ID A0A067QUX9_ZOONE Unreviewed; 2091 AA.
AC A0A067QUX9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein Mi-2-like protein {ECO:0000313|EMBL:KDR09554.1};
GN ORFNames=L798_00513 {ECO:0000313|EMBL:KDR09554.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR09554.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR09554.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR09554.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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DR EMBL; KK853235; KDR09554.1; -; Genomic_DNA.
DR STRING; 136037.A0A067QUX9; -.
DR EnsemblMetazoa; KDR09554; KDR09554; L798_00513.
DR eggNOG; KOG0383; Eukaryota.
DR InParanoid; A0A067QUX9; -.
DR OMA; TWRWAVR; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000027135; 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:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; cd17994; DEXHc_CHD3_4_5; 1.
DR CDD; cd00084; HMG-box_SF; 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; 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:SF13; 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; 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; 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; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000313|EMBL:KDR09554.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KDR09554.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000027135};
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 426..473
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 484..531
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 554..623
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 661..710
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 807..989
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1121..1285
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2007..2033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2056..2078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..83
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..408
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2056..2071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2091 AA; 236717 MW; 804F2C85CCDCEE46 CRC64;
MASDEMDDES FGGGDDDLGD ESGTRMSRPD GTTEENSPES EEGQPGGDDD DDYEPEDGRN
KRKKGKKRKA RSEDKKGKKK KKKKKADSGD ESDYGFDEDG GGNDSDFVSG SSSRKSRKSR
ASQKHVPQAA PVQDSNSGMP TVEEVCMTFG LTDVDVEYTE ADFQNLTTYK LFQQHVRPLL
GKENPKVPMS KLMMLVAAKW RDFTNINPNT EQEPEPMAED SYARKTSRSR PSKDSSKAES
DLAGLDDDDD EEREEKIKKK RGRSGKKSST AGGSSKKSTS KVPTLKIKLG KRKRGSSGSM
LQVPHCTATD VNGSPCLSQE DEGDASGGAS DRDSDAEFEQ MLAEAEEANK ISTEADDDEV
GGESNVEEES GGSGDTPPSS QAPNQAPVRR KAKTKIGNKS KKKKKTKTTS KFPGGDGEDG
YETDHQDYCE VCQQGGEIIL CDTCPRAYHL VCLDPELEET PEGKWSCPHC EGEGVQEQDD
DEHMEFCRVC KDGGELLCCD SCPSAYHTFC LNPPLTDIPD GDWKCPRCSA KPLPGKVAKI
LTWRWAEAKK SDGREEEDKL SEEPSTSKRP PRTPKPQREF FVKWHEKSYW HCEWVSELQM
DVFHPLMIRN YMRKYDMDEP PKLEEPIDEL DNRMKRIKEA NADDSALEDK YYRYGIKPEW
MIVHRIINHR TMRDGRTLYL VKWRDLSYDQ ATWEEENESI LGLKQAIDFY MDLRASCNVD
GSGRKGKKGK GKRMKTRELQ DEDGDKTPWF HPSSVTSRHV HLFRRYTPPP EKPLTDLKKK
LDKQPDYIDQ TGMQLHPYQL EGLNWLRYCW GQGIDTILAD EMGLGKTIQT ITFLYSLYKE
GHCKGPFLLS VPLSTIINWE REFETWAPDF YVVTYVGDKD SRAVIRENEL SFEEGAVRGG
RASRIRANTI KFNVLLTSYE LISIDAACLG SIDWAVLVVD EAHRLKSNQS KFFRLLASYN
ITYKLLLTGT PLQNNLEELF HLLNFLCREK FNDLAAFQNE FADISKEDQV KKLHEMLGPH
MLRRLKTDVL KSMPSKSEFI VRVELSPMQK KYYKFILTRN FEALNPKGGG QQVSLLNIMM
DLKKCCNHPY LFPAAAQEAP TTPNGTYETT ALIKASGKLV LLSTMLRKLK EQGHRVLIFS
QMTKMLDILE DYLEGEGYKY ERIDGNITGS VRQEAIDRFN APGAQQFVFL LSTRAGGLGI
NLATADTVII YDSDWNPHND IQAFSRAHRI GQANKVMIYR FVTRNSVEER VTQVAKRKMM
LTHLVVRPGM GGRGATFSKQ ELDDILRFGT EELFKEEEGK EDEAIHYDDR AIDELLDRTK
EGIEQKENWA NEYLSSFKVA SYVTKEGEEE EEPTEIIKQE AENTDPAYWV KLLRHHYEQQ
QEDMARTLGK GKRVRKQVNY NDGTVEGRDD ATWQENLSDY NSDFSAPSDD DKEDDDFDEK
TDGEPGRRSR RRLERRDEKD RPLPPLLARV GGNIEVLGFN ARQRKAFLNA IMRYGMPPQD
AFNSQWLVRD LRGKSEKNFK AYVSLFMRHL CEPGADNAET FADGVPREGL SRQHVLTRIG
VMSLIRKKVQ EFEHINGYYS MPEMIRKPVE PIKTAAGVVP PGMEQGGEMP RSATTSTSAT
PATSAAASPA PTLNSQDESK DKEGEDIANK EETNKEASKE EPKDVTEIRK EDVEVEVDER
KETAKEECAE KEGEMKEKVT GAEEEKLEEM DTSEKKECAG SDEVKAEEVV VKEEKGKEGE
MSDEEKSKPV TPSQEQKKED DDIVVVKDEG EERKDERKEG TKEDKKEDKE DIKGVDDIDK
PKRKFMFNIA DGGFTELHTL WLNEEKAAVP GREYEIWHRR HDYWLLAGIV THGYGRWQDI
QNDIRFAIIN EPFKMDVGKG NFLEIKNKFL ARRFKLLEQA LVIEEQLRRA AYLNLTQDPN
HPAMSLNARF AEVECLAESH QHLSKESLAG NKPANAVLHK VLNQLEELLS DMKSDVSRLP
ATLARIPPVA QRLQMSERSI LSRLAATTTA GSTPTTPTTS QQGPTGLLSS QFPGGFQAGQ
LPAGFATANF ASFRPQYSVP GQPTQGFPET SPDIDVSRVP LFHDGNWRES W
//
