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Database: UniProt
Entry: G0WFZ3_NAUDC
LinkDB: G0WFZ3_NAUDC
Original site: G0WFZ3_NAUDC 
ID   G0WFZ3_NAUDC            Unreviewed;      1135 AA.
AC   G0WFZ3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   13-SEP-2023, entry version 69.
DE   RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN   Name=NDAI0I01350 {ECO:0000313|EMBL:CCD26704.1};
GN   OrderedLocusNames=NDAI_0I01350 {ECO:0000313|EMBL:CCD26704.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26704.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD26704.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE580275; CCD26704.1; -; Genomic_DNA.
DR   RefSeq; XP_003671947.1; XM_003671899.1.
DR   AlphaFoldDB; G0WFZ3; -.
DR   STRING; 1071378.G0WFZ3; -.
DR   GeneID; 11493558; -.
DR   KEGG; ndi:NDAI_0I01350; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   OMA; PRMDEWQ; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000000689; Chromosome 9.
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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProt.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000000689}.
FT   DOMAIN          133..298
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          431..582
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          809..862
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          68..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          989..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          867..894
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        68..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1021
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1035..1113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1135 AA;  131110 MW;  4EA604C419F75FA3 CRC64;
     MTTTPAMSNS NYLITDPKRK KEQFDIESTV KRFKHLLSLS GLFKHFIENK AQKDEKFAKV
     LTILNNDDDS KKKNSQKKRR KTEREEDAEL LKEEEIETTE DTNDEVGFQF RESPTYIHGE
     LRPYQIQGLN WLVSLHTNGI AGILADEMGL GKTLQTIAFL GYLRYMENIN GPFLVIAPKS
     TLNNWLREIN KWTPDVKAFV LQGDKQERAD IIKDKLLTCD FDIVVASYEI TIREKAALKK
     MNWQYIVIDE AHRIKNEESL LSQVLREFTS RNRLLITGTP LQNNLHELWA LLNFLLPDIF
     SDSQDFDDWF SSETSEEDQD KVVKQLHTVL QPFLLRRIKS DVETSLLPKK ELNLYVGMSS
     MQKKWYKQIL EKDLDAVNGS NPNKESKTRL LNIVMQLRKC CNHPYLFDGA EPGPPYTTDE
     HLVYNSAKLK VLDKLLKKMK EEGSRVLIFS QMSRVLDILE DYCFFRGYKY CRIDGSTDHE
     DRIKSIDDYN SPDSDKFIFL LTTRAGGLGI NLTSADVVVL YDSDWNPQAD LQAMDRAHRI
     GQKKQVKVFR FVTNNSVEEK ILERATQKLR LDQLVIQQKK TLKKENRKEA KDALLSMIQH
     GAADIFMSAS TASSSPTPSA TTSQSEPDAV EDVDLQSILT MSEDKTKSLN AKYETLGLDD
     LQKFNQESAY EWDGQNFKKQ TQKGIIDPTW IQPTKRERKE NYSIDNYYRD VLTTKKAVTP
     LQPRMPKPKV FYSHQLHSPL LNELYEKDRM WIAKKTKYVP TLDDVKVTYG EDLTNAEMKD
     KLKLLKESID KAQPLTEEEE KSKQELEAKG FSNWNKTEFR KFITLSGKYG RNSIQAIATE
     LAQTKSVQDV RDYAKAFWAN LDSIEDSDKY VKLIEADEEK LKKLKLQQEA LRLKVSKYKN
     PLFELTLKHP PSNSNKRTFS EEEDRFLLIT LSKYDLGRDD LYDMIRDEIR DSPFFELDFF
     FQSRTPLELA RRAFTLLQCI EKESQSGIVG PEFNEKKPKA VKGEKRGPSN DNKDRKPAIK
     KIKLTMNQKI SNEGKKDIAI SEEKETTTAA EDKQEIMEDK QEVTEENQEA HRTVGETNEE
     SHKESQNEVD TDTKEEHIEP KEEHTEPKEE STNDSKSSAQ GVTEGKVAPP VVLEP
//
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