ID A0A164YDQ3_9CRUS Unreviewed; 1951 AA.
AC A0A164YDQ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Chromodomain-Helicase-DNA-binding protein Mi-2 {ECO:0000313|EMBL:KZS15154.1};
GN ORFNames=APZ42_019189 {ECO:0000313|EMBL:KZS15154.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS15154.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS15154.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS15154.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS15154.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS15154.1}.
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DR EMBL; LRGB01000915; KZS15154.1; -; Genomic_DNA.
DR STRING; 35525.A0A164YDQ3; -.
DR Proteomes; UP000076858; 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; 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; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 1.
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; 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; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 1.
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; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
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; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000313|EMBL:KZS15154.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KZS15154.1};
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:UP000076858};
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 358..405
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 600..635
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 734..917
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1024..1187
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..86
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1951 AA; 220645 MW; E00C896EE4264019 CRC64;
MASFDRESTH KAGEDSDGGE GEEDEIVKGG GYEDEDQSMM DSDGVEKDDD DDFDPDTGGG
KKKKKSKKHK SRNEDKKSKK KKKKKKVESA EPSEAEEEQP VDEPVSKKKP KASKAASAQN
VVATDMPSVE EVCSNFGLQD VEIDYESPEF QNLNNCKLFQ QHVRPLIQKE NPKVPMSKLM
MLVSAKWREF SATLPAGNDT PPEEEAVEAS TSRPLRSSRS AASGREEPEL PEDDEDEDDE
FAEKGRKKRS RKPTKSGNAV AGKKGKVPTI KIKLGKRKRT SSDDFSADEK DSDAEFEQML
KEAEEASKVV EESKGQVAAV PRKKAKTKIG DKNKKKKKTR TTAKFPSEEG DGYETDHQDY
CEVCQQGGEI ILCDTCPRAY HLVCFDPELE EAPEGRWSCP HCEGEGXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXLTIQ EVFHGAMYRY
YIRKVDMEEP PKLDCEEVDL DEALEAEEEA AAQKKKRIEG FEEMDLENRF YRYGIRPEWL
VVHRVINHRT LRDNRTQYLV KWRELNYDMA SWEEEGPEVE IPGLKRGIEE YFDLRVACGV
DTPAKKKSKG KSHKKGKSKE AAVEEERETP RRYNPPPEKP SSNLSRKWER QPDYIDASGM
ALHPYQMEGL NWLRYSWGQG TDTILADEMG LGKTIQTITF LYSLYKEGHC RGPFLVAVPL
STIINWEREF ETWAPDFYVV TYVGDKDSRV VIREHELSFE EGAVRGGNKA CKIRTSSVKF
HVLLTSYELV SIDAALLNSL EWAVLVVDEA HRLKNNQSKF FRILNSYNLR YKLLLTGTPL
QNNLEELFHL LNFLCPDKFN DLLAFTNEFA DLAKEEQVKR LHDMLVELSP MQKKYYKYVL
TRNFEALNSR TGGQQVSLLN IMMDLKKCCN HPYLFPVASQ EAPCLQNGMY ETTALVKASG
KLVLLSKMLR VLKEQGHRVL IFSQMTKMLD ILEDFLEGEQ YKYERIDGGI TGTLRQDAID
RFNAPGAPQF VFLLSTRAGG LGINLATADT VVIYDSDWNP HNDIQAFSRA HRIGQANKVM
IYRFVTRNSV EERVTQVAKK KMMLTHLVVR PGMGAKGTFS KQELDDILRF GTEELFKEEE
GKEDEAIHYD DEAINQLVDR SNEGIEQKES WANDYLSSFK VASYVTKEGD DEEEQDTEII
KQEAENTDPA YWEKLLRHHY EQQQEDLARS LGKGKRVRKQ VNYNDGVEGR DDTSWQENVS
DYNSDFSGAS DDDKEDDDFD DRGDEPGRGR RRKGTERRDE KDRPLPPLLA RVGGNMEVLG
FNARQRKAFL NAVMRYGMPP QDAFNTQWLV RDLRGKSERN FKAYVSLFMR HLCEPGADNA
ETFADGVPRE GLNRQHVLTR IGVMSLIRKK VHEFEHINGF YSMPEVAARA AELVAAKDKA
IEDKMTTSHA PSGESSSATP AVSAPSTACP SPTTIATNEE TKKKDGEGKT DPDDKKETDF
KKESEEKSNH VTEREKKEDE APKSEQTESM EIDDENSKTI KVEDESKKDS KTEEKIKKEP
KMEEKAESPE VEIEKVVVVK EEKSAEEKAK ERELAKEERS KRKFMFNIAD GGFTELHTLW
QNEEKAAVPG REYEIWHRRH DYWLLAGIVT HGYGRWQDIQ NDVRYAIINE PFKMDVGKGN
FLEIKNKFLA RRFKLLEQAL VIEEQLRRAA YLNLTQDSTH PAMALNARFA EVECLAESHQ
HLSKESLAGN KPANAVLHKV LNQLEELLSD MKSDVSRLPA TLARIPPVAQ RLQMSERSIL
SRLATSASQQ AAQQQAQAAF GNHFPPGLTG GQIPFTGLNL ANFRPQFTLP GQTSTSNLAM
TAAAAAAAAA AAAGVPQAAF PGTSPPGSDS K
//
