ID G1NA16_MELGA Unreviewed; 1804 AA.
AC G1NA16;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD2 {ECO:0000313|Ensembl:ENSMGAP00000009319.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000009319.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000009319.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000009319.3}
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR Ensembl; ENSMGAT00000010138.3; ENSMGAP00000009319.3; ENSMGAG00000008966.3.
DR GeneTree; ENSGT00940000155888; -.
DR HOGENOM; CLU_000315_8_1_1; -.
DR TreeFam; TF313461; -.
DR Proteomes; UP000001645; Chromosome 12.
DR Bgee; ENSMGAG00000008966; Expressed in pectoralis major and 17 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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; 1.10.10.60; Homeodomain-like; 1.
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; 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; 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:SF19; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 2; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 226..325
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 350..421
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 461..631
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 760..911
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1648..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..165
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1765
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1804 AA; 209660 MW; 51A6ABF11E64CB7F CRC64;
ESEQGSEQGS ESNSSSESSE SQSESESEST GSKSQQTPPE TKEKPASKKE RIADVKKMWE
EYPDVYGVRR SNRSRQEPSR FNIKDEAGIC IEIRWPLISY FSDRRKKWKR EISGEEEDED
GGDQGTSAES EPEPKRIKAK RPVQRRTMAK TSVKKPPKLQ RGKKRKRQVS SEDDDDDEDG
ETPKRQTRRR AAKNVSYKED DDFETDSDDL IEMTGEGADE HEDNSETIEK VLDIRLGKKG
GVLISFAATG ASTTVYATEA NGNPSADFDP EKDEGEVHYL IKWKGWSYIH STWESEESLQ
QQKVKGLKKL ENFKKKEEEI KQWLAKVSPE DVEYFNCQQE LASELNKQYQ IVERVIGLGF
FAYFAANSRK TSSNDPEYLC KWMGLPYAEC SWEDEALISK KFQHCIDSFN NRNNSKTIPT
RDCKVLKQRP RFVALKKQPS YIGSENLELR DYQLEGLNWL AHSWCKSNSV ILADEMGLGK
TIQTISFLSY LFHQHQLYGP FLVVVPLSTL TSWQREFEVW APEINVVVYI GDLMSRNMIR
EYEWIHSQSK RLKFNALITT YEILLKDKAV LGSISWAFLG VDEAHRLKND DSLLYKTLID
FKSNHRLLIT GTPLQNSLKE LWSLLHFIMP EKFEFWEDFE EDHGKGRENG YQSLHKVLEP
FLLRRVKKDV EKSLPAKVEQ ILRVEMSALQ KQYYKWILTR NYKALSKGTR GSTSGFLNIV
MELKKCCNHC YLIKPPEENE RENGIETLQS LIRSSGKLIL LDKLLTRLRD RGNRVLIFSQ
MVRMLDILAE YLTIKHYPFQ RLDGSIKGEI RKQALDHFNA DGSEDFCFLL STRAGGLGIN
LASADTVVIF DSDWNPQNDL QAQARAHRIG QKKQVNIYRL VTKGTVEEEI IERAKKKMVL
DHLVIQRMDT TGRTVLDNNS GRSNSNPFNK EELTAILKFG AEDLFKELEG EESEPQEMDI
DEILRLAETR ENEVSTSATD ELLSQFKVAN FATMEEEETE LDERPQKDWD DIIPEEQRKK
VEEEERQKEL EEIYMLPRIR SSTKKAQTND SESDAETKRR LQRSSGSESE TDDTDDEKRP
KRRGRPRSVR KDTVEGFTDA EIRRSKCYIK YKTCNLFFPF PRLECIARDA ELVDKSVADL
KRLGELIHNS CVSAMQEYEE QLKENPGETG KGPGKRRGPT IKISGVQVNV KSIIQHEEEF
EMLHKSIPAD PEERKKYRLT CRVKAAHFDV DWGVEEDSRL LVGIYEHGYG NWELIKTDPE
LKLSDKILPV ETDKKPQGKQ LQTRVDYLLK LLKKDLEKKE NMKDGEEGKL KKRKPRIKKE
NKAPKVKDEH GNELSPPRHS DNQSEEGEVK DDGLDKSPVK KKQKKKENKE NKEKQTSTKK
EKESDKEKKK TKEKKEKPKG GEAKSGSKGK RSQGPVHITA GSEPVPIGED EDDDLDQETF
SICKERMRPV KKALKQLDKP DKGLTVQEQL EHTRNCLLKI GDRISECLKA YTDQDLIKLW
RRNLWIFVSK FTEFDARKLH KLYKMAHKKR SQEEEEQKKK EDMASMPSMK KPFRPEPSGS
SRDPAMSQSH VPHNPHSQKL HMPPSHAQQQ MHGHPRESYG HPPKRHFSNT DRGEWQRDRK
FSYSGNSNQM WGGERHHQYE QHWYKDHHYG DRRSRGDPHR SSGNYRPNNL SRKRPYEQYS
SDRDHRGHRD YYDRHHHDSK RRRSDEFRPQ NYHQQDFRRM SDHRPPMGYH GQGPSDHYRS
FHTDKPGDYK QPLPPPHPSV SDPRSPPSQK SPHDSKSPLD HRSPLDRSLE QKNNPDYNWN
IRKT
//
