ID A0A3M6VFE9_9STRA Unreviewed; 1401 AA.
AC A0A3M6VFE9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chromatin-remodeling complex ATPase chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=DD237_001679 {ECO:0000313|EMBL:RQM18548.1}, DD238_005262
GN {ECO:0000313|EMBL:RMX65755.1};
OS Peronospora effusa.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Peronospora.
OX NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX65755.1, ECO:0000313|Proteomes:UP000282087};
RN [1] {ECO:0000313|Proteomes:UP000282087, ECO:0000313|Proteomes:UP000286097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R13 {ECO:0000313|EMBL:RQM18548.1,
RC ECO:0000313|Proteomes:UP000286097}, and R14
RC {ECO:0000313|EMBL:RMX65755.1, ECO:0000313|Proteomes:UP000282087};
RA Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA Reyes Chin-Wo S., Mou B., Michelmore R.;
RT "Comparative genomics of downy mildews reveals potential adaptations to
RT biotrophy.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMX65755.1}.
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DR EMBL; QLLG01000231; RMX65755.1; -; Genomic_DNA.
DR EMBL; QKXF01000043; RQM18548.1; -; Genomic_DNA.
DR STRING; 542832.A0A3M6VFE9; -.
DR VEuPathDB; FungiDB:DD237_001679; -.
DR Proteomes; UP000282087; Unassembled WGS sequence.
DR Proteomes; UP000286097; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00084; HMG-box_SF; 2.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
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; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
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; PTHR10799:SF1017; -; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09011; HMG_box_2; 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; SM00398; HMG; 2.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF47095; HMG-box; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 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.
DR PROSITE; PS50118; HMG_BOX_2; 2.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000282087}.
FT DOMAIN 30..106
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 297..468
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 601..752
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 948..999
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 1331..1400
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 30..106
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT DNA_BIND 1331..1400
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 225..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..198
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 237..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1401 AA; 162283 MW; 4C5353CBA6B4E799 CRC64;
MSKNEEKESR ADWVAVEAQF QNGEVGANQP IRPKSAYQFF QKRVIDDVKR DLSVKAAQLN
EPLELGSISK EISVRWAQLS TGDREEFVKL AAADKKRYDD ECRVRDEEVE KERARKREEM
YSIVQGKRER KKVCEEEMQT QVVIKETSLK HQPRELTEKQ MEAKRLRKEI RQQGMDERDE
LKAEEKRQKE ALAKKRSEIA SARLKYLLSQ SDMFAHFSGQ VQKKGKKGVA LDANENAPDT
DAKKTRGNKK GKKSTLTHEE DELDSSHHVG VRITKQPSVI KFGTMRAYQL EGLSWMVNLA
RQGINGILAD EMGLGKTLQT ISVLGYFLEF ENITGPHIVL VPKSTLSNWL AEFERWCPSL
RAVKFHGNKE ERLRCVQEVL CPGLSDAKRK FDVCVTTFEM CLKEKSALCK FAWRYLVIDE
AHRIKNESSQ FSTVVRMLDT EHRLLLTGTP LQNNLHELWA LLNFLLPDVF ASSQEFDDWF
NLDVDDDEAK KQMISQLHKI LRPFMLRRLK ADVEKSLPPK KETLLFVGMS EMQKVLYKSL
LLRDINTIMG GSGGVSKSAL QNIVMQLRKC CGHPYLFEGQ EDRSLDPLGE HVVENCGKMV
LVDRLLKKLK QRGSRVLIFT QMTRVLDIME DFCRMRQYNY CRIDGQTSYE DRESSIDEYN
APNSSKFLFL LSTRAGGLGI NLYTADVVIL YDSDWNPQAD LQAQDRAHRI GQKKEVNVYR
LVTTDSVEEK IIERAQQKLK LDAMIVQQGR LQEKQAKLTK NDMLEMIRFG ADQVFRTTDS
TITDEDIDAI LAKGEQRTEE MKQKMQVHDK GDMLDFKLDG GGCQNHDGID YSNEKERQEE
LKRLADAELA RQMAEGMGKR ERRTVLRHSL VPSESKHRTK QKQLPKALRL PRLEEWQFYN
RKRLIELHEI ECANYEQAKA EMEKPPLPPH AQYLTDEELK EKEQLLTEGF SDWNKPQFFL
FIKLLARYGR GNIEAVAREM MKPLEEIEEY SKIFLARGQD ELSDWHKIMK SIEKGESKLL
EIERLTEETT RKVKRYANPW EDMPINYQGK GGKVFTEEED RVLLCLVNQF GYGAWDRIKQ
EICSMEMFAF DYYLRSRTAA EIGRRCDSLM RICEKDNADL ELREKKENDV RHVLQEQRAK
LDQQLAAARA DVKQHQARVD ELIMKEAKRM QKQRENKRAK KRKQRDQNED IVDQYTEALV
SFLLQATSMD AAKVALDFCA KIRQESDEEL QPSYVLKKIR QVAEPDENAS KGALAWIIKA
EYSNVEKLSR KKEKKIMKQE HMSDVSDTTA MQSGQDDTGR LPRSPWSPTA MKQKVKKEKK
VKREGSVLKS VRKPRSAYVL FSVASRVEVK QSLGNNASLV DAMRQIAQTW KDMSPEQKAP
WIEAAKQDQL RYESEMNETA A
//
