ID A0A267F0V9_9PLAT Unreviewed; 1875 AA.
AC A0A267F0V9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BOX15_Mlig023617g1 {ECO:0000313|EMBL:PAA67378.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA67378.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA67378.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA67378.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA67378.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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:PAA67378.1}.
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DR EMBL; NIVC01001486; PAA67378.1; -; Genomic_DNA.
DR STRING; 282301.A0A267F0V9; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
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; cd17994; DEXHc_CHD3_4_5; 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; 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; 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; 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: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; 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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
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; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
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 364..411
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 434..479
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 601..651
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 734..918
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1052..1215
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1379
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1875 AA; 210214 MW; 8CC2CC2F3D0CC012 CRC64;
MDPDELTDAD TSVRDDGRRK RRNRGSDARE SRSGKAKRNR TVEIDFEDYG AATASSGSRA
ASSRRSAGRQ QRSKQKKSVE EICEELGIQD VDLSYTSENF ENWTIQKLFN RYFQPLLEER
NPDASEDDLK TVLDAKWKEF ASLNPYIPKE DLADDSPDES TAAAEDDSEL AADESAAAPA
EDEEPAVAEA AATPSRRGKK RKGRGGGRPS AAAAAAAAAA AASASVESPD ADASESGQAS
GLKIKISRGQ KNKKKRPPAE APAAGAVAAS PSSAGPPSSK KKKKRGGGGG GGGGGGNNTS
DEEFERQLEE AERVQEEEKE IRKSRKSNAA AKRAAAAGGG SAGGSHLRTT DRFPGEDGYE
TDHQDYCDVC QAGGEIILCD TCPRAFHLVC LEPELEEAPS GRWSCPHCEK EGISAAAVAD
EAEKAAAEQK DHHQEYCSEC RDGGDLIICE SCPQAFHLHC LNMKELPEGD WHCPRCSCEP
PKAKVESILT WRWAEPPKVD KLDELDHSHH IQAHLNKRPP KREFFVKFKG LSHWHDEWIP
ELQLEVHQPN SWRAYWKKFD MDEPPALDDG SVYRGREGDR PDDPHNLEER FFKWGIRPEW
LQIQRVINYR KTKSGHWYLI KWRDLSYEEC TWENPEEIEI PNFEKAIEEY FTMKKVLTGE
LSATLNPKKS SKAARAAAAA AKEDISPELA KKLPPEKPIT NLKSGAGWET QPGYLDDTGG
RLHPYQLEGV NWLRYSYGCG IDTILADEMG LGKTIQTIVF LYSLYKEGHT KGPFLVSVPL
STVINWEREF EFWAPDFYVV TYVGTKDSRG VIRENEMSYD QAAIRSGPKA SRIRSGSQVK
FHVLLTSYEL ISIDQATLSS VDWAALVVDE AHRLKNNQSK FFRVLSSYDI KYKLLLTGTP
LQNNLEELFH LLNFMSPDKF HDLQGFLDEF ADISKEDQVK KLHDMLGAHM LRRLKSDVLK
SMPSKSEFIV RVELSPMQKK YYKYILTRNY DALSSRGKTG CNQVSLLNIM MDLKKCCNHP
YLFPSAAEEA PKMANGAYEG SQLVKACGKL ELLERMLKKL RDEGHRVLIF SQMTKMLDIL
EDFCEHERLK YERIDGAITG QLRQDAIDRF NNGESDSFVF LLSTRAGGLG INLATADTVV
IYDSDWNPHN DIQAFSRAHR IGQANKVMIY RFVTRNTVEE RVTQVAKKKM MLTHLVVRPG
FGQKGGATMS KQELDDILKF GTAELFKDEN EESDKDRIVY DDETIARLLD RSQEGMEEKE
LALNDYLTSF KVAKYSVKET AKKDDEDDED EDEGREIIKE ALEPADPSYW DTLLRHHHEQ
YQADQHNSMG KGKRNRKQVN YYTVGMVGVQ QDEDEVDVGQ SDDESEFSGR PEDDEEFGEG
EGQAGGRRRR DRDVKMPPLL SKLNNQIEVF GFNPRQRRAF LNAIMRYGLP PSEVYNSPWM
SRDLRSKPEK VFRAYTALFM RHLCEPDSDV TDTFSDGVPR EGINRQHVLT RIGTMALLRK
KVQEFEKVNG EYSMPSMAAA AETEAETVGD EAKDSAEQQP QDKDEKTAVE QSETVAKDED
QSEMKPAEEA EKTDDAKPVT EEASNAKDNQ EKAKEADQKD DEASTKPKAE AEDAKPASSD
EAKPDASQPQ QQFMFNIADG GFTELHTIWL NEQRALQAGR EHEIWHRRHD YWLLAGVVRH
GYGRWGDIQS DPRCAILNEA FKTEDLKGNF VEIKNKFLAR RFKLLEQALI IEEQLRRAAY
LNLSHDAQDP VMRLNRKFAE LECLAESHQH LSRESQAGNK PANTVLHRVL SQLEDLLSDM
KCEVARLPPT VARLPPVSQR LAISQTSIIT QLTQAARDAA AAAAAADSAA APASGDGAEK
TDAPVASGES AATAE
//
