ID A0A2K6CWH3_MACNE Unreviewed; 1826 AA.
AC A0A2K6CWH3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSMNEP00000028015.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000028015.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000028015.1}
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR Ensembl; ENSMNET00000052314.1; ENSMNEP00000028015.1; ENSMNEG00000036875.1.
DR GeneTree; ENSGT00940000155888; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000036875; Expressed in cerebellum and 12 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; 6.10.140.1440; -; 1.
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 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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 261..361
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 386..464
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 505..675
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 804..955
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..200
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1826 AA; 211344 MW; EA9E351A1837C252 CRC64;
MMRNKDKSQE EDSSLHSNAS SHSASEEASG SDSGSQSESE QGSDPGSGHG SESNSSSESS
ESQSESESES AGSKSQPVLP EAKEKPASKK ERIADVKKMW EEYPDVYGVR RSNRSRQEPS
RFNIKEEASS GSESGSPKRR GQRQLKKQEK WKQEPSEDEQ EQGTSAESEP EQKKVKARRP
VPRRTVPKPR VKKQPKTQRG KRKKQDSSDE DDDDDEAPKR QTRRRAAKNV SYKEDDDFET
DSDDLIEMTG EGVDEQQDNS ETIEKVLDSR LGKKGGIVLN PFAATGASTT VYAIEANGDP
SGDFDTEKDE GEIQYLIKWK GWSYIHSTWE SEESLQQQKV KGLKKLENFK KKEDEIKQWL
GKVSPEDVEY FNCQQELASE LNKQYQIVER VIAVKTSKST LGQTDFPAHS RKPAPSNEPE
YLCKWMGLPY SECSWEDEAL IGKKFQNCID SFHSRNNSKT IPTRECKVWP LKQRPPISLK
KQPAYLGGEN LELRDYQLEG LNWLAHSWCK NNSVILADEM GLGKTIQTIS FLSYLFHQHQ
LYGPFLIVVP LSTLTSWQRE FEIWAPEINV VVYIGDLMSR NTIREYEWIH SQTKRLKFNA
LITTYEILLK DKTVLGSINW AFLGVDEAHR LKNDDSLLYK TLIDFKSNHR LLITGTPLQN
SLKELWSLLH FIMPEKFEFW EDFEEDHGKG RENGYQSLHK VLEPFLLRRV KKDVEKSLPA
KVEQILRVEM SALQKQYYKW ILTRNYKALA KGTRGSTSGF LNIVMELKKC CNHCYLIKPP
EENERENGQE ILLSLIRSSG KLILLDKLLT RLRERGNRVL IFSQMVRMLD ILAEYLTIKH
YPFQRLDGSI KGEIRKQALD HFNADGSEDF CFLLSTRAGG LGINLASADT VVIFDSDWNP
QNDLQAQARA HRIGQKKQVN IYRLVTKGTV EEEIIERAKK KMVLDHLVIQ RMDTTGRTIL
ENNSGRSNSN PFNKEELTAI LKFGAEDLFK ELEGEESEPQ EMDIDEILRL AETRENEVST
SATDELLSQF KVANFATMED EEELEERPHK DWDEIIPEEQ RKKVEEEERQ KELEEIYMLP
RIRSSTKKAQ TNDSDSDTES KRQAQRSSAS ESETEDSDDD KKPKRRGRPR SVRKDLVEGF
TDAEIRRFIK AYKKFGLPLE RLECIARDAE LVDKSVADLK RLGELIHNSC VSAMQEYEEQ
LKENASEGKG PGKRRGPTIK ISGVQVNVKS IIQHEEEFEM LHKSIPVDPE EKKKYCLTCR
VKAAHFDVEW GVEDDSRLLL GIYEHGYGNW ELIKTDPELK LTDKILPVET DKKPQGKQLQ
TRADYLLKLL RKGLEKKGTV TGGEEAKLKK RKPRVKKENK VPRLKEEHGI ELSSPRHSDN
PSEEGEVKDD GLEKSPMKKK QKKKENKENK EKQMSSRKDK EGDKERKKSK DKKEKVMVPF
CSQPLHAISK GQDLLSADCL CLYSFVLLQC KERMRPVKKA LKQLDKPDKG LNVQEQLEHT
RNCLLKIGDR IAECLKAYSD QEHIKLWRRN LWIFVSKFTE FDARKLHKLY KMAHKKRSQE
EEEQKKKDDV TGGKKPFRPE ASGSSRDSLI SQSHTSHNLH PQKPHLPASH GPQMHGHPRD
NYNHPNKRHF SNADRGDWQR ERKFNYGGGN NNPPWGSDRH HQYEQHWYKD HHYGDRRHMD
AHRSGSYRPN NMSRKRPYDQ YSSDRDHRGH RDYYDRHHHD SKRRRSDEFR PQNYHQQDFR
RMSDHRPPMG YHGQGPSDHY RSFHTDKLGE YKQPLPPLHP AVSDPRSPPS QKSPHDSKSP
LDHRSPLERS LEQKNNPDYN WNVRKT
//
