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Database: UniProt
Entry: A0A0L8HB58_OCTBM
LinkDB: A0A0L8HB58_OCTBM
Original site: A0A0L8HB58_OCTBM 
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
//
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