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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//