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Database: UniProt
Entry: A0A0D1Y828_9EURO
LinkDB: A0A0D1Y828_9EURO
Original site: A0A0D1Y828_9EURO 
ID   A0A0D1Y828_9EURO        Unreviewed;      1122 AA.
AC   A0A0D1Y828;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 44.
DE   RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV08_10406 {ECO:0000313|EMBL:KIW11106.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW11106.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW11106.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW11106.1,
RC   ECO:0000313|Proteomes:UP000053328};
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 spinifera CBS89968.";
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; KN847499; KIW11106.1; -; Genomic_DNA.
DR   RefSeq; XP_016231322.1; XM_016384720.1.
DR   AlphaFoldDB; A0A0D1Y828; -.
DR   STRING; 91928.A0A0D1Y828; -.
DR   GeneID; 27337489; -.
DR   VEuPathDB; FungiDB:PV08_10406; -.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000053328; 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:UP000053328}.
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..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          822..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1122
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..174
FT                   /note="Basic and acidic 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        1092..1115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1122 AA;  128422 MW;  D42FBA9EEBF67D0F CRC64;
     MAPTKPQQTD SENSSIADTS MIDAHSVLQP RRPSFGHLNR YMDDTPDYTD SDTNPNTTAS
     SVAGDSVAPD GRKRRSEAFQ LRKSILGRKH GQLDESKEDD TVRRFKYLLG LTDLFRHFIE
     TNPNPKIREV MEEIDRQNAE DAAKAKKGVS RKGGAAAGAK RKTEQEEDAE LLRDEKRGTA
     SQTIFRESPA FIQGGEMRDY QVAGLNWLIS LHENGISGIL ADEMGLGKTL QTISFLGYLR
     HICDIKGPHL VAVPKSTLDN WAREFKKWTP EVDVLVLQGA KDDRHALIND RLIEEKFDVC
     ITSYEMILRE KSHLKKFAWE YIIVDEAHRI KNEESSLAQI IRMFTSRNRL LITGTPLQNN
     LHELWALLNF LLPDVFGDSE AFDSWFSSQN NDQDTVVQQL HRVLRPFLLR RVKSDVEKSL
     LPKKEVNLYV GMSEMQVKWY QRILEKDIDA VNGAGGKRES KTRLLNIVMQ LRKCCNHPYL
     FEGAEPGPPY TTDEHLVYNS GKMIILDKIL NRMKEEGSRV LIFSQMSRVL DILEDYCVFR
     GHKYCRIDGG TAHEDRIAAI DEYNKPGSEK FVFLLTTRAG GLGINLTTAN IVVLYDSDWN
     PQADLQAMDR AHRIGQTKQV KVFRFVTENA IEEKVLERAA QKLRLDQLVI QQGRAQQQVK
     QAASKDDLLN MIQHGAEKVF ETKGATGALD DIDEILQRGE ARTAELNKKY EKLGIDDLQK
     FSSENAYEWN GEDFTNRRKD IGINWINPAK RERKEQSYSM DKYYKQALST GGKPAETKPK
     VPRAPKQVNV HDWQFFPPGL QELQEKETAY YHKEIGYKVP LAEGTEEDLS DREADQRLNQ
     DEIDNAEPLT EEEKQRKAEM QEHGFGNWNR RDFQQFINGS AKFGRTNYEG IANEVDSKEP
     DEIEEYAKVF WKRYTEIADY DKHIKTIEAG EEKLRKTNLQ RKLLRKKMEM YRVPLQQLKI
     NYTVSTTNKK VYTEEEDRFL LVMLDKHGVD GEGLYDKIRD EIRDSPLFRF DWFFLSRTPV
     EIGRRCTTLL NTVLREFGDP EEKLTNGHGS GKGRGRDRDD DDDDDNESEA PPVKKKAKNG
     IVNKAVKAVK SGRGSKNTSP ATSRAQSVSS STPASKSKGR KK
//
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