ID A0A158Q8U5_9BILA Unreviewed; 1052 AA.
AC A0A158Q8U5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Chromatin-remodeling complex ATPase chain Iswi {ECO:0000313|WBParaSite:EEL_0000874201-mRNA-1};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000874201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000874201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR AlphaFoldDB; A0A158Q8U5; -.
DR STRING; 1147741.A0A158Q8U5; -.
DR WBParaSite; EEL_0000874201-mRNA-1; EEL_0000874201-mRNA-1; EEL_0000874201.
DR Proteomes; UP000050640; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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 InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 178..343
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 473..624
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 827..879
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 121288 MW; 3CD1392F169BCC6B CRC64;
MDTSENDINE APLSESTEGL IGTELFSVKD EPETVEKETM EMKMNPDINA MEIDGNKEDI
TETPTSSTSF NAGSQFEKDS FKRFEMLLKK TENFSHCLSA GDVESVDVGL SSGMGVKGRP
RNQSEGDHRH RKTEKEEDEE LINQVKKSET LIRFEKTPFY IENGEMRDYQ IRGLNWLISL
QHNGINGILA DEMGLGKTLQ TVAVIGFMKH YKNASGPHLV IAPKSTLQNW INEFGKWCPS
LKAVALIGIA EARADLIRNE ILPGKWDVLV TSYEMVLKEK SLLRKYAWQY LVIDEAHRIK
NEHSKLSEIV REFKSKHRLL ITGTPLQNNL HELWALLNFL LPDMFALASD FDSWFTTNDM
MGNQDLVARL HKVLKPFLLR RLKSDVEKTL LPKKEVKIYV GLSKMQREWY TKILMKDIDV
VNGAGKLEKA RIMNILMHLR KCCNHPYLFD GAEPGPPYTT DQHLVDNSGK MVLLDKLLAK
LKTQGSRVLI FSSMSRMLDL LEDYCWWRGY RYCRLDGQTV HDERQKSIDE FNKPDSDKFI
FMLTTRAGGL GINLTAADVV IIYDSDWNPQ VDLQAMDRAH RIGQKKQVRV FRFITDNTVD
ERIIERAEMK LHLDSIVIQQ GRLTDSQKAL GKEDMLDMIR HGADQVFASK DSTITDENID
TILEKAEQKT EALNKKIASL GETSLRNFAL DAPTFDADSS YTVYKFEGED YREKQKNVGG
IGYWIEPPKR ERKANYQVDA YFREAMRGGH AEPKAPKAPR PPKQPNVQDF QFYPKRLFEL
LEKEAQRPPD LPTKEAERKQ KEEQKKIDSA VPLTEEEQNE KLQLLTQGQS NWSRREFQQF
IKANEKYGRH DLENIAKEID TKSATEVEEY AKLFWERLDE LSDHERILAT IEKGEARIQR
RQSIKKALDE KIAKYKAPFH QLRIQYGTNK GKNYTEEEDR FMVCQLHKLG FDKDNVYEEL
RQAVRSAPQF RFDWFIKSRT STELQRRCNT LISLIEKEMG EVEVKRKHGQ KSSANTPTAN
NSDSKVTTVT KSGQKRKSEQ STSKGSSSKR QK
//
