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Database: UniProt
Entry: A0A0W8DXS5_PHYNI
LinkDB: A0A0W8DXS5_PHYNI
Original site: A0A0W8DXS5_PHYNI 
ID   A0A0W8DXS5_PHYNI        Unreviewed;      1362 AA.
AC   A0A0W8DXS5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Chromatin-remodeling complex ATPase chain {ECO:0000313|EMBL:KUG00934.1};
GN   ORFNames=AM587_10015544 {ECO:0000313|EMBL:KUG00934.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUG00934.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUG00934.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) 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:KUG00934.1}.
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DR   EMBL; LNFO01000510; KUG00934.1; -; Genomic_DNA.
DR   STRING; 4790.A0A0W8DXS5; -.
DR   EnsemblProtists; KUG00934; KUG00934; AM587_10015544.
DR   OMA; TAFYRKE; -.
DR   Proteomes; UP000052943; 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; cd00084; HMG-box_SF; 1.
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; 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; 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   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:UP000052943}.
FT   DOMAIN          25..101
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DOMAIN          289..429
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          562..713
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          909..960
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   DOMAIN          1292..1361
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        25..101
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   DNA_BIND        1292..1361
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          160..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1131..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1240..1290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1274..1290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1362 AA;  158231 MW;  952779B7947C8135 CRC64;
     MEKKESRADW VAVEAQFQSG EANQPAKAKT AYQFFQKRVV DDVKRDVAAK AAELNEPVEL
     GSISKEISAR WAQLSAGDRE EFVELAAQDK KRYDEECRAR DEEVERERAR KREEMYGAVE
     GKRERKKTQV VIEETRPKRQ PRELTEKQLE AKRLRQEIRQ QEIDERDELK AEEKRQKEAL
     AKKKSEIASA RLKYLLSQSD IFAHFSGQVK KGKTKGKKGA ALDADEDAET GEESAEDTKK
     GKGKKNKKRD DDEDEMDSST HVGVRITQQP SVIKFGTMRA YQLEGLSWMV NLAHQGPHIV
     LVPKSTLSNW LAEFERWCPS LRAVKFHGNK EERQRCVQEV LCPGLPDDKR KFDVCVTTFE
     MCLKEKTALC KFAWRYLIID EAHRIKNESS QFSTVVRMLD TEHRLLLTGT PLQNNLHELW
     ALLNFLLPDV FASSQEFDDW FNLDVDDDEA KKQMISQLHK ILRPFMLRRL KADVEKSLPP
     KKETLLFVGM SEMQKALYKS LLLRDMNTIM GGTGGVSKSA LQNIVMQLRK CCGHPYLFEG
     QEDRSLDPLG EHVVENCGKM VLLDKLLKKL KQRGSRVLIF TQMTRVLDIM EDFCRMRLYD
     YCRIDGQTSY EDRESSIDEY NKPNSSKFLF LLSTRAGGLG INLYTADVVI LYDSDWNPQA
     DLQAQDRAHR IGQKKEVNVY RLVTTDSVEE KIIERAQQKL KLDAMVVQQG RLQEKQSKLT
     KNDMLEMIRF GADQVFRTTD STITDEDIDA ILAKGEQRTE EMKQKMQAHD KGDLLDFKLD
     GGGCQNHDGI DYSNEKERQE ELKRLADAEL ARQMAEGMGK RERRTVLRHS HVSLEGKHRT
     KQKQLPKALR LPRIDEWQFY NRKRLIELHE IECANYEQAK TEMEKPPLPP HAQYLTEEQL
     QEKEQLLSEG FSDWNKPQFF LFIKLLARYG RNNIEAVARE MMKPLEEIER YSKVFLSRGQ
     DELSDWPKIL KSIEKGESKL LEIERLTEET ARKVKRYANP WEDMPINYQG KGGKVFTEEE
     DRVLLCLVNQ FGYGAWDRIK QEICSMEMFS FDYYLRSRTA AEIGRRCDAL MRICEKDNAD
     LEIREKKEND VRRVLQEQRA KLDQQLAAAR ADVKQHQARV DELIMKEAKR MQRQREAKRA
     KKRKERDEKE EMVDQHTEAL VSFLLQATSM DAAKVALDFC AKIRHEKHEE LQPSYVLKKI
     RQVAELDELA TKGTLPWTIK PEFANIGKVN LKKESKVLKQ EHMTDVSGGA TPIKSEDKSR
     LPRSPWSPTA MKQQQKVKKE KKVKKDGTLN TVRKPRSAYV QFSMATRAEV KRSLGENAQM
     VDIMKELVRL WKEMTPEQKA PWVEAAKLDK LRYEREMNEM AA
//
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