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Database: UniProt
Entry: A0A0D2DF97_9EURO
LinkDB: A0A0D2DF97_9EURO
Original site: A0A0D2DF97_9EURO 
ID   A0A0D2DF97_9EURO        Unreviewed;      1123 AA.
AC   A0A0D2DF97;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 43.
DE   RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z517_11122 {ECO:0000313|EMBL:KIW76376.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW76376.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW76376.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW76376.1,
RC   ECO:0000313|Proteomes:UP000053029};
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 Fonsecaea pedrosoi CBS 271.37.";
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; KN846975; KIW76376.1; -; Genomic_DNA.
DR   RefSeq; XP_013280184.1; XM_013424730.1.
DR   AlphaFoldDB; A0A0D2DF97; -.
DR   STRING; 1442368.A0A0D2DF97; -.
DR   GeneID; 25310612; -.
DR   VEuPathDB; FungiDB:Z517_11122; -.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000053029; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053029}.
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          863..915
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          920..947
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..20
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        1040..1059
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1095..1116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1123 AA;  128646 MW;  3EFC86C64711FFD6 CRC64;
     MAPSKPQQPD SETSSVAETP MTDGPDYIRP HRPSFGHLNR PVDDTPDYTD SDTNPNTTAS
     SVAGDTPLAD GRKKRSEAFQ LRKSILGKKH GQLDESKEDD TLRRFKYLLG LTDLFRHFID
     ASPNPKIREV LQQIDQENAE EEAKARKVVS RKGGAAGAAK RKTEQEEDAE LLRDEKRGTA
     SQTVFRDSPA FIKGGEMRDY QVAGLNWLIS LHENGISGIL ADEMGLGKTL QTISFLGYLR
     HICGIKGPHL ITVPKSTLDN WRREFEKWTP DVDVLVLQGA KEDRHALINE RLIDEKFDVC
     ITSYEMILRE KSHLKKFAWE YIIVDEAHRI KNEESSLAQI IRMFSSRNRL LITGTPLQNN
     LHELWALLNF LLPDVFGDSE AFDSWFSSQN EDQDTVVQQL HRVLRPFLLR RVKSDVEKSL
     LPKKEVNLYV GMSEMQVKWY KKILEKDIDA VNGAGGKRES KTRLLNIVMQ LRKCCNHPYL
     FEGAEPGPPY TTDEHLVFNS GKMIILDKIL KRMKDEGSRV LIFSQMSRVL DILEDYCVFR
     GHQYCRIDGG TAHEDRIAAI DEYNKPGSEK FVFLLTTRAG GLGINLTSAN IVILYDSDWN
     PQADLQAMDR AHRIGQTKQV VVFRFVTENA IEEKVLERAA QKLRLDQLVI QQGRAQQQVK
     QAASKDELLT MIQHGAEKVF ETKGTTGELD DIDEILRRGE ARTAELSAKY EKLGIDDLQK
     FSSENAYEWN GEDFTNRKKD ISLHWINPSK RERKEQSYSM DKYYKQALST GGRPADTKPK
     IPRAPKQVVV HDWQFFPPGL QELQEKETAY YHKEIGFKVP LTDGTEEDLS DREADQRLAQ
     NEIDNAEPLT EEEKQLKAEM QEHGFGNWNR RDFQQFINGS AKFGRTNYEG IATEVDSKEP
     DEVEKYAKVF WKRYTEIAEF DKYIKNIEAG EEKLRKTERQ RKMLRKKMEM YRVPLQQLKI
     NYTVSTTNKK VYTEEEDRFL LVMLDKYGVD GEGLYERIRD EIRESPLFRF DWFFLSRTPV
     EIGRRCTTLL NTVSREFGET EEKLTNGHAP GKGRGRDRDD EEDEENDSEA PPVKKKAKNG
     IVNKQVKAVK SGRGSKATSP ATSRAQSVSS TTPTASKSKG KKK
//
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