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Database: UniProt
Entry: A0A1J9PXU2_9EURO
LinkDB: A0A1J9PXU2_9EURO
Original site: A0A1J9PXU2_9EURO 
ID   A0A1J9PXU2_9EURO        Unreviewed;      1163 AA.
AC   A0A1J9PXU2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACJ73_07511 {ECO:0000313|EMBL:OJD21152.1};
OS   Blastomyces percursus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD21152.1, ECO:0000313|Proteomes:UP000242791};
RN   [1] {ECO:0000313|EMBL:OJD21152.1, ECO:0000313|Proteomes:UP000242791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI222 {ECO:0000313|EMBL:OJD21152.1,
RC   ECO:0000313|Proteomes:UP000242791};
RA   Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA   Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (AUG-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}.
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:OJD21152.1}.
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DR   EMBL; LGTZ01001532; OJD21152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9PXU2; -.
DR   STRING; 1658174.A0A1J9PXU2; -.
DR   VEuPathDB; FungiDB:ACJ73_07511; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000242791; 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:UP000242791}.
FT   DOMAIN          239..404
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          535..686
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          901..953
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1078..1163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1090..1114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1120..1154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1163 AA;  133374 MW;  8CE6239AD0F0CA53 CRC64;
     MAPSLSHLSG SESPAHTDTP MADANGYPSN TMEGTRDEDQ SMMDYQDTPD YTVWLLPIYA
     TRKDRYLLEA FRPNALTLRQ DSDTNPNTTA SSIAGDIAQQ DGRKRRSEAF QLRKSVLGRK
     HGRLDESKED DSIRRFRYLL GLTDLFRHFI ETNPNPRIKE IMAEIDRQNE AQSNSRKGLT
     RKGGASGERR RRTEQEEDAE LLKDEKRGGQ AETVFRESPA FVKGGEMRDY QVAGLNWLVS
     LHENGISGIL ADEMGLGKTL QTIAFLGYLR HLCGITGPHL ITVPKSTLDN WHREFSKWTP
     DVNVLVLQGA KEDRHKLINE RLVDEKFDVC ITSYEMVLRE KSHLKKFAWE YIIIDEAHRI
     KNEESSLAQI IRVFHSRNRL LITGTPLQNN LHELWALLNF LLPDVFGDSD AFDQWFSNQE
     ADQDTVVQQL HRVLRPFLLR RVKSDVEKSL LPKKEMNLYV GMSDMQVKWY QKILEKDIDA
     VNGAQGKRES KTRLLNIVMQ LRKCCNHPYL FEGAEPGPPY TTDEHLIDNA GKMVILDKIL
     KRMKNQGSRV LIFSQMSRVL DILEDYCVFR EHQYCRIDGS TAHEDRIAAI DEYNRPGSEK
     FIFLLTTRAG GLGINLTSAD IVILYDSDWN PQADLQAMDR AHRIGQTKQV IVFRFVTENA
     IEEKVLERAA QKLRLDQLVI QQGRAQQQVK NAASKDELLS MIQHGAASVF NTKGPTGALA
     KGNDISEDDI DEILRKGEER TAELNKKYEK LGIDDLQKFT SDNAYEWNGE DFTNRKKDIG
     INWINPAKRE RKEQSYSMDQ YYRQALATGG RTADPKPKVP RAPKQIAVHD WQFFPPKLQE
     LQEKETAYFH KEIGYKAVLP DGPDEELSDR EAERELEQQE IDNAVPLTEE EQEQKAALSE
     EGFGNWNRRD FQQFINGSAK FGRTNYTEIA TEVDSKEPDE IKEYAKVFWK RYTEIQDYPK
     HIRVIEQGEE KMRKMNHQRK LLRKKMEMYR VPLQQLKVNY TVSTTNKKVY TEEEDRFLLV
     MLDRHGVDGE GLYEKIREEI RESPLFRFDW FFLSRTPVEI GRRCTTLLNT VAKEFEVDGG
     KIPNGDTGGG KGRGRDRDDD VENEEVEAPA KKKTKNGAVN KQLKAVQSAS GSRATSTATS
     RAGSVSSSAP ATNKSKGKRK QKE
//
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