ID W7I9X3_9PEZI Unreviewed; 1149 AA.
AC W7I9X3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 22-FEB-2023, entry version 47.
DE SubName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0000313|EMBL:EWC48907.1};
GN ORFNames=DRE_00212 {ECO:0000313|EMBL:EWC48907.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC48907.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC48907.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC48907.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KI966371; EWC48907.1; -; Genomic_DNA.
DR AlphaFoldDB; W7I9X3; -.
DR HOGENOM; CLU_000315_0_2_1; -.
DR Proteomes; UP000024837; Unassembled 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; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
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; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
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; PF09110; HAND; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000024837}.
FT DOMAIN 186..351
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 483..634
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 848..900
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 131108 MW; D11165D076066D8B CRC64;
MPKAKPRSKN VSEDEAAMKD EDVTMNDAQS ESDAASSAEE QADDEDDGDV TQPITKRQRR
NEINSERRKH FGQQKENLKS AKYADSAKRF AYLIGLTDLF RHFIGLNPEL AKAVEEADAI
NKAKKRAKAV AQGNRTRRTE KEEDAELLED EVNAEDSEQR TIFSENPSFI EGQMRDYQIA
GLNWLISLHE NGISGILADE MGLGKTLQTI SFVGYLRFIR SIDGPHLVIV PKSTLDNWKR
EFARWIPDIH TLVLQGAKEE RQGLINERLL TEDFDVCITS YEMVMREKHH LKKFAWKYII
VDEAHRIKNE ESSLSKIVRM FDSQGRLLIT GTPLQNNLHE LWALLNFLLP DVFSSSEAFD
QWFESSGHDQ DTVVKQLHKV LRPFLLRRVK SDVEKSLLPK KECNIYVGMS QMQIKQYRNI
LEKDIDALNG QNMGKRESKT RLLNIVMQLR KCCNHPYLFD GAEPGPPYTT DEHLVFNCGK
MVVLDKLLRK MQEDGSRVLI FSQMSRLLDI LEDYCLFRGF KYNRIDGSTA HEDRIAAIDE
YNKPGSEKFI FLLTTRAGGL GINLTTADIV ILYDSDWNPQ ADLQAMDRAH RIGQTKQVHV
YRFITEDAIE EKILERAAQK LRLDQLVIQQ GRAQPAVKNA AGSDDLLGII QHGAQEIMNK
ASERDNKGTI RDDEDIISYI TKGSAKTEKM KAKFSTMGLD DLQKFSSESA YEWNGEDFQK
KDMGLAFNWI EPAKRERKEQ VYSVDKYYSN ILNPKVPKGE QKPRAPRPPT QIRIQDHQFY
PIRLIQLQEQ ETAYYRKTIG YKVPMVEPQE GEDADAKNDD RELEQMEIDN AVPLTEEEIQ
EKERLAEQGF SDWSKRDFQQ FVNLSARYGR KALESIAAEM DYKDVKQVKA YTKVFWERYT
EIDGYDRAIQ TIVGGEERAE KVRKQQENLR KKIEQYRVPL QQMKINYSVS TTNKKVYTEE
EDRFLLVQLD RYGLESENLY EYIQNDIRDC PLFRFDWFFL SRTPAELSRR CQTLLTTVDR
EFDPKLKVAD DDDEPKPGRK GAKSSGKTSR QRSVEDDDET GPPPKKGKTT NGVATNGKGP
KNKNIDSVKS AGGSKAASSN TSRANSVGSN SDAGGSSKPG PKPKANGTKG GPSKAGTPTS
ASKGKGKKR
//