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Database: UniProt
Entry: A0A100I3X6_ASPNG
LinkDB: A0A100I3X6_ASPNG
Original site: A0A100I3X6_ASPNG 
ID   A0A100I3X6_ASPNG        Unreviewed;      1121 AA.
AC   A0A100I3X6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=SNF2 family helicase/ATPase {ECO:0000313|EMBL:GAQ34259.1};
GN   ORFNames=ABL_00602 {ECO:0000313|EMBL:GAQ34259.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ34259.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:GAQ34259.1}.
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DR   EMBL; BCMY01000001; GAQ34259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100I3X6; -.
DR   PaxDb; 5061-CADANGAP00000890; -.
DR   VEuPathDB; FungiDB:An01g09180; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1205919; -.
DR   VEuPathDB; FungiDB:ATCC64974_15960; -.
DR   VEuPathDB; FungiDB:M747DRAFT_264211; -.
DR   OMA; VHDYQFF; -.
DR   Proteomes; UP000068243; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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   Helicase {ECO:0000313|EMBL:GAQ34259.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          209..374
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          505..656
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          870..922
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1047..1121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1047..1063
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1092..1114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1121 AA;  128178 MW;  5ED2EC5273B32E77 CRC64;
     MAPSVEPTPD SPSQADTPMT DANAEPVTSV PVDSADAPMT GYQDTPDYTD SDTNPNTTAS
     SVAGDAAPLD GRRPRSEAFH MRKSILGKKH GRLDESKEDD SIRRFRYLLG LTDLFRHFIE
     TNPNPRIKEI MAEIDRQNAE EEAKAKKKGS SRSGGAGSER RRRTEQEEDA ELLKDEKSGG
     ETNTVFRDSP PFIKGEMRDY QIAGLNWLVS LHENGISGIL ADEMGLGKTL QTISFLGYLR
     HVCDITGPHL IAVPKSTLDN WKREFGKWTP EVNVLVLQGD KEQRHKLINE ELLDENFDVC
     ITSYEMILRE KAHLKKFAWE YIIIDEAHRI KNEESSLAQI IRVFHSRNRL LITGTPLQNN
     LHELWALLNF LLPDVFGDSE AFDQWFSGQD SDQDTVVQQL HRVLRPFLLR RVKSDVEKSL
     LPKKEVNLYV PMSEMQVKWY QKILEKDIDA VNGAAGKRES KTRLLNIVMQ LRKCCNHPYL
     FEGAEPGPPY TTDEHLIYNA GKMTILDKLL ARMQKQGSRV LIFSQMSRVL DILEDYCVFR
     EYNYCRIDGT TAHEDRIAAI DEYNKPGSEK FIFLLTTRAG GLGINLTTAD IVVLFDSDWN
     PQADLQAMDR AHRIGQTKQV VVFRFVTENA IEEKVLERAA QKLRLDQLVI QQGRAQQQTK
     NAASKEELLG MIQHGAANVF NTQANTTISA EHQISEDDID NILRKGEERT AQLNKKYEKL
     GIDDLQKFSS ESAYEWNGKD FTDRKKDIGI NWINPAKRER KEQFYSIDKY YRQALATGGR
     TADPKPKVPR APKQITVHDW QFFPPGLQEL QEKETAYFHK EIGYKVPLPD GPEEELSERE
     AERDLEQQEI DNAVPLTEDE QAEKAKMSEE GFSNWNRRDF QQFVNGSAKF GRTDYVGIAT
     EVDSKEPEEI EEYAQVFWER YTEIQDYPKY LRVIEQGEDK LRKMNHQRKM LRKKMEMYRV
     PLQQVKINYT VSTTNKKVYT EEEDRFLLVM LDKYGVDGEG LYEKIRDEIR ESPLFRFDWF
     FLSRTPVEIG RRCTTLLNTV AKEFETDGKA NGESGKGRGR DRDDDEAEED EGPPAKKKTK
     GGAVNKQVKA VKGGSKATST STSRAASVSS NAAPKSRSRK K
//
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