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Database: UniProt
Entry: Q0CSV6_ASPTN
LinkDB: Q0CSV6_ASPTN
Original site: Q0CSV6_ASPTN 
ID   Q0CSV6_ASPTN            Unreviewed;      1119 AA.
AC   Q0CSV6;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   03-MAY-2023, entry version 95.
DE   SubName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0000313|EMBL:EAU36502.1};
GN   ORFNames=ATEG_03228 {ECO:0000313|EMBL:EAU36502.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU36502.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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; CH476597; EAU36502.1; -; Genomic_DNA.
DR   RefSeq; XP_001212406.1; XM_001212406.1.
DR   AlphaFoldDB; Q0CSV6; -.
DR   STRING; 341663.Q0CSV6; -.
DR   EnsemblFungi; EAU36502; EAU36502; ATEG_03228.
DR   GeneID; 4317356; -.
DR   VEuPathDB; FungiDB:ATEG_03228; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   OMA; VHDYQFF; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000007963; 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:UP000007963}.
FT   DOMAIN          204..369
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          500..651
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          866..918
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1043..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1061
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1090..1112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1119 AA;  127825 MW;  AB91D0BF343B2638 CRC64;
     MAPVPDSDTP SQADTPMTDA NEEPVTSVPV DNADAPMTDQ TNAIQDSDTN PNTTASSVAG
     DTVPMDGRKR RSEAFHLRKS VLGKKHGRLD ESKEEDSIRR FRYLLGLTDL FRHFIETNPN
     PRIKEIMAEI DRQNAAEEAK AKKGSSRSGG AGGERRRRTE QEEDAELLKD EKSGAETGTV
     FRESPPFVNG EMRDYQIAGL NWLVSLHENG ISGILADEMG LGKTLQTISF LGYLRHVCDI
     PGPHLVAVPK STLDNWKREF QKWTPEVNVL VLQGDKEERH KLINERLLDE DFDVCITSYE
     MVLREKSHLK KFAWEYIIID EAHRIKNEES SLSQIIRVFH SRNRLLITGT PLQNNLHELW
     ALLNFLLPDV FGDSEAFDQW FSSQDSDQDT VVQQLHRVLR PFLLRRVKSD VEKSLLPKKE
     VNLYVPMSEM QVKWYQKILE KDIDAVNGAA GKRESKTRLL NIVMQLRKCC NHPYLFEGAE
     PGPPYTTDEH LVYNAGKMVI LDKLLSRMQK QGSRVLIFSQ MSRVLDILED YCVFREYNYC
     RIDGTTAHED RIAAIDDYNR PGSDKFIFLL TTRAGGLGIN LTTADIVVLY DSDWNPQADL
     QAMDRAHRIG QTKQVVVFRF VTENAIEEKV LERAAQKLRL DQLVIQQGRA QQQTKNAASK
     EELLGMIQHG AANVFSTQGS TGPLTTEKQI SEDDIDAILR KGEERTAELN KKYEKLGIDD
     LQKFSSENAY EWNGKDFTDR KKDIGLTWIN PAKRERKEQF YSIDKYYRQA LATGGRTADP
     KPKVPRAPKQ VNVHDWQFFP PGLQDLQDKE TAYFHKEIGY KVPLPEGPEE ELSEREAERD
     LEQQEIDNAV PLTEEEQALK AKMSEEGFAT WNRRDFQQFI NGSAKFGRTD YEGIATEVDS
     KDPDEVEAYA QVFWKRYTEI QDYPKYLRVI EQGEEKLRKM NHQRKMLRKK MQMYRVPLQQ
     LKINYTVSTT NKKVYTEEED RFLLVMLDKY GVDGEGLYEK IRDEIRESPL FRFDWFFLSR
     TPVEIGRRCT TLLNTVAKEF EAPDGKANGE AGKGRGRDRD DDDVENDDDG APAKKKSKSG
     AVNKQVKAVK GGSKANSTST SRAASVSSNP APKSKSRKK
//
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