ID F1KRC8_ASCSU Unreviewed; 1053 AA.
AC F1KRC8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Chromatin-remodeling complex ATPase chain isw-1 {ECO:0000313|EMBL:ADY40432.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY40432.1};
RN [1] {ECO:0000313|EMBL:ADY40432.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; JI164616; ADY40432.1; -; mRNA.
DR AlphaFoldDB; F1KRC8; -.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 166..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 461..612
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..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1053
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 121690 MW; AA24FD8B4E123E4E CRC64;
MSVSSDKEVM DEAKVEVKFS VHDDDDDEQE QEEERVDAEE VEEEQEEDEF TQEMQFEKDS
YKRFEMLLKK TENFSHCLSA GDIEAITPSS PIKGSAGGRV GLSSSGQTPI SGVGDHRHRK
TEKEEDEELI HLARKSETLI RFEKTPFYIE NGEMRDYQIR GLNWLISLQH NGINGILADE
MGLGKTLQTI AMLGFMKHYK NAAGPHLVIT PKSTLQNWLN EFEKWCPSLK AIALIGYAEA
RAELIRDVIL PGGWDVLVTS YEMVLREKSL LRKYVWKFLV IDEAHRIKNE NSKLSEIVRE
FKSKNRLLIT GTPLQNNLHE LWALLNFLLP DMFALASDFD SWFTTNEMMG NQNLVSRLHQ
VLKPFLLRRL KSDVETTLLP KKEVKIYVGL SKMQREWYTK ILLKDIDVVN GAGKLEKARI
MNILMHLRKC CNHPYLFDGA EPGPPYTTDQ HLVDNAGKMV LLDKLLKKLK EQGSRVLIFS
QMSRMLDLLE DYCWWRNYQY CRLDGQTAHA DRQMSIDEFN RPDSEKFIFM LTTRAGGLGI
NLTAADVVII YDSDWNPQVD LQAMDRAHRI GQKKQVRVFR FITESTVDER IIERAEMKLH
LDSIVIQQGR LADSQKALGK DDMLDMIRHG ADQVFASKDS TITDEDIDTI LEKAEQKTEA
LKKKLDSLGE SSLRNFTMDV PGPSFVEDSN YTLYKFEGED YREKQKHTGV GYWIEPPKRE
RKANYQVDAY FREAMRGGHS EPKAPKAPRP PKQPNVQDFQ FYPKRLFELL EKEVYLHRKT
IGYKAQKQPD LPVKEAEKKQ KEEQKKIDSA VPLTEEEQAE KAELLTQGQG NWSRREFQQF
VKANEKYGRN DLESIAKDID TKTLTEVEDY SKVFWERLEE LSDHDRILAT IEKGEARIQR
RQSIKKALDE KIAKYKAPFH QLRIQYGTNK GKNYTEEEDR FMVCQLHKLG FDKDNVYDEL
RQAVRAAPQF RFDWFIKSRT STELQRRCNT LISLIEKEMG EVEVVKRNRG PKSANSASNA
ATPNDTKASS ASKGPQKRKA EMPSSKGSAK RQK
//
