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Database: UniProt
Entry: A0A0D2AUU4_9EURO
LinkDB: A0A0D2AUU4_9EURO
Original site: A0A0D2AUU4_9EURO 
ID   A0A0D2AUU4_9EURO        Unreviewed;      1123 AA.
AC   A0A0D2AUU4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV06_04637 {ECO:0000313|EMBL:KIW43546.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW43546.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW43546.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW43546.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) 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; KN847335; KIW43546.1; -; Genomic_DNA.
DR   RefSeq; XP_016263762.1; XM_016405556.1.
DR   AlphaFoldDB; A0A0D2AUU4; -.
DR   STRING; 215243.A0A0D2AUU4; -.
DR   GeneID; 27356711; -.
DR   VEuPathDB; FungiDB:PV06_04637; -.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000053342; 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; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 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:UP000053342}.
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          864..916
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          823..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1060
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1093..1116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1123 AA;  128542 MW;  7A2EE3C85ECA5298 CRC64;
     MAPIKPQQTD SENSSVADIS MTDAHSIIQP RRPSFGHLNR YMDDTPDYTD SDTNPNTTTS
     SVAGDIVAPD GRKRRSEAFQ LRKSILGRKH GQLDESKEDD TIRRFKYLLG LTDLFRHFIE
     TNPNPKIRDV VEEIDRQNAD DAAKAKKGVS RKGGAAAGAK RKTEQEEDAE LLRDEKRGTA
     SQTIFRDSPA FIQGGEMRDY QVAGLNWLIS LHENGISGIL ADEMGLGKTL QTISFLGYLR
     HICDIKGPHL IAVPKSTLDN WAREFKKWTP EVDVLVLQGA KDDRHALIQD RLIEEKFDVC
     ITSYEMILRE KSHLKKFAWE YIIVDEAHRI KNEESSLAQI IRMFTSRNRL LITGTPLQNN
     LHELWALLNF LLPDVFGDSE AFDSWFSSQN DDQDTVVQQL HRVLRPFLLR RVKSDVEKSL
     LPKKEVNLYV GMSEMQVKWY QRILEKDIDA VNGAGGKRES KTRLLNIVMQ LRKCCNHPYL
     FEGAEPGPPY TTDEHLVYNS GKMIILDKIL NRMKEEGSRV LIFSQMSRVL DILEDYCVFR
     GHKYCRIDGG TAHEDRIAAI DDYNKPDSEK FVFLLTTRAG GLGINLTTAN IVVLYDSDWN
     PQADLQAMDR AHRIGQTKQV RVFRFVTENA IEEKVLERAA QKLRLDQLVI QQGRAQQQVK
     QAASKDDLLN MIQHGAEKVF ETKGATGALD DIDEILQRGE ARTAELNKKY EKLGIDDLQK
     FSSENAYEWN GEDFTQRRKD IAVSWINPAK RERKEQFYSV DKYYKQALST GGGKPAEPKP
     KVPRAPKQVN VHDWQFFPPG LQELQEKETA YYHKEIGYKV PLADGTEEDL SDREADQRLN
     QDEIDNAEPL TEEEKQKKAE MQEHGFGNWN RRDFQQFING SAKFGRNNYE GIANEVDSKE
     PDEIEEYAKV FWKRYTEIAD YDKHIKTIEA GEEKLRKTNL QRKLLRKKME MYRVPLQQLK
     INYTVSTTNK KVYTEEEDRF LLVMLDKHGV DGEGLYDKIR DEIRESPLFR FDWFFLSRTP
     VEIGRRCTTL LNTVLREFGD PEEKLTNGHG SGKGRGRDRD DEEDEDNDSE AAPVKKKAKN
     GIVNKAVKAV KSGRGSKNTS PATSRAQSVS STAPASKSKG KKK
//
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