSEPVSP KNGVLPQATG DQKSGGKSET
DRRMVAARTE PLTPNPASKK PRVHKRGSES SSDSDSDSER SSCSSRSSSS SSSSSSCSHS
RSGSSSSSSS SCSSASSSSS SSTSSSSSSS SSSSEESDSD EEEAQKRAES TTHMKAYDEE
SVASLSTTQD ETQDSFQMNN GTPESAYILQ GGYMLAASYW PKDRVMINRL DSICQTVLKG
KWPSARRSYD ANTVASFYTT KLLDSPGAAT EYSEPSVPTP PGAGVKEEHD QSTQMSKVKK
HVREKEFTVK IKDEGGLKLT FQKQGLAQKR PFDGEDGALG QQQYLTRLRE LQNASETSLV
NFPKSIPVSG TSIQPTLGAN GVILDNQPIV KKRRGRRKNV EGVDIFFFNR SKPPNHVSLG
LTSSQISTGI NPALSYTQPQ GISDTESPVP VINLKDGTRL AGDDAPKRKD LEKWLKEHPG
YVEDLGAFIP RMQLHEGRPK QKRHRCRNPN KLDVNSLTGE ERVQLINRRN ARKVGGAFAP
PLKDLCRFLK ENSEYGVAPE WGDVVKQSGF LPESMYERIL TGPVVREEVS RRGRRPKSGI
AKATAAAAAA ASATSVSGNP LLANGLLPGV DLTTLQALQQ NLQNLQSLQV TAGLMGMPTG
LSSGGEAKNM AAMFPMLLSG MAGLPNLLGM GGLLTKPTES GTEDKKGSDS KESEGKKERT
ESQSSENGGE NSVSSSPSTS STAALNTAAA ANPLALNPLL LSNILYPGML LTPGLNLHIP
TLSQSNTFDV QNKNKNSDLG SSKSVEVKEE DSRIKDQEDK GGTEPSPLNE NSTDEGSEKA
DASSGSDSTS SSSEDSDSSN ED
//
