ID A0A232LUF5_9EURO Unreviewed; 1126 AA.
AC A0A232LUF5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 18-JUN-2025, entry version 35.
DE RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Egran_04491 {ECO:0000313|EMBL:OXV07746.1};
OS Elaphomyces granulatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Elaphomycetaceae; Elaphomyces.
OX NCBI_TaxID=519963 {ECO:0000313|EMBL:OXV07746.1, ECO:0000313|Proteomes:UP000243515};
RN [1] {ECO:0000313|EMBL:OXV07746.1, ECO:0000313|Proteomes:UP000243515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSC145934 {ECO:0000313|EMBL:OXV07746.1,
RC ECO:0000313|Proteomes:UP000243515};
RX PubMed=25753751; DOI=10.1111/1462-2920.12840;
RA Quandt C.A., Kohler A., Hesse C.N., Sharpton T.J., Martin F.,
RA Spatafora J.W.;
RT "Metagenome sequence of Elaphomyces granulatus from sporocarp tissue
RT reveals Ascomycota ectomycorrhizal fingerprints of genome expansion and a
RT Proteobacteria-rich microbiome.";
RL Environ. Microbiol. 17:2952-2968(2015).
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:OXV07746.1}.
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DR EMBL; NPHW01004590; OXV07746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232LUF5; -.
DR OrthoDB; 5857104at2759; -.
DR Proteomes; UP000243515; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:TreeGrafter.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0034728; P:nucleosome organization; IEA:TreeGrafter.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.300:FF:000082; ISWI chromatin remodeling complex ATPase ISW1; 1.
DR FunFam; 1.10.10.60:FF:000022; ISWI chromatin-remodeling complex ATPase CHR11 isoform A; 1.
DR FunFam; 3.40.50.10810:FF:000002; ISWI chromatin-remodeling complex ATPase CHR11 isoform A; 1.
DR FunFam; 1.20.5.1190:FF:000005; ISWI chromatin-remodeling complex ATPase ISW1; 1.
DR FunFam; 1.10.10.60:FF:000234; ISWI chromatin-remodeling complex ATPase ISW2; 1.
DR FunFam; 1.10.1040.30:FF:000003; ISWI chromatin-remodeling complex ATPase ISW2; 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-like.
DR InterPro; IPR009057; Homeodomain-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 5; 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 Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000243515};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 210..375
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 506..657
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 872..924
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1076
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1094
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1120
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1126 AA; 128994 MW; 0D635EC5B8B75480 CRC64;
MAPLQAIALE SDPPSQVDTP MTDANEEPVT RIPVDGVDVP VTDYQDTPEY TDSDTNPNTT
ASSVADELAR IDGRKRRSEA FALRKSVLGK KHGRLDESKE DDSIRRFRYL LGLTDLFRHF
IETNPNPRIK EIMAEIDRQN EEDAANAKKG ASRKGGAPGD RRRRTEQEED AELLKDEKRG
GETTTVFRGS PSFIRGEMRD YQIAGLNWLI SLHENGISGI LADEMGLGKT LQTIAFLGYL
RHLCAITGPH LIAVPKSTLD NWKREFERWT PEVNVLVLQG AKEERHQLIN ERLIDEHFDV
CITSYEMVLR EKSHLKKFAW EYIIIDEAHR IKNEESSLAQ IIRVFNSRNR LLITGTPLQN
NLHELWALLN FLLPDVFGDS DAFDQWFSSQ DADQDTVVQQ LHRVLRPFLL RRVKSDVEKS
LLIKKEMNLY VGMSEMQVKW YQKILEKDID AVNGAAGKRE TKTRLLNIVM QLRKCCNHPY
LFEGAEPGPP YTTDEHLVNN AGKMVILDKI LDRMKKQDSR VLIFSQMSRV LDILEDYCVF
RGHKYCRIDG STAHEDRIAA IDDYNRPGSE KFVFLLTTRA GGLGINLTTA DIVVLYDSDW
NPQADLQAMD RAHRIGQTKQ VIVFRFVTEH AIEEKVLERA AQKLRLDQLV IQQGRAQQQV
KNAASKEELL GMIQHGAVDI VKSKGGTGSL AGGNDISEDA IDNILRKGEE RTAELKEKYE
KLGIDELQKF TSDNAYEWNG EDFTNRKKDI GINWINPAKR ERKEQFYSID KYYRQALATG
GRTADPKPKM PRPPKQIVVH DWQFFPPGLQ DLQEKETAYF HKEIGYKAVL PDGPEEDLSD
REAERELEQQ EIDNAVPLTE EEQAEKAKMS EEGFSYWNRR DFQQFVNGSA KFGRTDYEGI
STEVDSKAPE EIKEYAKVFW KRYTEIQDYP KYLRVIEQGE EKMRKMNHQR KMLRKKMEMY
RVPLQQLKIN YTVSTTNKKV YTEEEDRFLL VMLDRYGVDG EGLYDKIRDE IRESPLFRFD
WFFLSRTPVE IGRRCTTLLN TVAREFEAPD GKANGEGGKG RGRDRDEDDA DEEEVEAPAK
KKTKNGAVNK HIKAVKGSSK VTSTSTSRAA SVSSTAPASK AKGRKK
//
