ID A0A125YKZ7_TOXGV Unreviewed; 1249 AA.
AC A0A125YKZ7; A0A0F7UTS0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin, putative {ECO:0000313|EMBL:CEL71826.1};
DE SubName: Full=SWI2/SNF2 ISWI-like SANT {ECO:0000313|EMBL:ESS29580.1};
GN ORFNames=BN1205_059090 {ECO:0000313|EMBL:CEL71826.1}, TGVEG_321440
GN {ECO:0000313|EMBL:ESS29580.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS29580.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|EMBL:ESS29580.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS29580.1};
RA Paulsen I.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ESS29580.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS29580.1};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CEL71826.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:CEL71826.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; LN714490; CEL71826.1; -; Genomic_DNA.
DR EMBL; AAYL02000292; ESS29580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A125YKZ7; -.
DR STRING; 432359.A0A125YKZ7; -.
DR PaxDb; 5811-TGME49_121440; -.
DR EnsemblProtists; ESS29580; ESS29580; TGVEG_321440.
DR VEuPathDB; ToxoDB:TGVEG_321440; -.
DR eggNOG; KOG0385; Eukaryota.
DR OMA; VHDYQFF; -.
DR Proteomes; UP000002226; Partially assembled 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
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; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-1; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226}.
FT DOMAIN 269..497
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 640..791
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 985..1037
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 140151 MW; A622109BDE14E76E CRC64;
MEVEPEGDVE AGGPVETHAS DFPGKDGTCA QVSSVSSSPC GHLDAAALRN GHSVFTPGSN
AVLSSQFPSS PPSSSPSSSP SSPSASCLGT REKSDSRSLT SGHLNGSAAD AESPGTRGGD
SAVSRDGRED SMGKLQMLLE YGESYLLSLC HHSRKQEATR QFSASREAVE SGAASGLGPC
GEKAVGSGPS RRSRRVVSSD DEDGPDFEEG KSGEDARRAR KRRRGPEEGS PYLEEEFRSR
PVITRLSTHP SILRCPPKPY QLEGLNWLIQ LHERGMNGIL ADEMGLGKTY QTISLLAFLK
EGKGVDGPHL VLAPKSTIGN WMTEFRKFCP SINAVRVLGD KETRRRTLAH IVSRTQASSF
PFSFPGEKTL RSESSPESEE EKSDDETQKD LKGAERPDED GEEGAKEEKE EDDGVLPDRV
DVVVTSFEMC ILERAQFLKV DWEYIIIDEA HRIKNESSKL AQTARLFNTK HRLLLTGTPL
QNNLRELWAL LNFLFPSLFS SSAEFEHLFD LTGTGEAGSE MTAEEREERN MKIVTRLHRI
LRPFMLRRVK KEVLKEMPPK KELLLVVPLS AMQKQLYKDL LTKNVAALQG AEGAGRTQLL
NLAMQLRKAC NHPYLFDGYE SEHADPFGEH VIENAGKLRF CDRLLRRLIQ ENRRCLIFTQ
MTKMIDILED YCRIRLFKYC RIDGNTSGDE RDRQIEAFNA PGSDIPIFLL STRAGGLGIN
LATADTVILY DSDWNPQVDL QAMDRVHRIG QKSAVNVYRL VHEHTIEQKI IERAMLKLQL
DTAIIQQGRL SDQQNQQKQL SKNELMTMVQ FGADHIFKSG AGEDVTEEEL EAILARGQER
TDAMNEKLQA HVKKSLLDFT INSAPSSSLY EYDGIDYTDQ QRKADREAWA SLAVQTLEAQ
NERESRRRIR MQKEQEMQLQ QSAEQRKVKH VPRAVRLPAM QEWQFYDRRR IEELHAVELM
YYRNQGTTRA PTDEEREEKQ RLLREGFGSW GKRDFIQFVK GNEMYGRHDI ARIATEVDGK
SVEEVAAYSR VFWSRYPEIQ GWEKWIRRIE EGEAVINKRR ELEQVIVRRQ QQCEVPWRRL
LIPYGGAAKS RSIFTEQEDR WILNMTTLLG YGNWDKMRDL LLRDTQWRLD WFVRSRTAGD
VGKRAEALVR LLKKEEGERF TRGRRRLDLP DTRPTVSAPV ASAPVAGVSP AAGGAPGTAA
QSGGDSGAGV SSGETPGSVP FLGLGTNAGA ERPASGRAKR LRSTAWAAA
//