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Database: UniProt
Entry: A0A0F0I8Q2_ASPPU
LinkDB: A0A0F0I8Q2_ASPPU
Original site: A0A0F0I8Q2_ASPPU 
ID   A0A0F0I8Q2_ASPPU        Unreviewed;      1900 AA.
AC   A0A0F0I8Q2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=SNF2 family N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=P875_00095405 {ECO:0000313|EMBL:KJK62368.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK62368.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK62368.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KJK62368.1}.
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DR   EMBL; JZEE01000622; KJK62368.1; -; Genomic_DNA.
DR   STRING; 1403190.A0A0F0I8Q2; -.
DR   Proteomes; UP000033540; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   CDD; cd17999; DEXHc_Mot1; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR044972; Mot1.
DR   InterPro; IPR044078; Mot1_ATP-bd.
DR   InterPro; IPR022707; Mot1_central_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   Pfam; PF12054; DUF3535; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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:UP000033540};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1323..1496
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1670..1821
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          187..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..740
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1900 AA;  210552 MW;  A2E193E6315ED7D6 CRC64;
     MTSRLDRLVT LLETGSTPLI RNTAAQQLAD VQKQHPDELF NLLGRILPYL KSKSWDTRTA
     AAKAIGLIVT NADIFDPNEE DGLGIKKADD EDDLAVEIKS EEAQLSPSDE LLQLESLDLT
     SILKYGKRLL GSAGKEYEYS LAAMDPISRL QHQKKTLNSR LGLAGEYIEE DLIDDTDLGL
     KTPAIKEDSS HTAVSRENSH QLSAPVTTPS EPANGEESGL SKRQLNQLKR KNKQSAKMGA
     NKVRVVDLSA RKTSDVTTPS VTTPHPIKAE NGEERNGDSK SDYFSLERPS GDDDSKIVSE
     FKGEAAPEKP LIQPESSDEG PSIAWPYEPM CDFLMVDLFD PNWEVRHGAA MALREVIRVQ
     GAGAGRLRGK SRSENDTLNR KWLDDLACRL ICVLMLDRFG DYISDNVVAP IRETVGQTLG
     ALLSQLPSRS VIAVYRCLYR IIMQNDLGLE RPIWEVCHGG MIGLRYLVAV RKDLLVKDAK
     LMDGVLEAVM KGLGDYDDDV RAVSAATLVP IAEEFVTSRQ NTLGTLMNIV WECLSNLQDD
     LSASTGSVMD LLAKLCTFRE VLDAMKANAA VDPESSFGNL VPRLYPFLRH TITSVRSAVL
     RALMTFLQLE GDGTNEWVNG KALRLIFQNL LVERNETVLK LSLQVWSELL KALDKHGSFK
     SEAELLSHIQ PLITLSMAPF GVPRYPIPMN ASLFIKPSGV PFPMSAAAPA KSSPSAFNNT
     SDATKKRGRK AEKKEVPPPS AHNVDGHMLQ GDIDLVGADT MLRSKIHAAK ALGQLLSFWD
     KNGLPSLWQP ILHGLKHSAS TSQLATAMII EEYARIQGSD SPYASVLCEQ LRPIIEGDRP
     SWYGDIACYL HVARAQCHSL LNAFRDHAHV PGSRLPVLAV IVQGEAEAGP SAFSLADAEK
     VVGPDFERLK KGLAPAQRIT ALQVLNDTRA TAESAINEAR SVREARDLRI LAAAAGALVA
     MHNIPKKPSH IIKGMMDSIK KEENAELQQR SATAVVTLVE YYTTATKRGP VDKVIGNLVK
     YCCVDTSETP EFHHNAGLEK SILSLRKEED RRDHPDAAKF EREAKEARIM RRGAKEALEQ
     LAVKFGPALL EKVPNLASLV ERPLTDALAN ELPADIHNPD NELGQEVVDG LSTLRALLPK
     FHPGLHPWVV SLMPLIAKAL QCRLSVIRYA AAKCFATVCS VITVEGMTML VEKVLPTISN
     GLDVHHRQGA VECIYHLIHV MEDGILPYVI FLVVPVLGRM SDSDNDVRLL ATTSFATLVK
     LVPLEAGIPD PPGLSEELLK GRERERKFMS QMLDVRKVEE FTLPVAIKAE LRPYQQEGVN
     WLAFLNRYNL HGILCDDMGL GKTLQTICIV ASDHHLRAEE FARTQAPEVR KLPSLIVCPP
     SLSGHWQQEI KQYAPFLKCV AYVGPPVERA RLKGSIGDAD IVITSYDICR NDSDVITPLN
     WNYCVLDEGH LIKNPKAKVT LAVKRVASNH RLILSGTPIQ NNVLELWSLF DFLMPGFLGT
     EKVFLDRFAK PIAASRFSKS SSKEQEAGAL AIEALHKQVL PFLLRRLKEE VLNDLPPKII
     QNYYCDPSEL QKKLFEDFTK KEQKQLANKM GSSEKSDKEH IFQALQYMRR LCNSPALVVK
     DGHKQYDEVQ QYLHAKNSYI RDVAHAPKLS ALRDLLLDCG IGVDPPSEGD LGTGASYVSP
     HRALIFCQMK EMLDIVQSEV LKKLLPSVQY LRLDGSVEAT KRQDIVNRFN TDPSYDALLL
     TTSVGGLGLN LTGADTVIFV EHDWNPQKDI QAMDRAHRIG QKKVVNVYRL ITRGTLEEKI
     LNLQRFKIDV ASTVVNQQNA GLNTMDTDQL LDLFNLGETA ENAEKPNDNA AGNEVDMVDI
     DGEVKEKGKK GWLDDLGELW DDRQYQEEYN LDSFLQTMKG
//
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