ID A0A3Q1EJX4_9TELE Unreviewed; 1169 AA.
AC A0A3Q1EJX4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000004108.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000004108.1}
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A3Q1EJX4; -.
DR STRING; 80966.ENSAPOP00000004108; -.
DR Ensembl; ENSAPOT00000010612.1; ENSAPOP00000004108.1; ENSAPOG00000005764.1.
DR GeneTree; ENSGT00940000156579; -.
DR InParanoid; A0A3Q1EJX4; -.
DR Proteomes; UP000257200; Unplaced.
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; 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:SF7; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 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; 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:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 47..116
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 141..205
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 245..415
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 544..695
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 782..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 134428 MW; CE61C0E068F4FAD5 CRC64;
VCDRTNALVE ELSKIPINTL LNFVDTLPGR VEAVTAAKAT GSATTVYAIE ADGDPNANFS
HNKETGEVQY LIKWKNWAHI HNTWETEETL KLQNVKGMKK LDNFKKKEQE KKKWLKAASP
EDIEYFNCQE ELMDDLHSQY QLVERIIAGH SNQKSAAGYP DYLCKWQGLP YSECSWEDGA
LIAKKFQKCI DDYMSRNQSK TIPSRDCKVL KQRPRFVPMK KQPAYIGGEG LELRDYQLDS
LNWMAHSWCK GNSCILADEM GLGKTIQTIS FLNYLFNEHQ LYGPFLLVVP LSTLTSWQRE
IHLWAPQMNV VVYLGDISSR NMIRTHEWIH VHSKRLKFNI LLTTYEILLK DKSFLGSVNW
AFIGVDEAHR LKNDDSLLYK TMIDFKSNHR LLITGTPLQN SLKELWSLLH FIMPEKFHSW
ELFEEEHGKG RDSGYTSLHK ELEPFLLRRV KKDVEKSLPA KVEQILRVEM SAIQKQYYKW
ILTRNYKALS KGTKGSTSGF LNIMMELKKC CNHCYLIKPP EDNEFLNKAE ALQQLVRCSG
KLVLLDKLLV RLKERGHRVL IFSQMVRMLD ILAEYLRSRQ FYFQRLDGSI KGEMRKQALD
HFNAEGSEDF CFLLSTRAGG LGINLASADT VVIFDSDWNP QNDLQAQARA HRIGQKRQVN
IYRLVTKGSV EEDIIERAKK KMVLDHLVIQ RMDTTGKTVL HTGAAPSSSA PFNKEELSAI
LKFGAEELFK EPEGEEQEPQ EMDIDEILKR AETRENDPGP STVGEELLSQ FKVANFSMME
DEEIDIDSER SQRSWDDIIP EEQRRRMEEE ERQKELEEIY MLPRMRNCAK QISFNANEGR
QSRNRRYSGS DSDSPSDRKR PKKRGRPRTI PRENIKGFSD AEIRRFVKSY KKFGGPLERL
DAIARDAELV DKSEHDLKRL AETVHNGCVR TLRENPCGPE KTSGGRRGKV KGPTFRISGV
QVNAKLVISH EEELAPLHKA IPADPEERKK YMIPCHSKAA HFDIEWGKED DSSLLIGIYE
YGYGSWEMIK MDPDLNLTHK LLPDDPDKKP QAKQLQTRAD YLIKLLSKDL AKKEAQKQAG
TANSRKRKPR SKKIKNLKPV KTDEVLKSPS SDLPSDKSEV KTEVRERTKK SSDVPASGEN
VPLSEESEEL DQRTFSVVCS ADTCIFRLK
//
