ID A0A1I8HJS6_9PLAT Unreviewed; 1445 AA.
AC A0A1I8HJS6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=DNA helicase {ECO:0000313|WBParaSite:maker-uti_cns_0006585-snap-gene-0.1-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0006585-snap-gene-0.1-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0006585-snap-gene-0.1-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR WBParaSite; maker-uti_cns_0006585-snap-gene-0.1-mRNA-1; maker-uti_cns_0006585-snap-gene-0.1-mRNA-1; maker-uti_cns_0006585-snap-gene-0.1.
DR Proteomes; UP000095280; Unplaced.
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: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; 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; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; 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 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; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 2.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 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; 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; 1.
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 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 345..392
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 721..771
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 855..1090
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1224..1388
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..312
FT /note="Basic and acidic 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"
SQ SEQUENCE 1445 AA; 162132 MW; 511E0289774FD522 CRC64;
MDADDLNESE MSVQDETTRR KRRSRGEGRE SRSKRSKRAK QEIEFSDYEA ASSAARTSSR
RSTARQRSRR TKSVEEICEE LEIQDVELSY TSENFENWTI QKLFNQYVQP LLEERNPEAS
KENIRTVLDA KWKEFASLNP YIPKDDLTDY TDEEIVDDEG EAAAEPAAPV APAESKRGRK
RKGRGGGGGG GGRRSSAAAP APTADISGGL DSPSTETAAA EAATAATSAG GGSGLKIKIS
RQKKSAGSTS SGQAAAASTA AAASATPSSS TKKKRRRGGG GNNTSDEEFE RQLEEAERAQ
EEEKEQRKSR KSAGGAAAKR ATGSADHVRT TERFPGEDGY ETDHQDYCDV CQAGGEIILC
DTCPRAFHLV CLDPELEEAP SGRWSCPHCE KEGVQVGQEP AAEPEPKDHH QEFCSECRDD
GDLILCDSCP QAFHLHCLNM KEAQDLKKGD DGPLLLQKQP LYMWRISAHA ASKCAPVRAS
EAFRCAIVAP IPDSVTLLGA NRLALREFSL TGFGPCWPAG ASDRRCASSR TVGAAVSLPL
DAIFLDSAST DGCNPSSWRC PAASQRCSRR CTFLLDAAAS CQCCFAPEGD WHCPRCSCEP
PKAKVESILT WRWVEPPSVN KLDELDHSHH VQAHLSKRPP KREFFVKFKG LSHWHDEWIP
ELQLEVHQAN SWRAYWKKND MDEPPVLDDG SVYRGREKDQ PDDPHNLEDR FFKWGIRPEW
LQIQRIINYR KTKSGDWYLI KWRDLSYEEC TWENPEEIEI PNFERAIEEY FTMKKVLTGE
LAASLANKKP KKSGVGRPSS SSAKEEVSPD LAKKLPPEKP ITNLKTSQWE TQPAYLDETG
GRLHPYQLEG VNWLRYSYGC GTDTILADEM GLGKTIQTIV FLYSLYKEGH TKGPFLVSVP
LSTVINWERE FEFWAPDFYV VTYVGTKDSR GVIRENEMSY DQAAIRAGPK ASRIRSGSQV
KFHVLLTSYE LISIDQATLN SVEWAALVVD EAHRLKNNQS KFFRVLSSYD INVPNDGMSL
SWENSLPLMS MHFTNSMVTQ TPAGLVILLE QLTPVGHLTP ARRYKLLLTG TPLQNNLEEL
FHLLNFMSPG KFHDLQGFLD EFADISKEDQ VKKLHEMLGA HMLRRLKSDV LKSMPSKSEF
IVRVELSPMQ KKYYKYILTR NYDALSSRGK TGCNQVSLLN IMMDLKKCCN HPYLFPSAAE
EAPKRANGAY EGSQLVKACG KLELLERMLR KLRAEGHRVL VFSQMTKMLD ILEDFCEHEQ
LKYERIDGAI TGQLRQDAID RFNNGESDSF VFLLSTRAGG LGINLATADT VIIYDSDWNP
HNDIQAFSRA HRIGQANKVM IYRFVTRNTV EERVTQVAKK KMMLTHLVVR PGFGQKGGSA
AMSKQELDDI LRFGTAELFK DDNNEDSDKD RIVYDDETIS RLLDRTQEGM EEKELALNDY
LTSFK
//
