ID A0A2A2LH28_9BILA Unreviewed; 1494 AA.
AC A0A2A2LH28;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=WR25_12784 {ECO:0000313|EMBL:PAV85357.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV85357.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV85357.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV85357.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:PAV85357.1}.
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DR EMBL; LIAE01006781; PAV85357.1; -; Genomic_DNA.
DR Proteomes; UP000218231; 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; 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; 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; 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; 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; 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; 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:UP000218231};
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 318..365
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 380..427
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 466..523
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 554..587
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 682..866
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 998..1159
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 52..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..91
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1494 AA; 172650 MW; F13A5E481495C1B7 CRC64;
MRNGRRGNFE DYCGESLWLA TSSRRDFPLA SLHPPLASRV RNVSHTVQNY RSMADAEADR
DDAHEEEPME EDSMMTNEEA EDGDAVDDEQ DNEESHGAGA STSEKKKGGK RGRKGKKAKK
SGPTIPDTAT TNSANMAAAI GISDVGFKYS EDDYSNITSL KSFTNRVKED IMGANPTCNI
TKVYPLIQVK YREFQEELAR QGRQMAVKKP GKGGTAKQST SIVEKEKTVA PLKIRLSARK
AKKRNEDTDE DAAVDSDTEF ETLLKQHEQQ QDDIEKEREE KKQSRAAAKE DKKKLDLEKA
HQAKKAKRAK GEDEEEHNDY CEECRMGGEI ILCDTCPRAY HLVCVDENME SAPEGEWFCP
HCEKYGPPAV KEEEPQKTNM EYCRVCKETG SLLCCESCPS SYHAYCLNPP LEEIPDGDWN
CPRCTLSDIG QKKIEKILCW RWIEIVYPDP VEPKEGEEVD PNVIRVKPTK KMEPRKEKEF
FVKWKNMSYW HCEWLSETFM EVYFMPLLRM YWRKYDSENP PIFDESTIQR HHKDNDPYEL
REKYYQYGVK PEWMQVHRII NHVQYGKSQF DYLVKWKELA YEQSTWERDD MDIVYYEDAI
IKYWQHREKL FGDTIPKVIQ KKIATKREAK GLPPIDDEQS KKKKKDKVTI DIRKKYEVQP
DYVSETGGAL HPYQLEGINW LRHCWSNGTD AILADEMGLG KTVQSLTFLY TLLKEGHSKG
PFLIAAPLST IINWEREAEQ WCPDFYVVTY VGDRDSRAVI REHEFSFQEG AVRGGPRASR
LKSQENMKFH VLLTSYECIN MDKAILSSIE WAALVVDEAH RLKNNQSTFF KNLREYKINY
RLLLTGTPLQ NNLEELFHLL NFLDPTRFFD LESFTSEFAE ISKEDQIQKL HSLLGPHMLR
RLKADVLIGM PSKSELIVRV ELSPMQKKYY KNILTRNFEA LNVKNGGTQM SLINIIMELK
KCSNHPYLFV KASLEAPKLK NGMYEGTALI KNAGKFILLQ KMLRKLKDDG HRVLIFSQMT
MMLDILEDFC EVESYKYERI DGSITGQARQ DAIDRFNAPG AQQFIFLLST RAGGLGINLA
TADTVIIYDS DWNPHNDIQA FSRAHRIGQQ NKVMIYRFVT RNSVEERITS VAKKKMLLTH
LVVRAGIGQK GPSMSKTELD DVLRWGTEEL FKDEEQQQPA AEGAEGQEGA GKKANEHEIV
WDDGAVDALL DRNRETEGKQ EEGKKEHWTN EYLSSFKVAT YTTKEAEEHE EEEEEMEVIK
EGDKEPDPDY WEKLLRHHYE QDQETEAQKL GKGKRVRKQV NYASENMGQD WNNQMNNAIF
SIQNDYYWEN EAIEFQQNQD DDDDLSSGEY SEGMDGTHSD EEFDGEVKRR KKERDGEKLP
PLLAKVNGQI EVLGFNPRQR RAFYNAVMRW GMPPQDAYQS QWLVRDLKGK SERAFKAYTS
LFMRHLCEPG ADTQETYNDG VPREGLNRQH VLTRIGIMSL IRKKVQVSVV CQSE
//
