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Database: UniProt
Entry: N6UHB5_DENPD
LinkDB: N6UHB5_DENPD
Original site: N6UHB5_DENPD 
ID   N6UHB5_DENPD            Unreviewed;      1584 AA.
AC   N6UHB5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   Flags: Fragment;
GN   ORFNames=D910_02640 {ECO:0000313|EMBL:ERL85219.1}, YQE_02473
GN   {ECO:0000313|EMBL:ENN81105.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN81105.1};
RN   [1] {ECO:0000313|Proteomes:UP000019118, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
RN   [2] {ECO:0000313|EnsemblMetazoa:ENN81105}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JAN-2017) 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   EMBL; APGK01020350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB740193; ENN81105.1; -; Genomic_DNA.
DR   EMBL; KB631669; ERL85219.1; -; Genomic_DNA.
DR   STRING; 77166.N6UHB5; -.
DR   EnsemblMetazoa; ENN81105; ENN81105; YQE_02473.
DR   HOGENOM; CLU_000315_8_1_1; -.
DR   OMA; YLWHRNE; -.
DR   Proteomes; UP000019118; Unassembled WGS sequence.
DR   Proteomes; UP000030742; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProt.
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   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR   CDD; cd18659; CD2_tandem; 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; 2.
DR   InterPro; IPR040793; CDH1_2_SANT_HL1.
DR   InterPro; IPR025260; CHD1-like_C.
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; IPR002464; DNA/RNA_helicase_DEAH_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:SF14; 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; PF13907; CHD1-like_C; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01176; DUF4208; 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; 1.
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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000030742};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          174..267
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          292..353
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          395..537
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          666..817
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1205..1255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1272..1300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1404..1584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..945
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..1007
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1216..1234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1235..1254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1406..1445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1455..1511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1521..1550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1556..1584
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ENN81105.1"
SQ   SEQUENCE   1584 AA;  184373 MW;  D9DCFB9E81CC7406 CRC64;
     MNEEYTQQAS QFVSSIPGPS EEQFRSDSSK DHNSEVLIYN IFAIPEIRRS ARSKREPPRP
     DGNSKIRTSR DEWKYNDASS SESDSERERP PPSKRVGARS RATAQKRIVT RKTRYSSDES
     TDGDSEDEKR RTVSRRTAAA VSYKEDSEEK TDSEDLVEVD PSELIEPVTE EKCETIERVL
     AQRRGKKGVT GNITTCYYVE EHGDLNADVN PNDYENTEYQ FLIKWKDWAH IHNTWESEQT
     LKEQKVKGIK KLDNYMKKDA EIQKWISYST PEDVEYYECQ LELSQELLKS YNEVERIIAM
     YNKPDGGTDF FVKWESLSYA ESTWEDSLLI HRKWPQKVQE FQGREQSTKT PTKHCKVLKY
     RPKFHEVKSQ PEYMMGKENA LVLRDYQIHG LNWMIHSWTK ENSVILADEM GLGKTIQTIC
     FLYYLFNTHN LHGPFLCVVP LSTMTSWQRE FAQWAPELNF VTYLGDVQSR EIDKAFLGSL
     SWAVLLVDEA HRLKNDDSLL YKALMEFHTN HRLLITGTPL QNSLKELWAL LHFIMPNKFV
     TWEEFEKDHE HASTKGYSKL HKQLEPFILR RVKKDVEKSL PAKVEQILRV EMTSIQKQYY
     KWILTKNYNA LRKGVKGSSN TFLNIVIELK KCCNHAFLTK PSEAEPQYTC QDKLQSLLRG
     SGKLVLLDKL LIRLKETGHR VLIFSQMVRM LDILAEYLQL RHFPFQRLDG SIKGDIRRQA
     LDHFNADGSP DFCFLLSTRA GGLGINLATA DTVIIFDSDW NPQNDLQAQA RAHRIGQKNQ
     VNIYRLVTAR SVEEEIVERA KQKMVLDHLV IQRMDTTGRT VLNQKASTNN NPFNKEDLTA
     ILKFGAEELF KDEDVDEEPN CDIDEILRRA ETRDEAPSMV GDELLSAFKV ASFAAFDEDA
     TPSPVRTKNE NDEESKDWDE IIPENLRKKV EDEERNKEME DLYLPPRNRK TLQQINQSES
     DGDGAEHRKT NKKENDESGS SIEGEESDDE RPKRRGRPPV GNREKIKNFT DAEIRRFVKS
     YKKFSAPLKR LEAVACEAEL QEKPLAELRK LGELLHERCV AYMNEQSKEN NDANNADNQG
     KKRIRGPSFK LGGVSVNAKT MMQCEEELAA LDELLPTNED ERNKWMLEVR TKPAHFDVEW
     GAEEDSKLLR GIYVYGIGSW EQIKLDPSLK IGDKVLLNED KKPQAKHLQS RAEYLLKLLK
     KQLDPNKKVQ KPKRPRKAKE IKDAKSKEIV DNDFSSNDES TLHSSQSVSS STAKKVKVPV
     VKKEINNDKD AEDVAIKKEK KEKKKAKKEK KSAGPMHFTA NNEPKAINVL GDLDPAIFTE
     CKERMRPVKK ALKALDNPDQ SMTESEQVQH TRECLIQIGE QINTVLGQYT DAEKIKEWRS
     NLWYFVSKFT EYDAKKLYKL YKKAKAKDAK KAEKKEKLEK KDRNREQVAS TSKEKDRTRK
     DSDKEPHYHH HHKRKHEPEE NNEREERPTK KHRDGTEKRE RREKHPDKDR KRNREEISTE
     EEGEYRYNRH RTAPTFRHTA PPVHLEHERW SATGLPRERF PGEHPKRPFS DYPRVPGYHR
     GERDYNRGDK RNSADNEKRT FKFI
//
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