ID A0A0L8HB58_OCTBM Unreviewed; 1948 AA.
AC A0A0L8HB58;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=DNA helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=OCBIM_22018364mg {ECO:0000313|EMBL:KOF86548.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF86548.1};
RN [1] {ECO:0000313|EMBL:KOF86548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF86548.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF86548.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KQ418610; KOF86548.1; -; Genomic_DNA.
DR EnsemblMetazoa; Ocbimv22018358m; Ocbimv22018358m.p; Ocbimv22018364m.g.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
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:SF17; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 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; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF47095; HMG-box; 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; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 245..292
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 342..399
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 433..487
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 561..745
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 875..1025
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..171
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1948 AA; 222132 MW; 3D38B83410B0C5C9 CRC64;
MDSGGEVSKD SDSAAVQQSD HEAEEISPKE RKKKAKAQDK ERTSDEICAE YGLNNVDVEF
CAEDYQTLNN YKAFSQFIRP LITKENPKIA MAKLITIVAA KWREFCEKNP HKSKAKQRAM
DDEQLDAVLR ENQEGEGSEA MDERSPTKTK KTKTKKAVAP LKIKITKKKK RRKASTDDED
AGFNTSDEEF ERQLEEASII SDSKAEANAG KRRTKRTKAK RKKTKTTSKF PDDGDGEGYE
VTDHQDYCEV CQQGGEIILC DTCPRAYHLV CLDPELEEAP EGKWSCPHCL KNEGKESSNQ
TPSEGEVGPV IECEPLKGKV HKILTWRWSE PPKSAEDELD HTHNEKKLEH KPTREFFIKW
QDMSYWHCSW ILELQLDVYH PAMYRNYMRK NDMDEPPPLE DGSSYGQKDR SNFDNIENLE
ERFYRYGVRP EWLQIHRAIN HKVTRDGKVW YLMKWRDLPY DQSTWECEDT LKDLNLDWKK
YVDDYENLRN MMYGGGGVDK KKSKVKGKKM KDGRESDNVS RTPPLYPTSD LRKKLDIQAD
YIDSTGGTLH GYQLEGLNWL RYSWANGTDT ILADEMGLGK TIQTITFLYS LFKEGHSRGP
FLVSAPLSTI INWEREFEFW APELYVVTYV GDKDSRAVIR EHEFSFDEGA IRGGSKACKM
KQGYNVKFHV LLTSYELVSI DQATLGSVEW GVLVVDEAHR LKNNQSKFFR VLSAYKIGYK
LLLTGTPLQN NLEELFHLLN FMSPENFNDL QGFLDEFADL SKEEQVKKLH DLLGPHLLRR
LKADVLKGIP AKSEFIVRVE LSNMQKKYYK YILTRNFEAL NSKGGNQVSL LNIMMDLKKC
CNHPYLFPIA SAEAPRLPNG AFEGNSLTKA CGKLELLQNM LRLLKDGGHR VLIFSQMTKM
LDILEDFLEF EGYKYERIDG GITGSQRQDA IDRFNAPGAP QFCFLLSTRA GGLGINLASA
DTVIIYDSDW NPHNDIQAFS RAHRIGQANK VMIYRFVTRA SVEERITQVA KKKMMLTHLV
VRPGLGNKGG TMSKQELDDI LKFGTEELFK ENGENSDWSC YDDEKKIVYD IEAISKLLDR
TQEGQVEKEI AMNEYLSSFK VASYQVKEGE QEEEPETEIL KQEAEHADPA YWEKLLRHHY
EQQQEDLART LGKGKRVRKQ VNYNDAMNGQ DDDAWKDSMS DFDSDFSGPT EDDDDFEDKQ
ESRSNRKRSG VSDRDKPLPP LLARVNGQIE VLGFNARQRK AFLNAVMRYG MPPQDAFNSQ
WLVRDLRGKS EKVFRAYVSL FMRHLCEPGA DNAETFADGV PREGLSRQHV LTRIGIMSLV
RKKVQEFEAI NGTHSMPYMK ATEALERIKK EKDAPAAGAD DAKSEDIDVD EETKDQSISA
SDVKKENDGK DTDKTEKSEK TDKTDKTDKT EKTEKTEKTE ITEKTEKTEK TEKTETTDKT
DKPDKTEKPD SVDKPDSVDK TEKPEESEKT ETTDTTEESD KTEQTGAAST EKGGGDKSDK
EESKLGGDKG NKPGDKDNED MDVDKPEEKK DDKEKAATEE AGEKSEKKEV ASPESKDKEE
SMQIDEPISK KEEESNAKGK DEDKEKDTKM EVDEVKDLKS DKEKTGTDTK ESKSEDKVET
LDKVKKEDKV KDKKEGEKAT EEKEEKKQDE TDEQSSTQSQ PPKTVDLKKE EQNQKFMFNI
ADGGFTELHT LWQNEQRALQ PGKEHEVWHR RHDYWLLAGI VTHGYGRWQD IQNDIRFQII
NEPFQSEQGK GNFLEIKNKF LARRFKLLEQ ALVIEEQLRR AAYLNLTQDP NHPAMALNAR
FAELECLAES HQHLSKESLA GNKPANAVLH KVLNQLEELL SDMKQDVSRL PATLARIPPV
TQRLQMSERN ILNRLVNPGQ TTTTAPPSAP PTIPPQQSPA ATPTPTSAVS AQSSPQASPF
MNTSNFSSPY SSSVPPYRPQ YGMPPQGR
//