ID W2YC72_PHYPR Unreviewed; 1394 AA.
AC W2YC72;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chromatin-remodeling complex ATPase chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=F442_18685 {ECO:0000313|EMBL:ETP32655.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP32655.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP32655.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP32655.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) 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:ETP32655.1}.
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DR EMBL; ANIY01003954; ETP32655.1; -; Genomic_DNA.
DR EnsemblProtists; ETP32655; ETP32655; F442_18685.
DR Proteomes; UP000018948; 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; 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; 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 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:UP000018948}.
FT DOMAIN 25..101
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 290..461
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 594..745
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 941..992
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 1324..1393
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 1324..1393
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 1163..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1322
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 1306..1322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1394 AA; 161695 MW; 9D0ABC3E3C870205 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 NLAHQGINGI
LADEMGLGKT LQTISVLAYF YEFENITGPH IVLVPKSTLS NWLAEFERWC PSLRAVKFHG
NKEERQRCVQ EVLCPGLPDD KRKFDVCVTT FEMCLKEKTA LCKFAWRYLI IDEAHRIKNE
SSQFSTVVRM LDTEHRLLLT GTPLQNNLHE LWALLNFLLP DVFASSQEFD DWFNLDVDDD
EAKKQMISQL HKILRPFMLR RLKADVEKSL PPKKETLLFV GMSEMQKALY KSLLLRDMNT
IMGGTGGVSK SALQNIVMQL RKCCGHPYLF EGQEDRSLDP LGEHVVENCG KMVLLDKLLK
KLKQRGSRVL IFTQMTRVLD IMEDFCRMRL YDYCRIDGQT SYEDRESSID EYNKPNSSKF
LFLLSTRAGG LGINLYTADV VILYDSDWNP QADLQAQDRA HRIGQKKEVN VYRLVTTDSV
EEKIIERAQQ KLKLDAMVVQ QGRLQEKQSK LTKNDMLEMI RFGADQVFRT TDSTITDEDI
DAILAKGEQR TEEMKQKMQA HDKGDLLDFK LDGGGCQNHD GIDYSNEKER QEELKRLADA
ELARQMAEGM GKRERRTVLR HSHVSLEGKH RTKQKQLPKA LRLPRIDEWQ FYNRKRLIEL
HEIECANYEQ AKTEMEKPPL PPHAQYLTEE QLQEKEQLLS EGFSDWNKPQ FFLFIKLLAR
YGRNNIEAVA REMMKPLEEI ERYSKVFLSR GQDELSDWPK ILKSIEKGES KLLEIERLTE
ETARKVKRYA NPWEDMPINY QGKGGKVFTE EEDRVLLCLV NQFGYGAWDR IKQEICSMEM
FSFDYYLRSR TAAEIGRRCD ALMRICEKDN ADLEIREKKE NDVRRVLQEQ RAKLDQQLAA
ARADVKQHQA RVDELIMKEA KRMQRQREAK RAKKRKERDE NEEMVDQHTE ALVSFLLQAT
SMDAAKVALD FCAKIRHEKH EELQPSYVLK KIRQVAELDE LATKGTLAWT IKPEFANIGK
VNLKKESKVL KQEHMTDVSG GATPIKSEDK SRLPRSPWSP TAMKQQQKVK KEKKVKKDGT
LNTVRKPRSA YVQFSMATRA EVKRSLGENA QMVDIMKELV RLWKEMTPEQ KAPWVEAAKL
DKLRYEREMN EMAA
//
