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Database: UniProt
Entry: G8JMI9_ERECY
LinkDB: G8JMI9_ERECY
Original site: G8JMI9_ERECY 
ID   G8JMI9_ERECY            Unreviewed;      1034 AA.
AC   G8JMI9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   13-SEP-2023, entry version 68.
DE   RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=Ecym_1481 {ECO:0000313|EMBL:AET37706.1};
OS   Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS   NRRL Y-17582) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=931890 {ECO:0000313|EMBL:AET37706.1, ECO:0000313|Proteomes:UP000006790};
RN   [1] {ECO:0000313|Proteomes:UP000006790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC   {ECO:0000313|Proteomes:UP000006790};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
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; CP002497; AET37706.1; -; Genomic_DNA.
DR   RefSeq; XP_003644523.1; XM_003644475.1.
DR   AlphaFoldDB; G8JMI9; -.
DR   STRING; 931890.G8JMI9; -.
DR   GeneID; 11470434; -.
DR   KEGG; erc:Ecym_1481; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   InParanoid; G8JMI9; -.
DR   OMA; VHDYQFF; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000006790; Chromosome 1.
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; 1.10.1040.30; 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; 1.
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:UP000006790}.
FT   DOMAIN          141..306
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          439..590
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          810..862
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          70..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          986..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1002
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1034
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1034 AA;  120108 MW;  B87B083B5959515D CRC64;
     MSETITKDSK YWKDRKKRFL LDVDAKVAKQ RDKDDTYVRF KHLLGLTDLF RHFIGMRAKR
     DKNMQKLLRM VDGESRGNNN KSLRNRDSSR HYRKTEKEED AELIQDEEGR LSETTVLTES
     PNYVKAGKLR EYQIYGLNWL ISLHENKLSG ILADEMGLGK TLQTISFLGY LKFIKNIDGP
     FIVVVPKSTL DNWKREFSKW TPDVRTLILQ GDKETRAKLL EDRILSCDFD VLITSYEMVI
     KEKAALKKFA WQYIVIDEAH RIKNEQSTLS QIIRLFYSKG RLLITGTPLQ NNLHELWALL
     NFLLPDVFGE SEVFDEWFQQ NDKDQDQEVV VQQLHAVLQP FLLRRVKAEV EKSLLPKIET
     NVYVGMAGMQ LQWYKSLLEK DIDAVNGAVA KREGKTRLLN IVMQLRKCCN HPYLFEGAEP
     GPPFTTDEHL IYNSGKMIVL DKLLKRKQME GSRVLIFSQM SRLLDILEDY CYFREYEYCR
     MDGSTSHEER IQAIDDFNAP DSNKFIFLLT TRAGGLGINL VTADTVVLYD SDWNPQADLQ
     AMDRAHRIGQ KKQVHVYRFV TENAIEEKVI ERAAQKLRLD QLVIQQGTGK KSANLGNSKD
     ELIDMIQFGA KDVFDKKSTE VTMDDDIDEI LKKGEQKTQK LNAKYEALGL DDLQKFNGMA
     DQSAYEWNGT IFEKKKTEAK SLEWINPSRR ERRREQTYSV DDYYKEIIGG AANKNSSKTT
     PQPKMPKAPR AVLIQDFQFP SPNLNFLQEK EQLSYKRKIN YKVASYDLGS DDEEDDGSIS
     ERIASEQAKI DNAEEFTEED ELMKQKCIDE SFTSWTKREF ITFINGSSKF GRTNFKAIAS
     MLENKTVKEV EEYGNVFWSR YKEIQGYEKY LNTIEAGERK TEKLRQQESL LKMKIAQCES
     PLHEMIIQYP PNNARRTYNS MEDKFILITV NKYGLFSDNL YDKVKQEIMK CNLFHFDWFI
     RTRSVHELSK RVTTLLTMIT REYEGPDSAA KRKRKTKDDT PAISNGDRGV STGLDPSEQP
     LKKIRAEEGV FVPH
//
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