ID F0VIN7_NEOCL Unreviewed; 1613 AA.
AC F0VIN7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=SWI2/SNF2 ISWI-like (AT hook) {ECO:0008006|Google:ProtNLM};
GN ORFNames=NCLIV_033850 {ECO:0000313|EMBL:CBZ53598.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ53598.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
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DR EMBL; FR823390; CBZ53598.1; -; Genomic_DNA.
DR RefSeq; XP_003883630.1; XM_003883581.1.
DR GeneID; 13442930; -.
DR VEuPathDB; ToxoDB:NCLIV_033850; -.
DR eggNOG; KOG0385; Eukaryota.
DR InParanoid; F0VIN7; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000007494; Chromosome VIII.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR027417; P-loop_NTPase.
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; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007494}.
FT DOMAIN 228..394
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 526..677
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1545
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1613 AA; 180994 MW; 0292CD83214C64B4 CRC64;
MNAVSDSPSP HGEGEKEGEK SVSASAFGTD AGPTDSAACT GQETALSSES RDVNMDDMSP
GNEPTSEGKE DREEDEEDDA EEMREEDDDE DEKEDDEEGL REGEEETMFG DGPENSVKGE
YGLANAELEA KLRELLRQAD TFSSRIHGGG NASAPPKTKG PGSRSRERRM LSEAEEDDIL
LRRLEEDSGE AEGDGASQGD VFVRITEQPS CIEGKMKHYQ IEGLNWLYQL HCLDINGILA
DEMGLGKTLQ TISILAFLQF EKNIPGPHLV ICPRSTLDNW FNEVKKWCPR FRPARLHGTK
EERQELYDTV LDPGHFDICI TTYEMVIKDY HRLASRFQWN YLIMDEAHRI KNEKSVLSEV
VRRFRPRRRL LITGTPLQNN LRELWALLNF IMPQLFDATL DFAALFDFSR LNTEQQQHQV
ITTLHRILRP FMLRRLKSDV ARDLPPKREI YIFVGMSKLQ KKLYADILSK NVEVLNAMSG
SKTQMLNILM QLRKCCNHPY LFDGVEPGPP YVEGEHMVEA AGKMALLDKL LPRLKAEGSR
VLLFSQMTRL LDIVDDYCRW RGFDYCRIDG GTPGTERQER IDEFNAEGSS KFLFLLSTRA
GGLGINLATA DVVILFDSDF NPQMDLQAMD RAHRIGQKKR VVVYRFVTGD TVEAKIVERA
AKKLKLDSLV IQKGRLSQSN QAQKGPSTNE LHAILQFGAQ EVYRTQDESS ITEADIDVIL
ADAEQRTAEI QAQLTSLERT FDLSNMSLDG GLHMYGEEED ELRNQPRKPG RKKAVKLNRP
ATFFELGDRK TKWRGDGGAA AMAMVKKERK LSRKALTGWR AEINGGYDFQ FFNADQLDAL
DAIQRNWQAY LDNRRRKLLE NLKRERGSTL ASAAGAKKEA ETAEKGEKGD EAPPAKKQRT
SEEEGAKAVL GDFQKPAAAD LLRACEEPVE TEQEGSDAWT NGVEHLTVPQ ARQVETLLES
FAAAAGLSLS TFDGKNAEDV EMEDASSSSP SSRIEKICRL LRPAEDKAQK SVFSTEAPSF
AAALKQLAED FVSGQAAALG VPLAVAASQR FAASFSAGQP DAEKRGVKRE REDSKEDSKG
ESKEDIKDES KEDSKDESKE ESKDESKEES KDESKEESKE ESKEDNKEES KEESKAEIKE
ESGGPAPEAE DEAPGEEEDG EKPSPPPSVG GSPAAEEGTT VKKKAGRPRK NVKEEERGVD
EDEEDEALLA LLKEEDLDDE NDPDRPEEFT EDMRKEKDRL LAEGFGNWNR TEFSKFVSGL
IHYGRDRLAE AWCAHFRGTN KSLEELERYT EVFFKRYSEV EGGDRIMQRV EKAADIRGAL
DSQRRAVQAM VEEQLREERT DGGVARPIER PDELRLPKRL APSAHFTPQE DAMLLWGLYE
QGVTAYAAIH ALLKYYWFDS RGFFHVASRS MKQVEDRCKE IVMAIELEET AKTGQKEYMR
YRQFRPTSHR IGRPPTRLSA GGRPGRGHAS QCSRSRDKNG ENLFFPGDEG EEGRSVCWEN
EEDERRDERR DRLFSEGAKN PEGRGGSQKG RRCTGRKRGR PRGGRGRNST RGLAPSHLSP
GGVGAGVGSG ESDRGGEEQE PRPEGEENES GREDVREKVD EEKDGEEESK TAA
//