ID G3Q4E0_GASAC Unreviewed; 1807 AA.
AC G3Q4E0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000024744.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000024744.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000024744.1}
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 Ensembl; ENSGACT00000024793.1; ENSGACP00000024744.1; ENSGACG00000018705.1.
DR GeneTree; ENSGT00940000155088; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000018705; Expressed in embryo and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd15532; PHD2_CHD_II; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF22; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 4; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 318..365
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 386..455
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 492..525
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 609..793
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 925..1074
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1807 AA; 205504 MW; 674F6AF3EBE3588F CRC64;
MDLVGAEEAE GQRSDSEGSD YTPGRKKKRR GGSGKEKKRS SSGAERSSSR KKEPEPEEPK
SSSQLLDDWG MEDIDHVFNE EDYRSLTNYK AFSQFVRPLI AAKNPKIAVS KMMMVLGAKW
REFSTNNPLR LRKAKTKEGK GPNARKKSKP TPKQLEKKNS AKTKKVAPLK IKLGGFSSKR
KRSSSEEDEP EVDSDFEDGS ITGFSFSEGY NNRSIRTKKK PSKSNPKKKK AEEGDGYETD
PQDYCEVCQQ GGEIILCDIT YQGHTHSLDP DQRGLFRGLS GSPHREKEGI QWEAREEASE
GEEDIGDTGD MEEDDLHMEF CRVCKDGGEL LCCDSCPSSY HIHCLNPPLP EIPNGEWICP
RCTCPSMKGK VQKILTWRWG EAPPPTPVPR PLDLAADAPD PKPLAGRPDR EFFAKWSNMS
YWHCSWVTEL QLELHCQVMF RNYQRKNDMD DPPPIDFAEG EEDKSVKRKA KDPMYAQLDE
KYLRFGIKFE WLMMHRIINH SVDRKNNVHY LIKWRELAYD QATWEADDMD IPDYDTYKVQ
YWNHRELMMG DEGKPGKKIK VKGRVKRPDR PPENPVVDPT IKFERQPDYL DSTGGTLHPY
QLEGLNWLRF SWAQGTDTIL ADEMGLGKTV QTAVFLYSLY KEGHSKGPFL VSAPLSTIIN
WEREFEMWAP DMYVVTYVGD KDSRAVIREN EFSFEDNAIR GGKKASRMKK DSSIKFHVLL
TSYELITIDM AILGSIDWAC LVVDEAHRLK NNQSKFFRVL NNYPLQHKLL LTGTPLQNNL
EELFHLLNFL TPERFSKLEI FLEEFADIAK EDQIKKLHDM LGPHMLRRLK ADVFKHMPSK
TELIVRVELS PLQKKYYKFI LTKNFEALNT KGGGNQVSLL NVVMDLKKCC NHPYLFPTAA
IEAPKMPNGM YDGNSLTKAA GKLTLLQTMM RKLKAGGHRV LIFSQMTKML DLLEDFLENE
GYKYERIDGG ITGGMRQEAI DRFNAPGAPQ FAFLLSTRAG GLGINLATAD TVIIYDSDWN
PHNDIQAFSR AHRIGQNKKV MIYRFVTKAS VEERITQVAK KKMMLTHLVV RPGLGSKTGS
MSKQELDDIL KFGTEQLFKD EFDGGLGENK NKEEDSSVIH YDEKAIDRLL DRNQDATEDK
ELQSMNEYLS SFKVAQYVVK DEEEEEEEVQ REIIKQEESV DPDYWEKLLR HHYEQQQEDL
ARNLGKGKRI RKQVNYNDGS QEDRADWQDD QSDGQSDYSV ASEEGDEDFD ERTEANSRRP
SRKGLRNDKD KPLPPLLARV GGNIEVLGFN SRQRKAFLNA VMRYGMPPQD AFTTQWLVRD
LRGKSEKEFK AYVSLFMRHL CEPGADGAET FADGVPREGL SRQHVLTRIG VMSLIRKKVQ
EFEHVNGQWS MPWMAELEES KKAAAAGQPD SPGKTPSTGT PADTQPNTPA PGKAPPPPRS
SPRTHPREAR RKRPNEVFLG SLSTGDDSNS KCSPSPESSE GGEDTKSTPE AKAEGSEVKP
EDAEVKAEEK KEEKMDVALP ADEKKGGERV SSPSTRSRSS RALLSDLKDE KEPLKAEDVA
KLQNGDGSKE GGASEEKKKA KSRFMFNIAD GGFLCPLSEL HSLWQNEERA ATVTKKTNEI
WHRRHDYWLL AGIIQHGYAR WQDIQNDVKF AILNEPFKGE MNRGNFLEIK NKFLARRFKL
LEQALVIEEQ LRRAAYLNMS EDPSHPSMAL NTRFSEVECL AESHQHLSKE SMSGNKPANA
VLHKVLKQLE ELLSDMKADV TRLPATIARI PPVAVRLQMS ERNILSRLAS RGPETQTQSQ
TQQMSQQ
//
