ID A0A3Q1GCX9_9TELE Unreviewed; 1751 AA.
AC A0A3Q1GCX9;
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:ENSAPOP00000025402.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000025402.1}
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; ENSAPOT00000006352.1; ENSAPOP00000025402.1; ENSAPOG00000008935.1.
DR GeneTree; ENSGT00940000155088; -.
DR Proteomes; UP000257200; Unplaced.
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; cd15531; PHD1_CHD_II; 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); 2.
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; IPR011011; Znf_FYVE_PHD.
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; 2.
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; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
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; 2.
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:UP000257200};
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 244..291
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 321..368
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 401..458
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 495..528
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 612..796
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 928..1077
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 114..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1751 AA; 199233 MW; 33CCC344486008E8 CRC64;
MKIFEARLFP SPSEPKSSSQ LLDDWGMEDI DHVFSEEDYR SLTNYKAFSQ FVRPLIAAKN
PKIAVSKMMM VLGAKWREFS TNNPLRGAAA ANAALATANV PAAVDTMVAE VAPPAAAPPA
PAAPQQAPPA PLRKAKTKEG KGPNARKKSK PAPKPQEKKN NAKTKKVAPL KIKLGGFNSK
RKRSSSEEDE PDVDSDFEDG SMNSVSVSEG SNSRSSRSKK KPSKSKPKKK KEAEDGDGYE
TDHQDYCEVC QQGGEIILCD TCPRAYHMVC LDPDMEKAPE GTWSCPHCEK EGIQWEAREE
GSDAEEDNGE AGEMEEDDHH MEFCRVCKDG GELLCCDSCP SSYHIHCLNP PLPEIPNGEW
ICPRCTCPPM KGKVQKILTW RWGDPPPPTP VPRPPDLAPD APDPAPLAGR PEREFFAKWS
NMSYWHCSWV TELQLELHCQ VMFRNYQRKN DMDEPPPIDF GDGEEDKSVK RKHKDPMYAQ
LEEKYLRFGI KMEWLMIHRI LNHRSAQKNN VHYLIKWREL PYDQATWEAD DMDVPEFDPY
KVQYWNHREL MMGEDGRPGK KIKVKGRVKR PDRPPENPVI DPTIKFDRQP DYLDSTGGTL
HPYQLEGLNW LRFSWAQGTD TILADEMGLG KTVQTAVFLY SLYKEGHSKG PFLVSAPLST
IINWEREFEM WAPDMYVVTY VGDKDSRAVI RENEFSFEDN AIRGGKKASR MKKDSSIKFH
VLLTSYELIT IDMAILGSID WACLVVDEAH RLKNNQSKFF RVLNNYPLQH KLLLTGTPLQ
NNLEELFHLL NFLTPERFNK LEVFLEEFAD IAKEDQIKKL HDMLGPHMLR RLKADVFKHM
PSKTELIVRV ELSPMQKKYY KFILTKNFEA LNTKGGGNQV SLLNVVMDLK KCCNHPYLFP
AAAMEAPKMP NGMYDGAALT KAAGKLLLLQ KMMRKLKEGG HRVLVFSQMT KMLDLLEDFL
ENEGYKYERI DGGITGGMRQ EAIDRFNAPG AQQFAFLLST RAGGLGINLA TADTVIIYDS
DWNPHNDIQA FSRAHRIGQN KKVMIYRFVT KASVEERITQ VAKKKMMLTH LVVRPGLGSK
TGSMSKQELD DILKFGTEEL FKDEGEGENK EEDSSIIHYD DKAIDRLLDR NQDATDDTEL
QSMNEYLSSF KVAQYVVKDE EEEEEVQREI IKQEESVDPD YWEKLLRHHY EQQQEDLARN
LGKGKRIRKQ VNYNDGSQED RADWQDDQSD GQSDYSVASE EGDEDFDERT EANSRRPNRK
GLRNDKDKPL PPLLARVGGN IEVLGFNSRQ RKAFLNAVMR YGMPPQDAFT TQWLVRDLRG
KSEKEFKAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ HVLTRIGVMS LIRKKVQEFE
HVNGQWSMPW MAELEENKRA AAQPDSPGKT PSTGTPADTQ PNTPAPGSAH SQTNKHTPST
IFGTVIAIPD DDEKSPTEEQ EKKKNGEEPM ETDKPSNGEA EGVKEKEREK ETEGEAEKKS
EEKPEEATKL EEKKKAKTRF MFNIADGGFT ELHSLWQNEE RAATVTKKTN EIWHRRHDYW
LLAGIIQHGY ARWQDIQNDV KFAILNEPFK GEMNRGNFLE IKNKFLARRF KLLEQALVIE
EQLRRAAYLN MSEDPSHPSM ALNTRFSEVE CLAESHQHLS KESMSGNKPA NAVLHKVLKQ
LEELLSDMKA DVTRLPATIA RIPPVAVRLQ MSERNILSRL ASRGPDTQAQ TQQVAHIRHL
DLGFSSPPVN H
//
